Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P02820
|
OSTCN_BOVIN
|
MRTPMLLALLALATLCLAGRADAKPGDAESGKGAAFVSKQEGSEVVKRLRRYLDHWLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGPV
| null | null |
biomineral tissue development [GO:0031214]; bone development [GO:0060348]; brain development [GO:0007420]; cellular response to insulin stimulus [GO:0032869]; cognition [GO:0050890]; glucose homeostasis [GO:0042593]; learning or memory [GO:0007611]; negative regulation of bone development [GO:1903011]; osteoblast differentiation [GO:0001649]; positive regulation of neurotransmitter secretion [GO:0001956]; regulation of bone mineralization [GO:0030500]; regulation of cellular response to insulin stimulus [GO:1900076]; regulation of testosterone biosynthetic process [GO:2000224]; response to vitamin K [GO:0032571]; type B pancreatic cell proliferation [GO:0044342]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; hormone activity [GO:0005179]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147]
| null | null |
Osteocalcin/matrix Gla protein family
|
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium (By similarity) (PubMed:1068450, PubMed:12820886). Decarboxylation promotes the hormone activity (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:1068450, ECO:0000269|PubMed:12820886}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1068450}.
| null | null | null | null | null |
FUNCTION: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein (PubMed:1068450). It acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly to apatite and calcium (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000269|PubMed:1068450}.; FUNCTION: The uncarboxylated form acts as a hormone secreted by osteoblasts, which regulates different cellular processes, such as energy metabolism, male fertility and brain development. Regulates of energy metabolism by acting as a hormone favoring pancreatic beta-cell proliferation, insulin secretion and sensitivity and energy expenditure. Uncarboxylated osteocalcin hormone also promotes testosterone production in the testes: acts as a ligand for G protein-coupled receptor GPRC6A at the surface of Leydig cells, initiating a signaling response that promotes the expression of enzymes required for testosterone synthesis in a CREB-dependent manner. Also acts as a regulator of brain development: osteocalcin hormone crosses the blood-brain barrier and acts as a ligand for GPR158 on neurons, initiating a signaling response that prevents neuronal apoptosis in the hippocampus, favors the synthesis of all monoamine neurotransmitters and inhibits that of gamma-aminobutyric acid (GABA). Osteocalcin also crosses the placenta during pregnancy and maternal osteocalcin is required for fetal brain development. {ECO:0000250|UniProtKB:P86546}.
|
Bos taurus (Bovine)
|
P02821
|
OSTCN_FELCA
|
YLAPGLGAPAPYPDPLEPKREICELNPDCDELADHIGFQDAYRRFYGTV
| null | null |
biomineral tissue development [GO:0031214]; bone development [GO:0060348]; brain development [GO:0007420]; cellular response to insulin stimulus [GO:0032869]; cognition [GO:0050890]; glucose homeostasis [GO:0042593]; learning or memory [GO:0007611]; negative regulation of bone development [GO:1903011]; osteoblast differentiation [GO:0001649]; positive regulation of neurotransmitter secretion [GO:0001956]; regulation of bone mineralization [GO:0030500]; regulation of cellular response to insulin stimulus [GO:1900076]; regulation of testosterone biosynthetic process [GO:2000224]; response to vitamin K [GO:0032571]; type B pancreatic cell proliferation [GO:0044342]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; hormone activity [GO:0005179]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147]
| null | null |
Osteocalcin/matrix Gla protein family
|
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium (By similarity) (PubMed:6334077). Decarboxylation promotes the hormone activity (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6334077}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6334077}.
| null | null | null | null | null |
FUNCTION: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein (PubMed:6334077). It acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly to apatite and calcium (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000269|PubMed:6334077}.; FUNCTION: The uncarboxylated form acts as a hormone secreted by osteoblasts, which regulates different cellular processes, such as energy metabolism, male fertility and brain development. Regulates of energy metabolism by acting as a hormone favoring pancreatic beta-cell proliferation, insulin secretion and sensitivity and energy expenditure. Uncarboxylated osteocalcin hormone also promotes testosterone production in the testes: acts as a ligand for G protein-coupled receptor GPRC6A at the surface of Leydig cells, initiating a signaling response that promotes the expression of enzymes required for testosterone synthesis in a CREB-dependent manner. Also acts as a regulator of brain development: osteocalcin hormone crosses the blood-brain barrier and acts as a ligand for GPR158 on neurons, initiating a signaling response that prevents neuronal apoptosis in the hippocampus, favors the synthesis of all monoamine neurotransmitters and inhibits that of gamma-aminobutyric acid (GABA). Osteocalcin also crosses the placenta during pregnancy and maternal osteocalcin is required for fetal brain development. {ECO:0000250|UniProtKB:P86546}.
|
Felis catus (Cat) (Felis silvestris catus)
|
P02822
|
OSTCN_CHICK
|
MKAAALLLLAALLTFSLCRSAPDGSDARSAKAFISHRQRAEMVRRQKRHYAQDSGVAGAPPNPLEAQREVCELSPDCDELADQIGFQEAYRRFYGPV
| null | null |
biomineral tissue development [GO:0031214]; bone development [GO:0060348]; cellular response to insulin stimulus [GO:0032869]; glucose homeostasis [GO:0042593]; negative regulation of bone development [GO:1903011]; osteoblast differentiation [GO:0001649]; regulation of bone mineralization [GO:0030500]; regulation of cellular response to insulin stimulus [GO:1900076]; response to vitamin K [GO:0032571]; type B pancreatic cell proliferation [GO:0044342]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; hormone activity [GO:0005179]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147]
| null | null |
Osteocalcin/matrix Gla protein family
|
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium. {ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6792200}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6792200}.
| null | null | null | null | null |
FUNCTION: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein (PubMed:6792200). The carboxylated form binds strongly to apatite and calcium (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000269|PubMed:6792200}.
|
Gallus gallus (Chicken)
|
P02825
|
HSP71_DROME
|
MPAIGIDLGTTYSCVGVYQHGKVEIIANDQGNRTTPSYVAFTDSERLIGDPAKNQVAMNPRNTVFDAKRLIGRKYDDPKIAEDMKHWPFKVVSDGGKPKIGVEYKGESKRFAPEEISSMVLTKMKETAEAYLGESITDAVITVPAYFNDSQRQATKDAGHIAGLNVLRIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTFDVSILTIDEGSLFEVRSTAGDTHLGGEDFDNRLVTHLADEFKRKYKKDLRSNPRALRRLRTAAERAKRTLSSSTEATIEIDALFEGQDFYTKVSRARFEELCADLFRNTLQPVEKALNDAKMDKGQIHDIVLVGGSTRIPKVQSLLQDFFHGKNLNLSINPDEAVAYGAAVQAAILSGDQSGKIQDVLLVDVAPLSLGIETAGGVMTKLIERNCRIPCKQTKTFSTYADNQPGVSIQVYEGERAMTKDNNALGTFDLSGIPPAPRGVPQIEVTFDLDANGILNVSAKEMSTGKAKNITIKNDKGRLSQAEIDRMVNEAEKYADEDEKHRQRITSRNALESYVFNVKQAVEQAPAGKLDEADKNSVLDKCNDTIRWLDSNTTAEKEEFDHKLEELTRHCSPIMTKMHQQGAGAGAGGPGANCGQQAGGFGGYSGPTVEEVD
| null | null |
chaperone cofactor-dependent protein refolding [GO:0051085]; heat shock-mediated polytene chromosome puffing [GO:0035080]; protein refolding [GO:0042026]; response to heat [GO:0009408]; response to hypoxia [GO:0001666]; response to unfolded protein [GO:0006986]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; heat shock protein binding [GO:0031072]; protein folding chaperone [GO:0044183]
|
PF00012;
|
1.20.1270.10;3.30.30.30;3.30.420.40;
|
Heat shock protein 70 family
| null | null | null | null | null | null | null | null |
Drosophila melanogaster (Fruit fly)
|
P02828
|
HSP83_DROME
|
MPEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELYIKLIPNKTAGTLTIIDTGIGMTKSDLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVADKVTVTSKNNDDEQYVWESSAGGSFTVRADNSEPLGRGTKIVLYIKEDQTDYLEESKIKEIVNKHSQFIGYPIKLLVEKEREKEVSDDEADDEKKEGDEKKEMETDEPKIEDVGEDEDADKKDKDAKKKKTIKEKYTEDEELNKTKPIWTRNPDDISQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRTPFDLFENQKKRNNIKLYVRRVFIMDNCEDLIPEYLNFMKGVVDSEDLPLNISREMLQQNKVLKVIRKNLVKKTMELIEELTEDKENYKKFYDQFSKNLKLGVHEDSNNRAKLADFLRFHTSASGDDFCSLADYVSRMKDNQKHVYFITGESKDQVSNSAFVERVKARGFEVVYMTEPIDEYVIQHLKEYKGKQLVSVTKEGLELPEDESEKKKREEDKAKFESLCKLMKSILDNKVEKVVVSNRLVDSPCCIVTSQFGWSANMERIMKAQALRDTATMGYMAGKKQLEINPDHPIVETLRQKADADKNDKAVKDLVILLFETSLLSSGFSLDSPQVHASRIYRMIKLGLGIDEDEPMTTDDAQSAGDAPSLVEDTEDASHMEEVD
| null | null |
cellular response to heat [GO:0034605]; centrosome cycle [GO:0007098]; cold acclimation [GO:0009631]; membrane bending [GO:0097753]; multivesicular body fusion to apical plasma membrane [GO:0098866]; negative regulation of cell population proliferation [GO:0008285]; oogenesis [GO:0048477]; pole plasm mRNA localization [GO:0019094]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of neuroblast proliferation [GO:0002052]; proteasome assembly [GO:0043248]; protein folding [GO:0006457]; protein stabilization [GO:0050821]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]; response to heat [GO:0009408]; RISC complex assembly [GO:0070922]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum chaperone complex [GO:0034663]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; polytene chromosome interband [GO:0005705]; protein folding chaperone complex [GO:0101031]; protein-containing complex [GO:0032991]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; insulin receptor binding [GO:0005158]; TPR domain binding [GO:0030911]; unfolded protein binding [GO:0051082]
|
PF13589;PF00183;
|
3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10;
|
Heat shock protein 90 family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Together with Hop and piwi, mediates canalization, also known as developmental robustness, likely via epigenetic silencing of existing genetic variants and suppression of transposon-induced new genetic variation. Required for piRNA biogenesis by facilitating loading of piRNAs into PIWI proteins. {ECO:0000269|PubMed:21186352, ECO:0000269|PubMed:22902557}.
|
Drosophila melanogaster (Fruit fly)
|
P02829
|
HSP82_YEAST
|
MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIPEEEKKDEEKKDEEKKDEDDKKPKLEEVDEEEEKKPKTKKVKEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSEQFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPTSFASRINRLISLGLNIDEDEETETAPEASTAAPVEEVPADTEMEEVD
| null | null |
'de novo' protein folding [GO:0006458]; box C/D snoRNP assembly [GO:0000492]; cellular response to heat [GO:0034605]; positive regulation of telomere maintenance via telomerase [GO:0032212]; proteasome assembly [GO:0043248]; protein folding [GO:0006457]; protein maturation [GO:0051604]; protein refolding [GO:0042026]; protein stabilization [GO:0050821]; protein targeting to mitochondrion [GO:0006626]; regulation of telomere maintenance [GO:0032204]; response to osmotic stress [GO:0006970]; response to oxygen levels [GO:0070482]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; identical protein binding [GO:0042802]; unfolded protein binding [GO:0051082]
|
PF13589;PF00183;
|
3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10;
|
Heat shock protein 90 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
| null | null | null | null | null |
FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures. {ECO:0000269|PubMed:17114002}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P02830
|
HXA7_MOUSE
|
MSSSYYVNALFSKYTAGASLFQNAEPTSCSFAPNSQRSGYGPGAGAFASTVPGLYNVNSPLYQSPFASGYGLGADAYNLPCASYDQNIPGLCSDLAKGACDKADEGVLHGPAEASFRIYPWMRSSGPDRKRGRQTYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLTERQIKIWFQNRRMKWKKEHKDESQAPTAAPEDAVPSVSTAADKADEEEEEEEEEEEEEEE
| null | null |
angiogenesis [GO:0001525]; anterior/posterior pattern specification [GO:0009952]; embryonic skeletal system morphogenesis [GO:0048704]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of keratinocyte differentiation [GO:0045617]; negative regulation of leukocyte migration [GO:0002686]; negative regulation of monocyte differentiation [GO:0045656]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; stem cell differentiation [GO:0048863]
|
nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00046;
|
1.10.10.60;
|
Antp homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
|
Mus musculus (Mouse)
|
P02831
|
HXA3_MOUSE
|
MQKATYYDSSAIYGGYPYQAANGFAYNASQQPYAPSAALGTDGVEYHRPACSLQSPASAGGHPKTHELSEACLRTLSGPPSQPPGLGEPPLPPPPPQAAPPAPQPPQPPPQPPAPTPAAPPPPSSVSPPQSANSNPTPASTAKSPLLNSPTVGKQIFPWMKESRQNTKQKTSGSSSGESCAGDKSPPGQASSKRARTAYTSAQLVELEKEFHFNRYLCRPRRVEMANLLNLTERQIKIWFQNRRMKYKKDQKGKGMLTSSGGQSPSRSPVPPGAGGYLNSMHSLVNSVPYEPQSPPPFSKPPQGAYGLPPASYPAPLPSCAPPPPPQKRYTAAGSGAGGTPDYDPHAHGLQGNGSYGTPHLQGSPVFVGGSYVEPMSNSGPLFGLTHLPHTTSAAMDYGGTGPLGSGHHHGPGPGEPHPTYTDLTAHHPSQGRIQEAPKLTHL
| null | null |
angiogenesis [GO:0001525]; animal organ formation [GO:0048645]; animal organ morphogenesis [GO:0009887]; anterior/posterior pattern specification [GO:0009952]; blood vessel remodeling [GO:0001974]; cartilage development [GO:0051216]; cell population proliferation [GO:0008283]; embryonic skeletal system development [GO:0048706]; embryonic skeletal system morphogenesis [GO:0048704]; gene expression [GO:0010467]; glossopharyngeal nerve morphogenesis [GO:0021615]; parathyroid gland development [GO:0060017]; positive regulation of stem cell proliferation [GO:2000648]; regulation of transcription by RNA polymerase II [GO:0006357]; specification of animal organ position [GO:0010159]; stem cell proliferation [GO:0072089]; thymus development [GO:0048538]; thyroid gland development [GO:0030878]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; HMG box domain binding [GO:0071837]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF13293;PF00046;
|
1.10.10.60;
|
Antp homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds 5' to its own homeobox.
|
Mus musculus (Mouse)
|
P02833
|
ANTP_DROME
|
MTMSTNNCESMTSYFTNSYMGADMHHGHYPGNGVTDLDAQQMHHYSQNANHQGNMPYPRFPPYDRMPYYNGQGMDQQQQHQVYSRPDSPSSQVGGVMPQAQTNGQLGVPQQQQQQQQQPSQNQQQQQAQQAPQQLQQQLPQVTQQVTHPQQQQQQPVVYASCKLQAAVGGLGMVPEGGSPPLVDQMSGHHMNAQMTLPHHMGHPQAQLGYTDVGVPDVTEVHQNHHNMGMYQQQSGVPPVGAPPQGMMHQGQGPPQMHQGHPGQHTPPSQNPNSQSSGMPSPLYPWMRSQFGKCQERKRGRQTYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLTERQIKIWFQNRRMKWKKENKTKGEPGSGGEGDEITPPNSPQ
| null | null |
anterior/posterior axis specification [GO:0009948]; anterior/posterior pattern specification [GO:0009952]; heart development [GO:0007507]; lymph gland development [GO:0048542]; midgut development [GO:0007494]; muscle cell fate specification [GO:0042694]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuroblast development [GO:0014019]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of neurogenesis [GO:0050767]; specification of segmental identity, antennal segment [GO:0007383]; specification of segmental identity, thorax [GO:0007384]; ventral cord development [GO:0007419]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
|
PF00046;
|
1.10.10.60;
|
Antp homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that regulates segmental identity in the mesothorax. Provides cells with specific positional identities on the anterior-posterior axis.
|
Drosophila melanogaster (Fruit fly)
|
P02835
|
FTZ_DROME
|
MATTNSQSHYSYADNMNMYNMYHPHSLPPTYYDNSGSNAYYQNTSNYQGYYPQESYSESCYYYNNQEQVTTQTVPPVQPTTPPPKATKRKAEDDAASIIAAVEERPSTLRALLTNPVKKLKYTPDYFYTTVEQVKKAPAVSTKVTASPAPSYDQEYVTVPTPSASEDVDYLDVYSPQSQTQKLKNGDFATPPPTTPTSLPPLEGISTPPQSPGEKSSSAVSQEINHRIVTAPNGAGDFNWSHIEETLASDCKDSKRTRQTYTRYQTLELEKEFHFNRYITRRRRIDIANALSLSERQIKIWFQNRRMKSKKDRTLDSSPEHCGAGYTAMLPPLEATSTATTGAPSVPVPMYHHHQTTAAYPAYSHSHSHGYGLLNDYPQQQTHQQYDAYPQQYQHQCSYQQHPQDLYHLS
| null | null |
anterior/posterior pattern specification [GO:0009952]; cell fate specification [GO:0001708]; central nervous system development [GO:0007417]; germ cell migration [GO:0008354]; gonadal mesoderm development [GO:0007506]; negative regulation of transcription by RNA polymerase II [GO:0000122]; periodic partitioning by pair rule gene [GO:0007366]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; segmentation [GO:0035282]
|
nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF03867;PF00046;
|
1.10.10.60;
|
Antp homeobox family
|
PTM: Phosphorylated at as many as 16 sites. {ECO:0000269|PubMed:2743978}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:3049237}.
| null | null | null | null | null |
FUNCTION: May play a role in determining neuronal identity, may be directly involved in specifying identity of individual neurons. Required during embryogenesis for the process of body segmentation. Homeotic protein, required in alternating segment primordia, it specifies the correct number of segments. {ECO:0000269|PubMed:2892267, ECO:0000269|PubMed:3049237, ECO:0000269|PubMed:6330566}.
|
Drosophila melanogaster (Fruit fly)
|
P02836
|
HMEN_DROME
|
MALEDRCSPQSAPSPITLQMQHLHHQQQQQQQQQQQMQHLHQLQQLQQLHQQQLAAGVFHHPAMAFDAAAAAAAAAAAAAAHAHAAALQQRLSGSGSPASCSTPASSTPLTIKEEESDSVIGDMSFHNQTHTTNEEEEAEEDDDIDVDVDDTSAGGRLPPPAHQQQSTAKPSLAFSISNILSDRFGDVQKPGKSMENQASIFRPFEASRSQTATPSAFTRVDLLEFSRQQQAAAAAATAAMMLERANFLNCFNPAAYPRIHEEIVQSRLRRSAANAVIPPPMSSKMSDANPEKSALGSLCKAVSQIGQPAAPTMTQPPLSSSASSLASPPPASNASTISSTSSVATSSSSSSSGCSSAASSLNSSPSSRLGASGSGVNASSPQPQPIPPPSAVSRDSGMESSDDTRSETGSTTTEGGKNEMWPAWVYCTRYSDRPSSGPRYRRPKQPKDKTNDEKRPRTAFSSEQLARLKREFNENRYLTERRRQQLSSELGLNEAQIKIWFQNKRAKIKKSTGSKNPLALQLMAQGLYNHTTVPLTKEEEELEMRMNGQIP
| null | null |
analia development [GO:0007487]; anterior head segmentation [GO:0035288]; anterior/posterior lineage restriction, imaginal disc [GO:0048099]; axon guidance [GO:0007411]; compartment pattern specification [GO:0007386]; genital disc anterior/posterior pattern formation [GO:0035224]; genital disc development [GO:0035215]; gonad development [GO:0008406]; imaginal disc-derived wing vein specification [GO:0007474]; negative regulation of gene expression [GO:0010629]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuroblast fate determination [GO:0007400]; neuron differentiation [GO:0030182]; positive regulation of transcription by RNA polymerase II [GO:0045944]; posterior compartment specification [GO:0007388]; posterior head segmentation [GO:0035289]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; segment polarity determination [GO:0007367]; spiracle morphogenesis, open tracheal system [GO:0035277]; trunk segmentation [GO:0035290]; ventral midline development [GO:0007418]; wing disc anterior/posterior pattern formation [GO:0048100]; wing disc morphogenesis [GO:0007472]
|
nucleus [GO:0005634]; RSC-type complex [GO:0016586]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]
|
PF10525;PF00046;
|
1.10.10.60;
|
Engrailed homeobox family
|
PTM: Phosphorylated. Phosphorylation may directly or allosterically modify its function. {ECO:0000269|PubMed:2899884}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:3935318}.
| null | null | null | null | null |
FUNCTION: This protein specifies the body segmentation pattern. It is required for the development of the central nervous system. Transcriptional regulator that represses activated promoters. Wg signaling operates by inactivating the SGG repression of EN autoactivation.
|
Drosophila melanogaster (Fruit fly)
|
P02843
|
VIT1_DROME
|
MNPMRVLSLLACLAVAALAKPNGRMDNSVNQALKPSQWLSGSQLEAIPALDDFTIERLENMNLERGAELLQQVYHLSQIHHNVEPNYVPSGIQVYVPKPNGDKTVAPLNEMIQRLKQKQNFGEDEVTIIVTGLPQTSETVKKATRKLVQAYMQRYNLQQQRQHGKNGNQDYQDQSNEQRKNQRTSSEEDYSEEVKNAKTQSGDIIVIDLGSKLNTYERYAMLDIEKTGAKIGKWIVQMVNELDMPFDTIHLIGQNVGAHVAGAAAQEFTRLTGHKLRRVTGLDPSKIVAKSKNTLTGLARGDAEFVDAIHTSVYGMGTPIRSGDVDFYPNGPAAGVPGASNVVEAAMRATRYFAESVRPGNERSFPAVPANSLQQYKQNDGFGKRAYMGIDTAHDLEGDYILQVNPKSPFGRNAPAQKQSSYHGVHQAWNTNQDSKDYQ
| null | null |
lipid catabolic process [GO:0016042]; sex differentiation [GO:0007548]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; vesicle [GO:0031982]
|
serine hydrolase activity [GO:0017171]
|
PF00151;
|
3.40.50.1820;
|
AB hydrolase superfamily, Lipase family
|
PTM: Tyrosine sulfation occurs in the female only and plays an essential functional role. {ECO:0000269|PubMed:3922974}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Vesicle {ECO:0000269|PubMed:19050045}. Note=Yp1 secreted by fat body cells is taken up by oocytes via clathrin-mediated endocytosis and stored in endocytic derived lysosome-like vesicles called yolk granules. {ECO:0000269|PubMed:19050045}.
| null | null | null | null | null |
FUNCTION: Vitellogenin is the major yolk protein of eggs where it is used as a food source during embryogenesis. Along with Yp2 and Yp3, and their receptor yl/yolkless, required for maintenance of microtubule plus-end orientation towards the posterior pole of oocytes (PubMed:33891588). Involved in polarized localization of germ plasm components, such as osk mRNA and vas protein, to the oocyte posterior cortex (PubMed:33891588). Receptor-mediated endocytosis by yl/yolkless is crucial for actin reorganization, mediated by osk isoform A/Long, required to anchor germ plasm components to the oocyte cortex (PubMed:33891588). {ECO:0000269|PubMed:33891588}.
|
Drosophila melanogaster (Fruit fly)
|
P02844
|
VIT2_DROME
|
MNPLRTLCVMACLLAVAMGNPQSGNRSGRRSNSLDNVEQPSNWVNPREVEELPNLKEVTLKKLQEMSLEEGATLLDKLYHLSQFNHVFKPDYTPEPSQIRGYIVGERGQKIEFNLNTLVEKVKRQQKFGDDEVTIFIQGLPETNTQVQKATRKLVQAYQQRYNLQPYETTDYSNEEQSQRSSSEEQQTQRRKQNGEQDDTKTGDLIVIQLGNAIEDFEQYATLNIERLGEIIGNRLVELTNTVNVPQEIIHLIGSGPAAHVAGVAGRQFTRQTGHKLRRITALDPTKIYGKPEERLTGLARGDADFVDAIHTSAYGMGTSQRLANVDFFPNGPSTGVPGADNVVEATMRATRYFAESVRPGNERNFPSVAASSYQEYKQNKGYGKRGYMGIATDFDLQGDYILQVNSKSPFGRSTPAQKQTGYHQVHQPWRQSSSNQGSRRQ
| null | null |
lipid catabolic process [GO:0016042]; sex differentiation [GO:0007548]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
serine hydrolase activity [GO:0017171]
|
PF00151;
|
3.40.50.1820;
|
AB hydrolase superfamily, Lipase family
|
PTM: Tyrosine sulfation occurs in the female only and plays an essential functional role. {ECO:0000269|PubMed:3139663, ECO:0000269|PubMed:3922974}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Vitellogenin is the major yolk protein of eggs where it is used as a food source during embryogenesis. Vitellogenins and their receptor yl/yolkless are required for maintenance of microtubule plus-end orientation towards the posterior pole of oocytes (PubMed:33891588). Involved in polarized localization of germ plasm components, such as osk mRNA and vas protein, to the oocyte posterior cortex (PubMed:33891588). Receptor-mediated endocytosis by yl/yolkless is crucial for actin reorganization, mediated by osk isoform A/Long, required to anchor germ plasm components to the oocyte cortex (PubMed:33891588). {ECO:0000269|PubMed:33891588}.
|
Drosophila melanogaster (Fruit fly)
|
P02845
|
VIT2_CHICK
|
MRGIILALVLTLVGSQKFDIDPGFNSRRSYLYNYEGSMLNGLQDRSLGKAGVRLSSKLEISGLPENAYLLKVRSPQVEEYNGVWPRDPFTRSSKITQVISSCFTRLFKFEYSSGRIGNIYAPEDCPDLCVNIVRGILNMFQMTIKKSQNVYELQEAGIGGICHARYVIQEDRKNSRIYVTRTVDLNNCQEKVQKSIGMAYIYPCPVDVMKERLTKGTTAFSYKLKQSDSGTLITDVSSRQVYQISPFNEPTGVAVMEARQQLTLVEVRSERGSAPDVPMQNYGSLRYRFPAVLPQMPLQLIKTKNPEQRIVETLQHIVLNNQQDFHDDVSYRFLEVVQLCRIANADNLESIWRQVSDKPRYRRWLLSAVSASGTTETLKFLKNRIRNDDLNYIQTLLTVSLTLHLLQADEHTLPIAADLMTSSRIQKNPVLQQVACLGYSSVVNRYCSQTSACPKEALQPIHDLADEAISRGREDKMKLALKCIGNMGEPASLKRILKFLPISSSSAADIPVHIQIDAITALKKIAWKDPKTVQGYLIQILADQSLPPEVRMMACAVIFETRPALALITTIANVAMKESNMQVASFVYSHMKSLSKSRLPFMYNISSACNIALKLLSPKLDSMSYRYSKVIRADTYFDNYRVGATGEIFVVNSPRTMFPSAIISKLMANSAGSVADLVEVGIRVEGLADVIMKRNIPFAEYPTYKQIKELGKALQGWKELPTETPLVSAYLKILGQEVAFININKELLQQVMKTVVEPADRNAAIKRIANQIRNSIAGQWTQPVWMGELRYVVPSCLGLPLEYGSYTTALARAAVSVEGKMTPPLTGDFRLSQLLESTMQIRSDLKPSLYVHTVATMGVNTEYFQHAVEIQGEVQTRMPMKFDAKIDVKLKNLKIETNPCREETEIVVGRHKAFAVSRNIGELGVEKRTSILPEDAPLDVTEEPFQTSERASREHFAMQGPDSMPRKQSHSSREDLRRSTGKRAHKRDICLKMHHIGCQLCFSRRSRDASFIQNTYLHKLIGEHEAKIVLMPVHTDADIDKIQLEIQAGSRAAARIITEVNPESEEEDESSPYEDIQAKLKRILGIDSMFKVANKTRHPKNRPSKKGNTVLAEFGTEPDAKTSSSSSSASSTATSSSSSSASSPNRKKPMDEEENDQVKQARNKDASSSSRSSKSSNSSKRSSSKSSNSSKRSSSSSSSSSSSSRSSSSSSSSSSNSKSSSSSSKSSSSSSRSRSSSKSSSSSSSSSSSSSSKSSSSRSSSSSSKSSSHHSHSHHSGHLNGSSSSSSSSRSVSHHSHEHHSGHLEDDSSSSSSSSVLSKIWGRHEIYQYRFRSAHRQEFPKRKLPGDRATSRYSSTRSSHDTSRAASWPKFLGDIKTPVLAAFLHGISNNKKTGGLQLVVYADTDSVRPRVQVFVTNLTDSSKWKLCADASVRNAHKAVAYVKWGWDCRDYKVSTELVTGRFAGHPAAQVKLEWPKVPSNVRSVVEWFYEFVPGAAFMLGFSERMDKNPSRQARMVVALTSPRTCDVVVKLPDIILYQKAVRLPLSLPVGPRIPASELQPPIWNVFAEAPSAVLENLKARCSVSYNKIKTFNEVKFNYSMPANCYHILVQDCSSELKFLVMMKSAGEATNLKAINIKIGSHEIDMHPVNGQVKLLVDGAESPTANISLISAGASLWIHNENQGFALAAPGHGIDKLYFDGKTITIQVPLWMAGKTCGICGKYDAECEQEYRMPNGYLAKNAVSFGHSWILEEAPCRGACKLHRSFVKLEKTVQLAGVDSKCYSTEPVLRCAKGCSATKTTPVTVGFHCLPADSANSLTDKQMKYDQKSEDMQDTVDAHTTCSCENEECST
| null | null |
cellular response to estrogen stimulus [GO:0071391]; response to estradiol [GO:0032355]
| null |
lipid transporter activity [GO:0005319]; nutrient reservoir activity [GO:0045735]
|
PF09175;PF09172;PF01347;PF00094;
|
2.20.80.10;2.20.50.20;2.20.90.10;1.25.10.20;
| null |
PTM: Phosvitin, an egg yolk storage protein, is one of the most highly phosphorylated (10%) proteins in nature.; PTM: Cathepsin D is responsible for intraoocytic processing of vitellogenin.; PTM: May contain intrachain disulfide bonds.
