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 |
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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 diffe... | 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-ProRu... | 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 for... | 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 diffe... | 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:... | 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 for... | 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 ce... | 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 | MPAIGIDLGTTYSCVGVYQHGKVEIIANDQGNRTTPSYVAFTDSERLIGDPAKNQVAMNPRNTVFDAKRLIGRKYDDPKIAEDMKHWPFKVVSDGGKPKIGVEYKGESKRFAPEEISSMVLTKMKETAEAYLGESITDAVITVPAYFNDSQRQATKDAGHIAGLNVLRIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTFDVSILTIDEGSLFEVRSTAGDTHLGGEDFDNRLVTHLADEFKRKYKKDLRSNPRALRRLRTAAERAKRTLSSSTEATIEIDALFEGQDFYTKVSRARFEELCADLFRNTLQPVEKALN... | 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 | MPEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELYIKLIPNKTAGTLTIIDTGIGMTKSDLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVADKVTVTSKNNDDEQYVWESSAGGSFTVRADNSEPLGRGTKIVLYIKEDQTDYLEESKIKEIVNKHSQFIGYPIKLLVEKEREKEVSDDEADDEKKEGDEKKEMETDEPKIEDVGEDEDADKKDKDAKKKKTIKEKYTEDEELNKTKPIWTRNPDDISQEEYGEFYKSLTNDWEDHLAVKHFSVEGQL... | 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 ... | 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 ... | 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... | Drosophila melanogaster (Fruit fly) |
P02829 | HSP82_YEAST | MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIPEEEKKDEEKKDEEKKDEDDKKPKLEEVDEEEEKKPKTKKVKEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAI... | 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]; ... | 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 confo... | 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]; neg... | 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 polymera... | 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 | MQKATYYDSSAIYGGYPYQAANGFAYNASQQPYAPSAALGTDGVEYHRPACSLQSPASAGGHPKTHELSEACLRTLSGPPSQPPGLGEPPLPPPPPQAAPPAPQPPQPPPQPPAPTPAAPPPPSSVSPPQSANSNPTPASTAKSPLLNSPTVGKQIFPWMKESRQNTKQKTSGSSSGESCAGDKSPPGQASSKRARTAYTSAQLVELEKEFHFNRYLCRPRRVEMANLLNLTERQIKIWFQNRRMKYKKDQKGKGMLTSSGGQSPSRSPVPPGAGGYLNSMHSLVNSVPYEPQSPPPFSKPPQGAYGLPPASYPAPLPSC... | 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:... | 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 | MTMSTNNCESMTSYFTNSYMGADMHHGHYPGNGVTDLDAQQMHHYSQNANHQGNMPYPRFPPYDRMPYYNGQGMDQQQQHQVYSRPDSPSSQVGGVMPQAQTNGQLGVPQQQQQQQQQPSQNQQQQQAQQAPQQLQQQLPQVTQQVTHPQQQQQQPVVYASCKLQAAVGGLGMVPEGGSPPLVDQMSGHHMNAQMTLPHHMGHPQAQLGYTDVGVPDVTEVHQNHHNMGMYQQQSGVPPVGAPPQGMMHQGQGPPQMHQGHPGQHTPPSQNPNSQSSGMPSPLYPWMRSQFGKCQERKRGRQTYTRYQTLELEKEFHFNR... | 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:000... | 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 | MATTNSQSHYSYADNMNMYNMYHPHSLPPTYYDNSGSNAYYQNTSNYQGYYPQESYSESCYYYNNQEQVTTQTVPPVQPTTPPPKATKRKAEDDAASIIAAVEERPSTLRALLTNPVKKLKYTPDYFYTTVEQVKKAPAVSTKVTASPAPSYDQEYVTVPTPSASEDVDYLDVYSPQSQTQKLKNGDFATPPPTTPTSLPPLEGISTPPQSPGEKSSSAVSQEINHRIVTAPNGAGDFNWSHIEETLASDCKDSKRTRQTYTRYQTLELEKEFHFNRYITRRRRIDIANALSLSERQIKIWFQNRRMKSKKDRTLDSSPE... | 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... | 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|Pu... | Drosophila melanogaster (Fruit fly) |
P02836 | HMEN_DROME | MALEDRCSPQSAPSPITLQMQHLHHQQQQQQQQQQQMQHLHQLQQLQQLHQQQLAAGVFHHPAMAFDAAAAAAAAAAAAAAHAHAAALQQRLSGSGSPASCSTPASSTPLTIKEEESDSVIGDMSFHNQTHTTNEEEEAEEDDDIDVDVDDTSAGGRLPPPAHQQQSTAKPSLAFSISNILSDRFGDVQKPGKSMENQASIFRPFEASRSQTATPSAFTRVDLLEFSRQQQAAAAAATAAMMLERANFLNCFNPAAYPRIHEEIVQSRLRRSAANAVIPPPMSSKMSDANPEKSALGSLCKAVSQIGQPAAPTMTQPPLS... | 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];... | 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-specif... | 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 | MNPMRVLSLLACLAVAALAKPNGRMDNSVNQALKPSQWLSGSQLEAIPALDDFTIERLENMNLERGAELLQQVYHLSQIHHNVEPNYVPSGIQVYVPKPNGDKTVAPLNEMIQRLKQKQNFGEDEVTIIVTGLPQTSETVKKATRKLVQAYMQRYNLQQQRQHGKNGNQDYQDQSNEQRKNQRTSSEEDYSEEVKNAKTQSGDIIVIDLGSKLNTYERYAMLDIEKTGAKIGKWIVQMVNELDMPFDTIHLIGQNVGAHVAGAAAQEFTRLTGHKLRRVTGLDPSKIVAKSKNTLTGLARGDAEFVDAIHTSVYGMGTPI... | 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 localizatio... | Drosophila melanogaster (Fruit fly) |
