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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O89039 | ACKR3_RAT | MDVHLFDYVEPGNYSDINWPCNSSDCIVVDTVQCPAMPNKNVLLYTLSFIYIFIFVIGMIANSVVVWVNIQAKTTGYDTHCYILNLAIADLWVVITIPVWVVSLVQHNQWPMGELTCKITHLIFSINLFGSIFFLACMSVDRYLSITYFTSTSSYKKKMVRRVVCVLVWLLAFFVSLPDTYYLKTVTSASNNETYCRSFYPEHSIKEWLIGMELVSVILGFAVPFTIIAIFYFLLARAMSASGDQEKHSSRKIIFSYVVVFLVCWLPYHFVVLLDIFSILHYIPFTCQLENVLFTALHVTQCLSLVHCCVNPVLYSFINR... | null | null | angiogenesis [GO:0001525]; calcium-mediated signaling [GO:0019722]; cell adhesion [GO:0007155]; cell chemotaxis [GO:0060326]; chemokine-mediated signaling pathway [GO:0070098]; immune response [GO:0006955]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of intrinsic apoptotic sig... | cell surface [GO:0009986]; clathrin-coated pit [GO:0005905]; early endosome [GO:0005769]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037] | C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; C-X-C chemokine binding [GO:0019958]; C-X-C chemokine receptor activity [GO:0016494]; coreceptor activity [GO:0015026]; scavenger receptor activity [GO:0005044] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Atypical chemokine receptor subfamily | PTM: The Ser/Thr residues in the C-terminal cytoplasmic tail may be phosphorylated. {ECO:0000250|UniProtKB:P25106}.; PTM: Ubiquitinated at the Lys residues in its C-terminal cytoplasmic tail and is essential for correct trafficking from and to the cell membrane. Deubiquitinated by CXCL12-stimulation in a reversible man... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21655198}; Multi-pass membrane protein {ECO:0000269|PubMed:21655198}. Early endosome {ECO:0000305|PubMed:21655198}. Recycling endosome {ECO:0000305|PubMed:21655198}. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internal... | null | null | null | null | null | FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing recept... | Rattus norvegicus (Rat) |
O89040 | PLCB2_RAT | MSLLNPVLLPPKVKAYLSQGERFIKWDDETSIASPVILRVDPKGYYLYWTHQSKEMEFLDVTSIRDTRFGKFAKIPKSQKLREVFNMDFPDNHFLLKTFTVVSGPDMVGLTFHNFVSYKENVGKDWAEDVLALAKHPMTANASRSTFLDKILVKLKMQLSPEGKIPVKNFFQMFPADRKRVEAALSACHLAKGKNDAINPEDFPESVYKSFLMSLCPRPEIDEIFTSYHAKAKPYMTKEHLTKFINQKQRDPRLNSLLFPPARPEQVQALIDKYEPSGINVQRGQLSPEGMVWFLCGPENSVLAHDTLRIHQDMTQPLNH... | 3.1.4.11 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q00722}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q00722}; | detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]; G protein-coupled receptor signaling pathway [GO:0007186]; lipid catabolic process [GO:0016042]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol-mediated signaling [GO:0048015]; phospholipase C-activati... | cytoplasm [GO:0005737]; G-protein beta/gamma-subunit complex [GO:0031680]; neuronal dense core vesicle [GO:0098992] | calcium ion binding [GO:0005509]; G-protein beta/gamma-subunit complex binding [GO:0031683]; phosphatidylinositol phospholipase C activity [GO:0004435]; phospholipase C activity [GO:0004629]; phospholipid binding [GO:0005543] | PF00168;PF09279;PF17787;PF00388;PF00387;PF08703; | 2.30.29.240;2.60.40.150;1.10.238.10;3.20.20.190;1.20.1230.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={EC... | null | null | null | null | FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This protein may be involved in the transduction of bitter taste stimuli. {ECO:0000250|UniProtKB:Q00722, ECO:0000303|PubM... | Rattus norvegicus (Rat) |