| null | null | null | null | null | null |
FUNCTION: Precursor of the major egg-yolk proteins that are sources of nutrients during early development of oviparous organisms.; FUNCTION: Phosvitin is believed to be of importance in sequestering calcium, iron and other cations for the developing embryo.
|
Gallus gallus (Chicken)
|
P02866
|
CONA_CANEN
|
MAISKKSSLFLPIFTFITMFLMVVNKVSSSTHETNALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFEATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDANVIRNSTTIDFNAAYNADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVDKRLSAVVSYPNADSATVSYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNEIPDIATVV
| null | null |
defense response [GO:0006952]; regulation of defense response to virus [GO:0050688]
| null |
mannose binding [GO:0005537]; metal ion binding [GO:0046872]
|
PF00139;
|
2.60.120.200;
|
Leguminous lectin family
|
PTM: The mature chain consists of residues 164-281 followed by 30-148. To form a mature chain the precursor undergoes further post-translational modification after removal of the signal sequence; cleavage after Asn at positions 148, 163, and 281 is followed by transposition and ligation (By formation of a new peptide bond) of residues 164-281 and 30-148 (PubMed:34235541). This maturation (circular permutation) relies on the legumain AEP1 activity and leads to an increased stability of conA after heat stress and at various pH (PubMed:34235541). {ECO:0000269|PubMed:34235541}.
| null | null | null | null | null | null |
FUNCTION: D-mannose specific lectin (PubMed:2792084). Displays antiviral activity and therefore may contribute to defense against infections (PubMed:7481093). {ECO:0000269|PubMed:2792084, ECO:0000269|PubMed:7481093}.
|
Canavalia ensiformis (Jack bean) (Dolichos ensiformis)
|
P02870
|
LEC_LENCU
|
MASLQTQMISFYLIFLSILLTTIFFFKVNSTETTSFSITKFSPDQKNLIFQGDGYTTKGKLTLTKAVKSTVGRALYSTPIHIWDRDTGNVANFVTSFTFVIDAPSSYNVADEFTFFIAPVDTKPQTGGGYLGVFNSKEYDKTSQTVAVEFDTFYNAAWDPSNKERHIGIDVNSIKSVNTKSWNLQNGERANVVIAFNAATNVLTVTLTYPNSLEEENVTSYTLNEVVPLKDVVPEWVRIGFSATTGAEFAAHEVHSWSFHSELGGTSSSKQAADA
| null | null |
carbohydrate mediated signaling [GO:0009756]
| null |
calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; manganese ion binding [GO:0030145]; mannose binding [GO:0005537]
|
PF00139;
|
2.60.120.200;
|
Leguminous lectin family
|
PTM: The mature form consists of two chains, alpha and beta, produced by cleavage of the immature protein. These remain cleaved, yet fold together to form one subunit. {ECO:0000269|PubMed:7592736, ECO:0000269|PubMed:7731952, ECO:0000269|PubMed:8364026}.
| null | null | null | null | null | null |
FUNCTION: D-mannose specific lectin. {ECO:0000250}.
|
Lens culinaris (Lentil) (Cicer lens)
|
P02879
|
RICI_RICCO
|
MKPGGNTIVIWMYAVATWLCFGSTSGWSFTLEDNNIFPKQYPIINFTTAGATVQSYTNFIRAVRGRLTTGADVRHEIPVLPNRVGLPINQRFILVELSNHAELSVTLALDVTNAYVVGYRAGNSAYFFHPDNQEDAEAITHLFTDVQNRYTFAFGGNYDRLEQLAGNLRENIELGNGPLEEAISALYYYSTGGTQLPTLARSFIICIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSVITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKFSVYDVSILIPIIALMVYRCAPPPSSQFSLLIRPVVPNFNADVCMDPEPIVRIVGRNGLCVDVRDGRFHNGNAIQLWPCKSNTDANQLWTLKRDNTIRSNGKCLTTYGYSPGVYVMIYDCNTAATDATRWQIWDNGTIINPRSSLVLAATSGNSGTTLTVQTNIYAVSQGWLPTNNTQPFVTTIVGLYGLCLQANSGQVWIEDCSSEKAEQQWALYADGSIRPQQNRDNCLTSDSNIRETVVKILSCGPASSGQRWMFKNDGTILNLYSGLVLDVRASDPSLKQIILYPLHGDPNQIWLPLF
|
3.2.2.22
| null |
defense response [GO:0006952]; killing of cells of another organism [GO:0031640]; negative regulation of translation [GO:0017148]
| null |
AMP binding [GO:0016208]; carbohydrate binding [GO:0030246]; rRNA N-glycosylase activity [GO:0030598]; toxin activity [GO:0090729]
|
PF00652;PF00161;
|
2.80.10.50;3.40.420.10;4.10.470.10;
|
Ribosome-inactivating protein family, Type 2 RIP subfamily
| null | null |
CATALYTIC ACTIVITY: [Ricin A chain]: Reaction=Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.; EC=3.2.2.22;
| null | null | null | null |
FUNCTION: Ricin is highly toxic to animal cells, and to a lesser extent to plant cells.; FUNCTION: [Ricin A chain]: Acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. Can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single molecule can kill an animal cell.; FUNCTION: [Ricin B chain]: Binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain. Also responsible for cell agglutination (Lectin activity).
|
Ricinus communis (Castor bean)
|
P02886
|
DIS1A_DICDI
|
MSTQGLVQLLANAQCHLRTSTNYNGVHTQFNSALNYKNNGTNTIDGSEAWCSSIVDTNQYIVAGCEVPRTFMCVALQGRGDADQWVTSYKIRYSLDNVSWFEYRNGAAVTGVTDRNTVVNHFFDTPIRARSIAIHPLTWNGHISLRCEFYTQPVQSSVTQVGADIYTGDNCALNTGSGKREVVVPVKFQFEFATLPKVALNFDQIDCTDATNQTRIGVQPRNITTKGFDCVFYTWNENKVYSLRADYIATALE
| null | null |
asexual reproduction [GO:0019954]; cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; cell-substrate adhesion [GO:0031589]; cortical cytoskeleton organization [GO:0030865]; cytoskeleton organization [GO:0007010]; lectin-induced modified bacterial internalization [GO:0106136]; mitotic cytokinesis [GO:0000281]; protein localization to cell cortex [GO:0072697]; regulation of gene expression [GO:0010468]; regulation of protein complex stability [GO:0061635]; response to bacterium [GO:0009617]; response to catechin [GO:1902168]; response to curcumin [GO:1904643]
|
cell cortex [GO:0005938]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular matrix [GO:0031012]; intracellular vesicle [GO:0097708]; phagocytic vesicle [GO:0045335]; protein complex involved in cell adhesion [GO:0098636]; symbiont cell surface [GO:0106139]
|
carbohydrate binding [GO:0030246]; lipooligosaccharide binding [GO:1990458]; N-acetylgalactosamine binding [GO:0046871]; oligosaccharide binding [GO:0070492]; polysaccharide binding [GO:0030247]
|
PF00754;PF09458;
|
2.60.40.2080;2.60.120.260;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Galactose- and N-acetylgalactosamine-binding lectin. May play a role in cell-substratum adhesion rather than in cell-cell adhesion. May be necessary for the maintenance of normal elongate morphology during aggregation.
|
Dictyostelium discoideum (Social amoeba)
|
P02887
|
DIS1B_DICDI
|
MSTQGLVQLISNAQCHLRTSTNYNDVHTQFNAVLNYKNKGTNTIDGSEAWCSSIVDTNQYIVAGCEVPRTFMCVALQGRGDHDQWVTSYKIRYSLDNVTWSEYRNGAAITGVTDRNTVVNHFFDTPIRARSIAIHPLTWNNHISLRCEFYTQPVQSSVTQVGADIYTGDNCALNTGSGKREVVVPVKFQFEFATLPKVALNFDQIDCTDATNQTRIGVQPRNITTKGFDCVFYTWNANKVYSLRADYIATALE
| null | null |
cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; cytoskeleton organization [GO:0007010]; response to cAMP [GO:0051591]; response to folic acid [GO:0051593]
|
cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; phagocytic vesicle [GO:0045335]; protein complex involved in cell adhesion [GO:0098636]
|
carbohydrate binding [GO:0030246]; N-acetylgalactosamine binding [GO:0046871]; oligosaccharide binding [GO:0070492]; polysaccharide binding [GO:0030247]
|
PF00754;PF09458;
|
2.60.40.2080;2.60.120.260;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Galactose- and N-acetylgalactosamine-binding lectin. May play a role in cell-substratum adhesion rather than in cell-cell adhesion. May be necessary for the maintenance of normal elongate morphology during aggregation.
|
Dictyostelium discoideum (Social amoeba)
|
P02888
|
DIS1D_DICDI
|
MSTQGLVTLLGNAQCHLRTSTNYNGVHTQFNAALNYKNKGTNTIDGSEAWCSSIVDTNQYIVAGCEVPRTFMCVALQGRGDHDQWVTSYKIRYSLDNVTWSEYRNGAAITGVTDRNTVVNHFFDTPIRARSIAIHPLTWNNHISLRCEFYTQPVQSSVTQVGADIYTGDNCALNTGSGKREVVVPVKFQFEFATLPKVALNFDQIDCTDATNQTRIGVQPRNITTKGFDCVFYTWNENKVYSLRADYIATALE
| null | null |
cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; cytoskeleton organization [GO:0007010]
|
cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; phagocytic vesicle [GO:0045335]; protein complex involved in cell adhesion [GO:0098636]
|
carbohydrate binding [GO:0030246]; N-acetylgalactosamine binding [GO:0046871]; oligosaccharide binding [GO:0070492]; polysaccharide binding [GO:0030247]
|
PF00754;PF09458;
|
2.60.40.2080;2.60.120.260;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Galactose- and N-acetylgalactosamine-binding lectin. May play a role in cell-substratum adhesion rather than in cell-cell adhesion. May be necessary for the maintenance of normal elongate morphology during aggregation.
|
Dictyostelium discoideum (Social amoeba)
|
P02893
|
CSP_PLAFA
|
MMRKLAILSVSSFLFVEALFQEYQCYGSSSNTRVLNELNYDNAGTNLYNELEMNYYGKQENWYSLKKNSRSLGENDDGNNNNGDNGREGKDEDKRDGNNEDNEKLRKPKHKKLKQPGDGNPDPNANPNVDPNANPNVDPNANPNVDPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNVDPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNKNNQGNGQGHNMPNDPNRNVDENANANNAVKNNNNEEPSDKHIEQYLKKIKNSISTEWSPCSVTCGNGIQVRIKPGSANKPKDELDYENDIEKKICKMEKCSSVFNVVNSSIGLIMVLSFLFLN
| null | null |
entry into host cell by a symbiont-containing vacuole [GO:0085017]
|
cell surface [GO:0009986]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
| null |
PF00090;
|
2.20.100.10;
|
Plasmodium circumsporozoite protein family
|
PTM: During host cell invasion, proteolytically cleaved at the cell membrane in the region I by a papain-like cysteine protease of parasite origin (PubMed:15630135, PubMed:29554083). Cleavage is triggered by the sporozoite contact with highly sulfated heparan sulfate proteoglycans (HSPGs) present on the host hepatocyte cell surface (By similarity). Cleavage exposes the TSP type-1 (TSR) domain and is required for productive invasion of host hepatocytes but not for adhesion to the host cell membrane (PubMed:15630135). Cleavage is dispensable for sporozoite development in the oocyst, motility and for traversal of host and vector cells (By similarity). {ECO:0000250|UniProtKB:P23093, ECO:0000269|PubMed:15630135, ECO:0000269|PubMed:29554083}.; PTM: O-glycosylated; maybe by POFUT2. {ECO:0000250|UniProtKB:P19597}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19597}; Lipid-anchor, GPI-anchor {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P23093}. Note=Localizes to the cytoplasm and the cell membrane in oocysts at day 6 post infection and then gradually distributes over the entire cell surface of the sporoblast and the budding sporozoites. {ECO:0000250|UniProtKB:P23093}.
| null | null | null | null | null |
FUNCTION: Essential sporozoite protein (PubMed:29195810, PubMed:29554083). In the mosquito vector, required for sporozoite development in the oocyst, migration through the vector hemolymph and entry into the vector salivary glands (By similarity). In the vertebrate host, required for sporozoite migration through the host dermis and infection of host hepatocytes (PubMed:29195810, PubMed:29554083). Binds to highly sulfated heparan sulfate proteoglycans (HSPGs) on the surface of host hepatocytes (By similarity). {ECO:0000250|UniProtKB:P23093, ECO:0000269|PubMed:29195810, ECO:0000269|PubMed:29554083}.; FUNCTION: [Circumsporozoite protein C-terminus]: In the vertebrate host, binds to highly sulfated heparan sulfate proteoglycans (HSPGs) on the surface of host hepatocytes and is required for sporozoite invasion of the host hepatocytes. {ECO:0000250|UniProtKB:P23093}.
|
Plasmodium falciparum
|
P02911
|
ARGT_SALTY
|
MKKTVLALSLLIGLGATAASYAALPQTVRIGTDTTYAPFSSKDAKGEFIGFDIDLGNEMCKRMQVKCTWVASDFDALIPSLKAKKIDAIISSLSITDKRQQEIAFSDKLYAADSRLIAAKGSPIQPTLESLKGKHVGVLQGSTQEAYANDNWRTKGVDVVAYANQDLIYSDLTAGRLDAALQDEVAASEGFLKQPAGKEYAFAGPSVKDKKYFGDGTGVGLRKDDTELKAAFDKALTELRQDGTYDKMAKKYFDFNVYGD
| null | null |
amino acid transport [GO:0006865]
|
outer membrane-bounded periplasmic space [GO:0030288]
| null |
PF00497;
|
3.40.190.10;
|
Bacterial solute-binding protein 3 family
| null |
SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:6273842}.
| null | null | null | null | null |
FUNCTION: Part of the ABC transporter complex HisPMQ-ArgT involved in lysine/arginine/ornithine transport (PubMed:24021237). Binds lysine, arginine and ornithine (PubMed:1400387, PubMed:6273842, PubMed:7929349, PubMed:8496186). Can also bind histidine, with much lower affinity (PubMed:1400387, PubMed:7929349). Stimulates ATPase activity of HisP (PubMed:24021237). {ECO:0000269|PubMed:1400387, ECO:0000269|PubMed:24021237, ECO:0000269|PubMed:6273842, ECO:0000269|PubMed:7929349, ECO:0000269|PubMed:8496186}.
|
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
|
P02915
|
HISP_SALTY
|
MMSENKLHVIDLHKRYGGHEVLKGVSLQARAGDVISIIGSSGSGKSTFLRCINFLEKPSEGAIIVNGQNINLVRDKDGQLKVADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKHDARERALKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPDVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGDPEQVFGNPQSPRLQQFLKGSLK
|
7.4.2.1
| null | null |
plasma membrane [GO:0005886]
|
ABC-type amino acid transporter activity [GO:0015424]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]
|
PF00005;
|
3.40.50.300;
|
ABC transporter superfamily
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2033074}; Peripheral membrane protein {ECO:0000269|PubMed:2033074}. Note=Binds much more tightly to the membrane in the presence of HisQ and HisM. {ECO:0000269|PubMed:2033074}.
|
CATALYTIC ACTIVITY: Reaction=a polar amino acid(out) + ATP + H2O = a polar amino acid(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:14673, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:62031, ChEBI:CHEBI:456216; EC=7.4.2.1; Evidence={ECO:0000305|PubMed:24021237, ECO:0000305|PubMed:7050725, ECO:0000305|PubMed:9520394}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14674; Evidence={ECO:0000305|PubMed:24021237, ECO:0000305|PubMed:7050725, ECO:0000305|PubMed:9520394}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-histidine(out) = ADP + H(+) + L-histidine(in) + phosphate; Xref=Rhea:RHEA:29891, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57595, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:7050725, ECO:0000305|PubMed:9520394}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29892; Evidence={ECO:0000305|PubMed:7050725, ECO:0000305|PubMed:9520394}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-lysine(out) = ADP + H(+) + L-lysine(in) + phosphate; Xref=Rhea:RHEA:29887, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.4.2.1; Evidence={ECO:0000305|PubMed:24021237}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29888; Evidence={ECO:0000305|PubMed:24021237}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-arginine(out) = ADP + H(+) + L-arginine(in) + phosphate; Xref=Rhea:RHEA:29879, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.4.2.1; Evidence={ECO:0000305|PubMed:24021237}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29880; Evidence={ECO:0000305|PubMed:24021237}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-ornithine(out) = ADP + H(+) + L-ornithine(in) + phosphate; Xref=Rhea:RHEA:29883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:456216; EC=7.4.2.1; Evidence={ECO:0000305|PubMed:24021237}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29884; Evidence={ECO:0000305|PubMed:24021237};
| null | null | null | null |
FUNCTION: Part of the ABC transporter complex HisPMQJ involved in histidine transport (PubMed:7050725, PubMed:9520394). Is also part of the ABC transporter complex HisPMQ-ArgT involved in lysine/arginine/ornithine transport (PubMed:24021237). Shows ATPase activity (PubMed:9520394). Responsible for energy coupling to the transport system (PubMed:9520394). {ECO:0000269|PubMed:24021237, ECO:0000269|PubMed:7050725, ECO:0000269|PubMed:9520394}.
|
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
|
P02916
|
MALF_ECOLI
|
MDVIKKKHWWQSDALKWSVLGLLGLLVGYLVVLMYAQGEYLFAITTLILSSAGLYIFANRKAYAWRYVYPGMAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQEVLLDRSWQAGKTYNFGLYPAGDEWQLALSDGETGKNYLSDAFKFGGEQKLQLKETTAQPEGERANLRVITQNRQALSDITAILPDGNKVMMSSLRQFSGTQPLYTLDGDGTLTNNQSGVKYRPNNQIGFYQSITADGNWGDEKLSPGYTVTTGWKNFTRVFTDEGIQKPFLAIFVWTVVFSLITVFLTVAVGMVLACLVQWEALRGKAVYRVLLILPYAVPSFISILIFKGLFNQSFGEINMMLSALFGVKPAWFSDPTTARTMLIIVNTWLGYPYMMILCMGLLKAIPDDLYEASAMDGAGPFQNFFKITLPLLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDRLGTTTPAGYTDLLVNYTYRIAFEGGGGQDFGLAAAIATLIFLLVGALAIVNLKATRMKFD
| null | null |
DNA damage response [GO:0006974]; maltodextrin transmembrane transport [GO:0042956]; maltose transport [GO:0015768]; negative regulation of maltose transport [GO:1902344]; negative regulation of transmembrane transport [GO:0034763]
|
ATP-binding cassette (ABC) transporter complex [GO:0043190]; enzyme IIA-maltose transporter complex [GO:1990154]; maltose transport complex [GO:1990060]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
ABC-type maltose transporter activity [GO:0015423]
|
PF00528;PF20872;PF14785;
|
2.40.430.10;1.20.58.370;3.10.650.10;1.10.3720.10;
|
Binding-protein-dependent transport system permease family, MalFG subfamily
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:18456666}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:18456666}; Periplasmic side {ECO:0000269|PubMed:18456666}. Note=A substantial portion of it protrudes into the periplasmic space; inserts in an SRP- and Sec-dependent, YidC-independent fashion into the membrane.
| null | null | null | null | null |
FUNCTION: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane. {ECO:0000269|PubMed:2026607, ECO:0000269|PubMed:2155217}.
|
Escherichia coli (strain K12)
|
P02918
|
PBPA_ECOLI
|
MKFVKYFLILAVCCILLGAGSIYGLYRYIEPQLPDVATLKDVRLQIPMQIYSADGELIAQYGEKRRIPVTLDQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKEVFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLNEMAVIAGLPKAPSTFNPLYSMDRAVARRNVVLSRMLDEGYITQQQFDQTRTEAINANYHAPEIAFSAPYLSEMVRQEMYNRYGESAYEDGYRIYTTITRKVQQAAQQAVRNNVLDYDMRHGYRGPANVLWKVGESAWDNNKITDTLKALPTYGPLLPAAVTSANPQQATAMLADGSTVALSMEGVRWARPYRSDTQQGPTPRKVTDVLQTGQQIWVRQVGDAWWLAQVPEVNSALVSINPQNGAVMALVGGFDFNQSKFNRATQALRQVGSNIKPFLYTAAMDKGLTLASMLNDVPISRWDASAGSDWQPKNSPPQYAGPIRLRQGLGQSKNVVMVRAMRAMGVDYAAEYLQRFGFPAQNIVHTESLALGSASFTPMQVARGYAVMANGGFLVDPWFISKIENDQGGVIFEAKPKVACPECDIPVIYGDTQKSNVLENNDVEDVAISREQQNVSVPMPQLEQANQALVAKTGAQEYAPHVINTPLAFLIKSALNTNIFGEPGWQGTGWRAGRDLQRRDIGGKTGTTNSSKDAWFSGYGPGVVTSVWIGFDDHRRNLGHTTASGAIKDQISGYEGGAKSAQPAWDAYMKAVLEGVPEQPLTPPPGIVTVNIDRSTGQLANGGNSREEYFIEGTQPTQQAVHEVGTTIIDNGEAQELF
|
2.4.99.28; 3.4.16.4
| null |
cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360]; response to antibiotic [GO:0046677]
|
plasma membrane [GO:0005886]
|
penicillin binding [GO:0008658]; peptidoglycan glycosyltransferase activity [GO:0008955]; serine-type D-Ala-D-Ala carboxypeptidase activity [GO:0009002]
|
PF17092;PF00912;PF00905;
|
1.10.3810.10;3.40.710.10;
|
Glycosyltransferase 51 family; Transpeptidase family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:7006606}; Single-pass type II membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+); Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603, ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033, ChEBI:CHEBI:78435; EC=2.4.99.28; Evidence={ECO:0000269|PubMed:7006606}; CATALYTIC ACTIVITY: Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000269|PubMed:7006606};
| null |
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000269|PubMed:7006606}.
| null | null |
FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). {ECO:0000269|PubMed:7006606}.
|
Escherichia coli (strain K12)
|
P02919
|
PBPB_ECOLI
|
MAGNDREPIGRKGKPTRPVKQKVSRRRYEDDDDYDDYDDYEDEEPMPRKGKGKGKGRKPRGKRGWLWLLLKLAIVFAVLIAIYGVYLDQKIRSRIDGKVWQLPAAVYGRMVNLEPDMTISKNEMVKLLEATQYRQVSKMTRPGEFTVQANSIEMIRRPFDFPDSKEGQVRARLTFDGDHLATIVNMENNRQFGFFRLDPRLITMISSPNGEQRLFVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGASTLTQQLVKNLFLSSERSYWRKANEAYMALIMDARYSKDRILELYMNEVYLGQSGDNEIRGFPLASLYYFGRPVEELSLDQQALLVGMVKGASIYNPWRNPKLALERRNLVLRLLQQQQIIDQELYDMLSARPLGVQPRGGVISPQPAFMQLVRQELQAKLGDKVKDLSGVKIFTTFDSVAQDAAEKAAVEGIPALKKQRKLSDLETAIVVVDRFSGEVRAMVGGSEPQFAGYNRAMQARRSIGSLAKPATYLTALSQPKIYRLNTWIADAPIALRQPNGQVWSPQNDDRRYSESGRVMLVDALTRSMNVPTVNLGMALGLPAVTETWIKLGVPKDQLHPVPAMLLGALNLTPIEVAQAFQTIASGGNRAPLSALRSVIAEDGKVLYQSFPQAERAVPAQAAYLTLWTMQQVVQRGTGRQLGAKYPNLHLAGKTGTTNNNVDTWFAGIDGSTVTITWVGRDNNQPTKLYGASGAMSIYQRYLANQTPTPLNLVPPEDIADMGVDYDGNFVCSGGMRILPVWTSDPQSLCQQSEMQQQPSGNPFDQSSQPQQQPQQQPAQQEQKDSDGVAGWIKDMFGSN
|
2.4.99.28; 3.4.16.4
| null |
cell wall repair [GO:0071433]; peptidoglycan biosynthetic process [GO:0009252]; positive regulation of bipolar cell growth [GO:0051518]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360]; response to antibiotic [GO:0046677]
|
membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
|
penicillin binding [GO:0008658]; peptidoglycan glycosyltransferase activity [GO:0008955]; serine-type D-Ala-D-Ala carboxypeptidase activity [GO:0009002]
|
PF14812;PF00912;PF00905;PF14814;
|
1.10.3810.10;1.20.5.100;3.40.710.10;3.30.2060.10;
|
Glycosyltransferase 51 family; Transpeptidase family
| null |
SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein.
|
CATALYTIC ACTIVITY: Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+); Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603, ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033, ChEBI:CHEBI:78435; EC=2.4.99.28; Evidence={ECO:0000269|PubMed:19458048, ECO:0000269|PubMed:6389538}; CATALYTIC ACTIVITY: Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000269|PubMed:6389538};
| null |
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
| null | null |
FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
|
Escherichia coli (strain K12)
|
P02920
|
LACY_ECOLI
|
MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQPLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNAGAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALCASIVGIMFTINNQFVFWLGSGCALILAVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFDQQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMSVRIIGSSFATSALEVVILKTLHMFEVPFLLVGCFKYITSQFEVRFSATIYLVCFCFFKQLAMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTLSGPGPLSLLRRQVNEVA
| null | null |
carbohydrate transport [GO:0008643]; lactose transport [GO:0015767]; organic substance transport [GO:0071702]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]
|
carbohydrate:proton symporter activity [GO:0005351]; cytidine transmembrane transporter activity [GO:0015212]; lactose binding [GO:0030395]; lactose:proton symporter activity [GO:0015528]; uridine transmembrane transporter activity [GO:0015213]
|
PF01306;
|
1.20.1250.20;
|
Major facilitator superfamily, Oligosaccharide:H(+) symporter (OHS) (TC 2.A.1.5) family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2164211, ECO:0000269|PubMed:7000781, ECO:0000269|PubMed:7028742}; Multi-pass membrane protein {ECO:0000269|PubMed:2164211}.
|
CATALYTIC ACTIVITY: Reaction=H(+)(in) + lactose(in) = H(+)(out) + lactose(out); Xref=Rhea:RHEA:28867, ChEBI:CHEBI:15378, ChEBI:CHEBI:17716; Evidence={ECO:0000269|PubMed:1848449, ECO:0000269|PubMed:7000781, ECO:0000269|PubMed:7028742}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28869; Evidence={ECO:0000269|PubMed:1848449, ECO:0000269|PubMed:7000781, ECO:0000269|PubMed:7028742}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + melibiose(in) = H(+)(out) + melibiose(out); Xref=Rhea:RHEA:28855, ChEBI:CHEBI:15378, ChEBI:CHEBI:28053; Evidence={ECO:0000269|PubMed:1848449}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28857; Evidence={ECO:0000269|PubMed:1848449};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.62 mM for lactose {ECO:0000269|PubMed:18177889}; KM=0.24 mM for melibiose {ECO:0000269|PubMed:18177889}; KM=0.24 mM for lactulose {ECO:0000269|PubMed:22106930}; KM=0.54 mM for TMG {ECO:0000269|PubMed:18177889}; Vmax=191 nmol/min/mg enzyme with lactose as substrate {ECO:0000269|PubMed:18177889}; Vmax=105 nmol/min/mg enzyme with melibiose as substrate {ECO:0000269|PubMed:18177889}; Vmax=49 nmol/min/mg enzyme with lactulose as substrate {ECO:0000269|PubMed:22106930}; Vmax=180 nmol/min/mg enzyme with TMG as substrate {ECO:0000269|PubMed:18177889};
| null | null | null |
FUNCTION: Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system). Can transport lactose, melibiose, the synthetic disaccharide lactulose or the analog methyl-1-thio-beta,D-galactopyranoside (TMG), but not sucrose or fructose (PubMed:18177889, PubMed:1848449, PubMed:22106930, PubMed:7000781, PubMed:7028742). The substrate specificity is directed toward the galactopyranosyl moiety of the substrate (PubMed:22106930). {ECO:0000269|PubMed:18177889, ECO:0000269|PubMed:1848449, ECO:0000269|PubMed:22106930, ECO:0000269|PubMed:7000781, ECO:0000269|PubMed:7028742}.