P02844 | VIT2_DROME | MNPLRTLCVMACLLAVAMGNPQSGNRSGRRSNSLDNVEQPSNWVNPREVEELPNLKEVTLKKLQEMSLEEGATLLDKLYHLSQFNHVFKPDYTPEPSQIRGYIVGERGQKIEFNLNTLVEKVKRQQKFGDDEVTIFIQGLPETNTQVQKATRKLVQAYQQRYNLQPYETTDYSNEEQSQRSSSEEQQTQRRKQNGEQDDTKTGDLIVIQLGNAIEDFEQYATLNIERLGEIIGNRLVELTNTVNVPQEIIHLIGSGPAAHVAGVAGRQFTRQTGHKLRRITALDPTKIYGKPEERLTGLARGDADFVDAIHTSAYGMGTS... | 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 ge... | Drosophila melanogaster (Fruit fly) |
P02845 | VIT2_CHICK | MRGIILALVLTLVGSQKFDIDPGFNSRRSYLYNYEGSMLNGLQDRSLGKAGVRLSSKLEISGLPENAYLLKVRSPQVEEYNGVWPRDPFTRSSKITQVISSCFTRLFKFEYSSGRIGNIYAPEDCPDLCVNIVRGILNMFQMTIKKSQNVYELQEAGIGGICHARYVIQEDRKNSRIYVTRTVDLNNCQEKVQKSIGMAYIYPCPVDVMKERLTKGTTAFSYKLKQSDSGTLITDVSSRQVYQISPFNEPTGVAVMEARQQLTLVEVRSERGSAPDVPMQNYGSLRYRFPAVLPQMPLQLIKTKNPEQRIVETLQHIVLN... | 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 b... | 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 | MKPGGNTIVIWMYAVATWLCFGSTSGWSFTLEDNNIFPKQYPIINFTTAGATVQSYTNFIRAVRGRLTTGADVRHEIPVLPNRVGLPINQRFILVELSNHAELSVTLALDVTNAYVVGYRAGNSAYFFHPDNQEDAEAITHLFTDVQNRYTFAFGGNYDRLEQLAGNLRENIELGNGPLEEAISALYYYSTGGTQLPTLARSFIICIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSVITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKFSVYDVSILIPIIALMVYRCAPPPSSQFSLLIRPVVPNFNADVCMD... | 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, modi... | 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];... | 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 | MMRKLAILSVSSFLFVEALFQEYQCYGSSSNTRVLNELNYDNAGTNLYNELEMNYYGKQENWYSLKKNSRSLGENDDGNNNNGDNGREGKDEDKRDGNNEDNEKLRKPKHKKLKQPGDGNPDPNANPNVDPNANPNVDPNANPNVDPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNVDPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNKNNQGNGQGHNMPNDPNRNVDENANANNAVKN... | 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... | 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... | 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 ho... | 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). Stimulat... | 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|PubM... | 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 th... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P02916 | MALF_ECOLI | MDVIKKKHWWQSDALKWSVLGLLGLLVGYLVVLMYAQGEYLFAITTLILSSAGLYIFANRKAYAWRYVYPGMAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQEVLLDRSWQAGKTYNFGLYPAGDEWQLALSDGETGKNYLSDAFKFGGEQKLQLKETTAQPEGERANLRVITQNRQALSDITAILPDGNKVMMSSLRQFSGTQPLYTLDGDGTLTNNQSGVKYRPNNQIGFYQSITADGNWGDEKLSPGYTVTTGWKNFTRVFTDEGIQKPFLAIFVWTVVFSLITVFLTVAVGMVLACLVQWEALRGKAVYRVL... | 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-depe... | 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 | MKFVKYFLILAVCCILLGAGSIYGLYRYIEPQLPDVATLKDVRLQIPMQIYSADGELIAQYGEKRRIPVTLDQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKEVFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLNEMAVIAGLPKAPSTFNPLYSMDRAVARRNVVLSRMLDEGYITQQQFDQTRTEAINANYHAPEIAFSAPYLSEMVRQEMYNRYGESAYEDGYRIYTTITRKVQQAAQQAVRNNVLDYDMRHGYRGPA... | 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... | 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:0... | Escherichia coli (strain K12) |
P02919 | PBPB_ECOLI | MAGNDREPIGRKGKPTRPVKQKVSRRRYEDDDDYDDYDDYEDEEPMPRKGKGKGKGRKPRGKRGWLWLLLKLAIVFAVLIAIYGVYLDQKIRSRIDGKVWQLPAAVYGRMVNLEPDMTISKNEMVKLLEATQYRQVSKMTRPGEFTVQANSIEMIRRPFDFPDSKEGQVRARLTFDGDHLATIVNMENNRQFGFFRLDPRLITMISSPNGEQRLFVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGASTLTQQLVKNLFLSSERSYWRKANEAYMALIMDARYSKDRILELYMNEVYLGQSG... | 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... | 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 | MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQPLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNAGAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALCASIVGIMFTINNQFVFWLGSGCALILAVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFDQQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMSVRIIGSSFATSALEVVILKT... | 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|Pub... | 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 substrat... | 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:184844... | Escherichia coli (strain K12) |