O89042 | DPOLA_RAT | MAPVHGDDCKLETSAVSDSGSFVASRARREKKSKKGRQEALERLKKAKAGEKYKYEVEDLTSVYEEVDEEQYSKLVQARQDDDWIVDDDGIGYVEDGREIFDDDLEDDALDTCGEGSDGKAHRKDRKDVKKPSVTKPNNIKAMFIASAGKKTTDKTVDLSKDDLLGDILQDLNTETPQIAPPPVLIPKKKRSTGASPNPFSVHTATAVPSGKIASPVSRKEPPLTPVPLKRAEFAGDLAQPECPEDEQESGVIEFEDGDFDEPMDTEEVDEEEPVTAKIWDQESEPVEGVKHEADPETGTTSFLDSFLPDVSCWDIDQKD... | 2.7.7.7 | null | DNA biosynthetic process [GO:0071897]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; DNA replication, synthesis of RNA primer [GO:0006269]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA synthesis involved in DNA repair [GO:0000731]; double-strand b... | alpha DNA polymerase:primase complex [GO:0005658]; chromatin [GO:0000785]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA replication origin binding [GO:0003688]; DNA-directed DNA polymerase activity [GO:0003887]; double-stranded DNA binding [GO:0003690]; nucleotide binding [GO:0000166]; protein kinase binding [GO:0019901]; purine nucleotide binding [GO:0017076]; pyrimidine nuc... | PF12254;PF00136;PF03104;PF08996; | 2.40.50.730;3.30.70.2820;1.10.3200.20;1.10.132.60;1.10.287.690;3.90.1600.10;3.30.420.10; | DNA polymerase type-B family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09884}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P09884}. Note=In the cytosol, colocalizes with RNA:DNA hybrids with a speckled pattern. {ECO:0000250|UniProtKB:P09884}. | 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:0000269|PubMed:10541966}; PhysiologicalDirection=left-to-right; X... | null | null | null | null | FUNCTION: Catalytic subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis (PubMed:10541966). During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, a re... | Rattus norvegicus (Rat) |
O89046 | COR1B_RAT | MSFRKVVRQSKFRHVFGQPVKNDQCYEDIRVSRVTWDSTFCAVNPKFLAVIVEASGGGAFMVLPLNKTGRIDKAYPTVCGHTGPVLDIDWCPHNDEVIASGSEDCTVMVWQIPENGLTSPLTEPVVVLEGHTKRVGIITWHPTARNVLLSAGCDNVVLIWNVGTAEELYRLDSLHPDLIYNVSWNHNGSLFCTACKDKSVRIIDPRRGTLVAEREKAHEGARPMRAIFLADGKVFTAGFSRMSERQLALWDPENFEEPMALQELDSSNGALLPFYDPDTSVVYVCGKGDSSIRYFEITDEPPYIHFLNTFTSKEPQRGMG... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament branching [GO:0090135]; actin filament bundle assembly [GO:0051017]; actin filament organization [GO:0007015]; cell migration [GO:0016477]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; endothelial cell chemotaxis [GO:0035767]; ne... | actin filament [GO:0005884]; cell leading edge [GO:0031252]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; lamellipodium [GO:0030027]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; stress fiber [GO:0001725] | actin filament binding [GO:0051015]; Arp2/3 complex binding [GO:0071933]; cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877] | PF08953;PF00400;PF16300; | 2.130.10.10; | WD repeat coronin family | PTM: Phosphorylation on Ser-2 regulates the interaction with the Arp2/3 complex and cell motility in fibroblasts. Phosphorylation does not seem to affect subcellular location (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9BR76}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q9BR76}. Note=Localized to the leading edge in fibroblasts, as well as weakly along actin stress fibers. {ECO:0000250|UniProtKB:Q9BR76}. | null | null | null | null | null | FUNCTION: Regulates leading edge dynamics and cell motility in fibroblasts. May be involved in cytokinesis and signal transduction (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