|
Escherichia coli (strain K12)
|
P02921
|
MELB_ECOLI
|
MSISMTTKLSYGFGAFGKDFAIGIVYMYLMYYYTDVVGLSVGLVGTLFLVARIWDAINDPIMGWIVNATRSRWGKFKPWILIGTLANSVILFLLFSAHLFEGTTQIVFVCVTYILWGMTYTIMDIPFWSLVPTITLDKREREQLVPYPRFFASLAGFVTAGVTLPFVNYVGGGDRGFGFQMFTLVLIAFFIVSTIITLRNVHEVFSSDNQPSAEGSHLTLKAIVALIYKNDQLSCLLGMALAYNVASNIITGFAIYYFSYVIGDADLFPYYLSYAGAANLVTLVFFPRLVKSLSRRILWAGASILPVLSCGVLLLMALMSYHNVVLIVIAGILLNVGTALFWVLQVIMVADIVDYGEYKLHVRCESIAYSVQTMVVKGGSAFAAFFIAVVLGMIGYVPNVEQSTQALLGMQFIMIALPTLFFMVTLILYFRFYRLNGDTLRRIQIHLLDKYRKVPPEPVHADIPVGAVSDVKA
| null | null |
melibiose transport [GO:0015769]; methylgalactoside transport [GO:0015765]; organic substance transport [GO:0071702]
|
plasma membrane [GO:0005886]
|
melibiose:monoatomic cation symporter activity [GO:0015487]; melibiose:sodium symporter activity [GO:0043887]; methylgalactoside transmembrane transporter activity [GO:0015592]
|
PF13347;
|
1.20.1250.20;
|
Sodium:galactoside symporter (TC 2.A.2) family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:1730719, ECO:0000269|PubMed:7703254, ECO:0000269|PubMed:8672452}; Multi-pass membrane protein {ECO:0000269|PubMed:1730719, ECO:0000269|PubMed:8672452}.
|
CATALYTIC ACTIVITY: Reaction=melibiose(in) + Na(+)(in) = melibiose(out) + Na(+)(out); Xref=Rhea:RHEA:28851, ChEBI:CHEBI:28053, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:3311166, ECO:0000269|PubMed:3316227, ECO:0000269|PubMed:45782, ECO:0000269|PubMed:7703254}; CATALYTIC ACTIVITY: Reaction=Li(+)(in) + melibiose(in) = Li(+)(out) + melibiose(out); Xref=Rhea:RHEA:28847, ChEBI:CHEBI:28053, ChEBI:CHEBI:49713; Evidence={ECO:0000269|PubMed:3316227, ECO:0000269|PubMed:7703254}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + melibiose(in) = H(+)(out) + melibiose(out); Xref=Rhea:RHEA:28855, ChEBI:CHEBI:15378, ChEBI:CHEBI:28053; Evidence={ECO:0000269|PubMed:2185831, ECO:0000269|PubMed:3311166, ECO:0000269|PubMed:3316227, ECO:0000269|PubMed:45782, ECO:0000269|PubMed:7703254};
| null | null | null | null |
FUNCTION: Mediates the transport of melibiose and other galactosides by a symport mechanism (PubMed:2185831, PubMed:3311166, PubMed:3316227, PubMed:45782, PubMed:7703254). Can use sodium, lithium and protons as coupling cations, depending on the sugar substrate and the cationic environment (PubMed:3311166, PubMed:3316227, PubMed:45782, PubMed:7703254). Alpha-galactosides (melibiose, raffinose, p-nitrophenyl-alpha-galactoside or methyl-alpha-galactoside) are cotransported with either Na(+) or H(+), whereas beta-galactosides (lactose, L-arabinose-beta-D-galactoside, D-fructose-beta-D-galactoside, methyl-beta-galactoside or p-nitrophenyl-beta-galactoside) are cotransported with Na(+) or Li(+) but not H(+) (PubMed:3311166, PubMed:45782). The monosaccharide D-galactose can use either Na(+) or H(+) for cotransport whereas D-fucose, L-arabinose and D-galactosamine can use only Na(+) (PubMed:3311166). {ECO:0000269|PubMed:2185831, ECO:0000269|PubMed:3311166, ECO:0000269|PubMed:3316227, ECO:0000269|PubMed:45782, ECO:0000269|PubMed:7703254}.
|
Escherichia coli (strain K12)
|
P02925
|
RBSB_ECOLI
|
MNMKKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVKQ
| null | null |
D-ribose transmembrane transport [GO:0015752]; positive chemotaxis [GO:0050918]
|
ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288]
|
monosaccharide binding [GO:0048029]
|
PF13407;
|
3.40.50.2300;
|
Bacterial solute-binding protein 2 family
| null |
SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1583688}.
| null | null | null | null | null |
FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose import. Binds ribose. Also serves as the primary chemoreceptor for chemotaxis. {ECO:0000269|PubMed:25533465, ECO:0000269|PubMed:4608146, ECO:0000269|PubMed:6327617, ECO:0000269|PubMed:7982928}.
|
Escherichia coli (strain K12)
|
P02929
|
TONB_ECOLI
|
MTLDLPRRFPWPTLLSVCIHGAVVAGLLYTSVHQVIELPAPAQPISVTMVTPADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKEAPVVIEKPKPKPKPKPKPVKKVQEQPKRDVKPVESRPASPFENTAPARLTSSTATAATSKPVTSVASGPRALSRNQPQYPARAQALRIEGQVKVKFDVTPDGRVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPGSGIVVNILFKINGTTEIQ
| null | null |
cobalamin transport [GO:0015889]; colicin transport [GO:0042914]; intracellular iron ion homeostasis [GO:0006879]; intracellular monoatomic cation homeostasis [GO:0030003]; protein transport [GO:0015031]; receptor-mediated bacteriophage irreversible attachment to host cell [GO:0098002]; siderophore transport [GO:0015891]; transmembrane transport [GO:0055085]
|
cell envelope [GO:0030313]; cell outer membrane [GO:0009279]; membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797]; transmembrane transporter complex [GO:1902495]
|
energy transducer activity [GO:0031992]; protein domain specific binding [GO:0019904]
|
PF03544;PF16031;
|
3.30.2420.10;
|
TonB family
| null |
SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein; Periplasmic side.
| null | null | null | null | null |
FUNCTION: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment (PubMed:20005847). {ECO:0000269|PubMed:20005847}.
|
Escherichia coli (strain K12)
|
P02930
|
TOLC_ECOLI
|
MKKLLPILIGLSLSGFSSLSQAENLMQVYQQARLSNPELRKSAADRDAAFEKINEARSPLLPQLGLGADYTYSNGYRDANGINSNATSASLQLTQSIFDMSKWRALTLQEKAAGIQDVTYQTDQQTLILNTATAYFNVLNAIDVLSYTQAQKEAIYRQLDQTTQRFNVGLVAITDVQNARAQYDTVLANEVTARNNLDNAVEQLRQITGNYYPELAALNVENFKTDKPQPVNALLKEAEKRNLSLLQARLSQDLAREQIRQAQDGHLPTLDLTASTGISDTSYSGSKTRGAAGTQYDDSNMGQNKVGLSFSLPIYQGGMVNSQVKQAQYNFVGASEQLESAHRSVVQTVRSSFNNINASISSINAYKQAVVSAQSSLDAMEAGYSVGTRTIVDVLDATTTLYNAKQELANARYNYLINQLNIKSALGTLNEQDLLALNNALSKPVSTNPENVAPQTPEQNAIADGYAPDSPAPVVQQTSARTTTSNGHNPFRN
| null | null |
bile acid and bile salt transport [GO:0015721]; enterobactin transport [GO:0042930]; monoatomic ion transmembrane transport [GO:0034220]; response to antibiotic [GO:0046677]; response to organic cyclic compound [GO:0014070]; response to toxic substance [GO:0009636]; response to xenobiotic stimulus [GO:0009410]; xenobiotic detoxification by transmembrane export across the cell outer membrane [GO:0140330]; xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961]
|
cell outer membrane [GO:0009279]; efflux pump complex [GO:1990281]; MacAB-TolC complex [GO:1990196]; membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288]; periplasmic side of plasma membrane [GO:0098567]
|
bile acid transmembrane transporter activity [GO:0015125]; efflux transmembrane transporter activity [GO:0015562]; identical protein binding [GO:0042802]; monoatomic ion channel activity [GO:0005216]; porin activity [GO:0015288]
|
PF02321;
|
1.20.1600.10;
|
Outer membrane factor (OMF) (TC 1.B.17) family
| null |
SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:21778229, ECO:0000269|PubMed:6337123, ECO:0000269|PubMed:9044294}; Multi-pass membrane protein {ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:21778229, ECO:0000269|PubMed:6337123, ECO:0000269|PubMed:9044294}.
| null | null | null | null | null |
FUNCTION: Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells. {ECO:0000269|PubMed:11274125, ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:18955484, ECO:0000269|PubMed:23176499, ECO:0000269|PubMed:6337123}.
|
Escherichia coli (strain K12)
|
P02931
|
OMPF_ECOLI
|
MMKRNILAVIVPALLVAGTANAAEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQINSDLTGYGQWEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGRNYGVVYDALGYTDMLPEFGGDTAYSDDFFVGRVGGVATYRNSNFFGLVDGLNFAVQYLGKNERDTARRSNGDGVGGSISYEYEGFGIVGAYGAADRTNLQEAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPITNKFTNTSGFANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVGATYYFNKNMSTYVDYIINQIDSDNKLGVGSDDTVAVGIVYQF
| null | null |
monoatomic ion transmembrane transport [GO:0034220]; protein homotrimerization [GO:0070207]; protein transport [GO:0015031]
|
cell outer membrane [GO:0009279]; membrane [GO:0016020]; monoatomic ion channel complex [GO:0034702]; pore complex [GO:0046930]
|
colicin transmembrane transporter activity [GO:0042912]; disordered domain specific binding [GO:0097718]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; lipopolysaccharide binding [GO:0001530]; monoatomic ion channel activity [GO:0005216]; porin activity [GO:0015288]
|
PF00267;
|
2.40.160.10;
|
Gram-negative porin family
| null |
SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:2464593}; Multi-pass membrane protein {ECO:0000269|PubMed:16079137}.
| null | null | null | null | null |
FUNCTION: Forms pores that allow passive diffusion of small molecules across the outer membrane. {ECO:0000305|PubMed:19721064}.; FUNCTION: (Microbial infection) It is also a receptor for the bacteriophage T2. Is the major receptor for colicin E5 (Probable). {ECO:0000305|PubMed:27723824}.; FUNCTION: (Microbial infection) Probably translocates colicin E3 (and other A-type colicins) across the outer membrane (PubMed:18636093). {ECO:0000269|PubMed:18636093}.; FUNCTION: (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536 (ECL_04451); polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA-EC536-mediated toxicity. {ECO:0000269|PubMed:27723824}.
|
Escherichia coli (strain K12)
|
P02942
|
MCP1_ECOLI
|
MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNIGSGSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQDGFEKQYVAYMEQNDRLHDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQRETSAVVKTVTPAAPRKMAVADSEENWETF
| null | null |
cell motility [GO:0048870]; cellular response to amino acid stimulus [GO:0071230]; chemotaxis [GO:0006935]; detection of chemical stimulus [GO:0009593]; receptor clustering [GO:0043113]; regulation of bacterial-type flagellum-dependent cell motility [GO:1902021]; regulation of chemotaxis [GO:0050920]; regulation of protein histidine kinase activity [GO:0032110]; signal complex assembly [GO:0007172]; signal transduction [GO:0007165]
|
methyl accepting chemotaxis protein complex [GO:0098561]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; transmembrane signaling receptor activity [GO:0004888]
|
PF00672;PF00015;PF02203;
|
1.20.120.30;1.10.287.950;
|
Methyl-accepting chemotaxis (MCP) protein family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:22380631}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:22380631}. Note=Found predominantly at cell poles.
| null | null | null | null | null |
FUNCTION: Receptor for the attractant L-serine and related amino acids. Is also responsible for chemotaxis away from a wide range of repellents, including leucine, indole, and weak acids.; FUNCTION: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB.
|
Escherichia coli (strain K12)
|
P02943
|
LAMB_ECOLI
|
MMITLRKLPLAVAVAAGVMSAQAMAVDFHGYARSGIGWTGSGGEQQCFQTTGAQSKYRLGNECETYAELKLGQEVWKEGDKSFYFDTNVAYSVAQQNDWEATDPAFREANVQGKNLIEWLPGSTIWAGKRFYQRHDVHMIDFYYWDISGPGAGLENIDVGFGKLSLAATRSSEAGGSSSFASNNIYDYTNETANDVFDVRLAQMEINPGGTLELGVDYGRANLRDNYRLVDGASKDGWLFTAEHTQSVLKGFNKFVVQYATDSMTSQGKGLSQGSGVAFDNEKFAYNINNNGHMLRILDHGAISMGDNWDMMYVGMYQDINWDNDNGTKWWTVGIRPMYKWTPIMSTVMEIGYDNVESQRTGDKNNQYKITLAQQWQAGDSIWSRPAIRVFATYAKWDEKWGYDYTGNADNNANFGKAVPADFNGGSFGRGDSDEWTFGAQMEIWW
| null | null |
DNA damage response [GO:0006974]; maltodextrin transmembrane transport [GO:0042956]; monoatomic ion transport [GO:0006811]; polysaccharide transport [GO:0015774]
|
cell outer membrane [GO:0009279]; pore complex [GO:0046930]
|
carbohydrate transmembrane transporter activity [GO:0015144]; maltodextrin transmembrane transporter activity [GO:0042958]; maltose transporting porin activity [GO:0015481]; porin activity [GO:0015288]; virus receptor activity [GO:0001618]
|
PF02264;
|
2.40.170.10;
|
Porin LamB (TC 1.B.3) family
| null |
SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_01301, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:1988451, ECO:0000269|PubMed:4201774, ECO:0000269|Ref.9}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01301, ECO:0000269|PubMed:16079137}.
|
CATALYTIC ACTIVITY: Reaction=beta-maltose(in) = beta-maltose(out); Xref=Rhea:RHEA:29731, ChEBI:CHEBI:18147; Evidence={ECO:0000255|HAMAP-Rule:MF_01301, ECO:0000269|PubMed:7824948, ECO:0000269|PubMed:8805519, ECO:0000269|PubMed:9299337};
| null | null | null | null |
FUNCTION: Involved in the transport of maltose and maltodextrins (PubMed:11742115, PubMed:2832377, PubMed:3301537, PubMed:7824948, PubMed:8805519, PubMed:9299337). Indispensable for translocation of maltodextrins (alpha 1-4 linked polyglucosyls) containing more than three glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic residues serves to guide and select the sugars for transport through the channel (PubMed:11742115, PubMed:7824948, PubMed:8805519, PubMed:9299337). Also acts as a receptor for several bacteriophages including lambda (PubMed:4201774). Binds maltosaccharides; when LamB binds starch in soft agar, it inhibits motility (PubMed:2832377). {ECO:0000269|PubMed:11742115, ECO:0000269|PubMed:2832377, ECO:0000269|PubMed:3301537, ECO:0000269|PubMed:4201774, ECO:0000269|PubMed:7824948, ECO:0000269|PubMed:8805519, ECO:0000269|PubMed:9299337}.
|
Escherichia coli (strain K12)
|
P02945
|
BACR_HALSA
|
MLELLPTAVEGVSQAQITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARYADWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESMRPEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAEAPEPSAGDGAAATSD
| null | null |
phototransduction [GO:0007602]; proton transmembrane transport [GO:1902600]
|
plasma membrane [GO:0005886]
|
monoatomic ion channel activity [GO:0005216]; photoreceptor activity [GO:0009881]
|
PF01036;
|
1.20.1070.10;
|
Archaeal/bacterial/fungal opsin family
|
PTM: The covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin. {ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:10467143, ECO:0000269|PubMed:10548112, ECO:0000269|PubMed:10903866, ECO:0000269|PubMed:10949307, ECO:0000269|PubMed:10949309, ECO:0000269|PubMed:11829498, ECO:0000269|PubMed:28008064, ECO:0000269|PubMed:6706999, ECO:0000269|PubMed:6794028, ECO:0000269|PubMed:9287223, ECO:0000269|PubMed:9632391, ECO:0000269|PubMed:9751724}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:6706999}; Multi-pass membrane protein {ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:10467143, ECO:0000269|PubMed:10548112, ECO:0000269|PubMed:10903866, ECO:0000269|PubMed:10949309, ECO:0000269|PubMed:11829498, ECO:0000269|PubMed:2614846, ECO:0000269|PubMed:28008064, ECO:0000269|PubMed:6706999, ECO:0000269|PubMed:9287223, ECO:0000269|PubMed:9632391, ECO:0000269|PubMed:9751724}.
| null | null | null | null | null |
FUNCTION: Light-driven proton pump. {ECO:0000305|PubMed:10903866, ECO:0000305|PubMed:10949309, ECO:0000305|PubMed:28008064}.
|
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
|
P02974
|
FMM1_NEIGO
|
MNTLQKGFTLIELMIVIAIVGILAAVALPAYQDYTARAQVSEAILLAEGQKSAVTEYYLNHGKWPENNTSAGVASPPSDIKGKYVKEVEVKNGVVTATMLSSGVNNEIKGKKLSLWARRENGSVKWFCGQPVTRTDDDTVADAKDGKEIDTKHLPSTCRDNFDAK
| null | null |
cell adhesion [GO:0007155]; protein secretion by the type II secretion system [GO:0015628]
|
membrane [GO:0016020]; pilus [GO:0009289]; type II protein secretion system complex [GO:0015627]
| null |
PF07963;PF00114;
|
3.30.700.10;
|
N-Me-Phe pilin family
|
PTM: The O-linked glycan identified as Gal-GlcNAc disaccharide in PubMed:7477282 and PubMed:10048019 is now identified as either a hexosyl-diacetamidotrideoxyhexoside (DATDHex) by mass spectrometry in PubMed:15249686, or alpha-D-galactopyranosyl-(1->3)-2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranoside (DADDGlc) by X-ray diffraction in PubMed:16949362. It is not clear whether there is a chemical difference in the glycosylation of the two derivatives of strain MS11 used in these experiments, or not. {ECO:0000269|PubMed:10048019, ECO:0000269|PubMed:7477282}.; PTM: In some MS11 derivative strains, Ser-75 is modified to O-(2-aminoethylphosphoryl)serine, and in some other derivatives that can be secondarily modified to O-(2-cholinephosphoryl)serine by N-methylation. {ECO:0000269|PubMed:413571, ECO:0000269|PubMed:7477282}.
|
SUBCELLULAR LOCATION: Fimbrium. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Major component of the type IV pilus (T4P) that plays a role in cellular adherence, microcolony formation, resistance to neutrophil mediated killing, twitching motility as well as transformation (PubMed:27213957). Mediates the attachment and the formation of bacterial microcolonies on host epithelial cells. Mechanistically, pili retractation induces host NF-kappa-B activation in infected cells, which is temporally associated with the formation of gonococcal microcolonies (PubMed:27213957). {ECO:0000269|PubMed:27213957}.
|
Neisseria gonorrhoeae
|
P02976
|
SPA_STAA8
|
MKKKNIYSIRKLGVGIASVTLGTLLISGGVTPAANAAQHDEAQQNAFYQVLNMPNLNADQRNGFIQSLKDDPSQSANVLGEAQKLNDSQAPKADAQQNNFNKDQQSAFYEILNMPNLNEAQRNGFIQSLKDDPSQSTNVLGEAKKLNESQAPKADNNFNKEQQNAFYEILNMPNLNEEQRNGFIQSLKDDPSQSANLLSEAKKLNESQAPKADNKFNKEQQNAFYEILHLPNLNEEQRNGFIQSLKDDPSQSANLLAEAKKLNDAQAPKADNKFNKEQQNAFYEILHLPNLTEEQRNGFIQSLKDDPSVSKEILAEAKKLNDAQAPKEEDNNKPGKEDNNKPGKEDNNKPGKEDNNKPGKEDNNKPGKEDGNKPGKEDNKKPGKEDGNKPGKEDNKKPGKEDGNKPGKEDGNKPGKEDGNGVHVVKPGDTVNDIAKANGTTADKIAADNKLADKNMIKPGQELVVDKKQPANHADANKAQALPETGEENPFIGTTVFGGLSLALGAALLAGRRREL
| null | null | null |
extracellular region [GO:0005576]
|
IgG binding [GO:0019864]
|
PF02216;PF00746;PF01476;PF03373;PF04650;
|
1.20.5.420;3.10.350.10;
|
Immunoglobulin-binding protein SpA family
| null |
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10427003, ECO:0000269|PubMed:12700270, ECO:0000269|PubMed:1638631, ECO:0000269|PubMed:17416657, ECO:0000269|PubMed:3679545, ECO:0000269|PubMed:4163007, ECO:0000269|PubMed:9786922, ECO:0000305|PubMed:20472795, ECO:0000305|PubMed:7701329, ECO:0000305|PubMed:7830549}; Peptidoglycan-anchor {ECO:0000269|PubMed:10427003, ECO:0000269|PubMed:12700270, ECO:0000269|PubMed:17416657, ECO:0000269|PubMed:9786922, ECO:0000305|PubMed:1638631, ECO:0000305|PubMed:20472795, ECO:0000305|PubMed:7701329}; Extracellular side {ECO:0000269|PubMed:1638631, ECO:0000305|PubMed:7701329}. Secreted {ECO:0000269|PubMed:2938951, ECO:0000269|PubMed:3679545}. Note=Cell wall anchoring is conferred by the LPXTG motif and following sequences (PubMed:1638631). Anchored by sortase A (PubMed:10427003). SpA from strains A676 and V-I is secreted whereas SpA from Cowan 1 and 8325-4 is mostly attached to the cell wall (Probable). Newly synthesized protein is deposited at 2-4 foci/cell and eventually is distributed in a ring around the cell (PubMed:17416657). {ECO:0000269|PubMed:10427003, ECO:0000269|PubMed:1638631, ECO:0000269|PubMed:17416657, ECO:0000305|PubMed:2938951}.
| null | null | null | null | null |
FUNCTION: Plays a role in the inhibition of the host innate and adaptive immune responses. Possesses five immunoglobulin-binding domains that capture both the fragment crystallizable region (Fc region) and the Fab region (part of Ig that identifies antigen) of immunoglobulins (PubMed:10805799, PubMed:2938951, PubMed:4163007). In turn, Staphylococcus aureus is protected from phagocytic killing via inhibition of Ig Fc region. In addition, the host elicited B-cell response is prevented due to a decrease of antibody-secreting cell proliferation that enter the bone marrow, thereby decreasing long-term antibody production. Inhibits osteogenesis by preventing osteoblast proliferation and expression of alkaline phosphatase, type I collagen, osteopontin and osteocalcin. Acts directly as a pro-inflammatory factor in the lung through its ability to bind and activate tumor necrosis factor alpha receptor 1/TNFRSF1A (By similarity). {ECO:0000250|UniProtKB:A0A0H3K686, ECO:0000269|PubMed:10805799, ECO:0000269|PubMed:2938951, ECO:0000269|PubMed:4163007}.
|
Staphylococcus aureus (strain NCTC 8325 / PS 47)
|
P02992
|
EFTU_YEAST
|
MSALLPRLLTRTAFKASGKLLRLSSVISRTFSQTTTSYAAAFDRSKPHVNIGTIGHVDHGKTTLTAAITKTLAAKGGANFLDYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIDDPEMLELVEMEMRELLNEYGFDGDNAPIIMGSALCALEGRQPEIGEQAIMKLLDAVDEYIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIVGHNSTPLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMVLAKPGTVKAHTKILASLYILSKEEGGRHSGFGENYRPQMFIRTADVTVVMRFPKEVEDHSMQVMPGDNVEMECDLIHPTPLEVGQRFNIREGGRTVGTGLITRIIE
| null | null |
mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; translation elongation factor activity [GO:0003746]
|
PF00009;PF03144;PF03143;
|
3.40.50.300;2.40.30.10;
|
TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-Tu/EF-1A subfamily
|
PTM: The precursor is processed in two steps involving mitochondrial intermediate peptidase (MIP) and mitochondrial processing peptidase (MPP). {ECO:0000269|PubMed:7593000}.
|
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
| null | null |
PATHWAY: Protein biosynthesis; polypeptide chain elongation.
| null | null |
FUNCTION: G-protein that, in its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled before binding another molecule of aminoacyl-tRNA. Required for mitochondrial protein biosynthesis and maintenance of mitochondrial DNA. {ECO:0000269|PubMed:3905388}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P02994
|
EF1A_YEAST
|
MGKEKSHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYQVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGVGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSVKWDESRFQEIVKETSNFIKKVGYNPKTVPFVPISGWNGDNMIEATTNAPWYKGWEKETKAGVVKGKTLLEAIDAIEQPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFAPAGVTTEVKSVEMHHEQLEQGVPGDNVGFNVKNVSVKEIRRGNVCGDAKNDPPKGCASFNATVIVLNHPGQISAGYSPVLDCHTAHIACRFDELLEKNDRRSGKKLEDHPKFLKSGDAALVKFVPSKPMCVEAFSEYPPLGRFAVRDMRQTVAVGVIKSVDKTEKAAKVTKAAQKAAKK
| null | null |
actin filament bundle assembly [GO:0051017]; cellular response to amino acid starvation [GO:0034198]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein phosphorylation [GO:0001933]; sulfur compound metabolic process [GO:0006790]; translation [GO:0006412]; translational elongation [GO:0006414]; tRNA export from nucleus [GO:0006409]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; eukaryotic translation elongation factor 1 complex [GO:0005853]; fungal-type vacuole membrane [GO:0000329]; mitochondrion [GO:0005739]; ribosome [GO:0005840]
|
actin filament binding [GO:0051015]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; melatonin binding [GO:1904408]; protein kinase binding [GO:0019901]; ribosome binding [GO:0043022]; translation elongation factor activity [GO:0003746]
|
PF00009;PF03144;PF03143;
|
3.40.50.300;2.40.30.10;
|
TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-Tu/EF-1A subfamily
|
PTM: S-thiolated in response to oxidative stress, probably inhibiting the protein and causing a reduction in protein synthesis. {ECO:0000269|PubMed:12755685}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14562095}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.14 mM for GTP {ECO:0000269|PubMed:9786872};
|
PATHWAY: Protein biosynthesis; polypeptide chain elongation.
| null | null |
FUNCTION: GTP-binding component of the eukaryotic elongation factor 1 complex (eEF1). In its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled by its guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) before binding another molecule of aminoacyl-tRNA. Required for nuclear export of aminoacyl-tRNAs. May also be involved in translational quality control by targeting cotranslationally damaged proteins to the proteasome. Also exhibits actin filament-binding and -bundling activities and is involved in cytoskeleton organization. Plays a role as a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells (PubMed:21849502). {ECO:0000269|PubMed:10766739, ECO:0000269|PubMed:15601860, ECO:0000269|PubMed:21849502, ECO:0000269|PubMed:3066688}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P03001
|
TF3A_XENLA
|
MAAKVASTSSEEAEGSLVTEGEMGEKALPVVYKRYICSFADCGAAYNKNWKLQAHLCKHTGEKPFPCKEEGCEKGFTSLHHLTRHSLTHTGEKNFTCDSDGCDLRFTTKANMKKHFNRFHNIKICVYVCHFENCGKAFKKHNQLKVHQFSHTQQLPYECPHEGCDKRFSLPSRLKRHEKVHAGYPCKKDDSCSFVGKTWTLYLKHVAECHQDLAVCDVCNRKFRHKDYLRDHQKTHEKERTVYLCPRDGCDRSYTTAFNLRSHIQSFHEEQRPFVCEHAGCGKCFAMKKSLERHSVVHDPEKRKLKEKCPRPKRSLASRLTGYIPPKSKEKNASVSGTEKTDSLVKNKPSGTETNGSLVLDKLTIQ
| null | null |
ribosomal large subunit biogenesis [GO:0042273]
|
nucleus [GO:0005634]
|
DNA binding [GO:0003677]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]
|
PF00096;
|
3.30.160.60;
| null |
PTM: The N-terminus is blocked.