P02921 | MELB_ECOLI | MSISMTTKLSYGFGAFGKDFAIGIVYMYLMYYYTDVVGLSVGLVGTLFLVARIWDAINDPIMGWIVNATRSRWGKFKPWILIGTLANSVILFLLFSAHLFEGTTQIVFVCVTYILWGMTYTIMDIPFWSLVPTITLDKREREQLVPYPRFFASLAGFVTAGVTLPFVNYVGGGDRGFGFQMFTLVLIAFFIVSTIITLRNVHEVFSSDNQPSAEGSHLTLKAIVALIYKNDQLSCLLGMALAYNVASNIITGFAIYYFSYVIGDADLFPYYLSYAGAANLVTLVFFPRLVKSLSRRILWAGASILPVLSCGVLLLMALMS... | 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... | 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:33162... | 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:001589... | 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... | Escherichia coli (strain K12) |
P02930 | TOLC_ECOLI | MKKLLPILIGLSLSGFSSLSQAENLMQVYQQARLSNPELRKSAADRDAAFEKINEARSPLLPQLGLGADYTYSNGYRDANGINSNATSASLQLTQSIFDMSKWRALTLQEKAAGIQDVTYQTDQQTLILNTATAYFNVLNAIDVLSYTQAQKEAIYRQLDQTTQRFNVGLVAITDVQNARAQYDTVLANEVTARNNLDNAVEQLRQITGNYYPELAALNVENFKTDKPQPVNALLKEAEKRNLSLLQARLSQDLAREQIRQAQDGHLPTLDLTASTGISDTSYSGSKTRGAAGTQYDDSNMGQNKVGLSFSLPIYQGGMV... | 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]; xenobio... | 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|PubMe... | 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:000026... | Escherichia coli (strain K12) |
P02931 | OMPF_ECOLI | MMKRNILAVIVPALLVAGTANAAEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQINSDLTGYGQWEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGRNYGVVYDALGYTDMLPEFGGDTAYSDDFFVGRVGGVATYRNSNFFGLVDGLNFAVQYLGKNERDTARRSNGDGVGGSISYEYEGFGIVGAYGAADRTNLQEAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPITNKFTNTSGFANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVG... | 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... | Escherichia coli (strain K12) |
P02942 | MCP1_ECOLI | MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNIGSGSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQDGFEKQYVAYMEQNDRLHDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNA... | 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 pro... | 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, ... | Escherichia coli (strain K12) |
P02943 | LAMB_ECOLI | MMITLRKLPLAVAVAAGVMSAQAMAVDFHGYARSGIGWTGSGGEQQCFQTTGAQSKYRLGNECETYAELKLGQEVWKEGDKSFYFDTNVAYSVAQQNDWEATDPAFREANVQGKNLIEWLPGSTIWAGKRFYQRHDVHMIDFYYWDISGPGAGLENIDVGFGKLSLAATRSSEAGGSSSFASNNIYDYTNETANDVFDVRLAQMEINPGGTLELGVDYGRANLRDNYRLVDGASKDGWLFTAEHTQSVLKGFNKFVVQYATDSMTSQGKGLSQGSGVAFDNEKFAYNINNNGHMLRILDHGAISMGDNWDMMYVGMYQDI... | 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 ... | 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|PubM... | 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:2800... | 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-r... | 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. M... | Neisseria gonorrhoeae |
P02976 | SPA_STAA8 | MKKKNIYSIRKLGVGIASVTLGTLLISGGVTPAANAAQHDEAQQNAFYQVLNMPNLNADQRNGFIQSLKDDPSQSANVLGEAQKLNDSQAPKADAQQNNFNKDQQSAFYEILNMPNLNEAQRNGFIQSLKDDPSQSTNVLGEAKKLNESQAPKADNNFNKEQQNAFYEILNMPNLNEEQRNGFIQSLKDDPSQSANLLSEAKKLNESQAPKADNKFNKEQQNAFYEILHLPNLNEEQRNGFIQSLKDDPSQSANLLAEAKKLNDAQAPKADNKFNKEQQNAFYEILHLPNLTEEQRNGFIQSLKDDPSVSKEILAEAKKL... | 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:78... | 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:41... | Staphylococcus aureus (strain NCTC 8325 / PS 47) |
P02992 | EFTU_YEAST | MSALLPRLLTRTAFKASGKLLRLSSVISRTFSQTTTSYAAAFDRSKPHVNIGTIGHVDHGKTTLTAAITKTLAAKGGANFLDYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIDDPEMLELVEMEMRELLNEYGFDGDNAPIIMGSALCALEGRQPEIGEQAIMKLLDAVDEYIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIVGHNSTPLKTTVTGIEMFRKELDSAMAGDNAGVLLRG... | 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 ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P02994 | EF1A_YEAST | MGKEKSHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYQVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGVGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSVKWDESRFQEIVKETSNFIKKVGYNPKTVPFVPISGWNGDNMIEATTNAPWYKGWEKETKAGVVKGKTLLEAIDAIEQPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFAPAGVTTEVKSVEMHHEQLEQGVPGDNVGFNVKNVSVKEIRR... | 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 elongati... | 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 ribos... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P03001 | TF3A_XENLA | MAAKVASTSSEEAEGSLVTEGEMGEKALPVVYKRYICSFADCGAAYNKNWKLQAHLCKHTGEKPFPCKEEGCEKGFTSLHHLTRHSLTHTGEKNFTCDSDGCDLRFTTKANMKKHFNRFHNIKICVYVCHFENCGKAFKKHNQLKVHQFSHTQQLPYECPHEGCDKRFSLPSRLKRHEKVHAGYPCKKDDSCSFVGKTWTLYLKHVAECHQDLAVCDVCNRKFRHKDYLRDHQKTHEKERTVYLCPRDGCDRSYTTAFNLRSHIQSFHEEQRPFVCEHAGCGKCFAMKKSLERHSVVHDPEKRKLKEKCPRPKRSLASRL... | 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 i... | Xenopus laevis (African clawed frog) |