O89047 | KCNH3_RAT | MPAMRGLLAPQNTFLDTIATRFDGTHSNFVLGNAQVAGLFPVVYCSDGFCDLTGFSRAEVMQRGCACSFLYGPDTSELVRQQIRKALDEHKEFKAELILYRKSGLPFWCLLDVIPIKNEKGEVALFLVSHKDISETKNRGGPDNWKERGGGRRRYGRAGSKGFNANRRRSRAVLYHLSGHLQKQPKGKHKLNKGVFGEKPNLPEYKVAAIRKSPFILLHCGALRATWDGFILLATLYVAVTVPYSVCVSTAREPSAARGPPSVCDLAVEVLFILDIVLNFRTTFVSKSGQVVFAPKSICLHYVTTWFLLDVIAALPFDLL... | null | null | potassium ion transmembrane transport [GO:0071805]; regulation of membrane potential [GO:0042391] | monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886] | voltage-gated potassium channel activity [GO:0005249] | PF00027;PF00520;PF13426; | 1.10.1200.260;1.10.287.70;2.60.120.10;3.30.450.20; | Potassium channel family, H (Eag) (TC 1.A.1.20) subfamily, Kv12.2/KCNH3 sub-subfamily | null | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits an outward current with fast inactivation. Channel properties may be modulated by cAMP and subunit assembly. | Rattus norvegicus (Rat) |
O89049 | TRXR1_RAT | MNDSKDAPKSYDFDLIIIGGGSGGLAAAKEAAKFDKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKLEDTVKHDWEKMTESVQNHIGSLNWGYRVALREKKVVYENAYGKFIGPHKIMATNNKGKEKVYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQIEAGTPGRLKVTAKSTNSEETIEDEFNTVLLAVGRDSCTRTIGLETVGVKINEKTGKIPVTD... | 1.11.1.2; 1.8.1.9 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:10849437, ECO:0000269|PubMed:11481439}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11481439}; | benzene-containing compound metabolic process [GO:0042537]; cell population proliferation [GO:0008283]; cell redox homeostasis [GO:0045454]; cellular response to copper ion [GO:0071280]; cellular response to hyperoxia [GO:0071455]; cellular response to oxidative stress [GO:0034599]; gastrulation [GO:0007369]; glutathio... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleus [GO:0005634] | FAD binding [GO:0071949]; glutathione-disulfide reductase (NADP) activity [GO:0004362]; identical protein binding [GO:0042802]; mercury ion binding [GO:0045340]; NAD(P)H oxidase H2O2-forming activity [GO:0016174]; NADPH peroxidase activity [GO:0050137]; selenate reductase activity [GO:0033797]; thioredoxin-disulfide re... | PF07992;PF02852; | 3.30.390.30;3.50.50.60; | Class-I pyridine nucleotide-disulfide oxidoreductase family | PTM: ISGylated. {ECO:0000250|UniProtKB:Q16881}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16881}. | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9; Evidence={ECO:0000269|PubMed:10849437}; Phys... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.3 uM for thioredoxin {ECO:0000269|PubMed:10849437}; Note=kcat is 2500 min(-1) with thioredoxin as substrate. {ECO:0000269|PubMed:10849437}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:10849437}; | null | FUNCTION: Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form. Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis (PubMed:10849437). Also has re... | Rattus norvegicus (Rat) |
O89050 | MKLN1_MOUSE | MAAGGAVAVAPECRLLPYALHKWSSFSSTYLPENILVDKPNDQSSRWSSESNYPPQYLILKLERPAIVQNITFGKYEKTHVCNLKKFKVFGGMNEENMTELLSSGLKNDYNKETFTLKHKIDEQMFPCRFIKIVPLLSWGPSFNFSIWYVELSGIDDPDIVQPCLNWYSKYREQEAIRLCLKHFRQHNYTEAFESLQKKTKIALEHPMLTDMHDKLVLKGDFDACEELIEKAVNDGLFNQYISQQEYKPRWSQIIPKSTKGDGEDNRPGMRGGHQMVIDVQTETVYLFGGWDGTQDLADFWAYSVKENQWTCISRDTEKE... | null | null | actin cytoskeleton organization [GO:0030036]; cell-matrix adhesion [GO:0007160]; regulation of cell shape [GO:0008360]; regulation of receptor internalization [GO:0002090] | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; postsynapse [GO:0098794]; ruffle [GO:0001726]; ubiquitin ligase complex [GO:0000151] | identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF01344;PF13415;PF06588; | 2.60.120.260;2.120.10.80; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9724633}. Cytoplasm, cytosol {ECO:0000269|PubMed:18710924}. Nucleus, nucleoplasm {ECO:0000269|PubMed:18710924}. Cell projection, ruffle {ECO:0000269|PubMed:9724633}. Cytoplasm, cell cortex {ECO:0000269|PubMed:9724633}. Synapse {ECO:0000269|PubMed:21482357}. Postsynaps... | null | null | null | null | null | FUNCTION: Component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (By similarity). Required for internalization of the GABA receptor GABRA1 from the cell membrane via endos... | Mus musculus (Mouse) |