|
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Involved in ribosomal large subunit biogenesis (By similarity). Acts both as a positive transcription factor for 5S RNA genes, and as a specific RNA binding protein that complexes with 5S RNA in oocytes to form the 7S ribonucleoprotein storage particle. May play an essential role in the developmental change in 5S RNA gene expression. Interacts with the internal control region (ICR) of approximately 50 bases within the 5S RNA genes, is required for correct transcription of these genes by RNA polymerase III (PubMed:1538401, PubMed:1762917, PubMed:2253880). Also binds the transcribed 5S RNA's (By similarity). {ECO:0000250|UniProtKB:P17842, ECO:0000250|UniProtKB:Q92664, ECO:0000269|PubMed:1538401, ECO:0000269|PubMed:1762917, ECO:0000269|PubMed:2253880}.
|
Xenopus laevis (African clawed frog)
|
P03004
|
DNAA_ECOLI
|
MSLSLWQQCLARLQDELPATEFSMWIRPLQAELSDNTLALYAPNRFVLDWVRDKYLNNINGLLTSFCGADAPQLRFEVGTKPVTQTPQAAVTSNVAAPAQVAQTQPQRAAPSTRSGWDNVPAPAEPTYRSNVNVKHTFDNFVEGKSNQLARAAARQVADNPGGAYNPLFLYGGTGLGKTHLLHAVGNGIMARKPNAKVVYMHSERFVQDMVKALQNNAIEEFKRYYRSVDALLIDDIQFFANKERSQEEFFHTFNALLEGNQQIILTSDRYPKEINGVEDRLKSRFGWGLTVAIEPPELETRVAILMKKADENDIRLPGEVAFFIAKRLRSNVRELEGALNRVIANANFTGRAITIDFVREALRDLLALQEKLVTIDNIQKTVAEYYKIKVADLLSKRRSRSVARPRQMAMALAKELTNHSLPEIGDAFGGRDHTTVLHACRKIEQLREESHDIKEDFSNLIRTLSS
| null | null |
DNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; DNA unwinding involved in DNA replication [GO:0006268]; negative regulation of DNA-templated DNA replication initiation [GO:0032297]; positive regulation of DNA-templated DNA replication initiation [GO:0032298]; regulation of DNA replication [GO:0006275]; regulation of DNA-templated DNA replication initiation [GO:0030174]
|
cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; DnaA-DiaA complex [GO:1990102]; DnaA-Dps complex [GO:1990084]; DnaA-HU complex [GO:1990103]; DnaA-L2 complex [GO:1990082]; DnaA-oriC complex [GO:1990101]; plasma membrane [GO:0005886]; replication inhibiting complex [GO:1990078]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA replication origin binding [GO:0003688]; identical protein binding [GO:0042802]; sequence-specific DNA binding [GO:0043565]
|
PF00308;PF08299;PF11638;
|
1.10.1750.10;1.10.8.60;3.30.300.180;3.40.50.300;
|
DnaA family
|
PTM: Acetylated at Lys-178 by PatZ. Deacetylated by CobB. Is also acetylated nonenzymatically by acetyl-phosphate. Acetylation level increases in a growth phase-dependent manner and peaks at the stationnary phase. {ECO:0000269|PubMed:27484197}.
|
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Plays a key role in the initiation and regulation of chromosomal replication. Binds in an ATP-dependent fashion to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex exactly once per cell cycle. Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3'); subsequent binding of DNA polymerase III subunits leads to replisome formation. The DnaA-ATP form converts to DnaA-ADP; once converted to ADP the protein cannot initiate replication, ensuring only 1 round of replication per cell cycle. DnaA can inhibit its own gene expression as well as that of other genes such as dam, rpoH, ftsA and mioC.; FUNCTION: Also required for replication of plasmid DNA; binds 4 dnaA boxes in the minimal plasmid RK2 replication origin (oriV).
|
Escherichia coli (strain K12)
|
P03007
|
DPO3E_ECOLI
|
MSTAITRQIVLDTETTGMNQIGAHYEGHKIIEIGAVEVVNRRLTGNNFHVYLKPDRLVDPEAFGVHGIADEFLLDKPTFAEVADEFMDYIRGAELVIHNAAFDIGFMDYEFSLLKRDIPKTNTFCKVTDSLAVARKMFPGKRNSLDALCARYEIDNSKRTLHGALLDAQILAEVYLAMTGGQTSMAFAMEGETQQQQGEATIQRIVRQASKLRVVFATDEEIAAHEARLDLVQKKGGSCLWRA
|
2.7.7.7
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 2 divalent metal cations. Magnesium or manganese.;
|
DNA replication proofreading [GO:0045004]; DNA-templated DNA replication [GO:0006261]; lagging strand elongation [GO:0006273]; leading strand elongation [GO:0006272]
|
cytosol [GO:0005829]; DNA polymerase III complex [GO:0009360]; DNA polymerase III, core complex [GO:0044776]; replisome [GO:0030894]
|
3'-5' exonuclease activity [GO:0008408]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exonuclease activity [GO:0004527]; metal ion binding [GO:0046872]
|
PF00929;
|
3.20.20.140;3.30.420.10;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7;
| null | null | null | null |
FUNCTION: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease (PubMed:6340117). Contacts both the beta sliding clamp (dnaN) and the polymerase subunit (dnaE), stabilizing their interaction (PubMed:26499492). {ECO:0000269|PubMed:26499492, ECO:0000269|PubMed:6340117}.
|
Escherichia coli (strain K12)
|
P03015
|
GIN_BPMU
|
MLIGYVRVSTNDQNTDLQRNALVCAGCEQIFEDKLSGTRTDRPGLKRALKRLQKGDTLVVWKLDRLGRSMKHLISLVGELRERGINFRSLTDSIDTSSPMGRFFFHVMGALAEMERELIIERTMAGLAAARNKGRIGGRPPKLTKAEWEQAGRLLAQGIPRKQVALIYDVALSTLYKKHPAKRAHIENDDRIN
|
3.1.22.-; 6.5.1.-
| null |
DNA integration [GO:0015074]; symbiont entry into host cell [GO:0046718]; viral tropism switching [GO:0098678]
|
host cell cytoplasm [GO:0030430]
|
DNA binding [GO:0003677]; DNA strand exchange activity [GO:0000150]; hydrolase activity [GO:0016787]; ligase activity [GO:0016874]
|
PF02796;PF00239;
|
1.10.10.60;3.40.50.1390;
|
Site-specific recombinase resolvase family
| null |
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Performs inversion of a viral 3 kp segment (G-segment) that encodes two alternate pairs of tail fiber proteins thereby modifying the host specificity of the virus. Binds as a dimer to the viral gix sites which are 34-bp palindromic sequences that flank the invertible G-segment. Catalyzes site-specific recombination in the presence of the host factor Fis. Gin dimers bound to each of the gix sites and host factor Fis bound to the enhancer come together to form the synaptic complex. Each Gin monomer introduces a nick and becomes covalently attached to the 5'-phosphate of the DNA, resulting in double-stranded staggered breaks at both recombination sites. A 180 degrees rotation of one of the two Gin dimers followed by religation of the DNA leads to the inversion of the G-segment (G+ or G- orientation). {ECO:0000269|PubMed:23275567, ECO:0000269|PubMed:2974801, ECO:0000269|PubMed:3159478, ECO:0000269|PubMed:6232613}.
|
Escherichia phage Mu (Bacteriophage Mu)
|
P03018
|
UVRD_ECOLI
|
MDVSYLLDSLNDKQREAVAAPRSNLLVLAGAGSGKTRVLVHRIAWLMSVENCSPYSIMAVTFTNKAAAEMRHRIGQLMGTSQGGMWVGTFHGLAHRLLRAHHMDANLPQDFQILDSEDQLRLLKRLIKAMNLDEKQWPPRQAMWYINSQKDEGLRPHHIQSYGNPVEQTWQKVYQAYQEACDRAGLVDFAELLLRAHELWLNKPHILQHYRERFTNILVDEFQDTNNIQYAWIRLLAGDTGKVMIVGDDDQSIYGWRGAQVENIQRFLNDFPGAETIRLEQNYRSTSNILSAANALIENNNGRLGKKLWTDGADGEPISLYCAFNELDEARFVVNRIKTWQDNGGALAECAILYRSNAQSRVLEEALLQASMPYRIYGGMRFFERQEIKDALSYLRLIANRNDDAAFERVVNTPTRGIGDRTLDVVRQTSRDRQLTLWQACRELLQEKALAGRAASALQRFMELIDALAQETADMPLHVQTDRVIKDSGLRTMYEQEKGEKGQTRIENLEELVTATRQFSYNEEDEDLMPLQAFLSHAALEAGEGQADTWQDAVQLMTLHSAKGLEFPQVFIVGMEEGMFPSQMSLDEGGRLEEERRLAYVGVTRAMQKLTLTYAETRRLYGKEVYHRPSRFIGELPEECVEEVRLRATVSRPVSHQRMGTPMVENDSGYKLGQRVRHAKFGEGTIVNMEGSGEHSRLQVAFQGQGIKWLVAAYARLESV
|
5.6.2.4
| null |
DNA duplex unwinding [GO:0032508]; DNA unwinding involved in DNA replication [GO:0006268]; mismatch repair [GO:0006298]; mismatch repair involved in maintenance of fidelity involved in DNA-dependent DNA replication [GO:0070716]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA duplex unwinding [GO:0000717]; recombinational repair [GO:0000725]; replication fork processing [GO:0031297]; response to radiation [GO:0009314]; rolling circle DNA replication [GO:0070581]; SOS response [GO:0009432]
|
cytosol [GO:0005829]; DNA helicase complex [GO:0033202]; single-stranded DNA-dependent ATP-dependent DNA helicase complex [GO:0017117]
|
3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; DNA translocase activity [GO:0015616]; isomerase activity [GO:0016853]; protein homodimerization activity [GO:0042803]; single-stranded DNA helicase activity [GO:0017116]
|
PF21196;PF00580;PF13361;
|
1.10.10.160;3.40.50.300;
|
Helicase family, UvrD subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000269|PubMed:8419285}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; Evidence={ECO:0000269|PubMed:8419285};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.05 mM for ATP {ECO:0000269|PubMed:8419285};
| null | null | null |
FUNCTION: A helicase with DNA-dependent ATPase activity (PubMed:8419285). Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand. Initiates unwinding more efficiently from a nicked substrate than ds duplex DNA (PubMed:8419285). Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair, and probably also in repair of alkylated DNA (Probable). {ECO:0000269|PubMed:8419285, ECO:0000305|PubMed:25484163}.
|
Escherichia coli (strain K12)
|
P03023
|
LACI_ECOLI
|
MKPVTLYDVAEYAGVSYQTVSRVVNQASHVSAKTREKVEAAMAELNYIPNRVAQQLAGKQSLLIGVATSSLALHAPSQIVAAIKSRADQLGASVVVSMVERSGVEACKAAVHNLLAQRVSGLIINYPLDDQDAIAVEAACTNVPALFLDVSDQTPINSIIFSHEDGTRLGVEHLVALGHQQIALLAGPLSSVSARLRLAGWHKYLTRNQIQPIAEREGDWSAMSGFQQTMQMLNEGIVPTAMLVANDQMALGAMRAITESGLRVGADISVVGYDDTEDSSCYIPPLTTIKQDFRLLGQTSVDRLLQLSQGQAVKGNQLLPVSLVKRKTTLAPNTQTASPRALADSLMQLARQVSRLESGQ
| null | null |
negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA-templated transcription [GO:0006355]
|
cytosol [GO:0005829]
|
cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity [GO:0001217]; identical protein binding [GO:0042802]; transcription cis-regulatory region binding [GO:0000976]
|
PF00356;PF13377;
|
3.40.50.2300;1.10.260.40;
| null | null | null | null | null | null | null | null |
FUNCTION: Repressor of the lactose operon. Binds allolactose as an inducer.
|
Escherichia coli (strain K12)
|
P03069
|
GCN4_YEAST
|
MSEYQPSLFALNPMGFSPLDGSKSTNENVSASTSTAKPMVGQLIFDKFIKTEEDPIIKQDTPSNLDFDFALPQTATAPDAKTVLPIPELDDAVVESFFSSSTDSTPMFEYENLEDNSKEWTSLFDNDIPVTTDDVSLADKAIESTEEVSLVPSNLEVSTTSFLPTPVLEDAKLTQTRKVKKPNSVVKKSHHVGKDDESRLDHLGVVAYNRKQRSIPLSPIVPESSDPAALKRARNTEAARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER
| null | null |
amino acid biosynthetic process [GO:0008652]; cellular response to amino acid starvation [GO:0034198]; intracellular signal transduction [GO:0035556]; negative regulation of ribosomal protein gene transcription by RNA polymerase II [GO:0010688]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nitrogen catabolite activation of transcription from RNA polymerase II promoter [GO:0001080]; positive regulation of cellular response to amino acid starvation [GO:1903833]; positive regulation of RNA polymerase II transcription preinitiation complex assembly [GO:0045899]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; protein localization to nuclear periphery [GO:1990139]; regulation of cell cycle [GO:0051726]; response to amino acid starvation [GO:1990928]
|
nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; mediator complex binding [GO:0036033]; protein self-association [GO:0043621]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; TFIID-class transcription factor complex binding [GO:0001094]
|
PF07716;
|
3.30.160.60;
|
BZIP family, GCN4 subfamily
|
PTM: Phosphorylated by the cyclin-CDK PCL5-PHO85. Phosphorylation of Thr-165 induces degradation of GCN4 by the E3 ubiquitin ligase complex SCF(Cdc4). {ECO:0000269|PubMed:12101234}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12455686, ECO:0000269|PubMed:14648200}. Note=Localizes to the nucleus independently of cellular amino acid levels. {ECO:0000269|PubMed:12455686}.
| null | null | null | null | null |
FUNCTION: Master transcriptional regulator that mediates the response to amino acid starvation (PubMed:11390663, PubMed:29628310). Binds variations of the DNA sequence 5'-ATGA[CG]TCAT-3' in canonical nucleosome-depleted 5'-positioned promoters, and also within coding sequences and 3' non-coding regions (PubMed:11390663, PubMed:1473154, PubMed:1939099, PubMed:2204805, PubMed:2277632, PubMed:29628310, PubMed:3530496, PubMed:3532321, PubMed:3678204, PubMed:7664107). During nutrient starvation (low or poor amino acid, carbon or purine sources), it activates genes required for amino acid biosynthesis and transport, autophagy, cofactor biosynthesis and transport, mitochondrial transport, and additional downstream transcription factors (PubMed:10733573, PubMed:11390663, PubMed:1939099, PubMed:29628310, PubMed:7862116, PubMed:8336737). Activates transcription by recruiting multiple coactivators, including the mediator complex, the SAGA complex, and the SWI/SNF complex, to enable assembly of the pre-initiation complex at core promoters (PubMed:10549298, PubMed:19940160, PubMed:9488488). {ECO:0000269|PubMed:10549298, ECO:0000269|PubMed:10733573, ECO:0000269|PubMed:11390663, ECO:0000269|PubMed:1473154, ECO:0000269|PubMed:1939099, ECO:0000269|PubMed:19940160, ECO:0000269|PubMed:2204805, ECO:0000269|PubMed:2277632, ECO:0000269|PubMed:29628310, ECO:0000269|PubMed:3530496, ECO:0000269|PubMed:3532321, ECO:0000269|PubMed:3678204, ECO:0000269|PubMed:7664107, ECO:0000269|PubMed:7862116, ECO:0000269|PubMed:8336737, ECO:0000269|PubMed:9488488}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P03070
|
LT_SV40
|
MDKVLNREESLQLMDLLGLERSAWGNIPLMRKAYLKKCKEFHPDKGGDEEKMKKMNTLYKKMEDGVKYAHQPDFGGFWDATEIPTYGTDEWEQWWNAFNEENLFCSEEMPSSDDEATADSQHSTPPKKKRKVEDPKDFPSELLSFLSHAVFSNRTLACFAIYTTKEKAALLYKKIMEKYSVTFISRHNSYNHNILFFLTPHRHRVSAINNYAQKLCTFSFLICKGVNKEYLMYSALTRDPFSVIEESLPGGLKEHDFNPEEAEETKQVSWKLVTEYAMETKCDDVLLLLGMYLEFQYSFEMCLKCIKKEQPSHYKYHEKHYANAAIFADSKNQKTICQQAVDTVLAKKRVDSLQLTREQMLTNRFNDLLDRMDIMFGSTGSADIEEWMAGVAWLHCLLPKMDSVVYDFLKCMVYNIPKKRYWLFKGPIDSGKTTLAAALLELCGGKALNVNLPLDRLNFELGVAIDQFLVVFEDVKGTGGESRDLPSGQGINNLDNLRDYLDGSVKVNLEKKHLNKRTQIFPPGIVTMNEYSVPKTLQARFVKQIDFRPKDYLKHCLERSEFLLEKRIIQSGIALLLMLIWYRPVAEFAQSIQSRIVEWKERLDKEFSLSVYQKMKFNVAMGIGVLDWLRNSDDDDEDSQENADKNEDGGEKNMEDSGHETGIDSQSQGSFQAPQSSQSVHDHNQPYHICRGFTCFKKPPTPPPEPET
|
3.6.4.-
| null |
bidirectional double-stranded viral DNA replication [GO:0039686]; DNA unwinding involved in DNA replication [GO:0006268]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of JAK1 activity [GO:0039576]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral DNA genome replication [GO:0039693]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell nucleus [GO:0042025]
|
ATP binding [GO:0005524]; DNA replication origin binding [GO:0003688]; double-stranded DNA binding [GO:0003690]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; single-stranded DNA binding [GO:0003697]
|
PF06431;PF02217;
|
3.40.1310.20;1.10.287.110;1.20.1050.70;3.40.50.300;1.10.10.510;
| null |
PTM: Phosphorylated on both serine and threonine residues. Phosphorylation on Ser-120 and Ser-123 inhibits viral replication, while phosphorylation on Thr-124 enhances replication by activating the DNA-binding domain. Phosphorylation on Thr-701 is required for binding to host FBW7gamma isoform. Dephosphorylated preferentially by PP2A on Ser-120, Ser-123, Ser-677 and perhaps Ser-679. Small t antigen inhibits the dephosphorylation by the AC form of PP2A. {ECO:0000269|PubMed:2160857, ECO:0000269|PubMed:2552322, ECO:0000269|PubMed:2838952, ECO:0000269|PubMed:8648725}.; PTM: O-Glycosylated near the C-terminal region. {ECO:0000269|PubMed:3027978}.; PTM: Acetylated by CBP in a TP53-dependent manner. {ECO:0000269|PubMed:15254196, ECO:0000269|PubMed:205802}.
|
SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:3027978, ECO:0000269|PubMed:6096007}.
| null | null | null | null | null |
FUNCTION: Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription. May inactivate the growth-suppressing properties of the E3 ubiquitin ligase CUL7. {ECO:0000269|PubMed:15611062, ECO:0000269|PubMed:17341466, ECO:0000269|PubMed:18922873, ECO:0000269|PubMed:8647434, ECO:0000269|PubMed:9632777}.; FUNCTION: Isoform 17kT antigen targets host RBL2 for degradation and promotes cell proliferation. Transactivates host cyclin A promoter through its J domain. {ECO:0000269|PubMed:15680424}.
|
Simian virus 40 (SV40)
|
P03071
|
LT_POVBK
|
MDKVLNREESMELMDLLGLERAAWGNLPLMRKAYLRKCKEFHPDKGGDEDKMKRMNTLYKKMEQDVKVAHQPDFGTWSSSEVPTYGTEEWESWWSSFNEKWDEDLFCHEDMFASDEEATADSQHSTPPKKKRKVEDPKDFPSDLHQFLSQAVFSNRTLACFAVYTTKEKAQILYKKLMEKYSVTFISRHMCAGHNIIFFLTPHRHRVSAINNFCQKLCTFSFLICKGVNKEYLLYSALTRDPYHTIEESIQGGLKEHDFSPEEPEETKQVSWKLITEYAVETKCEDVFLLLGMYLEFQYNVEECKKCQKKDQPYHFKYHEKHFANAIIFAESKNQKSICQQAVDTVLAKKRVDTLHMTREEMLTERFNHILDKMDLIFGAHGNAVLEQYMAGVAWLHCLLPKMDSVIFDFLHCIVFNVPKRRYWLFKGPIDSGKTTLAAGLLDLCGGKALNVNLPMERLTFELGVAIDQYMVVFEDVKGTGAESKDLPSGHGINNLDSLRDYLDGSVKVNLEKKHLNKRTQIFPPGLVTMNEYPVPKTLQARFVRQIDFRPKIYLRKSLQNSEFLLEKRILQSGMTLLLLLIWFRPVADFATDIQSRIVEWKERLDSEISMYTFSRMKYNICMGKCILDITREEDSETEDSGHGSSTESQSQCSSQVSDTSAPAEDSQRSDPHSQELHLCKGFQCFKRPKTPPPK
|
3.6.4.-
| null |
DNA replication [GO:0006260]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of JAK1 activity [GO:0039576]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell nucleus [GO:0042025]
|
ATP binding [GO:0005524]; DNA replication origin binding [GO:0003688]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]
|
PF06431;PF02217;
|
3.40.1310.20;1.10.287.110;1.20.1050.70;3.40.50.300;1.10.10.510;
| null |
PTM: Phosphorylated on both serine and threonine residues. Small t antigen inhibits the dephosphorylation by the AC form of PP2A (By similarity). {ECO:0000250}.; PTM: O-Glycosylated near the C-terminal region. {ECO:0000250}.; PTM: Acetylated by CBP in a TP53-dependent manner. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription (By similarity). {ECO:0000250}.
|
BK polyomavirus (BKPyV) (Human polyomavirus 1)
|
P03077
|
MT_POVMA
|
MDRVLSRADKERLLELLKLPRQLWGDFGRMQQAYKQQSLLLHPDKGGSHALMQELNSLWGTFKTEVYNLRMNLGGTGFQVRRLHADGWNLSTKDTFGDRYYQRFCRMPLTCLVNVKYSSCSCILCLLRKQHRELKDKCDARCLVLGECFCLECYMQWFGTPTRDVLNLYADFIASMPIDWLDLDVHSVYNPKRRSEELRRAATVHYTMTTGHSAMEASTSQGNGMISSESGTPATSRRLRLPSLLSNPTYSVMRSHSYPPTRVLQQIHPHILLEEDEILVLLSPMTAYPRTPPELLYPESDQDQLEPLEEEEEEYMPMEDLYLDILPGEQVPQLIPPPIIPRAGLSPWEGLILRDLQRAHFDPILDASQRMRATHRAALRAHSMQRHLRRLGRTLLLVTFLAALLGICLMLFILIKRSRHF
| null | null | null |
host cell membrane [GO:0033644]; membrane [GO:0016020]
| null |
PF02380;
|
1.10.287.110;1.20.120.1860;
| null |
PTM: Tyrosine-phosphorylated on three residues 250, 315 and 322, providing docking sites for host Shc1, p85, and Plcg1, respectively. {ECO:0000269|PubMed:7759472, ECO:0000269|PubMed:8022784, ECO:0000269|PubMed:9420259}.
|
SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Plays a role in transformation by modulating the activities of cellular proteins involved in control of cell proliferation and by acting as a functional homolog of an activated tyrosine kinase-associated growth-factor receptor. Recruits upon association with host Ppp2/PP2A the Src tyrosine kinase components Src, Yes and Fyn, thereby activating their kinase activity. Activation of Shc1, Pclg1 and p85 mediate signal transduction pathways leading to cell cycle progression and cell division. MT also plays a role in regulation of early and late gene expression and in viral DNA replication. {ECO:0000269|PubMed:16840310}.
|
Murine polyomavirus (strain A2) (MPyV)
|
P03086
|
AGNO_POVJC
|
MVLRQLSRKASVKVSKTWSGTKKRAQRILIFLLEFLLDFCTGEDSVDGKKRQRHSGLTEQTYSALPEPKAT
| null | null |
protein complex oligomerization [GO:0051259]
|
host cell nuclear membrane [GO:0044200]; host cell plasma membrane [GO:0020002]; host cell rough endoplasmic reticulum membrane [GO:0044169]; membrane [GO:0016020]
|
DNA binding [GO:0003677]; monoatomic ion channel activity [GO:0005216]
|
PF01736;
| null |
Polyomavirus agnoprotein family
|
PTM: Phosphorylated by host PKC. Phosphorylation alters the stability and may also have an impact on the subcellular location (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. Host nucleus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host rough endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Mostly perinuclear. {ECO:0000269|PubMed:11517407, ECO:0000269|PubMed:15864296, ECO:0000269|PubMed:20300659}.
| null | null | null | null | null |
FUNCTION: Alters the structure of the nuclear envelope by interacting with host CBX5 and disrupting CBX5 association with LBR. Involved in the perinuclear-nuclear localization of the capsid protein VP1 during virion assembly and maturation. Plays an important role in the release of progeny virions from infected cells and in viral propagation, probably by acting as a viral ionic channel in the host plasma membrane. Allows influx of extracellular calcium ions in the host cell. May contribute to viral genome transcription and translation of viral late proteins. {ECO:0000269|PubMed:11517407, ECO:0000269|PubMed:12165856, ECO:0000269|PubMed:20300659}.
|
JC polyomavirus (JCPyV) (JCV)
|
P03087
|
VP1_SV40
|
MAPTKRKGSCPGAAPKKPKEPVQVPKLVIKGGIEVLGVKTGVDSFTEVECFLNPQMGNPDEHQKGLSKSLAAEKQFTDDSPDKEQLPCYSVARIPLPNINEDLTCGNILMWEAVTVKTEVIGVTAMLNLHSGTQKTHENGAGKPIQGSNFHFFAVGGEPLELQGVLANYRTKYPAQTVTPKNATVDSQQMNTDHKAVLDKDNAYPVECWVPDPSKNENTRYFGTYTGGENVPPVLHITNTATTVLLDEQGVGPLCKADSLYVSAVDICGLFTNTSGTQQWKGLPRYFKITLRKRSVKNPYPISFLLSDLINRRTQRVDGQPMIGMSSQVEEVRVYEDTEELPGDPDMIRYIDEFGQTTTRMQ
| null | null |
caveolin-mediated endocytosis of virus by host cell [GO:0075513]; viral capsid assembly [GO:0019069]; virion attachment to host cell [GO:0019062]
|
capsomere [GO:0046727]; host cell endoplasmic reticulum [GO:0044165]; host cell nucleus [GO:0042025]; T=7 icosahedral viral capsid [GO:0039620]
|
identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; structural molecule activity [GO:0005198]
|
PF00718;
|
2.60.175.10;
|
Polyomaviruses coat protein VP1 family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:8805523}. Host nucleus {ECO:0000269|PubMed:11462004}. Host endoplasmic reticulum {ECO:0000305|PubMed:19157478}. Note=Following host cell entry, the virion enters into the endoplasmic reticulum through a calveolar-dependent pathway. Then, viral DNA is translocated to the nucleus. Shortly after synthesis, a nuclear localization signal directs VP1 to the cell nucleus where virion assembly occurs. {ECO:0000305|PubMed:19157478}.
| null | null | null | null | null |
FUNCTION: Forms an icosahedral capsid with a T=7 symmetry and a 40 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Binds to N-glycolylneuraminic analog of the ganglioside GM1 on the cell surface to provide virion attachment to target cell (PubMed:18353982). Once attached, the virion is internalized by caveolin-mediated endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating (PubMed:17981119). Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus (PubMed:17981119). Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. The assembly takes place in the cell nucleus. Encapsulates the genomic DNA and participates in rearranging nucleosomes around the viral DNA. The viral progenies exit the cells by lytic release. {ECO:0000269|PubMed:17981119, ECO:0000269|PubMed:18353982, ECO:0000305|PubMed:19157478}.
|
Simian virus 40 (SV40)
|
P03089
|
VP1_POVJC
|
MAPTKRKGERKDPVQVPKLLIRGGVEVLEVKTGVDSITEVECFLTPEMGDPDEHLRGFSKSISISDTFESDSPNRDMLPCYSVARIPLPNLNEDLTCGNILMWEAVTLKTEVIGVTSLMNVHSNGQATHDNGAGKPVQGTSFHFFSVGGEALELQGVLFNYRTKYPDGTIFPKNATVQSQVMNTEHKAYLDKNKAYPVECWVPDPTRNENTRYFGTLTGGENVPPVLHITNTATTVLLDEFGVGPLCKGDNLYLSAVDVCGMFTNRSGSQQWRGLSRYFKVQLRKRRVKNPYPISFLLTDLINRRTPRVDGQPMYGMDAQVEEVRVFEGTEELPGDPDMMRYVDKYGQLQTKML
| null | null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; virion attachment to host cell [GO:0019062]
|
host cell nucleus [GO:0042025]; T=7 icosahedral viral capsid [GO:0039620]
|
structural molecule activity [GO:0005198]
|
PF00718;
|
2.60.175.10;
|
Polyomaviruses coat protein VP1 family
| null |
SUBCELLULAR LOCATION: Virion. Host nucleus {ECO:0000269|PubMed:15331723}. Note=Virions are efficiently assembled at nuclear domain 10 (ND10), which is also known as promyelocytic leukemia (PML) nuclear bodies. {ECO:0000269|PubMed:15331723}.