P03004 | DNAA_ECOLI | MSLSLWQQCLARLQDELPATEFSMWIRPLQAELSDNTLALYAPNRFVLDWVRDKYLNNINGLLTSFCGADAPQLRFEVGTKPVTQTPQAAVTSNVAAPAQVAQTQPQRAAPSTRSGWDNVPAPAEPTYRSNVNVKHTFDNFVEGKSNQLARAAARQVADNPGGAYNPLFLYGGTGLGKTHLLHAVGNGIMARKPNAKVVYMHSERFVQDMVKALQNNAIEEFKRYYRSVDALLIDDIQFFANKERSQEEFFHTFNALLEGNQQIILTSDRYPKEINGVEDRLKSRFGWGLTVAIEPPELETRVAILMKKADENDIRLPGE... | 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:000... | 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'); subseq... | 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), stabilizin... | 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 recombi... | Escherichia phage Mu (Bacteriophage Mu) |
P03018 | UVRD_ECOLI | MDVSYLLDSLNDKQREAVAAPRSNLLVLAGAGSGKTRVLVHRIAWLMSVENCSPYSIMAVTFTNKAAAEMRHRIGQLMGTSQGGMWVGTFHGLAHRLLRAHHMDANLPQDFQILDSEDQLRLLKRLIKAMNLDEKQWPPRQAMWYINSQKDEGLRPHHIQSYGNPVEQTWQKVYQAYQEACDRAGLVDFAELLLRAHELWLNKPHILQHYRERFTNILVDEFQDTNNIQYAWIRLLAGDTGKVMIVGDDDQSIYGWRGAQVENIQRFLNDFPGAETIRLEQNYRSTSNILSAANALIENNNGRLGKKLWTDGADGEPISL... | 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 [... | 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 act... | 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... | 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... | Escherichia coli (strain K12) |
P03023 | LACI_ECOLI | MKPVTLYDVAEYAGVSYQTVSRVVNQASHVSAKTREKVEAAMAELNYIPNRVAQQLAGKQSLLIGVATSSLALHAPSQIVAAIKSRADQLGASVVVSMVERSGVEACKAAVHNLLAQRVSGLIINYPLDDQDAIAVEAACTNVPALFLDVSDQTPINSIIFSHEDGTRLGVEHLVALGHQQIALLAGPLSSVSARLRLAGWHKYLTRNQIQPIAEREGDWSAMSGFQQTMQMLNEGIVPTAMLVANDQMALGAMRAITESGLRVGADISVVGYDDTEDSSCYIPPLTTIKQDFRLLGQTSVDRLLQLSQGQAVKGNQLLP... | 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]; ni... | 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 bind... | 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... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P03070 | LT_SV40 | MDKVLNREESLQLMDLLGLERSAWGNIPLMRKAYLKKCKEFHPDKGGDEEKMKKMNTLYKKMEDGVKYAHQPDFGGFWDATEIPTYGTDEWEQWWNAFNEENLFCSEEMPSSDDEATADSQHSTPPKKKRKVEDPKDFPSELLSFLSHAVFSNRTLACFAIYTTKEKAALLYKKIMEKYSVTFISRHNSYNHNILFFLTPHRHRVSAINNYAQKLCTFSFLICKGVNKEYLMYSALTRDPFSVIEESLPGGLKEHDFNPEEAEETKQVSWKLVTEYAMETKCDDVLLLLGMYLEFQYSFEMCLKCIKKEQPSHYKYHEKH... | 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 o... | 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 prefere... | 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 ... | Simian virus 40 (SV40) |
P03071 | LT_POVBK | MDKVLNREESMELMDLLGLERAAWGNLPLMRKAYLRKCKEFHPDKGGDEDKMKRMNTLYKKMEQDVKVAHQPDFGTWSSSEVPTYGTEEWESWWSSFNEKWDEDLFCHEDMFASDEEATADSQHSTPPKKKRKVEDPKDFPSDLHQFLSQAVFSNRTLACFAVYTTKEKAQILYKKLMEKYSVTFISRHMCAGHNIIFFLTPHRHRVSAINNFCQKLCTFSFLICKGVNKEYLLYSALTRDPYHTIEESIQGGLKEHDFSPEEPEETKQVSWKLITEYAVETKCEDVFLLLGMYLEFQYNVEECKKCQKKDQPYHFKYHE... | 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]; v... | 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 ... | BK polyomavirus (BKPyV) (Human polyomavirus 1) |
P03077 | MT_POVMA | MDRVLSRADKERLLELLKLPRQLWGDFGRMQQAYKQQSLLLHPDKGGSHALMQELNSLWGTFKTEVYNLRMNLGGTGFQVRRLHADGWNLSTKDTFGDRYYQRFCRMPLTCLVNVKYSSCSCILCLLRKQHRELKDKCDARCLVLGECFCLECYMQWFGTPTRDVLNLYADFIASMPIDWLDLDVHSVYNPKRRSEELRRAATVHYTMTTGHSAMEASTSQGNGMISSESGTPATSRRLRLPSLLSNPTYSVMRSHSYPPTRVLQQIHPHILLEEDEILVLLSPMTAYPRTPPELLYPESDQDQLEPLEEEEEEYMPMED... | 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 S... | 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... | 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 a... | JC polyomavirus (JCPyV) (JCV) |
P03087 | VP1_SV40 | MAPTKRKGSCPGAAPKKPKEPVQVPKLVIKGGIEVLGVKTGVDSFTEVECFLNPQMGNPDEHQKGLSKSLAAEKQFTDDSPDKEQLPCYSVARIPLPNINEDLTCGNILMWEAVTVKTEVIGVTAMLNLHSGTQKTHENGAGKPIQGSNFHFFAVGGEPLELQGVLANYRTKYPAQTVTPKNATVDSQQMNTDHKAVLDKDNAYPVECWVPDPSKNENTRYFGTYTGGENVPPVLHITNTATTVLLDEQGVGPLCKADSLYVSAVDICGLFTNTSGTQQWKGLPRYFKITLRKRSVKNPYPISFLLSDLINRRTQRVDGQ... | 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 ... | 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 c... | Simian virus 40 (SV40) |
P03089 | VP1_POVJC | MAPTKRKGERKDPVQVPKLLIRGGVEVLEVKTGVDSITEVECFLTPEMGDPDEHLRGFSKSISISDTFESDSPNRDMLPCYSVARIPLPNLNEDLTCGNILMWEAVTLKTEVIGVTSLMNVHSNGQATHDNGAGKPVQGTSFHFFSVGGEALELQGVLFNYRTKYPDGTIFPKNATVQSQVMNTEHKAYLDKNKAYPVECWVPDPTRNENTRYFGTLTGGENVPPVLHITNTATTVLLDEFGVGPLCKGDNLYLSAVDVCGMFTNRSGSQQWRGLSRYFKVQLRKRRVKNPYPISFLLTDLINRRTPRVDGQPMYGMDAQ... | 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... | JC polyomavirus (JCPyV) (JCV) |