O89051 | ITM2B_MOUSE | MVKVTFNSALAQKEAKKDEPKSSEEALIVPPDAVAVDCKDPGDVVPVGQRRAWCWCMCFGLAFMLAGVILGGAYLYKYFALQPDDVYYCGLKYIKDDVILNEPSADAPAARYQTIEENIKIFEEDAVEFISVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLNTSIVMPPKNLLELLINIKAGTYLPQSYLIHEHMVITDRIENVDNLGFFIYRLCHDKETYKLQRRETIRGIQKREASNCFTIRHFENKFAVETLICS | null | null | negative regulation of amyloid precursor protein biosynthetic process [GO:0042985] | endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi-associated vesicle membrane [GO:0030660]; organelle membrane [GO:0031090]; plasma membrane [GO:0005886] | amyloid-beta binding [GO:0001540]; ATP binding [GO:0005524] | PF04089; | null | ITM2 family | PTM: The ectodomain C-terminal part of the imBRI2 is processed by furin producing a secreted Bri23 peptide and a mature BRI2, membrane form (mBRI2). The remaining part of the ectodomain of mBRI2 containing the BRICHOS domain is cleaved by ADAM10 and is secreted (BRI2C, soluble form). The membrane-bound N-terminal fragm... | SUBCELLULAR LOCATION: [Integral membrane protein 2B]: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y287}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Y287}. Note=Immature BRI2 (imBRI2) is cleaved by furin in the Golgi into mBRI2 and a Bri23 peptide. mBRI2 is transported to the plasma membrane and... | null | null | null | null | null | FUNCTION: Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleava... | Mus musculus (Mouse) |
O89053 | COR1A_MOUSE | MSRQVVRSSKFRHVFGQPAKADQCYEDVRVSQTTWDSGFCAVNPKFMALICEASGGGAFLVLPLGKTGRVDKNVPLVCGHTAPVLDIAWCPHNDNVIASGSEDCTVMVWEIPDGGLVLPLREPVITLEGHTKRVGIVAWHPTAQNVLLSAGCDNVILVWDVGTGAAVLTLGPDVHPDTIYSVDWSRDGALICTSCRDKRVRVIEPRKGTVVAEKDRPHEGTRPVHAVFVSEGKILTTGFSRMSERQVALWDTKHLEEPLSLQELDTSSGVLLPFFDPDTNIVYLCGKGDSSIRYFEITSEAPFLHYLSMFSSKESQRGMG... | null | null | actin filament organization [GO:0007015]; calcium ion transport [GO:0006816]; cell migration [GO:0016477]; cell-substrate adhesion [GO:0031589]; cellular response to interleukin-4 [GO:0071353]; early endosome to recycling endosome transport [GO:0061502]; epithelial cell migration [GO:0010631]; establishment of localiza... | actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; axon [GO:0030424]; cell leading edge [GO:0031252]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; early endosome [GO:0005769]; glutamatergic synapse [GO:0098978]; immunological synapse [GO:0001772]; lamellipodium [GO:0030027]; pha... | actin filament binding [GO:0051015]; actin monomer binding [GO:0003785]; cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]; myosin heavy chain binding [GO:0032036]; phosphatidylinositol 3-kinase binding [GO:0043548]; protein homodimerization activity [GO:0042803] | PF08953;PF08954;PF00400;PF16300; | 2.130.10.10; | WD repeat coronin family | PTM: phosphorylation at Ser-412 by PKC strongly down-regulates the association with actin. {ECO:0000250}.; PTM: Polyubiquitinated by RNF128 with 'Lys-48'-linked chains, leading to proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10338208}. Cytoplasm, cell cortex {ECO:0000269|PubMed:10338208}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:10338208}. Note=In non-infected macrophages, associated with the cortical microtubule network. In mycobacteria-infected macrophag... | null | null | null | null | null | FUNCTION: May be a crucial component of the cytoskeleton of highly motile cells, functioning both in the invagination of large pieces of plasma membrane, as well as in forming protrusions of the plasma membrane involved in cell locomotion. In mycobacteria-infected cells, its retention on the phagosomal membrane prevent... | Mus musculus (Mouse) |