| null | null | null | null | null |
FUNCTION: Forms an icosahedral capsid with a T=7 symmetry and a 40 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with a N-linked glycoprotein containing terminal alpha(2-6)-linked sialic acids on the cell surface to provide virion attachment to target cell. The serotonergic receptor 5HT2AR also acts as a cellular receptor for JCV on human glial cells. Once attached, the virions enter predominantly by a ligand-inducible clathrin-dependent pathway and traffic to the ER. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA at nuclear domains called promyelocytic leukemia (PML) bodies, and participates in rearranging nucleosomes around the viral DNA. {ECO:0000269|PubMed:10666259, ECO:0000269|PubMed:9573227, ECO:0000305|PubMed:19157478}.
|
JC polyomavirus (JCPyV) (JCV)
|
P03093
|
VP2_SV40
|
MGAALTLLGDLIATVSEAAAATGFSVAEIAAGEAAAAIEVQLASVATVEGLTTSEAIAAIGLIPQAYAVISGAPAAIAGFAALLQTVTGVSAVAQVGYRFFSDWDHKVSTVGLYQQPGMAVDLYRPDDYYDILFPGVQTFVHSVQYLDPRHWGPTLFNAISQAFWRVIQNDIPRLTSQELERRTQRYLRDSLARFLEETTWTVINAPVNWYNSLQDYYSTLSPIRPTMVRQVANREGLQISFGHTYDNIDEADSIQQVTERWEAQSQSPNVQSGEFIEKFEAPGGANQRTAPQWMLPLLLGLYGSVTSALKAYEDGPNKKKRKLSRGSSQKTKGTSASAKARHKRRNRSSRS
| null | null |
permeabilization of host organelle membrane involved in viral entry into host cell [GO:0039665]; protein complex oligomerization [GO:0051259]; symbiont entry into host cell via permeabilization of inner membrane [GO:0099008]; viral penetration into host nucleus [GO:0075732]; virion attachment to host cell [GO:0019062]
|
host cell [GO:0043657]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; viral capsid [GO:0019028]
|
DNA binding [GO:0003677]; monoatomic ion channel activity [GO:0005216]; structural molecule activity [GO:0005198]
|
PF00761;
| null |
Polyomaviruses capsid protein VP2 family
| null |
SUBCELLULAR LOCATION: [Isoform VP2]: Virion {ECO:0000305}. Host nucleus {ECO:0000269|PubMed:1847270}. Host endoplasmic reticulum {ECO:0000269|PubMed:17189196}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:17189196}. Note=Following host cell entry, the virion enters into the endoplasmic reticulum through a calveolar-dependent pathway. Then, isoform VP2 integrates into the endoplasmic reticulum membrane and participates in the translocation of viral DNA to the nucleus. Shortly after synthesis, a nuclear localization signal directs isoform VP2 to the cell nucleus where virion assembly occurs. {ECO:0000269|PubMed:17189196, ECO:0000269|PubMed:1847270}.; SUBCELLULAR LOCATION: [Isoform VP3]: Virion {ECO:0000305}. Host nucleus {ECO:0000269|PubMed:1847270}. Host endoplasmic reticulum {ECO:0000269|PubMed:17189196}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:17189196, ECO:0000269|PubMed:25631089}. Note=Following host cell entry, the virion enters into the endoplasmic reticulum through a calveolar-dependent pathway. Then, isoform VP3 integrates into the endoplasmic reticulum membrane and participates in the translocation of viral DNA to the nucleus. Shortly after synthesis, a nuclear localization signal directs isoform VP3 to the cell nucleus where virion assembly occurs. {ECO:0000269|PubMed:17189196, ECO:0000269|PubMed:1847270}.; SUBCELLULAR LOCATION: [Isoform VP4]: Host nucleus {ECO:0000269|PubMed:17658947}.
| null | null | null | null | null |
FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly. The viral progenies exit the cells by lytic release. Isoform VP2 may repress SP1 activation of the SV40 early promoter, via specific protein-protein and protein-DNA interactions. {ECO:0000269|PubMed:17189196, ECO:0000269|PubMed:3031509, ECO:0000269|PubMed:7815491}.; FUNCTION: [Isoform VP3]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus entry, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane. Essential for focus formation and virus endoplasmic reticulum-to-cytosol membrane transport, required to recruit selective cellular components to the foci in the ER membrane. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Isoform VP3 represses SP1 activation of the SV40 early promoter, via specific protein-protein and protein-DNA interactions. SP1 additionally participates in recruiting VP3 to the SV40 minichromosome during SV40 assembly. Plays a role in virion assembly within the nucleus. May initiate host cell lysis when associated with VP4. {ECO:0000269|PubMed:12186919, ECO:0000269|PubMed:17189196, ECO:0000269|PubMed:25631089, ECO:0000269|PubMed:7815491, ECO:0000269|PubMed:9466902}.; FUNCTION: [Isoform VP4]: Viroporin inducing perforation of cellular membranes to trigger virus progeny release. Forms pores of 3 nm inner diameter. VP4 is expressed about 24 hours after the late structural proteins and is not incorporated into the mature virion. {ECO:0000269|PubMed:21738474}.
|
Simian virus 40 (SV40)
|
P03094
|
VP2_POVBK
|
MGAALALLGDLVASVSEAAAATGFSVAEIAAGEAAAAIEVQIASLATVEGITSTSEAIAAIGLTPQTYAVIAGAPGAIAGFAALIQTVSGISSLAQVGYRFFSDWDHKVSTVGLYQQSGMALELFNPDEYYDILFPGVNTFVNNIQYLDPRHWGPSLFATISQALWHVIRDDIPSITSQELQRRTERFFRDSLARFLEETTWTIVNAPINFYNYIQQYYSDLSPIRPSMVRQVAEREGTRVHFGHTYSIDDADSIEEVTQRMDLRNQQSVHSGEFIEKTIAPGGANQRTAPQWMLPLLLGLYGTVTPALEAYEDGPNQKKRRVSRGSSQKAKGTRASAKTTNKRRSRSSRS
| null | null |
permeabilization of host organelle membrane involved in viral entry into host cell [GO:0039665]; protein complex oligomerization [GO:0051259]; symbiont entry into host cell via permeabilization of inner membrane [GO:0099008]; viral penetration into host nucleus [GO:0075732]; virion attachment to host cell [GO:0019062]
|
host cell [GO:0043657]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; viral capsid [GO:0019028]
|
DNA binding [GO:0003677]; monoatomic ion channel activity [GO:0005216]; structural molecule activity [GO:0005198]
|
PF00761;
| null |
Polyomaviruses capsid protein VP2 family
| null |
SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP4]: Host nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly (By similarity). {ECO:0000250}.; FUNCTION: [Isoform VP3]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus. May participate in host cell lysis when associated with VP4 (By similarity). {ECO:0000250}.; FUNCTION: [Isoform VP4]: Viroporin inducing perforation of cellular membranes to trigger virus progeny release. Forms pores of 3 nm inner diameter. VP4 is expressed about 24 hours after the late structural proteins and is not incorporated into the mature virion (By similarity). {ECO:0000250}.
|
BK polyomavirus (BKPyV) (Human polyomavirus 1)
|
P03095
|
VP2_POVJC
|
MGAALALLGDLVATVSEAAAATGFSVAEIAAGEAAATIEVEIASLATVEGITSTSEAIAAIGLTPETYAVITGAPGAVAGFAALVQTVTGGSAIAQLGYRFFADWDHKVSTVGLFQQPAMALQLFNPEDYYDILFPGVNAFVNNIHYLDPRHWGPSLFSTISQAFWNLVRDDLPALTSQEIQRRTQKLFVESLARFLEETTWAIVNSPANLYNYISDYYSRLSPVRPSMVRQVAQREGTYISFGHSYTQSIDDADSIQEVTQRLDLKTPNVQSGEFIERSIAPGGANQRSAPQWMLPLLLGLYGTVTPALEAYEDGPNKKKRRKEGPRASSKTSYKRRSRSSRS
| null | null |
permeabilization of host organelle membrane involved in viral entry into host cell [GO:0039665]; protein complex oligomerization [GO:0051259]; symbiont entry into host cell via permeabilization of inner membrane [GO:0099008]; viral penetration into host nucleus [GO:0075732]; virion attachment to host cell [GO:0019062]
|
host cell [GO:0043657]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; viral capsid [GO:0019028]
|
DNA binding [GO:0003677]; monoatomic ion channel activity [GO:0005216]; structural molecule activity [GO:0005198]
|
PF00761;
| null |
Polyomaviruses capsid protein VP2 family
| null |
SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP4]: Host nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly (By similarity). {ECO:0000250}.; FUNCTION: [Isoform VP3]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus. May participate in host cell lysis when associated with VP4 (By similarity). {ECO:0000250}.; FUNCTION: [Isoform VP4]: Viroporin inducing perforation of cellular membranes to trigger virus progeny release. Forms pores of 3 nm inner diameter. VP4 is expressed about 24 hours after the late structural proteins and is not incorporated into the mature virion (By similarity). {ECO:0000250}.
|
JC polyomavirus (JCPyV) (JCV)
|
P03096
|
VP2_POVMA
|
MGAALTILVDLIEGLAEVSTLTGLSAEAILSGEALAALDGEITALTLEGVMSSETALATMGISEEVYGFVSTVPVFVSRTAGAIWLMQTVQGASTISLGIQRYLHNEEVPTVNRNMALIPWRDPALLDIYFPGVNQFAHALNVVHDWGHGLLHSVGRYVWQMVVQETQHRLEGAVRELTVRQTHTFLDGLARLLENTRWVVSNAPQSAIDAINRGASSASSGYSSLSDYYRQLGLNPPQRRALFNRIEGSMGNGGPTPAAHIQDESGEVIKFYQAQVVSHQRVTPDWMLPLILGLYGDITPTWATVIEEDGPQKKKRRL
| null | null |
symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732]
|
host cell [GO:0043657]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; viral capsid [GO:0019028]
|
DNA binding [GO:0003677]; structural molecule activity [GO:0005198]
|
PF00761;
| null |
Polyomaviruses capsid protein VP2 family
| null |
SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly (By similarity). {ECO:0000250}.; FUNCTION: [Isoform VP3]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus (By similarity). {ECO:0000250}.
|
Murine polyomavirus (strain A2) (MPyV)
|
P03097
|
VP2_POVM3
|
MGAALTILVDLIEGLAEVSTLTGLSAEAILSGEALAALDGEITALTLEGVMSSETALATMGISEEVYGFVSTVPVFVNRTAGAIWLMQTVQGASTISLGIQRYLHNEEVPTVNRNMALIPWRDPALLDIYFPGVNQFAHALNVVHDWGHGLLHSVGRYVWQMVVQETQHRLEGAVRELTVRQTHTFLDGLARLLENTRWVVSNAPQSAIDAINRGASSVSSGYSSLSDYYRQLGLNPPQRRALFNRIEGSMGNGGPTPAAHIQDESGEVIKFYQAPGGAHQRVTPDWMLPLILGLYGDITPTWATVIEEDGPQKKKRRL
| null | null |
symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732]
|
host cell [GO:0043657]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; viral capsid [GO:0019028]
|
DNA binding [GO:0003677]; structural molecule activity [GO:0005198]
|
PF00761;
| null |
Polyomaviruses capsid protein VP2 family
| null |
SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly (By similarity). {ECO:0000250}.; FUNCTION: [Isoform VP3]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus (By similarity). {ECO:0000250}.
|
Murine polyomavirus (strain A3) (MPyV)
|
P03107
|
VL2_HPV16
|
MRHKRSAKRTKRASATQLYKTCKQAGTCPPDIIPKVEGKTIAEQILQYGSMGVFFGGLGIGTGSGTGGRTGYIPLGTRPPTATDTLAPVRPPLTVDPVGPSDPSIVSLVEETSFIDAGAPTSVPSIPPDVSGFSITTSTDTTPAILDINNTVTTVTTHNNPTFTDPSVLQPPTPAETGGHFTLSSSTISTHNYEEIPMDTFIVSTNPNTVTSSTPIPGSRPVARLGLYSRTTQQVKVVDPAFVTTPTKLITYDNPAYEGIDVDNTLYFSSNDNSINIAPDPDFLDIVALHRPALTSRRTGIRYSRIGNKQTLRTRSGKSIGAKVHYYYDLSTIDPAEEIELQTITPSTYTTTSHAASPTSINNGLYDIYADDFITDTSTTPVPSVPSTSLSGYIPANTTIPFGGAYNIPLVSGPDIPINITDQAPSLIPIVPGSPQYTIIADAGDFYLHPSYYMLRKRRKRLPYFFSDVSLAA
| null | null |
microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732]
|
host cell [GO:0043657]; host cell endosome [GO:0044174]; host cell Golgi apparatus [GO:0044177]; host cell nucleus [GO:0042025]; viral capsid [GO:0019028]
|
DNA binding [GO:0003677]; structural molecule activity [GO:0005198]
|
PF00513;
| null |
Papillomaviridae L2 protein family
|
PTM: Highly phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04003, ECO:0000269|PubMed:1662690}.
|
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04003, ECO:0000269|PubMed:19095951}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04003, ECO:0000269|PubMed:19095951}. Host early endosome {ECO:0000269|PubMed:25693203, ECO:0000269|PubMed:30122350}. Host Golgi apparatus {ECO:0000269|PubMed:25693203, ECO:0000269|PubMed:30122350}.
| null | null | null | null | null |
FUNCTION: Minor protein of the capsid that localizes along the inner surface of the virion, within the central cavities beneath the L1 pentamers. Plays a role in capsid stabilization through interaction with the major capsid protein L1. Once the virion enters the host cell, L2 escorts the genomic DNA into the nucleus by promoting escape from the endosomal compartments and traffic through the host Golgi network. Mechanistically, the C-terminus of L2 possesses a cell-penetrating peptide that protudes from the host endosome, interacts with host cytoplasmic retromer cargo and thereby mediates the capsid delivery to the host trans-Golgi network. Plays a role through its interaction with host dynein in the intracellular microtubule-dependent transport of viral capsid toward the nucleus. Mediates the viral genome import into the nucleus through binding to host importins. Once within the nucleus, L2 localizes viral genomes to host PML bodies in order to activate early gene expression for establishment of infection. Later on, promotes late gene expression by interacting with the viral E2 protein and by inhibiting its transcriptional activation functions. During virion assembly, encapsidates the genome by direct interaction with the viral DNA. {ECO:0000255|HAMAP-Rule:MF_04003, ECO:0000269|PubMed:15507604, ECO:0000269|PubMed:15681049, ECO:0000269|PubMed:21166973, ECO:0000269|PubMed:25693203, ECO:0000269|PubMed:30122350, ECO:0000269|PubMed:8553535}.
|
Human papillomavirus type 16
|
P03116
|
VE1_BPV1
|
MANDKGSNWDSGLGCSYLLTEAECESDKENEEPGAGVELSVESDRYDSQDEDFVDNASVFQGNHLEVFQALEKKAGEEQILNLKRKVLGSSQNSSGSEASETPVKRRKSGAKRRLFAENEANRVLTPLQVQGEGEGRQELNEEQAISHLHLQLVKSKNATVFKLGLFKSLFLCSFHDITRLFKNDKTTNQQWVLAVFGLAEVFFEASFELLKKQCSFLQMQKRSHEGGTCAVYLICFNTAKSRETVRNLMANTLNVREECLMLQPAKIRGLSAALFWFKSSLSPATLKHGALPEWIRAQTTLNESLQTEKFDFGTMVQWAYDHKYAEESKIAYEYALAAGSDSNARAFLATNSQAKHVKDCATMVRHYLRAETQALSMPAYIKARCKLATGEGSWKSILTFFNYQNIELITFINALKLWLKGIPKKNCLAFIGPPNTGKSMLCNSLIHFLGGSVLSFANHKSHFWLASLADTRAALVDDATHACWRYFDTYLRNALDGYPVSIDRKHKAAVQIKAPPLLVTSNIDVQAEDRYLYLHSRVQTFRFEQPCTDESGEQPFNITDADWKSFFVRLWGRLDLIDEEEDSEEDGDSMRTFTCSARNTNAVD
|
3.6.4.12
| null |
DNA replication [GO:0006260]
|
host cell nucleus [GO:0042025]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]
|
PF00519;PF20450;PF00524;
|
3.40.1310.10;3.40.50.300;1.10.10.510;
|
Papillomaviridae E1 protein family
|
PTM: Phosphorylated. Probably phosphorylated by host PKA and PKC at Ser-109. Phosphorylated by host CDK1 at Thr-102. {ECO:0000255|HAMAP-Rule:MF_04000, ECO:0000269|PubMed:8382303, ECO:0000269|PubMed:9024804}.; PTM: Sumoylated. {ECO:0000255|HAMAP-Rule:MF_04000}.
|
SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04000, ECO:0000269|PubMed:8382303}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_04000};
| null | null | null | null |
FUNCTION: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication. {ECO:0000255|HAMAP-Rule:MF_04000, ECO:0000269|PubMed:11005821, ECO:0000269|PubMed:14747526, ECO:0000269|PubMed:16415033, ECO:0000269|PubMed:1846806}.
|
Bovine papillomavirus type 1
|
P03120
|
VE2_HPV16
|
METLCQRLNVCQDKILTHYENDSTDLRDHIDYWKHMRLECAIYYKAREMGFKHINHQVVPTLAVSKNKALQAIELQLTLETIYNSQYSNEKWTLQDVSLEVYLTAPTGCIKKHGYTVEVQFDGDICNTMHYTNWTHIYICEEASVTVVEGQVDYYGLYYVHEGIRTYFVQFKDDAEKYSKNKVWEVHAGGQVILCPTSVFSSNEVSSPEIIRQHLANHPAATHTKAVALGTEETQTTIQRPRSEPDTGNPCHTTKLLHRDSVDSAPILTAFNSSHKGRINCNSNTTPIVHLKGDANTLKCLRYRFKKHCTLYTAVSSTWHWTGHNVKHKSAIVTLTYDSEWQRDQFLSQVKIPKTITVSTGFMSI
| null | null |
DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; regulation of DNA replication [GO:0006275]; viral DNA genome replication [GO:0039693]
|
host cell nucleus [GO:0042025]; host cytoskeleton [GO:0044163]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; nucleotide binding [GO:0000166]
|
PF00511;PF00508;
|
3.30.70.330;1.10.287.30;2.170.200.10;
|
Papillomaviridae E2 protein family
|
PTM: Phosphorylated. Phosphorylation at Ser-243 mediates binding to host Brd4 and is required for host chromosome binding. {ECO:0000255|HAMAP-Rule:MF_04001, ECO:0000269|PubMed:25340539, ECO:0000269|PubMed:7645246}.; PTM: Sumoylation plays a regulatory role in E2 transcriptional activity. {ECO:0000255|HAMAP-Rule:MF_04001, ECO:0000269|PubMed:18619639}.
|
SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04001, ECO:0000269|PubMed:18619639, ECO:0000269|PubMed:25340539, ECO:0000269|PubMed:25911730, ECO:0000269|PubMed:7645246}.
| null | null | null | null | null |
FUNCTION: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex. {ECO:0000255|HAMAP-Rule:MF_04001, ECO:0000269|PubMed:1326651, ECO:0000269|PubMed:15681049, ECO:0000269|PubMed:16611886, ECO:0000269|PubMed:25340539, ECO:0000269|PubMed:26365679, ECO:0000269|PubMed:3033289}.
|
Human papillomavirus type 16
|
P03122
|
VE2_BPV1
|
METACERLHVAQETQMQLIEKSSDKLQDHILYWTAVRTENTLLYAARKKGVTVLGHCRVPHSVVCQERAKQAIEMQLSLQELSKTEFGDEPWSLLDTSWDRYMSEPKRCFKKGARVVEVEFDGNASNTNWYTVYSNLYMRTEDGWQLAKAGADGTGLYYCTMAGAGRIYYSRFGDEAARFSTTGHYSVRDQDRVYAGVSSTSSDFRDRPDGVWVASEGPEGDPAGKEAEPAQPVSSLLGSPACGPIRAGLGWVRDGPRSHPYNFPAGSGGSILRSSSTPVQGTVPVDLASRQEEEEQSPDSTEEEPVTLPRRTTNDGFHLLKAGGSCFALISGTANQVKCYRFRVKKNHRHRYENCTTTWFTVADNGAERQGQAQILITFGSPSQRQDFLKHVPLPPGMNISGFTASLDF
| null | null |
DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; regulation of DNA replication [GO:0006275]; viral DNA genome replication [GO:0039693]
|
host cell nucleus [GO:0042025]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; nucleotide binding [GO:0000166]
|
PF00511;PF00508;
|
3.30.70.330;1.10.287.30;2.170.200.10;
|
Papillomaviridae E2 protein family
|
PTM: Oxidation of Cys-340 in response to redox signaling leads to the loss of DNA-binding activity and the inactivation of gene activator or repressor function. {ECO:0000269|PubMed:1323841}.; PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04001}.
|
SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04001, ECO:0000269|PubMed:17189189}. Note=Colocalizes with DDX11 at early stages of mitosis.
| null | null | null | null | null |
FUNCTION: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex. {ECO:0000255|HAMAP-Rule:MF_04001}.
|
Bovine papillomavirus type 1
|
P03126
|
VE6_HPV16
|
MHQKRTAMFQDPQERPRKLPQLCTELQTTIHDIILECVYCKQQLLRREVYDFAFRDLCIVYRDGNPYAVCDKCLKFYSKISEYRHYCYSLYGTTLEQQYNKPLCDLLIRCINCQKPLCPEEKQRHLDKKQRFHNIRGRWTGRCMSCCRSSRTRRETQL
| null | null |
activation of GTPase activity [GO:0090630]; DNA-templated transcription [GO:0006351]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of proteolysis [GO:0030162]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity [GO:0039548]; symbiont-mediated suppression of host transcription [GO:0039653]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]
|
DNA binding [GO:0003677]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; PDZ domain binding [GO:0030165]
|
PF00518;
|
3.30.240.40;
|
Papillomaviridae E6 protein family
| null |
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04006, ECO:0000269|PubMed:16507364, ECO:0000269|PubMed:22483108}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04006, ECO:0000269|PubMed:16507364, ECO:0000269|PubMed:22483108}.
| null | null | null | null | null |
FUNCTION: Plays a major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6AP targets several other substrates to degradation via the proteasome including host DLG1 or NFX1, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents the shortening of telomere length leading to cell immortalization. Other cellular targets including BAK1, Fas-associated death domain-containing protein (FADD) and procaspase 8, are degraded by E6/E6AP causing inhibition of apoptosis. E6 also inhibits immune response by interacting with host IRF3 and TYK2. These interactions prevent IRF3 transcriptional activities and inhibit TYK2-mediated JAK-STAT activation by interferon alpha resulting in inhibition of the interferon signaling pathway. {ECO:0000255|HAMAP-Rule:MF_04006, ECO:0000269|PubMed:10523825, ECO:0000269|PubMed:10523853, ECO:0000269|PubMed:8598912, ECO:0000269|PubMed:9326658, ECO:0000269|PubMed:9649509}.
|
Human papillomavirus type 16
|
P03129
|
VE7_HPV16
|
MHGDTPTLHEYMLDLQPETTDLYCYEQLNDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPICSQKP
| null | null |
DNA-templated transcription [GO:0006351]; positive regulation of actin filament polymerization [GO:0030838]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; symbiont-mediated perturbation of host transcription [GO:0052026]; symbiont-mediated suppression of host apoptosis [GO:0033668]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host IRF9 activity [GO:0039560]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral process [GO:0016032]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]
|
cadmium ion binding [GO:0046870]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor binding [GO:0140297]; protein domain specific binding [GO:0019904]; zinc ion binding [GO:0008270]
|
PF00527;
|
3.30.160.330;
|
Papillomaviridae E7 protein family
|
PTM: Highly phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04004, ECO:0000269|PubMed:3033296}.
|
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04004, ECO:0000269|PubMed:18996550, ECO:0000269|PubMed:3033296}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04004, ECO:0000269|PubMed:18996550}. Note=Predominantly found in the host nucleus. {ECO:0000255|HAMAP-Rule:MF_04004, ECO:0000269|PubMed:18996550}.
| null | null | null | null | null |
FUNCTION: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta). {ECO:0000255|HAMAP-Rule:MF_04004, ECO:0000269|PubMed:11080488, ECO:0000269|PubMed:1316611, ECO:0000269|PubMed:2836062}.
|
Human papillomavirus type 16
|
P03132
|
REP68_AAV2S
|
MPGFYEIVIKVPSDLDGHLPGISDSFVNWVAEKEWELPPDSDMDLNLIEQAPLTVAEKLQRDFLTEWRRVSKAPEALFFVQFEKGESYFHMHVLVETTGVKSMVLGRFLSQIREKLIQRIYRGIEPTLPNWFAVTKTRNGAGGGNKVVDECYIPNYLLPKTQPELQWAWTNMEQYLSACLNLTERKRLVAQHLTHVSQTQEQNKENQNPNSDAPVIRSKTSARYMELVGWLVDKGITSEKQWIQEDQASYISFNAASNSRSQIKAALDNAGKIMSLTKTAPDYLVGQQPVEDISSNRIYKILELNGYDPQYAASVFLGWATKKFGKRNTIWLFGPATTGKTNIAEAIAHTVPFYGCVNWTNENFPFNDCVDKMVIWWEEGKMTAKVVESAKAILGGSKVRVDQKCKSSAQIDPTPVIVTSNTNMCAVIDGNSTTFEHQQPLQDRMFKFELTRRLDHDFGKVTKQEVKDFFRWAKDHVVEVEHEFYVKKGGAKKRPAPSDADISEPKRVRESVAQPSTSDAEASINYADRLARGHSL
|
3.6.4.12
|
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|PROSITE-ProRule:PRU01366};
|
DNA replication [GO:0006260]; permeabilization of host organelle membrane involved in viral entry into host cell [GO:0039665]; symbiont entry into host cell via permeabilization of inner membrane [GO:0099008]; symbiont-mediated arrest of host cell cycle during G2/M transition [GO:0039592]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; viral DNA genome replication [GO:0039693]
|
host cell nucleus [GO:0042025]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]
|
PF01057;PF08724;
|
1.10.10.950;3.40.1310.20;3.40.50.300;
| null | null |
SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|PROSITE-ProRule:PRU01366}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
| null | null | null | null |
FUNCTION: Plays an essential role in the initiation of viral DNA synthesis. Binds specifically to an inverted terminal repeat element (ITR) on the 3' and 5' ends of the viral DNA, where it cleaves a site specifically to generate a priming site for initiation of the synthesis of a complementary strand. Also plays a role as transcriptional regulator, DNA helicase and as key factor in site-specific integration of the viral genome. Inhibits the host cell cycle G1/S and G2/M transitions. These arrests may provide essential cellular factors for viral DNA replication. {ECO:0000269|PubMed:9882364}.
|
Adeno-associated virus 2 (isolate Srivastava/1982) (AAV-2)
|
P03134
|
NS1_MUMIP
|
MAGNAYSDEVLGATNWLKEKSNQEVFSFVFKNENVQLNGKDIGWNSYKKELQEDELKSLQRGAETTWDQSEDMEWETTVDEMTKKQVFIFDSLVKKCLFEVLNTKNIFPGDVNWFVQHEWGKDQGWHCHVLIGGKDFSQAQGKWWRRQLNVYWSRWLVTACNVQLTPAERIKLREIAEDNEWVTLLTYKHKQTKKDYTKCVLFGNMIAYYFLTKKKISTSPPRDGGYFLSSDSGWKTNFLKEGERHLVSKLYTDDMRPETVETTVTTAQETKRGRIQTKKEVSIKTTLKELVHKRVTSPEDWMMMQPDSYIEMMAQPGGENLLKNTLEICTLTLARTKTAFDLILEKAETSKLTNFSLPDTRTCRIFAFHGWNYVKVCHAICCVLNRQGGKRNTVLFHGPASTGKSIIAQAIAQAVGNVGCYNAANVNFPFNDCTNKNLIWVEEAGNFGQQVNQFKAICSGQTIRIDQKGKGSKQIEPTPVIMTTNENITVVRIGCEERPEHTQPIRDRMLNIHLTHTLPGDFGLVDKNEWPMICAWLVKNGYQSTMASYCAKWGKVPDWSENWAEPKVPTPINLLGSARSPFTTPKSTPLSQNYALTPLASDLEDLALEPWSTPNTPVAGTAETQNTGEAGSKACQDGQLSPTWSEIEEDLRACFGAEPLKKDFSEPLNLD
|
3.1.21.-; 3.6.4.12
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25528417}; Note=The endonuclease active site can probably bind other divalent cations. {ECO:0000269|PubMed:25528417};
|
DNA replication [GO:0006260]; rolling hairpin viral DNA replication [GO:0039685]; symbiont-mediated arrest of host cell cycle during G2/M transition [GO:0039592]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; symbiont-mediated perturbation of host transcription [GO:0052026]
|
host cell nucleus [GO:0042025]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; helicase activity [GO:0004386]; metal ion binding [GO:0046872]
|
PF12117;PF01057;PF12433;
|
3.40.1310.20;3.40.50.300;
|
Parvoviruses initiator protein NS1 family
|
PTM: Phosphorylated. {ECO:0000269|PubMed:10388664}.