P03093 | VP2_SV40 | MGAALTLLGDLIATVSEAAAATGFSVAEIAAGEAAAAIEVQLASVATVEGLTTSEAIAAIGLIPQAYAVISGAPAAIAGFAALLQTVTGVSAVAQVGYRFFSDWDHKVSTVGLYQQPGMAVDLYRPDDYYDILFPGVQTFVHSVQYLDPRHWGPTLFNAISQAFWRVIQNDIPRLTSQELERRTQRYLRDSLARFLEETTWTVINAPVNWYNSLQDYYSTLSPIRPTMVRQVANREGLQISFGHTYDNIDEADSIQQVTERWEAQSQSPNVQSGEFIEKFEAPGGANQRTAPQWMLPLLLGLYGSVTSALKAYEDGPNKK... | 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 ca... | 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... | Simian virus 40 (SV40) |
P03094 | VP2_POVBK | MGAALALLGDLVASVSEAAAATGFSVAEIAAGEAAAAIEVQIASLATVEGITSTSEAIAAIGLTPQTYAVIAGAPGAIAGFAALIQTVSGISSLAQVGYRFFSDWDHKVSTVGLYQQSGMALELFNPDEYYDILFPGVNTFVNNIQYLDPRHWGPSLFATISQALWHVIRDDIPSITSQELQRRTERFFRDSLARFLEETTWTIVNAPINFYNYIQQYYSDLSPIRPSMVRQVAEREGTRVHFGHTYSIDDADSIEEVTQRMDLRNQQSVHSGEFIEKTIAPGGANQRTAPQWMLPLLLGLYGTVTPALEAYEDGPNQKK... | 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 ... | 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 ret... | BK polyomavirus (BKPyV) (Human polyomavirus 1) |
P03095 | VP2_POVJC | MGAALALLGDLVATVSEAAAATGFSVAEIAAGEAAATIEVEIASLATVEGITSTSEAIAAIGLTPETYAVITGAPGAVAGFAALVQTVTGGSAIAQLGYRFFADWDHKVSTVGLFQQPAMALQLFNPEDYYDILFPGVNAFVNNIHYLDPRHWGPSLFSTISQAFWNLVRDDLPALTSQEIQRRTQKLFVESLARFLEETTWAIVNSPANLYNYISDYYSRLSPVRPSMVRQVAQREGTYISFGHSYTQSIDDADSIQEVTQRLDLKTPNVQSGEFIERSIAPGGANQRSAPQWMLPLLLGLYGTVTPALEAYEDGPNKK... | 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 ... | 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 ret... | 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 ret... | 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 ret... | Murine polyomavirus (strain A3) (MPyV) |
P03107 | VL2_HPV16 | MRHKRSAKRTKRASATQLYKTCKQAGTCPPDIIPKVEGKTIAEQILQYGSMGVFFGGLGIGTGSGTGGRTGYIPLGTRPPTATDTLAPVRPPLTVDPVGPSDPSIVSLVEETSFIDAGAPTSVPSIPPDVSGFSITTSTDTTPAILDINNTVTTVTTHNNPTFTDPSVLQPPTPAETGGHFTLSSSTISTHNYEEIPMDTFIVSTNPNTVTSSTPIPGSRPVARLGLYSRTTQQVKVVDPAFVTTPTKLITYDNPAYEGIDVDNTLYFSSNDNSINIAPDPDFLDIVALHRPALTSRRTGIRYSRIGNKQTLRTRSGKSI... | 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:... | 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 b... | Human papillomavirus type 16 |
P03116 | VE1_BPV1 | MANDKGSNWDSGLGCSYLLTEAECESDKENEEPGAGVELSVESDRYDSQDEDFVDNASVFQGNHLEVFQALEKKAGEEQILNLKRKVLGSSQNSSGSEASETPVKRRKSGAKRRLFAENEANRVLTPLQVQGEGEGRQELNEEQAISHLHLQLVKSKNATVFKLGLFKSLFLCSFHDITRLFKNDKTTNQQWVLAVFGLAEVFFEASFELLKKQCSFLQMQKRSHEGGTCAVYLICFNTAKSRETVRNLMANTLNVREECLMLQPAKIRGLSAALFWFKSSLSPATLKHGALPEWIRAQTTLNESLQTEKFDFGTMVQWA... | 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 ... | Bovine papillomavirus type 1 |
P03120 | VE2_HPV16 | METLCQRLNVCQDKILTHYENDSTDLRDHIDYWKHMRLECAIYYKAREMGFKHINHQVVPTLAVSKNKALQAIELQLTLETIYNSQYSNEKWTLQDVSLEVYLTAPTGCIKKHGYTVEVQFDGDICNTMHYTNWTHIYICEEASVTVVEGQVDYYGLYYVHEGIRTYFVQFKDDAEKYSKNKVWEVHAGGQVILCPTSVFSSNEVSSPEIIRQHLANHPAATHTKAVALGTEETQTTIQRPRSEPDTGNPCHTTKLLHRDSVDSAPILTAFNSSHKGRINCNSNTTPIVHLKGDANTLKCLRYRFKKHCTLYTAVSSTWH... | 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_0400... | 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 t... | Human papillomavirus type 16 |
P03122 | VE2_BPV1 | METACERLHVAQETQMQLIEKSSDKLQDHILYWTAVRTENTLLYAARKKGVTVLGHCRVPHSVVCQERAKQAIEMQLSLQELSKTEFGDEPWSLLDTSWDRYMSEPKRCFKKGARVVEVEFDGNASNTNWYTVYSNLYMRTEDGWQLAKAGADGTGLYYCTMAGAGRIYYSRFGDEAARFSTTGHYSVRDQDRVYAGVSSTSSDFRDRPDGVWVASEGPEGDPAGKEAEPAQPVSSLLGSPACGPIRAGLGWVRDGPRSHPYNFPAGSGGSILRSSSTPVQGTVPVDLASRQEEEEQSPDSTEEEPVTLPRRTTNDGFHL... | 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 t... | 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 cytoplas... | 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 the... | 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:0... | 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 ... | Human papillomavirus type 16 |
P03132 | REP68_AAV2S | MPGFYEIVIKVPSDLDGHLPGISDSFVNWVAEKEWELPPDSDMDLNLIEQAPLTVAEKLQRDFLTEWRRVSKAPEALFFVQFEKGESYFHMHVLVETTGVKSMVLGRFLSQIREKLIQRIYRGIEPTLPNWFAVTKTRNGAGGGNKVVDECYIPNYLLPKTQPELQWAWTNMEQYLSACLNLTERKRLVAQHLTHVSQTQEQNKENQNPNSDAPVIRSKTSARYMELVGWLVDKGITSEKQWIQEDQASYISFNAASNSRSQIKAALDNAGKIMSLTKTAPDYLVGQQPVEDISSNRIYKILELNGYDPQYAASVFLGWA... | 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 perturbatio... | 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... | Adeno-associated virus 2 (isolate Srivastava/1982) (AAV-2) |