O89084 | PDE4A_MOUSE | MEPPAAPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYSDSAERSEPERSPHRPIERADAVDTGDRPGLRTTRMSWPSSFHGTGTGGGSSRRLEAENGPTPSPGRSPLDSQASPGLMLHAGAATSQRRESFLYRSDSDYDMSPKTMSRNSSVASEAHGEDLIVTPFAQVLASLRNVRSNFSLLTNVPIPSNKRSPLGGPPSVCKATLSEETCQQLARETLEELDWCLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQHEVEIPSPTPRQRPFQQPPPAAVQQAQPMS... | 3.1.4.53 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P27815}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions. {ECO:0000250|UniProtKB:P27815}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P27815}; Name=Mn(2+); Xref=ChE... | cAMP catabolic process [GO:0006198]; cAMP-mediated signaling [GO:0019933]; cellular response to xenobiotic stimulus [GO:0071466]; modulation of chemical synaptic transmission [GO:0050804]; regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106070]; regulation of protein kinase ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; Schaffer collateral - CA1 synapse [GO:0098685] | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; cAMP binding [GO:0030552]; metal ion binding [GO:0046872] | PF18100;PF00233; | 1.10.1300.10; | Cyclic nucleotide phosphodiesterase family, PDE4 subfamily | PTM: Proteolytically cleaved by CASP3. {ECO:0000250|UniProtKB:P27815}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P27815}. Membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:P27815}. | CATALYTIC ACTIVITY: [Isoform 2]: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; EC=3.1.4.53; Evidence={ECO:0000269|PubMed:11267656}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278; Evidence={ECO:0000305|PubMed:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.2 uM for cAMP {ECO:0000269|PubMed:11267656}; Vmax=37.9 nmol/min/mg enzyme toward cAMP {ECO:0000269|PubMed:11267656}; | PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. {ECO:0000305|PubMed:11267656}. | null | null | FUNCTION: Hydrolyzes the second messenger 3',5'-cyclic AMP (cAMP), which is a key regulator of many important physiological processes. {ECO:0000269|PubMed:11267656}.; FUNCTION: [Isoform 2]: Efficiently hydrolyzes cAMP. {ECO:0000269|PubMed:11267656}. | Mus musculus (Mouse) |
O89086 | RBM3_MOUSE | MSSEEGKLFVGGLNFNTDEQALEDHFSSFGPISEVVVVKDRETQRSRGFGFITFTNPEHASDAMRAMNGESLDGRQIRVDHAGKSARGSRGGAFGGRGRSYSRGGGDQGYGSGRYDSRPGGYGYGYGRSRDYSGSQGGYDRYSGGNYRDNYDN | null | null | miRNA processing [GO:0035196]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; positive regulation of translation [GO:0045727]; regulation of translation [GO:0006417]; response to cold [GO:0009409]; translation [GO:0006412] | cytoplasm [GO:0005737]; dendrite [GO:0030425]; large ribosomal subunit [GO:0015934]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681] | ribosomal large subunit binding [GO:0043023]; RNA binding [GO:0003723] | PF00076; | 3.30.70.330; | null | PTM: Arg-103 is dimethylated, probably to asymmetric dimethylarginine. {ECO:0000250}.; PTM: Phosphorylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Localizes in mRNA granules in dentrites. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Cold-inducible mRNA binding protein that enhances global protein synthesis at both physiological and mild hypothermic temperatures. Reduces the relative abundance of microRNAs, when overexpressed. Enhances phosphorylation of translation initiation factors and active polysome formation. {ECO:0000269|PubMed:156... | Mus musculus (Mouse) |