|
SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:D0EZM8}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000269|PubMed:12050365, ECO:0000269|PubMed:1833878};
| null | null | null | null |
FUNCTION: Multifunctional protein which displays endonuclease and helicase activities required for initiating and directing viral DNA replication (PubMed:12050365). Also plays a role in viral packaging and transactivation of several promoters (PubMed:7636987). Binds site-specifically to 2-3 approximate tandem copies of the tetranucleotide 5'TGGT3' within the origins of replication (Ori), unwinds this hairpin region and nicks one DNA strand thereby initiating the rolling circle replication (RCR) (PubMed:12050365, PubMed:17898054, PubMed:9349487). Cooperatively binds Ori with host PIF and probably other host factors, which activate the nickase function of NS1 (PubMed:11435581, PubMed:12050365). Becomes covalently attached to the 5' end of the nick and provides a 3'OH for priming DNA synthesis (PubMed:12050365). The helicase activity unwinds DNA in a 3'-5' direction on the longer strand (PubMed:12050365). Participates in the transcriptional regulation of several promoters including the viral p38 promoter that regulates the expression of VP1 and VP2 transcripts (PubMed:7636987, PubMed:8551622). Inhibits the host cell cycle during the G1/S transition, the S-phase, and the G2/M transition (PubMed:11602746, PubMed:9188601). These arrests may provide essential cellular factors for viral DNA replication. Promotes apoptosis in host cell (PubMed:21295324). {ECO:0000269|PubMed:11435581, ECO:0000269|PubMed:11602746, ECO:0000269|PubMed:12050365, ECO:0000269|PubMed:17898054, ECO:0000269|PubMed:21295324, ECO:0000269|PubMed:7636987, ECO:0000269|PubMed:8551622, ECO:0000269|PubMed:9188601, ECO:0000269|PubMed:9349487}.
|
Murine minute virus (strain MVM prototype) (MVM) (Murine minute virus (strain MVM(p)))
|
P03138
|
HBSAG_HBVD3
|
MGQNLSTSNPLGFFPDHQLDPAFRANTANPDWDFNPNKDTWPDANKVGAGAFGLGFTPPHGGLLGWSPQAQGILQTLPANPPPASTNRQSGRQPTPLSPPLRNTHPQAMQWNSTTFHQTLQDPRVRGLYFPAGGSSSGTVNPVLTTASPLSSIFSRIGDPALNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQSPTSNHSPTSCPPTCPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRTCMTTAQGTSMYPSCCCTKPSDGNCTCIPIPSSWAFGKFLWEWASARFSWLSLLVPFVQWFVGLSPTVWLSVIWMMWYWGPSLYSILSPFLPLLPIFFCLWVYI
| null | null |
caveolin-mediated endocytosis of virus by host cell [GO:0075513]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062]
|
membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF00695;
| null |
Orthohepadnavirus major surface antigen family
|
PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region. {ECO:0000255|HAMAP-Rule:MF_04075, ECO:0000269|PubMed:10207016, ECO:0000269|PubMed:15218190}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04075}.
| null | null | null | null | null |
FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein. {ECO:0000255|HAMAP-Rule:MF_04075}.; FUNCTION: The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid. {ECO:0000255|HAMAP-Rule:MF_04075}.
|
Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)
|
P03139
|
HBSAG_HBVD1
|
MGQNLSTSNPLGFFPDHQLDPAFRANTNNPDWDFNPNKDTWPDANKVGAGAFGLGFTPPHGGLLGWSPQAQGIMQTLPANPPPASTNRQSGRQPTPLSPPLRTTHPQAMHWNSTTFHQTLQDPRVRGLYFPAGGSSSGTVNPVPTTTSPISSIFSRIGDPALNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQSPISNHSPTSCPPTCPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGSCRTCTTPAQGISMYPSCCCTKPSDGNCTCIPIPSSWAFGKFLWEWASARFSWLSLLVPFVQWFVGLSPIVWLSVIWMMWYWGPSLYSILSPFLPLLPIFFCLWAYI
| null | null |
caveolin-mediated endocytosis of virus by host cell [GO:0075513]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062]
|
membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF00695;
| null |
Orthohepadnavirus major surface antigen family
|
PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region. {ECO:0000250|UniProtKB:P03138, ECO:0000255|HAMAP-Rule:MF_04075}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04075}.
| null | null | null | null | null |
FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein. {ECO:0000255|HAMAP-Rule:MF_04075}.; FUNCTION: The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid. {ECO:0000255|HAMAP-Rule:MF_04075}.
|
Hepatitis B virus genotype D subtype adw (isolate United Kingdom/adyw/1979) (HBV-D)
|
P03140
|
HBSAG_HBVC5
|
MGGWSSKPRQGMGTNLSVPNPLGFFPDHQLDPAFGANSNNPDWDFNPNKDQWPEANQVGAGAFGPGFTPPHGGLLGWSPQAQGILTTVPAAPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTTFHQALLDPRVRGLYFPAGGSSSGTVNPVPTTASPISSIFSRTGDPAPNMENTTSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGAPTCPGQNSQSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLLPGTSTTSTGPCKTCTIPAQGTSMFPSCCCTKPSDGNCTCIPIPSSWAFARFLWEWASVRFSWLSLLVPFVQWFVGLSPTVWLSVIWMMWYWGPSLYNILSPFLPLLPIFFCLWVYI
| null | null |
caveolin-mediated endocytosis of virus by host cell [GO:0075513]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062]
|
membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF00695;
| null |
Orthohepadnavirus major surface antigen family
|
PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region. {ECO:0000250|UniProtKB:P03138, ECO:0000255|HAMAP-Rule:MF_04075}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04075}.
| null | null | null | null | null |
FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein. {ECO:0000255|HAMAP-Rule:MF_04075}.; FUNCTION: The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid. {ECO:0000255|HAMAP-Rule:MF_04075}.
|
Hepatitis B virus genotype C subtype ad (isolate Japan/S-179/1988) (HBV-C)
|
P03141
|
HBSAG_HBVA3
|
MGGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPAFGANSNNPDWDFNPVKDDWPAANQVGVGAFGPRLTPPHGGILGWSPQAQGILTTVSTIPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTAFHQTLQDPRVRGLYLPAGGSSSGTVNPAPNIASHISSISARTGDPVTNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGSPVCLGQNSQSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSTTTSTGPCKTCTTPAQGNSMFPSCCCTKPTDGNCTCIPIPSSWAFAKYLWEWASVRFSWLSLLVPFVQWFVGLSPTVWLSAIWMMWYWGPSLYSIVSPFIPLLPIFFCLWVYI
| null | null |
caveolin-mediated endocytosis of virus by host cell [GO:0075513]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062]
|
membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF00695;
| null |
Orthohepadnavirus major surface antigen family
|
PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region. {ECO:0000250|UniProtKB:P03138, ECO:0000255|HAMAP-Rule:MF_04075}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075, ECO:0000269|PubMed:11350599}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04075}.
| null | null | null | null | null |
FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein. {ECO:0000255|HAMAP-Rule:MF_04075}.; FUNCTION: The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid. {ECO:0000255|HAMAP-Rule:MF_04075}.
|
Hepatitis B virus genotype A2 subtype adw2 (strain Rutter 1979) (HBV-A)
|
P03142
|
HBSAG_HBVA2
|
MGTNLSVPNPLGFLPDHQLDPAFGANSTNPDWDFNPIKDHWPAANQVGVGAFGPGLTPPHGGILGWSPQAQGILTTVSTIPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTALHQALQDPRVRGLYLPAGGSSSGTVNPAPNIASHISSISARTGDPVTIMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGSPVCLGQNSQSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSTTTSTGPCKTCTTPAQGNSKFPSCCCTKPTDGNCTCIPIPSSWAFAKYLWEWASVRFSWLSLLVPFVQWFVGLSPTVWLSAIWMMWYWGPSLYSIVSPFIPLLPIFFCLWVYI
| null | null |
caveolin-mediated endocytosis of virus by host cell [GO:0075513]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062]
|
membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF00695;
| null |
Orthohepadnavirus major surface antigen family
|
PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region. {ECO:0000250|UniProtKB:P03138, ECO:0000255|HAMAP-Rule:MF_04075}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04075}.
| null | null | null | null | null |
FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein. {ECO:0000255|HAMAP-Rule:MF_04075}.; FUNCTION: The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid. {ECO:0000255|HAMAP-Rule:MF_04075}.
|
Hepatitis B virus genotype A2 subtype adw (isolate Japan/Nishioka/1983) (HBV-A)
|
P03145
|
HBSAG_DHBV1
|
MGQHPAKSMDVRRIEGGEILLNQLAGRMIPKGTLTWSGKFPTLDHVLDHVQTMEEINTLQNQGAWPAGAGRRVGLSNPTPQEIPQPQWTPEEDQKAREAFRRYQEERPPETTTIPPSSPPQWKLQPGDDPLLGNQSLLETHPLYQSEPAVPVIKTPPLKKKMSGTFGGILAGLIGLLVSFFLLIKILEILRRLDWWWISLSSPKGKMQCAFQDTGAQISPHYVGSCPWGCPGFLWTYLRLFIIFLLILLVAAGLLYLTDNGSTILGKLQWASVSALFSSISSLLPSDPKSLVALTFGLSLIWMTSSSATQTLVTLTQLATLSALFYKS
| null | null |
membrane fusion involved in viral entry into host cell [GO:0039663]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062]
|
membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF00695;
| null |
Avihepadnavirus major surface antigen family
|
PTM: Myristoylation contributes importantly to DHBV infectivity. It is most likely required for an early step of the life cycle involving the entry or uncoating of virus particles. {ECO:0000269|PubMed:1994583}.; PTM: Phosphorylated on pre-S domain for about 50% of L proteins, the L chains with internal pre-S region (Li-HBsAg). {ECO:0000269|PubMed:7933117, ECO:0000269|PubMed:9820150}.; PTM: Isoform S may be cleaved by a cellular protease to produce truncated S protein.
|
SUBCELLULAR LOCATION: Virion membrane.
| null | null | null | null | null |
FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. The large envelope protein probably also assumes fusion between virion and host membranes. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein (By similarity). {ECO:0000250}.; FUNCTION: Truncated S protein may be involved in translocation of pre-S domain through the virion membrane.
|
Duck hepatitis B virus (strain United States/DHBV-16) (DHBV)
|
P03146
|
CAPSD_HBVD3
|
MDIDPYKEFGATVELLSFLPSDFFPSVRDLLDTASALYREALESPEHCSPHHTALRQAILCWGELMTLATWVGVNLEDPASRDLVVSYVNTNMGLKFRQLLWFHISCLTFGRETVIEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC
| null | null |
microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732]
|
host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; T=4 icosahedral viral capsid [GO:0039619]
|
DNA binding [GO:0003677]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198]
|
PF00906;
|
1.10.4090.10;
|
Orthohepadnavirus core antigen family
|
PTM: Phosphorylated by host SRPK1, SRPK2, and maybe protein kinase C or GAPDH. Phosphorylation is critical for pregenomic RNA packaging. Protein kinase C phosphorylation is stimulated by HBx protein and may play a role in transport of the viral genome to the nucleus at the late step during the viral replication cycle. {ECO:0000255|HAMAP-Rule:MF_04076}.
|
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04076}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04076}.
| null | null | null | null | null |
FUNCTION: Self assembles to form an icosahedral capsid. Most capsids appear to be large particles with an icosahedral symmetry of T=4 and consist of 240 copies of capsid protein, though a fraction forms smaller T=3 particles consisting of 180 capsid proteins. Entering capsids are transported along microtubules to the nucleus. Phosphorylation of the capsid is thought to induce exposure of nuclear localization signal in the C-terminal portion of the capsid protein that allows binding to the nuclear pore complex via the importin (karyopherin-) alpha and beta. Capsids are imported in intact form through the nuclear pore into the nuclear basket, where it probably binds NUP153. Only capsids that contain the mature viral genome can release the viral DNA and capsid protein into the nucleoplasm. Immature capsids get stuck in the basket. Capsids encapsulate the pre-genomic RNA and the P protein. Pre-genomic RNA is reverse-transcribed into DNA while the capsid is still in the cytoplasm. The capsid can then either be directed to the nucleus, providing more genomes for transcription, or bud through the endoplasmic reticulum to provide new virions. {ECO:0000255|HAMAP-Rule:MF_04076}.
|
Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)
|
P03148
|
CAPSD_HBVA3
|
MDIDPYKEFGATVELLSFLPSDFFPSVRDLLDTASALYREALESPEHCSPHHTALRQAILCWGELMTLATWVGNNLEDPASRDLVVNYVNTNVGLKIRQLLWFHISCLTFGRETVLEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRDRGRSPRRRTPSPRRRRSPSPRRRRSQSRESQC
| null | null |
microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732]
|
host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; T=4 icosahedral viral capsid [GO:0039619]
|
DNA binding [GO:0003677]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198]
|
PF00906;
|
1.10.4090.10;
|
Orthohepadnavirus core antigen family
|
PTM: Phosphorylated by host SRPK1, SRPK2, and maybe protein kinase C or GAPDH. Phosphorylation is critical for pregenomic RNA packaging. Protein kinase C phosphorylation is stimulated by HBx protein and may play a role in transport of the viral genome to the nucleus at the late step during the viral replication cycle. {ECO:0000255|HAMAP-Rule:MF_04076, ECO:0000269|PubMed:7815479, ECO:0000269|PubMed:9680129}.
|
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04076, ECO:0000269|PubMed:3006057}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04076, ECO:0000269|PubMed:3006057}.
| null | null | null | null | null |
FUNCTION: Self assembles to form an icosahedral capsid. Most capsids appear to be large particles with an icosahedral symmetry of T=4 and consist of 240 copies of capsid protein, though a fraction forms smaller T=3 particles consisting of 180 capsid proteins. Entering capsids are transported along microtubules to the nucleus. Phosphorylation of the capsid is thought to induce exposure of nuclear localization signal in the C-terminal portion of the capsid protein that allows binding to the nuclear pore complex via the importin (karyopherin-) alpha and beta. Capsids are imported in intact form through the nuclear pore into the nuclear basket, where it probably binds NUP153. Only capsids that contain the mature viral genome can release the viral DNA and capsid protein into the nucleoplasm. Immature capsids get stuck in the basket. Capsids encapsulate the pre-genomic RNA and the P protein. Pre-genomic RNA is reverse-transcribed into DNA while the capsid is still in the cytoplasm. The capsid can then either be directed to the nucleus, providing more genomes for transcription, or bud through the endoplasmic reticulum to provide new virions. {ECO:0000255|HAMAP-Rule:MF_04076}.
|
Hepatitis B virus genotype A2 subtype adw2 (strain Rutter 1979) (HBV-A)
|
P03153
|
HBEAG_GSHV
|
MYLFHLCLVFACVPCPTVQASKLCLGWLWDMDIDPYKEFGSSYQLLNFLPLDFFPDLNALVDTAAALYEEELTGREHCSPHHTAIRQALVCWEELTRLITWMSENTTEEVRRIIVDHVNNTWGLKVRQTLWFHLSCLTFGQHTVQEFLVSFGVWIRTPAPYRPPNAPILSTLPEHTVIRRRGGSRAARSPRRRTPSPRRRRSQSPRRRRSQSPASNC
| null | null |
microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732]; virus-mediated perturbation of host defense response [GO:0019049]
|
extracellular region [GO:0005576]; host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; T=4 icosahedral viral capsid [GO:0039619]
|
DNA binding [GO:0003677]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198]
|
PF08290;PF00906;
|
1.10.4090.10;
|
Orthohepadnavirus precore antigen family
|
PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04076}.; PTM: Cleaved by host furin. {ECO:0000255|HAMAP-Rule:MF_04076}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_04076}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04076}.
| null | null | null | null | null |
FUNCTION: May regulate immune response to the intracellular capsid in acting as a T-cell tolerogen, by having an immunoregulatory effect which prevents destruction of infected cells by cytotoxic T-cells. This immune regulation may predispose to chronicity during perinatal infections and prevent severe liver injury during adult infections. {ECO:0000255|HAMAP-Rule:MF_04076}.
|
Ground squirrel hepatitis virus (strain 27) (GSHV)
|
P03155
|
DPOL_HBVD1
|
MPLSYQRFRRLLLLDDEAGPLEEELPRLADEDLNRRVAEDLNLGNLNVSIPWTHKVGNFTGLYSSTVPVFNPHWKPPSFPNIHLHQDIIKKCEQFVGPLTVNEKRRLKLIMPARFYPNFTKYLPLDKGIKPYYPEHLVNHYFQTRHYLHTLWKAGVLYKRVSTHSASFCGSPYSWEQELQHGAESFHQQSSGILSRPPVGSSLQSKHQQSRLGLQSQQGHLARRQQGRSWSIRARVHPTARRPFGVEPSGSGHNANLASKSASCLYQSPVRTAAYPAVSTSENHSSSGHALELHNLPPNSARSQSERPVFPCWWLQFRDSKPCSDYYLSHIVNLLEDWGPCAEHGEHHIRIPRTPARVTGGVFLVDKNPHNTAESRLVVDFSQFSRGNYRVSWPKFAVPNLQSLTNLLSSNLSWLSLDVSAAFYHLPLHPAAMPHLLVGSSGLSRYVARLSSNSRIINHQHGILQNLHDSCSRNLYVSLLLLYKTFGWKLHLYSHPIILGFRKIPMGVGLSPFLLAQFTSAICSVVRRAFPHCLAFSYMDDVVLGAKSVQHLESLFTAVTNFLLSLGIHLNPNKTKRWGYSLNFMGYVIGCWGSLPQDHIIHKIKECFRKLPVHRPIDWKVCQRIVGLLGFAAPFTQCGYPALMPLYACIQSKQAFTFSPTYKAFLCKQYLNLYPVAEQRPGLCQVFADATPTGWGLVMGHQRMRGTFLAPLPIHTAELLAACFARSRSGANILGTDNSVVLSRKYTSFP
|
2.7.7.49; 2.7.7.7; 3.1.26.4
| null |
DNA replication [GO:0006260]
| null |
DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]
|
PF00336;PF00242;PF00078;
|
3.30.70.270;3.10.10.10;
|
Hepadnaviridae P protein family
| null | null |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
| null | null | null | null |
FUNCTION: Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery (By similarity). {ECO:0000250, ECO:0000269|PubMed:1380455, ECO:0000269|PubMed:2854056}.
|
Hepatitis B virus genotype D subtype adw (isolate United Kingdom/adyw/1979) (HBV-D)
|
P03156
|
DPOL_HBVD3
|
MPLSYQHFRRLLLLDDEAGPLEEELPRLADEGLNRRVAEDLNLGNLNVSIPWTHKVGNFTGLYSSTVPVFNPHWKTPSFPNIHLHQDIIKKCEQFVGPLTVNEKRRLQLIMPARFYPKVTKYLPLDKGIKPYYPEHLVNHYFQTRHYLHTLWKAGILYKRETTHSASFCGSPYSWEQDLQHGAESFHQQSSGILSRPPVGSSLQSKHRKSRLGLQSQQGHLARRQQGRSWSIRAGFHPTARRPFGVEPSGSGHTTNFASKSASCLHQSPVRKAAYPAVSTFEKHSSSGHAVEFHNLPPNSARSQSERPVFPCWWLQFRNSKPCSDYCLSLIVNLLEDWGPCAEHGEHHIRIPRTPSRVTGGVFLVDKNPHNTAESRLVVDFSQFSRGNYRVSWPKFAVPNLQSLTNLLSSNLSWLSLDVSAAFYHLPLHPAAMPHLLVGSSGLSRYVARLSSNSRILNNQHGTMPDLHDYCSRNLYVSLLLLYQTFGRKLHLYSHPIILGFRKIPMGVGLSPFLLAQFTSAICSVVRRAFPHCLAFSYMDDVVLGAKSVQHLESLFTAVTNFLLSLGIHLNPNKTKRWGYSLNFMGYVIGCYGSLPQEHIIQKIKECFRKLPINRPIDWKVCQRIVGLLGFAAPFTQCGYPALMPLYACIQSKQAFTFSPTYKAFLCKQYLNLYPVARQRPGLCQVFADATPTGWGLVMGHQRMRGTFSAPLPIHTAELLAACFARSRSGANIIGTDNSVVLSRKYTSFPWLLGCAANWILRGTSFVYVPSALNPADDPSRGRLGLSRPLLRLPFRPTTGRTSLYADSPSVPSHLPDRVHFASPLHVAWRPP
|
2.7.7.49; 2.7.7.7; 3.1.26.4
| null |
DNA replication [GO:0006260]; virus-mediated perturbation of host defense response [GO:0019049]
| null |
DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]
|
PF00336;PF00242;PF00078;
|
3.30.70.270;
|
Hepadnaviridae P protein family
| null | null |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|HAMAP-Rule:MF_04073}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|HAMAP-Rule:MF_04073}; CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|HAMAP-Rule:MF_04073};
| null | null | null | null |
FUNCTION: Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery. {ECO:0000255|HAMAP-Rule:MF_04073}.
|
Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)
|
P03162
|
DPOL_DHBV1
|
MQKLTRNHWIGLGDCFGGITTVYCGEKLKLLTIFLVCVLGCQLLRNIEVEMPRPLKQSLDQSRWLREAEKQLRVLENLVDSNLEEEKLKPQLSMGEDVQSPGKGEPLHPNVRAPLSHVVRAATIDLPRLGNKLPARHHLGKLSGLYQMKGCTFNPEWKVPDISDTHFNLDVVNECPSRNWKYLTPAKFWPKSISYFPVQVGVKPKYPDNVMQHESIVGKYLTRLYEAGILYKRISKHLVTFKGQPYNWEQQHLVNQHHIYDGATSSKINGRQTDRRRRNTVKPTCRKDDPKRDFDMVRQVSNTRSRVRPCANNGGDKHPPESGSLACWGGKESRIIKSDSSRDSSAPVDSRGRPKSTRSFSPLSRRKTTGNHHHSSVFPSSVEATTRGRSTPGKSVSPRDSSAIPVRTSGASDKNSPLEEENVWYLRGNTSWPNRITGKLFLVDKNSRNTEEARLVVDFSQFSKGKNAMRFPRYWSPNLSTLRRILPVGMPRISLDLSQAFYHLPLNPASSSRLAVSDGQRVYYFRKAPMGVGLSPFLLHLFTTALGSEISRRFNVWTFTYMDDFLLCHPNARHLNAISHAVCSFLQELGIRINFDKTTPSPVNEIRFLGYQIDENFMKIEESRWKELRTVIKKIKVGEWYDWKCIQRFVGHLNFVLPFTKGNIEMLKPMYAAITNQVNFSFSSSYRTLLYKLTMGVCKLRIKPKSSVPLPRVATDATPTHGAISHITGGSAVFAFSKVRDIHVQELLMSCLAKIMIKPRCLLSDSTFVCHKRYQTLPWHFAMLAKQLLKPIQLYFVPSKYNPADGPSRHKPPDWTAFPYTPLSKAIYIPHRLCGT
|
2.7.7.49; 2.7.7.7; 3.1.26.4
| null |
DNA replication [GO:0006260]; reverse transcription [GO:0001171]
| null |
DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]
|
PF00336;PF00242;PF00078;
|
3.30.70.270;3.10.10.10;
|
Hepadnaviridae P protein family
| null | null |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
| null | null | null | null |
FUNCTION: Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery (By similarity). {ECO:0000250}.
|
Duck hepatitis B virus (strain United States/DHBV-16) (DHBV)
|
P03165
|
X_HBVD3
|
MAARLCCQLDPARDVLCLRPVGAESRGRPFSGSLGTLSSPSPSAVPTDHGAHLSLRGLPVCAFSSAGPCALRFTSARRMETTVNAHQILPKVLHKRTLGLSAMSTTDLEAYFKDCLFKDWEELGEEIRLKVFVLGGCRHKLVCAPAPCNFFTSA
| null | null |
DNA-templated transcription [GO:0006351]; symbiont-mediated arrest of host cell cycle during G2/M transition [GO:0039592]; viral genome replication [GO:0019079]
|
host cell mitochondrion [GO:0033650]; host cell nucleus [GO:0042025]
| null |
PF00739;
| null |
Orthohepadnavirus protein X family
|
PTM: A fraction may be phosphorylated in insect cells and HepG2 cells, a human hepatoblastoma cell line. Phosphorylated in vitro by host protein kinase C or mitogen-activated protein kinase. N-acetylated in insect cells. {ECO:0000255|HAMAP-Rule:MF_04074}.
|
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04074}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04074}. Host mitochondrion {ECO:0000255|HAMAP-Rule:MF_04074}. Note=Mainly cytoplasmic as only a fraction is detected in the nucleus. In cytoplasm, a minor fraction associates with mitochondria or proteasomes. {ECO:0000255|HAMAP-Rule:MF_04074}.
| null | null | null | null | null |
FUNCTION: Multifunctional protein that plays a role in silencing host antiviral defenses and promoting viral transcription. Does not seem to be essential for HBV infection. May be directly involved in development of cirrhosis and liver cancer (hepatocellular carcinoma). Most of cytosolic activities involve modulation of cytosolic calcium. The effect on apoptosis is controversial depending on the cell types in which the studies have been conducted. May induce apoptosis by localizing in mitochondria and causing loss of mitochondrial membrane potential. May also modulate apoptosis by binding host CFLAR, a key regulator of the death-inducing signaling complex (DISC). Promotes viral transcription by using the host E3 ubiquitin ligase DDB1 to target the SMC5-SMC6 complex to proteasomal degradation. This host complex would otherwise bind to viral episomal DNA, and prevents its transcription. Moderately stimulates transcription of many different viral and cellular transcription elements. Promoters and enhancers stimulated by HBx contain DNA binding sites for NF-kappa-B, AP-1, AP-2, c-EBP, ATF/CREB, or the calcium-activated factor NF-AT. {ECO:0000255|HAMAP-Rule:MF_04074, ECO:0000269|PubMed:15767425}.
|
Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)
|
P03169
|
VIE1_HCMVT
|
MESSAKRKMDPDNPDEGPSSKVPRPETPVTKATTFLQTMLRKEVNSQLSLGDPLFPELAEESLKTFERVTEDCNENPEKDVLAELVKQIKVRVDMVRHRIKEHMLKKYTQTEEKFTGAFNMMGGCLQNALDILDKVHEPFEEMKCIGLTMQSMYENYIVPEDKREMWMACIKELHDVSKGAANKLGGALQAKARAKKDELRRKMMYMCYRNIEFFTKNSAFPKTTNGCSQAMAALQNLPQCSPDEIMAYAQKIFKILDEERDKVLTHIDHIFMDILTTCVETMCNEYKVTSDACMMTMYGGISLLSEFCRVLSCYVLEETSVMLAKRPLITKPEVISVMKRRIEEICMKVFAQYILGADPLRVCSPSVDDLRAIAEESDEEEAIVAYTLATRGASSSDSLVSPPESPVPATIPLSSVIVAENSDQEESEQSDEEEEEGAQEEREDTVSVKSEPVSEIEEVAPEEEEDGAEEPTASGGKSTHPMVTRSKADQ
| null | null |
DNA-templated viral transcription [GO:0039695]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell nucleus [GO:0042025]
| null |
PF07340;
| null |
HHV-5 IE1 protein family
|
PTM: Sumoylated by host PML/nuclear domain 10 (By similarity). Sumoylation abolishes the interaction with host STAT2 and thus the IE1-mediated repression of interferon-stimulated genes (PubMed:18701593). {ECO:0000250|UniProtKB:P13202, ECO:0000269|PubMed:18701593}.
|
SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:15220454, ECO:0000269|PubMed:16497831, ECO:0000269|PubMed:28750047, ECO:0000269|PubMed:9151854}. Note=Colocalizes with host PML-associated nuclear bodies very early post infection. {ECO:0000269|PubMed:15220454, ECO:0000269|PubMed:9151854}.