P03134 | NS1_MUMIP | MAGNAYSDEVLGATNWLKEKSNQEVFSFVFKNENVQLNGKDIGWNSYKKELQEDELKSLQRGAETTWDQSEDMEWETTVDEMTKKQVFIFDSLVKKCLFEVLNTKNIFPGDVNWFVQHEWGKDQGWHCHVLIGGKDFSQAQGKWWRRQLNVYWSRWLVTACNVQLTPAERIKLREIAEDNEWVTLLTYKHKQTKKDYTKCVLFGNMIAYYFLTKKKISTSPPRDGGYFLSSDSGWKTNFLKEGERHLVSKLYTDDMRPETVETTVTTAQETKRGRIQTKKEVSIKTTLKELVHKRVTSPEDWMMMQPDSYIEMMAQPGGE... | 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... | Murine minute virus (strain MVM prototype) (MVM) (Murine minute virus (strain MVM(p))) |
P03138 | HBSAG_HBVD3 | MGQNLSTSNPLGFFPDHQLDPAFRANTANPDWDFNPNKDTWPDANKVGAGAFGLGFTPPHGGLLGWSPQAQGILQTLPANPPPASTNRQSGRQPTPLSPPLRNTHPQAMQWNSTTFHQTLQDPRVRGLYFPAGGSSSGTVNPVLTTASPLSSIFSRIGDPALNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQSPTSNHSPTSCPPTCPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRTCMTTAQGTSMYPSCCCTKPSDGNCTCIPIPSSWA... | 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 specifici... | Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D) |
P03139 | HBSAG_HBVD1 | MGQNLSTSNPLGFFPDHQLDPAFRANTNNPDWDFNPNKDTWPDANKVGAGAFGLGFTPPHGGLLGWSPQAQGIMQTLPANPPPASTNRQSGRQPTPLSPPLRTTHPQAMHWNSTTFHQTLQDPRVRGLYFPAGGSSSGTVNPVPTTTSPISSIFSRIGDPALNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQSPISNHSPTSCPPTCPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGSCRTCTTPAQGISMYPSCCCTKPSDGNCTCIPIPSSWA... | 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 specifici... | Hepatitis B virus genotype D subtype adw (isolate United Kingdom/adyw/1979) (HBV-D) |
P03140 | HBSAG_HBVC5 | MGGWSSKPRQGMGTNLSVPNPLGFFPDHQLDPAFGANSNNPDWDFNPNKDQWPEANQVGAGAFGPGFTPPHGGLLGWSPQAQGILTTVPAAPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTTFHQALLDPRVRGLYFPAGGSSSGTVNPVPTTASPISSIFSRTGDPAPNMENTTSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGAPTCPGQNSQSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLLPGTSTTSTGPCKTCTIPAQGTSMFPSCCCTKPSDGN... | 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 specifici... | Hepatitis B virus genotype C subtype ad (isolate Japan/S-179/1988) (HBV-C) |
P03141 | HBSAG_HBVA3 | MGGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPAFGANSNNPDWDFNPVKDDWPAANQVGVGAFGPRLTPPHGGILGWSPQAQGILTTVSTIPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTAFHQTLQDPRVRGLYLPAGGSSSGTVNPAPNIASHISSISARTGDPVTNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGSPVCLGQNSQSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSTTTSTGPCKTCTTPAQGNSMFPSCCCTKPTDGN... | 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 specifici... | Hepatitis B virus genotype A2 subtype adw2 (strain Rutter 1979) (HBV-A) |
P03142 | HBSAG_HBVA2 | MGTNLSVPNPLGFLPDHQLDPAFGANSTNPDWDFNPIKDHWPAANQVGVGAFGPGLTPPHGGILGWSPQAQGILTTVSTIPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTALHQALQDPRVRGLYLPAGGSSSGTVNPAPNIASHISSISARTGDPVTIMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGSPVCLGQNSQSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSTTTSTGPCKTCTTPAQGNSKFPSCCCTKPTDGNCTCIPIPSSWA... | 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 specifici... | Hepatitis B virus genotype A2 subtype adw (isolate Japan/Nishioka/1983) (HBV-A) |
P03145 | HBSAG_DHBV1 | MGQHPAKSMDVRRIEGGEILLNQLAGRMIPKGTLTWSGKFPTLDHVLDHVQTMEEINTLQNQGAWPAGAGRRVGLSNPTPQEIPQPQWTPEEDQKAREAFRRYQEERPPETTTIPPSSPPQWKLQPGDDPLLGNQSLLETHPLYQSEPAVPVIKTPPLKKKMSGTFGGILAGLIGLLVSFFLLIKILEILRRLDWWWISLSSPKGKMQCAFQDTGAQISPHYVGSCPWGCPGFLWTYLRLFIIFLLILLVAAGLLYLTDNGSTILGKLQWASVSALFSSISSLLPSDPKSLVALTFGLSLIWMTSSSATQTLVTLTQLAT... | 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... | 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 specifici... | 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. ... | 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 n... | 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. ... | 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 n... | 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 duri... | Ground squirrel hepatitis virus (strain 27) (GSHV) |
P03155 | DPOL_HBVD1 | MPLSYQRFRRLLLLDDEAGPLEEELPRLADEDLNRRVAEDLNLGNLNVSIPWTHKVGNFTGLYSSTVPVFNPHWKPPSFPNIHLHQDIIKKCEQFVGPLTVNEKRRLKLIMPARFYPNFTKYLPLDKGIKPYYPEHLVNHYFQTRHYLHTLWKAGVLYKRVSTHSASFCGSPYSWEQELQHGAESFHQQSSGILSRPPVGSSLQSKHQQSRLGLQSQQGHLARRQQGRSWSIRARVHPTARRPFGVEPSGSGHNANLASKSASCLYQSPVRTAAYPAVSTSENHSSSGHALELHNLPPNSARSQSERPVFPCWWLQFRDS... | 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... | 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... | Hepatitis B virus genotype D subtype adw (isolate United Kingdom/adyw/1979) (HBV-D) |