O89090 | SP1_MOUSE | MSDQDHSMDEVTAVVKIEKDVGGNNGGSGNGGGAAFSQTRSSSTGSSSSSGGGGGQESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTSKEQSGNSTNGSNGSESSKNRTVSGGQYVVAATPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQIIPNRGSGGNIIAAMPNLLQQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAGTISSSGSQESSSQPVTSGTAISSASLVSSQASSS... | null | null | cellular response to insulin stimulus [GO:0032869]; definitive hemopoiesis [GO:0060216]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic placenta development [GO:0001892]; embryonic process involved in female pregnancy [GO:0060136]; embryonic skeletal system development [GO:0048706]; enucleate erythrocy... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993] | bHLH transcription factor binding [GO:0043425]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; 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 acti... | PF00096; | 3.30.160.60; | Sp1 C2H2-type zinc-finger protein family | PTM: Phosphorylated on multiple serine and threonine residues. Phosphorylation is coupled to ubiquitination, sumoylation and proteolytic processing. Phosphorylation on Ser-61 enhances proteolytic cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein degradation. Hyperphosphorylation on Ser-103 in respo... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27918959}. Cytoplasm {ECO:0000250}. Note=Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immun... | Mus musculus (Mouse) |
O89091 | KLF10_MOUSE | MLNFGASLQQASEGKMELISEKPREGMHPWDKAEQSDFEAVEALMSMSCDWKSHFKKYLENRPVTPVSDTSEDDSLLPGTPDLQTVPAFCLTPPYSPSDFEPSQGSNLTASAPSTGHFKSFSDAAKPPGATPFKEEEKNPLAAPPLPKAQATSVIRHTADAQLCNHQSCPVKAASILNYQDNSFRRRTHGNVEATRKNIPCAAVSPNRSKPEPSTVSDGDEKAGAALYDFAVPSSETVICRSQPAPSSPVQKSVLVSSPTVSTGGVPPLPVICQMVPLPANNSLVSTVVPSTPPSQPPAVCSPVLFMGTQVPEGTVVFVV... | null | null | bone mineralization [GO:0030282]; cellular response to starvation [GO:0009267]; circadian rhythm [GO:0007623]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of osteoclast differentiation [GO:0045672]; regulation of circadian rhythm [GO:0042752]; regulation of DNA-templated transcr... | nucleus [GO:0005634] | core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory ... | PF00096; | 3.30.160.60; | Sp1 C2H2-type zinc-finger protein family | PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation. {ECO:0000250|UniProtKB:Q13118}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20070857}. | null | null | null | null | null | FUNCTION: Transcriptional repressor which binds to the consensus sequence 5'-GGTGTG-3'. May play a role in the cell cycle regulation (By similarity). Plays a role in the regulation of the circadian clock; binds to the GC box sequence in the promoter of the core clock component ARTNL/BMAL1 and represses its transcriptio... | Mus musculus (Mouse) |