| null | null | null | null | null |
FUNCTION: Plays an important role in transactivating viral early genes as well as activating its own promoter, probably by altering the viral chromatin structure (PubMed:15572445, PubMed:17331553, PubMed:23878222, PubMed:26812545, PubMed:35138119, PubMed:8876134). Expression of IE1 and IE2 proteins is critical for the establishment of lytic infection and reactivation from viral latency (By similarity). Disrupts PML-associated ND10 nuclear bodies by interfering with host PML and SP100 sumoylation thereby altering the regulation of type I and type II interferon-induced gene expression (PubMed:10233977, PubMed:15163746, PubMed:17367754, PubMed:9151854). Promotes efficient viral growth by interacting with and directing host SP100 to degradation, leading to enhanced acetylation level of histones (PubMed:21880768). In addition, functions in counteracting the host innate antiviral response. Inhibits the type I interferon pathway by directly interacting with and sequestrating host STAT2 (PubMed:16497831, PubMed:18701593, PubMed:19812155). Also targets type II interferon pathway by repressing IL6- and STAT3 target genes (PubMed:27387064). Repression of STAT3 genes is due to STAT3 nuclear accumulation and disruption of IL6-induced STAT3 phosphorylation by IE1 (By similarity). This repression is followed by phosphorylation and activation of STAT1 (PubMed:27387064). Inhibits host ISG transcription by sequestering host ISGF3 in a PML- and STAT2- binding dependent manner (PubMed:25812002). Alters host cell cycle progression, probably through its interaction with host E2F1 or RB1 that overcomes the RB1-mediated repression of E2F-responsive promoters (PubMed:8892909). May act as a E3 ubiquitin ligase targeting several host proteins including HES1 and SP100A for ubiquitination and subsequent proteasomal degradation (PubMed:28750047). Impairs the radial migration of immature neurons by downregulating Gap junction alpha-1 protein/GJA1 also via ubiquitination and degradation (PubMed:37097169). {ECO:0000250|UniProtKB:P13202, ECO:0000269|PubMed:10233977, ECO:0000269|PubMed:15163746, ECO:0000269|PubMed:15572445, ECO:0000269|PubMed:16497831, ECO:0000269|PubMed:17331553, ECO:0000269|PubMed:17367754, ECO:0000269|PubMed:18701593, ECO:0000269|PubMed:19812155, ECO:0000269|PubMed:21880768, ECO:0000269|PubMed:23878222, ECO:0000269|PubMed:25812002, ECO:0000269|PubMed:26812545, ECO:0000269|PubMed:27387064, ECO:0000269|PubMed:28750047, ECO:0000269|PubMed:35138119, ECO:0000269|PubMed:37097169, ECO:0000269|PubMed:8876134, ECO:0000269|PubMed:8892909, ECO:0000269|PubMed:9151854}.
|
Human cytomegalovirus (strain Towne) (HHV-5) (Human herpesvirus 5)
|
P03170
|
ICP47_HHV11
|
MSWALEMADTFLDTMRVGPRTYADVRDEINKRGREDREAARTAVHDPERPLLRSPGLLPEIAPNASLGVAHRRTGGTVTDSPRNPVTR
| null | null |
symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; virus-mediated perturbation of host defense response [GO:0019049]
|
endoplasmic reticulum membrane [GO:0005789]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]
|
molecular sequestering activity [GO:0140313]
|
PF05363;
| null |
Herpesviridae US12 family
| null |
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:8187174}. Host nucleus {ECO:0000269|PubMed:8187174}.
| null | null | null | null | null |
FUNCTION: Plays a role in the inhibition of host immune response. Binds specifically to transporters associated with antigen processing (TAP), thereby blocking peptide-binding and translocation by TAP as well as subsequent loading of peptides onto MHC class I molecules. Empty MHC I molecules are retained in the endoplasmic reticulum and ultimately directed to proteasomal degradation. In consequence, infected cells are masked for immune recognition by cytotoxic T-lymphocytes. {ECO:0000269|PubMed:11254939, ECO:0000269|PubMed:7760936, ECO:0000269|PubMed:8187174, ECO:0000269|PubMed:8670825}.
|
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
|
P03172
|
GD_HHV23
|
MGRLTSGVGTAALLVVAVGLRVVCAKYALADPSLKMADPNRFRGKNLPVLDRLTDPPGVKRVYHIQPSLEDPFQPPSIPITVYYAVLERACRSVLLHAPSEAPQIVRGASDEARKHTYNLTIAWYRMGDNCAIPITVMEYTECPYNKSLGVCPIRTQPRWSYYDSFSAVSEDNLGFLMHAPAFETAGTYLRLVKINDWTEITQFILEHRARASCKYALPLRIPPAACLTSKAYQQGVTVDSIGMLPRFIPENQRTVALYSLKIAGWHGPKPPYTSTLLPPELSDTTNATQPELVPEDPEDSALLEDPAGTVSSQIPPNWHIPSIQDVAPHHAPAAPSNPGLIIGALAGSTLAVLVIGGIAFWVRRRAQMAPKRLRLPHIRDDDAPPSHQPLFY
| null | null |
coreceptor-mediated virion attachment to host cell [GO:0046814]; entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]
|
membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
metal ion binding [GO:0046872]
|
PF01537;
|
2.70.230.10;
|
Herpesviridae glycoprotein D family
| null |
SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Envelope glycoprotein that binds to the potential host cell entry receptors TNFRSF14/HVEM and NECTIN1. May trigger fusion with host membrane, by recruiting the fusion machinery composed of gB and gH/gL (By similarity). {ECO:0000250}.
|
Human herpesvirus 2 (strain 333) (HHV-2) (Human herpes simplex virus 2)
|
P03186
|
LTP_EBVB9
|
MSNGDWGQSQRTRGTGPVRGIRTMDVNAPGGGSGGSALRILGTASCNQAHCKFGRFAGIQCVSNCVLYLVKSFLAGRPLTSRPELDEVLDEGARLDALMRQSGILKGHEMAQLTDVPSSVVLRGGGRVHIYRSAEIFGLVLFPAQIANSAVVQSLAEVLHGSYNGVAQFILYICDIYAGAIIIETDGSFYLFDPHCQKDAAPGTPAHVRVSTYAHDILQYVGAPGAQYTCVHLYFLPEAFETEDPRIFMLEHYGVYDFYEANGSGFDLVGPELVSSDGEAAGTPGADSSPPVMLPFERRIIPYNLRPLPSRSFTSDSFPAARYSPAKTNSPPSSPASAAPASAAPASAAPASAAPASAAPASAAPASAAPASAAPASSPPLFIPIPGLGHTPGVPAPSTPPRASSGAAPQTPKRKKGLGKDSPHKKPTSGRRLPLSSTTDTEDDQLPRTHVPPHRPPSAARLPPPVIPIPHQSPPASPTPHPAPVSTIAPSVTPSPRLPLQIPIPLPQAAPSNPKIPLTTPSPSPTAAAAPTTTTLSPPPTQQQPPQSAAPAPSPLLPQQQPTPSAAPAPSPLLPQQQPPPSAARAPSPLPPQQQPLPSATPAPPPAQQLPPSATTLEPEKNHPPAADRAGTEISPSPPFGQQPSFGDDASGGSGLVRYLSDLEEPFLSMSDSEEAESDLASDIPTTEDEDMFEDEVFSNSLESGSSAPTSPITLDTARSQYYQTTFDIETPEMDFVPLESNIARIAGHTYQEQAIVYDPASNREVPEADALSMIDYLLVTVVLEQGLIRSRDRSSVLNLLEFLKDWSGHLQVPTLDLEQLLTSELNIQNLANMLSENKGRAGEFHKHLAAKLEACLPSLATKDAVRVDAGAKMLAEIPQLAESDDGKFDLEAARRRLTDLLSGGDQEAGEGGGEPEDNSIYRGPHVDVPLVLDDESWKRLLSLAEAARTAVARQQAGVDEEDVRFLALLTAIEYGAPPAASVPPFVHNVAVRSKNAALHVRRCTADIRDKVASAASDYLSYLEDPSLPTVMDFDDLLTHLRHTCQIIASLPLLNIRYTSIEWDYRELLYLGTALSDMSGIPWPLERVEEDDPSIAPLPEFETVAKKQKELETTRENEKRLRTILDDIEAMLGLAGVASAPGAPISPASPSATPANHDNPEATPPLADTAALTIPVIEKYIANAGSIVGAAKNPTYIRLRDTIQQIVRSKKYLMNILKSITFYTIDNYIASFEESIDHLYRDLPVLDPEVQDGIDRILDPMVSEALHTFEMGNRLTLEPARLVALQNFATHSTLKETAAAVNLLPGLLAVYDATITGQAPEDALRLLSGLQNQLSQTLIPGKLKKRFLSYLQKLKNNNNDQLRQKEVQAWRLEAEGFKPATEEQLEAFLDTAPNKELKRQYEKKLRQLMETGRKEKEKLREQEDKERQERRAREANEAWARIRKALGARPEPAPTSPDDWNTLLASLLPDNTDSAAAAAAAVARNTDILDSLTQILAAMLLGITRVRRERLRSLLVDDGGAAERMEAAEPGWFTDIETGPLARLDAWPATPAATAKEGGGGRGAEEAAGALFRARTAADAIRSALAQTRQALQSPDMKSAVVNTDLEAPYAEYERGLAGLLEKRRAAEAALTAIVSEYVDRTLPEATNDPGQANLPPPPTIPQATAPPRLASDSALWPKKPQLLTRRERDDLLQATGDFFSELLTEAEAAEVRALEEQVRESQTLMAKAHEMAASTRRGFHTALEAVLSRSRDEAPDDELRSLLPSPPKAPVQAPLEAALARAAAGNGSWPYRKSLAAAKWIRGICEAVRGLSEGALALAGGAGAWLNLAAAADGEIHELTRLLEVEGMAQNSMDGMEELRLALATLDPKRVAGGKETVADWKRRLSRLEAIIQEAQEESQLQGTLQDLVTQARGHTDPRQLKIVVEAARGLALGASAGSQYALLKDKLLRYASAKQSFLAFYETAQPTVFVKHPLTNNLPLLITISAPPTGWGNGAPTRRAQFLAAAGPAKYAGTLWLETESPCDPLNPAYVSADTQEPLNYIPVYHNFLEYVMPTVLENPEAFSLTPAGRPQAIGPPQDDQERRRRTLASVASARLSAAAADSYWDTWPDVESNAGELLREYVSAPKALMEDLADNPIVAMTLLAHASLIASRNHPPYPAPATDREVILLEQREMMALLVGTHPAYAAAFLGAPSFYAGLGLVSALARDGGLGDLLSDSVLTYRLVRSPASGRGGMPSTTRGSNDGEDARRLTRHRIAGPPTGFIFFQDAWEEMDTRAALWPHPEFLGLVHNQSTARARACMLLLARRCFAPEALQQLWHSLRPLEGPVAFQDYLRDFVKQAYTRGEELPRAEGLEVPRETPSSYGTVTGRALRNLMPYGTPITGPKRGSGDTIPVSVFEAAVAAAFLGRPLTLFVSSQYLFNLKTLGQVRVVAPLLYCDGHSEPFRSLVETISLNFLQDLDGYSESFEPEMSIFARQAVWLRELLTEARAAKPKEARPPTVAILANRKNIIWKCFTYRHNLPDVQFYFNAAGASRWPTDVLNPSFYEHEDPPLPVGYQLPPNPRNVQELFSGFPPRVGHGLVSGDGFQSADNTPASSDRLQQLGGGETDQGEKGSTTAESEASGPPSPQSPLLEKVAPGRPRDWLSPTSSPRDVTVTPGLAAPITLPGPRLMARPYFGAETRASESPDRSPGSSPRPWPKDSLELLPQPAPQQPPSSPWASEQGPIVYTLSPHSTPSTASGSQKKHTIQIPGLVPSQKPSYPPSAPYKPGQSTGGIAPTPSAASLTTFGLQPQDTQASSQDPPYGHSIMQREKKQQGGREEAAEIRPSATRLPTAVGLRPRAPVVAAGAAASATPAFDPGEAPSGFPIPQAPALGSGLAAPAHTPVGALAPRPQKTQAQRPQDAAALPTPTIKAVGARPVPKATGALAAGARPRGQPTAAPPSAASPPRVSLPVRSRQQQSPAIPLPPMHSGSEPGARPEVRLSQYRHAGPQTYTVRKEAPPSAASQLPKMPKCKDSMYYPPSGSARYPAPFQALSFSQSVASPAPSSDQTTLLWNTPSVVTQFLSIEDIIREVVTGGSTSGDLVVPSGSPSSLSTAAPEQDLRYSLTLSQASRVLSRFVSQLRRKLERSTHRLIADLERLKFLYL
|
3.4.19.12; 3.4.22.-
| null |
proteolysis [GO:0006508]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]
|
host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; viral tegument [GO:0019033]
|
cysteine-type deubiquitinase activity [GO:0004843]
|
PF04843;
|
3.90.70.120;
|
Herpesviridae large tegument protein family
| null |
SUBCELLULAR LOCATION: Virion tegument {ECO:0000255|HAMAP-Rule:MF_04044, ECO:0000269|PubMed:15534216}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04044, ECO:0000269|PubMed:15534216, ECO:0000269|PubMed:24586164, ECO:0000269|PubMed:29357390, ECO:0000269|PubMed:31710640, ECO:0000269|PubMed:34543352}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04044, ECO:0000269|PubMed:34543352}. Note=Tightly associated with the capsid. {ECO:0000255|HAMAP-Rule:MF_04044}.
|
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000255|HAMAP-Rule:MF_04044, ECO:0000269|PubMed:20190741, ECO:0000269|PubMed:24586164, ECO:0000269|PubMed:33509017};
| null | null | null | null |
FUNCTION: Large tegument protein that plays multiple roles in the viral cycle. During viral entry, remains associated with the capsid while most of the tegument is detached and participates in the capsid transport toward the host nucleus. Plays a role in the routing of the capsid at the nuclear pore complex and subsequent uncoating. Within the host nucleus, acts as a deneddylase and promotes the degradation of nuclear CRLs (cullin-RING ubiquitin ligases) and thereby stabilizes nuclear CRL substrates, while cytoplasmic CRLs remain unaffected. These modifications prevent host cell cycle S-phase progression and create a favorable environment allowing efficient viral genome replication. Participates later in the secondary envelopment of capsids. Indeed, plays a linker role for the association of the outer viral tegument to the capsids together with the inner tegument protein (By similarity). Counteracts host TLR-mediated NF-kappa-B activation through both MYD88 and TICAM1-dependent pathways by interfering with 'Lys-63'- and 'Lys-48'-linked ubiquitination of signaling intermediates such as TRAF6 and IKBKG (PubMed:24586164). Inhibits type I interferon production by forming a tri-molecular complex with host TRIM25 and 14-3-3 thereby promoting TRIM25 autoubiquitination and sequestration of the ligase into inactive protein aggregates (PubMed:31710640). In turn, host RIGI is recruited to the complex but ubiquitination is severely impaired leading to inhibition of the pathway (PubMed:29357390). Catalyzes also the removal of 'Lys-48'- and 'Lys-63'-linked ubiquitin chains on host TBK1 and STING1 suppressing cGAS-STING signaling in addition to the RIGI-MAVS pathway (PubMed:36802409). Inhibits selective autophagy by deubiquitinating host SQSTM1. In turn, decreased SQSTM1 ubiquitination fails to recruit LC3 to SQSTM1-positive aggregates (PubMed:34543352). In the host nucleus, deubiquitinates topoisomerase II subunits TOP2A and TOP2B thereby stabilizing SUMOylated TOP2 which halts the DNA damage response to TOP2-induced double strand DNA breaks and promotes cell survival (PubMed:34543352). {ECO:0000255|HAMAP-Rule:MF_04044, ECO:0000269|PubMed:19244336, ECO:0000269|PubMed:20190741, ECO:0000269|PubMed:22474075, ECO:0000269|PubMed:24586164, ECO:0000269|PubMed:34543352, ECO:0000269|PubMed:36802409}.
|
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
|
P03188
|
GB_EBVB9
|
MTRRRVLSVVVLLAALACRLGAQTPEQPAPPATTVQPTATRQQTSFPFRVCELSSHGDLFRFSSDIQCPSFGTRENHTEGLLMVFKDNIIPYSFKVRSYTKIVTNILIYNGWYADSVTNRHEEKFSVDSYETDQMDTIYQCYNAVKMTKDGLTRVYVDRDGVNITVNLKPTGGLANGVRRYASQTELYDAPGWLIWTYRTRTTVNCLITDMMAKSNSPFDFFVTTTGQTVEMSPFYDGKNKETFHERADSFHVRTNYKIVDYDNRGTNPQGERRAFLDKGTYTLSWKLENRTAYCPLQHWQTFDSTIATETGKSIHFVTDEGTSSFVTNTTVGIELPDAFKCIEEQVNKTMHEKYEAVQDRYTKGQEAITYFITSGGLLLAWLPLTPRSLATVKNLTELTTPTSSPPSSPSPPAPSAARGSTPAAVLRRRRRDAGNATTPVPPTAPGKSLGTLNNPATVQIQFAYDSLRRQINRMLGDLARAWCLEQKRQNMVLRELTKINPTTVMSSIYGKAVAAKRLGDVISVSQCVPVNQATVTLRKSMRVPGSETMCYSRPLVSFSFINDTKTYEGQLGTDNEIFLTKKMTEVCQATSQYYFQSGNEIHVYNDYHHFKTIELDGIATLQTFISLNTSLIENIDFASLELYSRDEQRASNVFDLEGIFREYNFQAQNIAGLRKDLDNAVSNGRNQFVDGLGELMDSLGSVGQSITNLVSTVGGLFSSLVSGFISFFKNPFGGMLILVLVAGVVILVISLTRRTRQMSQQPVQMLYPGIDELAQQHASGEGPGINPISKTELQAIMLALHEQNQEQKRAAQRAAGPSVASRALQAARDRFPGLRRRRYHDPETAAALLGEAETEF
| null | null |
symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062]
|
host cell endosome membrane [GO:0044175]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF17416;PF17417;PF00606;
|
1.20.5.1890;2.30.29.100;2.30.30.1230;6.10.250.3280;
|
Herpesviridae glycoprotein B family
|
PTM: A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds. {ECO:0000305|PubMed:15534216, ECO:0000305|PubMed:17655906, ECO:0000305|PubMed:19218203}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-Rule:MF_04032}.
| null | null | null | null | null |
FUNCTION: Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress. {ECO:0000255|HAMAP-Rule:MF_04032}.
|
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
|
P03191
|
EAD_EBVB9
|
METTQTLRFKTKALAVLSKCYDHAQTHLKGGVLQVNLLSVNYGGPRLAAVANAGTAGLISFEVSPDAVAEWQNHQSPEEAPAAVSFRNLAYGRTCVLGKELFGSAVEQASLQFYKRPQGGSRPEFVKLTMEYDDKVSKSHHTCALMPYMPPASDRLRNEQMIGQVLLMPKTASSLQKWARQQGSGGVKVTLNPDLYVTTYTSGEACLTLDYKPLSVGPYEAFTGPVAKAQDVGAVEAHVVCSVAADSLAAALSLCRIPAVSVPILRFYRSGIIAVVAGLLTSAGDLPLDLSVILFNHASEEAAASTASEPEDKSPRVQPLGTGLQQRPRHTVSPSPSPPPPPRTPTWESPARPETPSPAIPSHSSNTALERPLAVQLARKRTSSEARQKQKHPKKVKQAFNPLI
| null | null |
bidirectional double-stranded viral DNA replication [GO:0039686]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]
|
host cell nucleus [GO:0042025]; viral tegument [GO:0019033]
|
DNA binding [GO:0003677]
|
PF04929;
|
3.70.10.10;
|
Herpesviridae DNA polymerase accessory subunit family
|
PTM: Phosphorylated by the viral BGLF4 kinase. {ECO:0000269|PubMed:18343828}.
|
SUBCELLULAR LOCATION: Virion tegument. Host nucleus. Note=BMRF1 shows homogeneous, not dot-like, distribution in the replication compartments, which coincides with the newly synthesized viral DNA.
| null | null | null | null | null |
FUNCTION: Acts as a DNA polymerase processivity factor; a transcriptional activator for several EBV promoters and inhibits the host DNA damage response (DDR) to double-stranded DNA breaks (PubMed:16641300, PubMed:19801550, PubMed:31462557, PubMed:8764021). Plays an essential role in the viral lytic DNA replication by acting as a polymerase accessory subunit (PubMed:16641300, PubMed:19801550). Stimulates the viral DNA polymerase activity and appears to function with it as a holoenzyme (PubMed:19801550). Increases the processivity of the viral polymerase, probably by acting as a sliding clamp that prevents dissociation of the polymerase from the active template (PubMed:19801550). In addition, BMRF1 transcriptionally activates the oriLyt early BHLF1 promoter (PubMed:8764021, PubMed:9126259). Promotes G1/S cell cycle arrest through p53 induction (PubMed:24501404). {ECO:0000269|PubMed:16641300, ECO:0000269|PubMed:19801550, ECO:0000269|PubMed:24501404, ECO:0000269|PubMed:31462557, ECO:0000269|PubMed:8764021, ECO:0000269|PubMed:9126259}.
|
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
|
P03200
|
GP350_EBVB9
|
MEAALLVCQYTIQSLIHLTGEDPGFFNVEIPEFPFYPTCNVCTADVNVTINFDVGGKKHQLDLDFGQLTPHTKAVYQPRGAFGGSENATNLFLLELLGAGELALTMRSKKLPINVTTGEEQQVSLESVDVYFQDVFGTMWCHHAEMQNPVYLIPETVPYIKWDNCNSTNITAVVRAQGLDVTLPLSLPTSAQDSNFSVKTEMLGNEIDIECIMEDGEISQVLPGDNKFNITCSGYESHVPSGGILTSTSPVATPIPGTGYAYSLRLTPRPVSRFLGNNSILYVFYSGNGPKASGGDYCIQSNIVFSDEIPASQDMPTNTTDITYVGDNATYSVPMVTSEDANSPNVTVTAFWAWPNNTETDFKCKWTLTSGTPSGCENISGAFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFADPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPWDNGTESKAPDMTSSTSPVTTPTPNATSPTPAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTLGKTSPTSAVTTPTPNATGPTVGETSPQANATNHTLGGTSPTPVVTSQPKNATSAVTTGQHNITSSSTSSMSLRPSSNPETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASISTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPQNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRPRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRFSNLSMLVLQWASLAVLTLLLLLVMADCAFRRNLSTSHTYTTPPYDDAETYV
| null | null | null |
host cell membrane [GO:0033644]; membrane [GO:0016020]; virion membrane [GO:0055036]
| null |
PF05109;PF20676;PF20677;PF20678;
|
2.60.40.2800;2.60.40.2810;2.60.40.2820;
|
Epstein-Barr GP350 family
|
PTM: Extensively glycosylated. {ECO:0000269|PubMed:6319581}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:15534216}; Single-pass membrane protein {ECO:0000269|PubMed:15534216}. Host membrane {ECO:0000269|PubMed:15534216}; Single-pass membrane protein {ECO:0000269|PubMed:15534216}. Note=Most abundant component of the viral envelope.
| null | null | null | null | null |
FUNCTION: Initiates virion attachment to host B-lymphocyte cell, leading to virus entry. Acts by binding to host CR2 at the surface of B-lymphocytes, facilitating the binding of viral glycoprotein gp42 to HLA class II molecules. Attachment triggers virion-host membrane fusion and invasion of the host cell.
|
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
|
P03205
|
GP42_EBVB9
|
MVSFKQVRVPLFTAIALVIVLLLAYFLPPRVRGGGRVAAAAITWVPKPNVEVWPVDPPPPVNFNKTAEQEYGDKEVKLPHWTPTLHTFQVPQNYTKANCTYCNTREYTFSYKGCCFYFTKKKHTWNGCFQACAELYPCTYFYGPTPDILPVVTRNLNAIESLWVGVYRVGEGNWTSLDGGTFKVYQIFGSHCTYVSKFSTVPVSHHECSFLKPCLCVSQRSNS
| null | null | null |
host cell membrane [GO:0033644]; membrane [GO:0016020]; virion membrane [GO:0055036]
|
carbohydrate binding [GO:0030246]
| null |
3.10.100.10;
|
Epstein barr virus gp42 family
| null |
SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:15534216}. Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. Note=virions synthesized in B-lymphocytes contain a lower amount of gp42 due to sequestration by cellular HLA class II protein, whereas virions made from epithelial cells has a higher amount of gp42. {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Plays a role in virion attachment to host B-lymphocytes, through binding to leukocyte antigen (HLA) class II and subsequently participates in fusion of the virion with host membranes. May act as a tropism switch that directs fusion with B-lymphocytes and inhibits fusion with epithelial cells. Additionally, hampers T-cell recognition via HLA class II molecules through steric hindrance of T-cell receptor-class II-peptide interaction. {ECO:0000269|PubMed:12042810, ECO:0000269|PubMed:15613312, ECO:0000269|PubMed:9151859}.; FUNCTION: Soluble gp42 inhibits HLA class II-restricted antigen presentation to T-cells through binding to immature and mature HLA class II complexes. {ECO:0000269|PubMed:15613312}.
|
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
|
P03206
|
BZLF1_EBVB9
|
MMDPNSTSEDVKFTPDPYQVPFVQAFDQATRVYQDLGGPSQAPLPCVLWPVLPEPLPQGQLTAYHVSTAPTGSWFSAPQPAPENAYQAYAAPQLFPVSDITQNQQTNQAGGEAPQPGDNSTVQTAAAVVFACPGANQGQQLADIGVPQPAPVAAPARRTRKPQQPESLEECDSELEIKRYKNRVASRKCRAKFKQLLQHYREVAAAKSSENDRLRLLLKQMCPSLDVDSIIPRTPDVLHEDLLNF
| null | null |
positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355]; release from viral latency [GO:0019046]; symbiont-mediated perturbation of host cell cycle G0/G1 transition checkpoint [GO:0039646]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity [GO:0039557]; virus-mediated perturbation of host defense response [GO:0019049]
|
chromatin [GO:0000785]; host cell nucleus [GO:0042025]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; protein dimerization activity [GO:0046983]; sequence-specific DNA binding [GO:0043565]
| null |
1.20.5.170;
|
BZIP family
| null |
SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:10849009, ECO:0000269|PubMed:8380464}.
| null | null | null | null | null |
FUNCTION: Transcription factor that acts as a molecular switch to induce the transition from the latent to the lytic or productive phase of the virus cycle (Probable) (PubMed:8404860). Mediates the switch from the latent to the lytic cycle of infection in cells containing a highly methylated viral genome (PubMed:15361873, PubMed:34893887). Probably binds to silenced chromatin and recruits host chromatin-remodeling enzymes (PubMed:30926617). Regulates this switch by binding to 2 types of ZEBRA response elements (ZREs): the CpG-free AP-1 like elements (latency) and the methylated CpG-containing elements (lytic replication) (Probable) (PubMed:22022468, PubMed:34893887). Activates preferentially the methylated forms of the viral lytic R (BRLF1) and Na (BRRF1) gene promoters, the latters being the first genes activated during Z-mediated reactivation in latently infected cells (PubMed:15361873, PubMed:19325883). BZLF1 and BRLF1 act together to trigger lytic replication (PubMed:10856251, PubMed:15361873). Also binds the lytic origin of replication, oriLyt (PubMed:20808903). Induces G1 cell cycle arrest by stabilizing the host CCAAT/enhancer binding protein CEBPA (PubMed:15078966). This function is important because the lytic cycle preferentially takes place in host cells arrested in G1 (PubMed:15078966). {ECO:0000269|PubMed:10856251, ECO:0000269|PubMed:15078966, ECO:0000269|PubMed:15361873, ECO:0000269|PubMed:17079287, ECO:0000269|PubMed:1847997, ECO:0000269|PubMed:19144704, ECO:0000269|PubMed:19325883, ECO:0000269|PubMed:20808903, ECO:0000269|PubMed:2157874, ECO:0000269|PubMed:22022468, ECO:0000269|PubMed:23678172, ECO:0000269|PubMed:30926617, ECO:0000269|PubMed:34893887, ECO:0000269|PubMed:8404860, ECO:0000305|PubMed:2157874}.
|
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
|
P03208
|
BILF1_EBVB9
|
MLSTMAPGSTVGTLVANMTSVNATEDACTKSYSAFLSGMTSLLLVLLILLTLAGILFIIFVRKLVHRMDVWLIALLIELLLWVLGKMIQEFSSTGLCLLTQNMMFLGLMCSVWTHLGMALEKTLALFSRTPKRTSHRNVCLYLMGVFCLVLLLIIILLITMGPDANLNRGPNMCREGPTKGMHTAVQGLKAGCYLLAAVLIVLLTVIIIWKLLRTKFGRKPRLICNVTFTGLICAFSWFMLSLPLLFLGEAGSLGFDCTESLVARYYPGPAACLALLLIILYAWSFSHFMDSLKNQVTVTARYFRRVPSQST
| null | null |
negative regulation of NLRP3 inflammasome complex assembly [GO:1900226]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host PKR/eIFalpha signaling [GO:0039580]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell mitochondrial outer membrane [GO:0044193]; host cell plasma membrane [GO:0020002]; mitochondrial outer membrane [GO:0005741]
|
protein serine/threonine kinase inhibitor activity [GO:0030291]; protein-macromolecule adaptor activity [GO:0030674]
| null |
1.20.1070.10;
|
Epstein-Barr virus BILF1 protein family
| null |
SUBCELLULAR LOCATION: Host cell membrane {ECO:0000269|PubMed:15596846}; Multi-pass membrane protein {ECO:0000305}. Host mitochondrion outer membrane {ECO:0000269|PubMed:37311461}.