P03156 | DPOL_HBVD3 | MPLSYQHFRRLLLLDDEAGPLEEELPRLADEGLNRRVAEDLNLGNLNVSIPWTHKVGNFTGLYSSTVPVFNPHWKTPSFPNIHLHQDIIKKCEQFVGPLTVNEKRRLQLIMPARFYPKVTKYLPLDKGIKPYYPEHLVNHYFQTRHYLHTLWKAGILYKRETTHSASFCGSPYSWEQDLQHGAESFHQQSSGILSRPPVGSSLQSKHRKSRLGLQSQQGHLARRQQGRSWSIRAGFHPTARRPFGVEPSGSGHTTNFASKSASCLHQSPVRKAAYPAVSTFEKHSSSGHAVEFHNLPPNSARSQSERPVFPCWWLQFRNS... | 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'-d... | 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... | Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D) |
P03162 | DPOL_DHBV1 | MQKLTRNHWIGLGDCFGGITTVYCGEKLKLLTIFLVCVLGCQLLRNIEVEMPRPLKQSLDQSRWLREAEKQLRVLENLVDSNLEEEKLKPQLSMGEDVQSPGKGEPLHPNVRAPLSHVVRAATIDLPRLGNKLPARHHLGKLSGLYQMKGCTFNPEWKVPDISDTHFNLDVVNECPSRNWKYLTPAKFWPKSISYFPVQVGVKPKYPDNVMQHESIVGKYLTRLYEAGILYKRISKHLVTFKGQPYNWEQQHLVNQHHIYDGATSSKINGRQTDRRRRNTVKPTCRKDDPKRDFDMVRQVSNTRSRVRPCANNGGDKHPP... | 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... | 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... | 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.... | 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 o... | Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D) |
P03169 | VIE1_HCMVT | MESSAKRKMDPDNPDEGPSSKVPRPETPVTKATTFLQTMLRKEVNSQLSLGDPLFPELAEESLKTFERVTEDCNENPEKDVLAELVKQIKVRVDMVRHRIKEHMLKKYTQTEEKFTGAFNMMGGCLQNALDILDKVHEPFEEMKCIGLTMQSMYENYIVPEDKREMWMACIKELHDVSKGAANKLGGALQAKARAKKDELRRKMMYMCYRNIEFFTKNSAFPKTTNGCSQAMAALQNLPQCSPDEIMAYAQKIFKILDEERDKVLTHIDHIFMDILTTCVETMCNEYKVTSDACMMTMYGGISLLSEFCRVLSCYVLEET... | 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 ... | 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 endopla... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P03172 | GD_HHV23 | MGRLTSGVGTAALLVVAVGLRVVCAKYALADPSLKMADPNRFRGKNLPVLDRLTDPPGVKRVYHIQPSLEDPFQPPSIPITVYYAVLERACRSVLLHAPSEAPQIVRGASDEARKHTYNLTIAWYRMGDNCAIPITVMEYTECPYNKSLGVCPIRTQPRWSYYDSFSAVSEDNLGFLMHAPAFETAGTYLRLVKINDWTEITQFILEHRARASCKYALPLRIPPAACLTSKAYQQGVTVDSIGMLPRFIPENQRTVALYSLKIAGWHGPKPPYTSTLLPPELSDTTNATQPELVPEDPEDSALLEDPAGTVSSQIPPNWH... | 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 | MSNGDWGQSQRTRGTGPVRGIRTMDVNAPGGGSGGSALRILGTASCNQAHCKFGRFAGIQCVSNCVLYLVKSFLAGRPLTSRPELDEVLDEGARLDALMRQSGILKGHEMAQLTDVPSSVVLRGGGRVHIYRSAEIFGLVLFPAQIANSAVVQSLAEVLHGSYNGVAQFILYICDIYAGAIIIETDGSFYLFDPHCQKDAAPGTPAHVRVSTYAHDILQYVGAPGAQYTCVHLYFLPEAFETEDPRIFMLEHYGVYDFYEANGSGFDLVGPELVSSDGEAAGTPGADSSPPVMLPFERRIIPYNLRPLPSRSFTSDSFPA... | 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:00002... | 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:201907... | 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 subsequ... | Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) |
P03188 | GB_EBVB9 | MTRRRVLSVVVLLAALACRLGAQTPEQPAPPATTVQPTATRQQTSFPFRVCELSSHGDLFRFSSDIQCPSFGTRENHTEGLLMVFKDNIIPYSFKVRSYTKIVTNILIYNGWYADSVTNRHEEKFSVDSYETDQMDTIYQCYNAVKMTKDGLTRVYVDRDGVNITVNLKPTGGLANGVRRYASQTELYDAPGWLIWTYRTRTTVNCLITDMMAKSNSPFDFFVTTTGQTVEMSPFYDGKNKETFHERADSFHVRTNYKIVDYDNRGTNPQGERRAFLDKGTYTLSWKLENRTAYCPLQHWQTFDSTIATETGKSIHFVTD... | 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_0... | 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 hos... | Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) |
P03191 | EAD_EBVB9 | METTQTLRFKTKALAVLSKCYDHAQTHLKGGVLQVNLLSVNYGGPRLAAVANAGTAGLISFEVSPDAVAEWQNHQSPEEAPAAVSFRNLAYGRTCVLGKELFGSAVEQASLQFYKRPQGGSRPEFVKLTMEYDDKVSKSHHTCALMPYMPPASDRLRNEQMIGQVLLMPKTASSLQKWARQQGSGGVKVTLNPDLYVTTYTSGEACLTLDYKPLSVGPYEAFTGPVAKAQDVGAVEAHVVCSVAADSLAAALSLCRIPAVSVPILRFYRSGIIAVVAGLLTSAGDLPLDLSVILFNHASEEAAASTASEPEDKSPRVQPL... | 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 a... | Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) |
P03200 | GP350_EBVB9 | MEAALLVCQYTIQSLIHLTGEDPGFFNVEIPEFPFYPTCNVCTADVNVTINFDVGGKKHQLDLDFGQLTPHTKAVYQPRGAFGGSENATNLFLLELLGAGELALTMRSKKLPINVTTGEEQQVSLESVDVYFQDVFGTMWCHHAEMQNPVYLIPETVPYIKWDNCNSTNITAVVRAQGLDVTLPLSLPTSAQDSNFSVKTEMLGNEIDIECIMEDGEISQVLPGDNKFNITCSGYESHVPSGGILTSTSPVATPIPGTGYAYSLRLTPRPVSRFLGNNSILYVFYSGNGPKASGGDYCIQSNIVFSDEIPASQDMPTNTT... | 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 h... | 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, ha... | 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 ... | 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:153618... | 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 inte... | 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 co... | Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) |