| null | null | null | null | null |
FUNCTION: Constitutively active, ligand-independent G protein-coupled receptor that has immunoevasive and oncogenic activities (PubMed:15596837, PubMed:15596846, PubMed:30647152, PubMed:34216564). Couples with the host inhibitory G protein (Gi) in order to disrupt the host chemokine signaling (PubMed:34216564). As a consequence of its constitutive activity, mediates host CXCR4 inhibition (PubMed:20622011). Enhances degradation of host major histocompatibility complex class I antigens via lysosomes, thereby modulating the antigen presentation to cytotoxic T cells (PubMed:19119421, PubMed:21123379, PubMed:23315076). Targets selectively HLA-A, HLA-Band HLA-E molecules (PubMed:23315076). Targets also newly synthesized MHC-I/peptide complexes en route to the host cell surface (PubMed:21123379). Inhibits the host EIF2AK2/PKR phosphorylation (PubMed:15596837). Displays tranforming activity (PubMed:20543866). Utilizes its C-terminal tail to trigger host MAVS UFMylation via PARK2, resulting in selective MAVS removal from mitochondrial membranes and routing to lysosomes to prevent viral activation of the NLRP3 inflammasome (PubMed:37311461). {ECO:0000269|PubMed:15596837, ECO:0000269|PubMed:15596846, ECO:0000269|PubMed:19119421, ECO:0000269|PubMed:20543866, ECO:0000269|PubMed:20622011, ECO:0000269|PubMed:21123379, ECO:0000269|PubMed:23315076, ECO:0000269|PubMed:30647152, ECO:0000269|PubMed:34216564, ECO:0000269|PubMed:37311461}.
|
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
|
P03211
|
EBNA1_EBVB9
|
MSDEGPGTGPGNGLGEKGDTSGPEGSGGSGPQRRGGDNHGRGRGRGRGRGGGRPGAPGGSGSGPRHRDGVRRPQKRPSCIGCKGTHGGTGAGAGAGGAGAGGAGAGGGAGAGGGAGGAGGAGGAGAGGGAGAGGGAGGAGGAGAGGGAGAGGGAGGAGAGGGAGGAGGAGAGGGAGAGGGAGGAGAGGGAGGAGGAGAGGGAGAGGAGGAGGAGAGGAGAGGGAGGAGGAGAGGAGAGGAGAGGAGAGGAGGAGAGGAGGAGAGGAGGAGAGGGAGGAGAGGGAGGAGAGGAGGAGAGGAGGAGAGGAGGAGAGGGAGAGGAGAGGGGRGRGGSGGRGRGGSGGRGRGGSGGRRGRGRERARGGSRERARGRGRGRGEKRPRSPSSQSSSSGSPPRRPPPGRRPFFHPVGEADYFEYHQEGGPDGEPDVPPGAIEQGPADDPGEGPSTGPRGQGDGGRRKKGGWFGKHRGQGGSNPKFENIAEGLRALLARSHVERTTDEGTWVAGVFVYGGSKTSLYNLRRGTALAIPQCRLTPLSRLPFGMAPGPGPQPGPLRESIVCYFMVFLQTHIFAEVLKDAIKDLVMTKPAPTCNIRVTVCSFDDGVDLPPWFPPMVEGAAAEGDDGDDGDEGGDGDEGEEGQE
|
3.1.21.-
| null |
positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA replication [GO:0006275]; symbiont-mediated disruption of host cell PML body [GO:0075342]; symbiont-mediated suppression of host antigen processing and presentation [GO:0039588]; viral latency [GO:0019042]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell PML body [GO:0075341]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; endonuclease activity [GO:0004519]; enzyme-substrate adaptor activity [GO:0140767]
|
PF02905;
|
3.30.70.390;
|
Herpesviridae EBNA1 family
|
PTM: Phosphorylation at Ser-385 increases the nuclear import efficiency of EBNA1. {ECO:0000269|PubMed:28104399}.; PTM: Phosphorylation at Ser-393 is required for interaction with CSNK2B. {ECO:0000269|PubMed:28701406}.
|
SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:20719947, ECO:0000269|PubMed:2161150, ECO:0000269|PubMed:31941781}.
| null | null | null | null | null |
FUNCTION: Responsible for the origin of replication (oriP) dependent replication and maintenance of viral episomes during latent infection (PubMed:15479791, PubMed:2996781). EBNA1 dimer interacts with the DS (dyad symmetry) element within the origin of replication oriP and with a host mitotic chromosome to initiate viral DNA replication during latency (PubMed:24067969, PubMed:2996781, PubMed:31142669, PubMed:8551585). EBNA1 binding to DS recruits the host origin recognition complex (ORC) (PubMed:12953058). Governs the faithful mitotic segregation of the viral episomes by binding both the FR (family of repeats) element within oriP and the host mitotic chromosomes (PubMed:11172042, PubMed:15479791, PubMed:24067969). Forms a cell cycle-dependent tyrosine-dependent DNA cross-link and single-strand cleavage at oriP required for terminating replication and maintaining viral episomes (PubMed:33482082). Counteracts the stabilization of host p53/TP53 by host USP7, thereby decreasing apoptosis and increasing host cell survival (PubMed:15808506). Induces degradation of host PML through the ubiquitin-proteasome system, which promotes lytic reactivation and may impair the host cell DNA repair (PubMed:18833293). Increases the association of CK2 with PML proteins which increases the phosphorylation of PML proteins by CK2, triggering the polyubiquitylation and degradation of PML (PubMed:20719947). Displays inhibitory effects on a SUMO2-modified complex that includes STUB1, KAP1 and USP7 (PubMed:32176739). This inhibitory effect possibly participates to the maintenance of latency linked to PML silencing (PubMed:32176739). {ECO:0000269|PubMed:11172042, ECO:0000269|PubMed:12953058, ECO:0000269|PubMed:15479791, ECO:0000269|PubMed:15808506, ECO:0000269|PubMed:18833293, ECO:0000269|PubMed:20719947, ECO:0000269|PubMed:24067969, ECO:0000269|PubMed:2996781, ECO:0000269|PubMed:31142669, ECO:0000269|PubMed:32176739, ECO:0000269|PubMed:33482082, ECO:0000269|PubMed:8551585}.
|
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
|
P03230
|
LMP1_EBVB9
|
MEHDLERGPPGPRRPPRGPPLSSSLGLALLLLLLALLFWLYIVMSDWTGGALLVLYSFALMLIIIILIIFIFRRDLLCPLGALCILLLMITLLLIALWNLHGQALFLGIVLFIFGCLLVLGIWIYLLEMLWRLGATIWQLLAFFLAFFLDLILLIIALYLQQNWWTLLVDLLWLLLFLAILIWMYYHGQRHSDEHHHDDSLPHPQQATDDSGHESDSNSNEGRHHLLVSGAGDGPPLCSQNLGAPGGGPDNGPQDPDNTDDNGPQDPDNTDDNGPHDPLPQDPDNTDDNGPQDPDNTDDNGPHDPLPHSPSDSAGNDGGPPQLTEEVENKGGDQGPPLMTDGGGGHSHDSGHGGGDPHLPTLLLGSSGSGGDDDDPHGPVQLSYYD
| null | null |
symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity [GO:0039574]; symbiont-mediated suppression of host TRAF-mediated signal transduction [GO:0039527]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; transformation of host cell by virus [GO:0019087]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell membrane [GO:0033644]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]
| null |
PF05297;
| null |
Herpesviridae LMP-1 family
|
PTM: Ubiquitinated on the N-terminus. {ECO:0000269|PubMed:10807912}.
|
SUBCELLULAR LOCATION: Host cell membrane {ECO:0000269|PubMed:10807912}; Multi-pass membrane protein {ECO:0000269|PubMed:10807912}.
| null | null | null | null | null |
FUNCTION: Acts as a CD40 functional homolog to prevent apoptosis of infected B-lymphocytes and drive their proliferation. Functions as a constitutively active tumor necrosis factor receptor that induces the activation of several signaling pathways, including those of the NF-kappa-B family. LMP1 signaling leads to up-regulation of antiapoptotic proteins and provide growth signals in latently infected cells. Interacts with host UBE2I and subsequently affects the sumoylation state of several cellular proteins. For example, induces the sumoylation of host IRF7 thereby limiting its transcriptional activity and modulating the activation of innate immune responses. Inhibits also host IFN-alpha-stimulated STAT2 nuclear translocation and interferon-stimulated response element transcriptional activity by interacting with and inhibiting host TYK2. Induces SUMO expression during viral latency thereby dysregulating the host sumoylation processes (PubMed:30659232). {ECO:0000269|PubMed:16987978, ECO:0000269|PubMed:19017798, ECO:0000269|PubMed:21795333, ECO:0000269|PubMed:22951831, ECO:0000269|PubMed:30659232}.
|
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
|
P03231
|
GH_EBVB9
|
MQLLCVFCLVLLWEVGAASLSEVKLHLDIEGHASHYTIPWTELMAKVPGLSPEALWREANVTEDLASMLNRYKLIYKTSGTLGIALAEPVDIPAVSEGSMQVDASKVHPGVISGLNSPACMLSAPLEKQLFYYIGTMLPNTRPHSYVFYQLRCHLSYVALSINGDKFQYTGAMTSKFLMGTYKRVTEKGDEHVLSLVFGKTKDLPDLRGPFSYPSLTSAQSGDYSLVIVTTFVHYANFHNYFVPNLKDMFSRAVTMTAASYARYVLQKLVLLEMKGGCREPELDTETLTTMFEVSVAFFKVGHAVGETGNGCVDLRWLAKSFFELTVLKDIIGICYGATVKGMQSYGLERLAAMLMATVKMEELGHLTTEKQEYALRLATVGYPKAGVYSGLIGGATSVLLSAYNRHPLFQPLHTVMRETLFIGSHVVLRELRLNVTTQGPNLALYQLLSTALCSALEIGEVLRGLALGTESGLFSPCYLSLRFDLTRDKLLSMAPQEATLDQAAVSNAVDGFLGRLSLEREDRDAWHLPAYKCVDRLDKVLMIIPLINVTFIISSDREVRGSALYEASTTYLSSSLFLSPVIMNKCSQGAVAGEPRQIPKIQNFTRTQKSCIFCGFALLSYDEKEGLETTTYITSQEVQNSILSSNYFDFDNLHVHYLLLTTNGTVMEIAGLYEERAHVVLAIILYFIAFALGIFLVHKIVMFFL
| null | null |
fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]
|
host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF17488;PF02489;
|
2.60.40.3190;3.90.380.20;
|
Herpesviridae glycoprotein H family
|
PTM: N-glycosylated, O-glycosylated, and sialylated. {ECO:0000255|HAMAP-Rule:MF_04033}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-Rule:MF_04033}.
| null | null | null | null | null |
FUNCTION: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis. The heterodimer gH/gL targets also host EPHA2 to promote viral entry. {ECO:0000255|HAMAP-Rule:MF_04033, ECO:0000269|PubMed:11021994, ECO:0000269|PubMed:29292383, ECO:0000269|PubMed:29292384}.
|
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
|
P03234
|
SCAF_EBVB9
|
MVQAPSVYVCGFVERPDAPPKDACLHLDPLTVKSQLPLKKPLPLTVEHLPDAPVGSVFGLYQSRAGLFSAASITSGDFLSLLDSIYHDCDIAQSQRLPLPREPKVEALHAWLPSLSLASLHPDIPQTTADGGKLSFFDHVSICALGRRRGTTAVYGTDLAWVLKHFSDLEPSIAAQIENDANAAKRESGCPEDHPLPLTKLIAKAIDAGFLRNRVETLRQDRGVANIPAESYLKASDAPDLQKPDKALQSPPPASTDPATMLSGNAGEGATACGGSAAAGQDLISVPRNTFMTLLQTNLDNKPPRQTPLPYAAPLPPFSHQAIATAPSYGPGAGAVAPAGGYFTSPGGYYAGPAGGDPGAFLAMDAHTYHPHPHPPPAYFGLPGLFGPPPPVPPYYGSHLRADYVPAPSRSNKRKRDPEEDEEGGGLFPGEDATLYRKDIAGLSKSVNELQHTLQALRRETLSYGHTGVGYCPQQGPCYTHSGPYGFQPHQSYEVPRYVPHPPPPPTSHQAAQAQPPPPGTQAPEAHCVAESTIPEAGAAGNSGPREDTNPQQPTTEGHHRGKKLVQASASGVAQSKEPTTPKAKSVSAHLKSIFCEELLNKRVA
|
3.4.21.97
| null |
proteolysis [GO:0006508]; viral release from host cell [GO:0019076]
|
host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]
|
identical protein binding [GO:0042802]; serine-type endopeptidase activity [GO:0004252]
|
PF00716;
|
3.20.16.10;
|
Herpesviridae capsid scaffolding protein family
|
PTM: Capsid scaffolding protein is cleaved by assemblin after formation of the spherical procapsid. As a result, the capsid obtains its mature, icosahedral shape. Cleavages occur at two or more sites: release and tail site. {ECO:0000255|HAMAP-Rule:MF_04008}.
|
SUBCELLULAR LOCATION: [Capsid scaffolding protein]: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assemblin]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Isoform pAP]: Host nucleus {ECO:0000269|PubMed:30710799}.
|
CATALYTIC ACTIVITY: Reaction=Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.; EC=3.4.21.97; Evidence={ECO:0000255|HAMAP-Rule:MF_04008};
| null | null | null | null |
FUNCTION: [Capsid scaffolding protein]: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein. Cleavages products are evicted from the capsid before or during DNA packaging. {ECO:0000255|HAMAP-Rule:MF_04008, ECO:0000269|PubMed:19158247}.; FUNCTION: [Assemblin]: Protease that plays an essential role in virion assembly within the nucleus. Catalyzes the cleavage of the assembly protein after formation of the spherical procapsid. By that cleavage, the capsid matures and gains its icosahedral shape. The cleavage sites seem to include -Ala-Ser-, -Ala-Ala-, as well as Ala-Thr bonds. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging. {ECO:0000255|HAMAP-Rule:MF_04008, ECO:0000269|PubMed:19158247}.; FUNCTION: [Assembly protein]: Plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging. {ECO:0000255|HAMAP-Rule:MF_04008, ECO:0000269|PubMed:19158247}.
|
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
|
P03240
|
E4RF4_ADE02
|
MVLPALPAPPVCDSQNECVGWLGVAYSAVVDVIRAAAHEGVYIEPEARGRLDALREWIYYNYYTERAKRRDRRRRSVCHARTWFCFRKYDYVRRSIWHDTTTNTISVVSAHSVQ
| null | null |
mRNA processing [GO:0006397]; RNA splicing [GO:0008380]
|
host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]
| null |
PF05385;
| null |
Adenoviridae E4 ORF4 family
|
PTM: May be phosphorylated by host SRC kinase.
|
SUBCELLULAR LOCATION: Host nucleus. Host cytoplasm. Note=When expressed alone ex-vivo the majority is found in the nucleus. Tyrosinephosphorylation would promote cytoplasmic localization.
| null | null | null | null | null |
FUNCTION: Plays a role in viral alternative pre-mRNA splicing. Activates dephosphorylation by protein phosphatase 2A of host SR proteins and converts their splicing properties. When expressed alone ex vivo, induces p53/TP53-independent apoptosis called cytoplasmic death. May mimic nutrient/growth signals to activate the host mTOR pathway. {ECO:0000269|PubMed:15775987, ECO:0000269|PubMed:8648720, ECO:0000269|PubMed:9603524, ECO:0000269|PubMed:9696808}.
|
Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
|
P03243
|
E1B55_ADE05
|
MERRNPSERGVPAGFSGHASVESGCETQESPATVVFRPPGDNTDGGAAAAAGGSQAAAAGAEPMEPESRPGPSGMNVVQVAELYPELRRILTITEDGQGLKGVKRERGACEATEEARNLAFSLMTRHRPECITFQQIKDNCANELDLLAQKYSIEQLTTYWLQPGDDFEEAIRVYAKVALRPDCKYKISKLVNIRNCCYISGNGAEVEIDTEDRVAFRCSMINMWPGVLGMDGVVIMNVRFTGPNFSGTVFLANTNLILHGVSFYGFNNTCVEAWTDVRVRGCAFYCCWKGVVCRPKSRASIKKCLFERCTLGILSEGNSRVRHNVASDCGCFMLVKSVAVIKHNMVCGNCEDRASQMLTCSDGNCHLLKTIHVASHSRKAWPVFEHNILTRCSLHLGNRRGVFLPYQCNLSHTKILLEPESMSKVNLNGVFDMTMKIWKVLRYDETRTRCRPCECGGKHIRNQPVMLDVTEELRPDHLVLACTRAEFGSSDEDTD
| null | null |
symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]
|
host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]
|
SUMO ligase activity [GO:0061665]; ubiquitin ligase-substrate adaptor activity [GO:1990756]
|
PF01696;PF04623;
|
2.160.20.10;
|
Adenoviridae E1B 55 kDa protein family
|
PTM: Phosphorylation at the C-terminus affects the subcellular location. {ECO:0000269|PubMed:18614635}.
|
SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:10211970, ECO:0000269|PubMed:20861261}. Host cytoplasm {ECO:0000269|PubMed:10211970, ECO:0000269|PubMed:18614635}. Note=Colocalizes with host TP53 to host PML nuclear bodies. PML localization of E1B-55K is necessary for E1B-55K-dependent SUMOylation of TP53. {ECO:0000269|PubMed:20861261}.
| null | null | null | null | null |
FUNCTION: Plays a major role to prevent cellular inhibition of viral genome replication (PubMed:12186903, PubMed:14657032, PubMed:18614635, PubMed:20484509, PubMed:20861261, PubMed:25772236). Assembles an SCF-like E3 ubiquitin ligase complex based on the cellular proteins ELOB, ELOC, CUL5 and RBX1, in cooperation with viral E4orf6 (PubMed:12186903, PubMed:14657032, PubMed:18614635). This viral RING-type ligase ubiquitinates cellular substrates and targets them to proteasomal degradation: TP53/p53, LIG4, MRE11-RAD50-NBS1 (MRN) complex, ITGA3, DAXX and BLM (PubMed:12186903, PubMed:18614635, PubMed:20484509). E1B-55K probably acts as the substrate-specific adapter of the SCF-like E3 ubiquitin ligase complex (PubMed:18614635). Degradation of host TP53/p53 activity is essential for preventing E1A-induced TP53 accumulation that would otherwise lead to cell apoptosis and growth arrest (PubMed:25772236). E1B-55K also inactivates TP53 transcription-factor activity by binding its transactivation domain (PubMed:25772236). E1B-55K also functions as a SUMO1 E3 ligase for TP53 which causes the latter to be sequestered in promyelocytic leukemia (PML) nuclear bodies thereby contributing to maximal inhibition of TP53 function (PubMed:20861261). {ECO:0000269|PubMed:12186903, ECO:0000269|PubMed:14657032, ECO:0000269|PubMed:18614635, ECO:0000269|PubMed:20484509, ECO:0000269|PubMed:20861261, ECO:0000269|PubMed:25772236}.
|
Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
|
P03244
|
E1B55_ADE02
|
MERRNPSERGVPAGFSGHASVESGGETQESPATVVFRPPGNNTDGGATAGGSQAAAAAGAEPMEPESRPGPSGMNVVQVAELFPELRRILTINEDGQGLKGVKRERGASEATEEARNLTFSLMTRHRPECVTFQQIKDNCANELDLLAQKYSIEQLTTYWLQPGDDFEEAIRVYAKVALRPDCKYKISKLVNIRNCCYISGNGAEVEIDTEDRVAFRCSMINMWPGVLGMDGVVIMNVRFTGPNFSGTVFLANTNLILHGVSFYGFNNTCVEAWTDVRVRGCAFYCCWKGVVCRPKSRASIKKCLFERCTLGILSEGNSRVRHNVASDCGCFMLVKSVAVIKHNMVCGNCEDRASQMLTCSDGNCHLLKTIHVASHSRKAWPVFEHNILTRCSLHLGNRRGVFLPYQCNLSHTKILLEPESMSKVNLNGVFDMTMKIWKVLRYDETRTRCRPCECGGKHIRNQPVMLDVTEELRPDHLVLACTRAEFGSSDEDTD
| null | null |
symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host PKR/eIFalpha signaling [GO:0039580]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]
|
protein serine/threonine kinase inhibitor activity [GO:0030291]; ubiquitin ligase-substrate adaptor activity [GO:1990756]
|
PF01696;PF04623;
|
2.160.20.10;
|
Adenoviridae E1B 55 kDa protein family
| null |
SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:10211970}. Host cytoplasm {ECO:0000269|PubMed:10211970}. Note=Colocalizes with host TP53 to host PML nuclear bodies. PML localization of E1B-55K is necessary for E1B-55K-dependent SUMOylation of TP53. {ECO:0000250|UniProtKB:P03243}.
| null | null | null | null | null |
FUNCTION: Plays a major role to prevent cellular inhibition of viral genome replication. Assembles an SCF-like E3 ubiquitin ligase complex based on the cellular proteins ELOB, ELOC, CUL5 and RBX1, in cooperation with viral E4orf6. This viral RING-type ligase ubiquitinates cellular substrates and targets them to proteasomal degradation: TP53/p53, LIG4, MRE11-RAD50-NBS1 (MRN) complex, ITGA3, DAXX and BLM. E1B-55K probably acts as the substrate-specific adapter of the SCF-like E3 ubiquitin ligase complex. Degradation of host TP53/p53 activity is essential for preventing E1A-induced TP53 accumulation that would otherwise lead to cell apoptosis and growth arrest. E1B-55K also inactivates TP53 transcription-factor activity by binding its transactivation domain. E1B-55K also functions as a SUMO1 E3 ligase for TP53 which causes the latter to be sequestered in promyelocytic leukemia (PML) nuclear bodies thereby contributing to maximal inhibition of TP53 function. {ECO:0000250|UniProtKB:P03243}.
|
Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
|
P03252
|
PRO_ADE02
|
MGSSEQELKAIVKDLGCGPYFLGTYDKRFPGFVSPHKLACAIVNTAGRETGGVHWMAFAWNPRSKTCYLFEPFGFSDQRLKQVYQFEYESLLRRSAIASSPDRCITLEKSTQSVQGPNSAACGLFCCMFLHAFANWPQTPMDHNPTMNLITGVPNSMLNSPQVQPTLRRNQEQLYSFLERHSPYFRSHSAQIRSATSFCHLKNM
|
3.4.22.39
| null |
proteolysis [GO:0006508]
|
host cell nucleus [GO:0042025]; virion component [GO:0044423]
|
cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; DNA binding [GO:0003677]
|
PF00770;
| null |
Peptidase C5 family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04059, ECO:0000269|PubMed:12645618}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04059, ECO:0000305|PubMed:12645618}. Note=Present in about 10 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04059}.
|
CATALYTIC ACTIVITY: Reaction=Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly-Xaa-|-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid).; EC=3.4.22.39; Evidence={ECO:0000255|HAMAP-Rule:MF_04059};
| null | null | null | null |
FUNCTION: Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cell cytoskeletal keratins K7 and K18. {ECO:0000255|HAMAP-Rule:MF_04059, ECO:0000269|PubMed:22791715}.
|
Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
|
P03254
|
E1A_ADE02
|
MRHIICHGGVITEEMAASLLDQLIEEVLADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFPPAPGSPEPPHLSRQPEQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDEEGEEFVLDYVEHPGHGCRSCHYHRRNTGDPDIMCSLCYMRTCGMFVYSPVSEPEPEPEPEPEPARPTRRPKLVPAILRRPTSPVSRECNSSTDSCDSGPSNTPPEIHPVVPLCPIKPVAVRVGGRRQAVECIEDLLNESGQPLDLSCKRPRP
| null | null |
DNA-templated viral transcription [GO:0039695]; regulation of DNA-templated transcription [GO:0006355]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host gene expression [GO:0039657]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell nucleus [GO:0042025]
|
metal ion binding [GO:0046872]
|
PF02703;
| null |
Adenoviridae E1A protein family
| null |
SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03255}.
| null | null | null | null | null |
FUNCTION: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. Interacts with host TBP protein; this interaction probably disrupts the TBP-TATA complex. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta). Promotes the sumoylation of host ZBED1/hDREF with SUMO1 (By similarity). {ECO:0000250|UniProtKB:P03255}.
|
Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
|
P03255
|
E1A_ADE05
|
MRHIICHGGVITEEMAASLLDQLIEEVLADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFPPAPGSPEPPHLSRQPEQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDEEGEEFVLDYVEHPGHGCRSCHYHRRNTGDPDIMCSLCYMRTCGMFVYSPVSEPEPEPEPEPEPARPTRRPKMAPAILRRPTSPVSRECNSSTDSCDSGPSNTPPEIHPVVPLCPIKPVAVRVGGRRQAVECIEDLLNEPGQPLDLSCKRPRP
| null | null |
positive regulation of cell population proliferation [GO:0008284]; positive regulation of protein sumoylation [GO:0033235]; regulation by virus of viral protein levels in host cell [GO:0046719]; regulation of DNA-templated transcription [GO:0006355]; regulation of protein localization [GO:0032880]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host gene expression [GO:0039657]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell nucleus [GO:0042025]
|
DNA-binding transcription factor binding [GO:0140297]; metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090]; molecular sequestering activity [GO:0140313]
|
PF02703;
| null |
Adenoviridae E1A protein family
| null |
SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:25194920, ECO:0000269|PubMed:25210186}.
| null | null | null | null | null |
FUNCTION: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:26405230). Promotes the sumoylation of host ZBED1/hDREF with SUMO1 (PubMed:25210186). {ECO:0000269|PubMed:15806172, ECO:0000269|PubMed:19679664, ECO:0000269|PubMed:20543865, ECO:0000269|PubMed:25210186, ECO:0000269|PubMed:26405230, ECO:0000269|PubMed:9685342, ECO:0000303|PubMed:12204530}.
|
Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
|
P03259
|
E1A_ADE12
|
MRTEMTPLVLSYQEADDILEHLVDNFFNEVPSDDDLYVPSLYELYDLDVESAGEDNNEQAVNEFFPESLILAASEGLFLPEPPVLSPVCEPIGGECMPQLHPEDMDLLCYEMGFPCSDSEDEQDENGMAHVSASAAAAAADREREEFQLDHPELPGHNCKSCEHHRNSTGNTDLMCSLCYLRAYNMFIYSPVSDNEPEPNSTLDGDERPSPPKLGSAVPEGVIKPVPQRVTGRRRCAVESILDLIQEEEREQTVPVDLSVKRPRCN
| null | null |
regulation of DNA-templated transcription [GO:0006355]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell nucleus [GO:0042025]
|
metal ion binding [GO:0046872]; molecular sequestering activity [GO:0140313]
|
PF02703;
| null |
Adenoviridae E1A protein family
| null |
SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03255}.
| null | null | null | null | null |
FUNCTION: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta). Promotes the sumoylation of host ZBED1/hDREF with SUMO1 (By similarity). {ECO:0000250|UniProtKB:P03255}.
|
Human adenovirus A serotype 12 (HAdV-12) (Human adenovirus 12)
|
P03264
|
DNB2_ADE02
|
MASREEEQRETTPERGRGAARRPPTMEDVSSPSPSPPPPRAPPKKRLRRRLESEDEEDSSQDALVPRTPSPRPSTSTADLAIASKKKKKRPSPKPERPPSPEVIVDSEEEREDVALQMVGFSNPPVLIKHGKGGKRTVRRLNEDDPVARGMRTQEEKEESSEAESESTVINPLSLPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHVIEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQISNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNSKPGHAPFLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCNPVYRNSRAQGGGPNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPEFKWSTKHQYRNVSLPVAHSDARQNPFDF
| null | null |
DNA replication [GO:0006260]; DNA unwinding involved in DNA replication [GO:0006268]; DNA-templated transcription [GO:0006351]; positive regulation of DNA replication [GO:0045740]; viral DNA strand displacement replication [GO:0039687]
|
nuclear viral factory [GO:0039715]; viral capsid [GO:0019028]
|
DNA binding [GO:0003677]; single-stranded DNA binding [GO:0003697]; zinc ion binding [GO:0008270]
|
PF02236;PF03728;
|
3.90.148.10;1.10.269.10;
|
Adenoviridae E2A DNA-binding protein family
| null |
SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04054}. Note=Accumulates in infected cells. {ECO:0000255|HAMAP-Rule:MF_04054}.
| null | null | null | null | null |
FUNCTION: Plays a role in the elongation phase of viral strand displacement replication by unwinding the template in an ATP-independent fashion, employing its capacity to form multimers. Also enhances the rate of initiation. Released from template upon second strand synthesis. Assembles in complex with viral pTP, viral pol, host NFIA and host POU2F1/OCT1 on viral origin of replication. Covers the whole ssDNA genome during synthesis. The complementary strand synthesis induces its release from DNA template. May inhibit cellular transcription mediated by the interaction between host SRCAP and CBP. {ECO:0000255|HAMAP-Rule:MF_04054, ECO:0000269|PubMed:12747551, ECO:0000269|PubMed:12954226, ECO:0000269|PubMed:9545375}.
|
Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
|
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