P03211 | EBNA1_EBVB9 | MSDEGPGTGPGNGLGEKGDTSGPEGSGGSGPQRRGGDNHGRGRGRGRGRGGGRPGAPGGSGSGPRHRDGVRRPQKRPSCIGCKGTHGGTGAGAGAGGAGAGGAGAGGGAGAGGGAGGAGGAGGAGAGGGAGAGGGAGGAGGAGAGGGAGAGGGAGGAGAGGGAGGAGGAGAGGGAGAGGGAGGAGAGGGAGGAGGAGAGGGAGAGGAGGAGGAGAGGAGAGGGAGGAGGAGAGGAGAGGAGAGGAGAGGAGGAGAGGAGGAGAGGAGGAGAGGGAGGAGAGGGAGGAGAGGAGGAGAGGAGGAGAGGAGGAGAGGGAGAG... | 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 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 vir... | Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) |
P03230 | LMP1_EBVB9 | MEHDLERGPPGPRRPPRGPPLSSSLGLALLLLLLALLFWLYIVMSDWTGGALLVLYSFALMLIIIILIIFIFRRDLLCPLGALCILLLMITLLLIALWNLHGQALFLGIVLFIFGCLLVLGIWIYLLEMLWRLGATIWQLLAFFLAFFLDLILLIIALYLQQNWWTLLVDLLWLLLFLAILIWMYYHGQRHSDEHHHDDSLPHPQQATDDSGHESDSNSNEGRHHLLVSGAGDGPPLCSQNLGAPGGGPDNGPQDPDNTDDNGPQDPDNTDDNGPHDPLPQDPDNTDDNGPQDPDNTDDNGPHDPLPHSPSDSAGNDGGP... | 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 ... | 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-re... | Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) |
P03231 | GH_EBVB9 | MQLLCVFCLVLLWEVGAASLSEVKLHLDIEGHASHYTIPWTELMAKVPGLSPEALWREANVTEDLASMLNRYKLIYKTSGTLGIALAEPVDIPAVSEGSMQVDASKVHPGVISGLNSPACMLSAPLEKQLFYYIGTMLPNTRPHSYVFYQLRCHLSYVALSINGDKFQYTGAMTSKFLMGTYKRVTEKGDEHVLSLVFGKTKDLPDLRGPFSYPSLTSAQSGDYSLVIVTTFVHYANFHNYFVPNLKDMFSRAVTMTAASYARYVLQKLVLLEMKGGCREPELDTETLTTMFEVSVAFFKVGHAVGETGNGCVDLRWLAK... | 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_0... | 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 th... | Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) |
P03234 | SCAF_EBVB9 | MVQAPSVYVCGFVERPDAPPKDACLHLDPLTVKSQLPLKKPLPLTVEHLPDAPVGSVFGLYQSRAGLFSAASITSGDFLSLLDSIYHDCDIAQSQRLPLPREPKVEALHAWLPSLSLASLHPDIPQTTADGGKLSFFDHVSICALGRRRGTTAVYGTDLAWVLKHFSDLEPSIAAQIENDANAAKRESGCPEDHPLPLTKLIAKAIDAGFLRNRVETLRQDRGVANIPAESYLKASDAPDLQKPDKALQSPPPASTDPATMLSGNAGEGATACGGSAAAGQDLISVPRNTFMTLLQTNLDNKPPRQTPLPYAAPLPPFSH... | 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 ... | 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 s... | 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 th... | Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2) |
P03243 | E1B55_ADE05 | MERRNPSERGVPAGFSGHASVESGCETQESPATVVFRPPGDNTDGGAAAAAGGSQAAAAGAEPMEPESRPGPSGMNVVQVAELYPELRRILTITEDGQGLKGVKRERGACEATEEARNLAFSLMTRHRPECITFQQIKDNCANELDLLAQKYSIEQLTTYWLQPGDDFEEAIRVYAKVALRPDCKYKISKLVNIRNCCYISGNGAEVEIDTEDRVAFRCSMINMWPGVLGMDGVVIMNVRFTGPNFSGTVFLANTNLILHGVSFYGFNNTCVEAWTDVRVRGCAFYCCWKGVVCRPKSRASIKKCLFERCTLGILSEGNS... | 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:0... | 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 ... | Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5) |
P03244 | E1B55_ADE02 | MERRNPSERGVPAGFSGHASVESGGETQESPATVVFRPPGNNTDGGATAGGSQAAAAAGAEPMEPESRPGPSGMNVVQVAELFPELRRILTINEDGQGLKGVKRERGASEATEEARNLTFSLMTRHRPECVTFQQIKDNCANELDLLAQKYSIEQLTTYWLQPGDDFEEAIRVYAKVALRPDCKYKISKLVNIRNCCYISGNGAEVEIDTEDRVAFRCSMINMWPGVLGMDGVVIMNVRFTGPNFSGTVFLANTNLILHGVSFYGFNNTCVEAWTDVRVRGCAFYCCWKGVVCRPKSRASIKKCLFERCTLGILSEGNSR... | 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 proteas... | 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 ... | 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 expres... | 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... | 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 pe... | 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... | 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:00395... | 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... | Human adenovirus A serotype 12 (HAdV-12) (Human adenovirus 12) |
P03264 | DNB2_ADE02 | MASREEEQRETTPERGRGAARRPPTMEDVSSPSPSPPPPRAPPKKRLRRRLESEDEEDSSQDALVPRTPSPRPSTSTADLAIASKKKKKRPSPKPERPPSPEVIVDSEEEREDVALQMVGFSNPPVLIKHGKGGKRTVRRLNEDDPVARGMRTQEEKEESSEAESESTVINPLSLPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHVIEMDVTSENGQRALKEQSSKAKIV... | 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... | Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2) |
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