O89093 | CCL20_MOUSE | MACGGKRLLFLALAWVLLAHLCSQAEAASNYDCCLSYIQTPLPSRAIVGFTRQMADEACDINAIIFHTKKRKSVCADPKQNWVKRAVNLLSLRVKKM | null | null | calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell chemotaxis [GO:0060326]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO:0070098]; che... | extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; CCR6 chemokine receptor binding [GO:0031731]; chemokine activity [GO:0008009]; cytokine activity [GO:0005125] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P78556}. | null | null | null | null | null | FUNCTION: Acts as a ligand for C-C chemokine receptor CCR6. Signals through binding and activation of CCR6 and induces a strong chemotactic response and mobilization of intracellular calcium ions (PubMed:20068036, PubMed:9862452). The ligand-receptor pair CCL20-CCR6 is responsible for the chemotaxis of dendritic cells ... | Mus musculus (Mouse) |
O89094 | CASPE_MOUSE | MESEMSDPQPLQEERYDMSGARLALTLCVTKAREGSEVDMEALERMFRYLKFESTMKRDPTAQQFLEELDEFQQTIDNWEEPVSCAFVVLMAHGEEGLLKGEDEKMVRLEDLFEVLNNKNCKALRGKPKVYIIQACRGEHRDPGEELRGNEELGGDEELGGDEVAVLKNNPQSIPTYTDTLHIYSTVEGYLSYRHDEKGSGFIQTLTDVFIHKKGSILELTEEITRLMANTEVMQEGKPRKVNPEVQSTLRKKLYLQ | 3.4.22.- | null | cell differentiation [GO:0030154]; positive regulation of neuron apoptotic process [GO:0043525]; proteolysis [GO:0006508] | cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; keratin filament [GO:0045095]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | cysteine-type endopeptidase activity [GO:0004197]; peptidase activity [GO:0008233] | PF00656; | 3.40.50.1460; | Peptidase C14A family | PTM: Maturation by proteolytic processing appears to be a two-step process. The precursor is processed by KLK7 to yield the p20/p8 intermediate form which acts the precursor to yield the p17/p10 mature form (By similarity). Initially it was reported that cleavage by granzyme B, caspase-8 and -10 generates the two activ... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11175259}. Nucleus {ECO:0000269|PubMed:11175259}. | null | null | null | null | null | FUNCTION: Non-apoptotic caspase which is involved in epidermal differentiation. Seems to play a role in keratinocyte differentiation and is required for cornification (PubMed:18156206). Regulates maturation of the epidermis by proteolytically processing filaggrin (PubMed:21654840). In vitro is equally active on the syn... | Mus musculus (Mouse) |
O89098 | CYTF_MOUSE | MWLAILLALCCLTSDTHGARPPDFCSKDLISSVKPGFPKTIETNNPGVLKAARHSVEKFNNCTNDIFLFKESHVSKALVQVVKGLKYMLEVKIGRTTCRKTMHHQLDNCDFQTNPALKRTLYCYSEVWVIPWLHSFEVPVLLCQ | null | null | immune response [GO:0006955]; negative regulation of microglial cell activation [GO:1903979]; negative regulation of peptidase activity [GO:0010466]; positive regulation of myelination [GO:0031643] | cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764]; multivesicular body [GO:0005771] | cysteine-type endopeptidase inhibitor activity [GO:0004869]; peptidase inhibitor activity [GO:0030414]; protein homodimerization activity [GO:0042803] | PF00031; | 3.10.450.10; | Cystatin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. | Mus musculus (Mouse) |
O89100 | GRAP2_MOUSE | MEATAKFDFMASGEDELSFRTGDILKILSNQEEWLKAELGSQEGYVPKNFIDIEFPEWFHEGLSRHQAENLLMGKDIGFFIIRASQSSPGDFSISVRHEDDVQHFKVMRDTKGNYFLWTEKFPSLNKLVDYYRTTSISKQKQVFLRDGTQDQGHRGNSLDRRSQGGPHPSGTVGEEIRPSVNRKLSDHLPLGPQQFHPHQQPSPQFTPGPQPPQQQRYLQHFHQDRRGGSLDINDGHCGLGSEVNATLMHRRHTDPVQLQAAGRVRWARALYDFEALEEDELGFRSGEVVEVLDSSNPSWWTGRLHNKLGLFPANYVAPM... | null | null | regulation of MAPK cascade [GO:0043408]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | phosphotyrosine residue binding [GO:0001784] | PF00017;PF00018; | 3.30.505.10;2.30.30.40; | GRB2/sem-5/DRK family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. | null | null | null | null | null | FUNCTION: Interacts with SLP-76 to regulate NF-AT activation. Binds to tyrosine-phosphorylated shc. | Mus musculus (Mouse) |
O89101 | FGF18_MOUSE | MYSAPSACTCLCLHFLLLCFQVQVLAAEENVDFRIHVENQTRARDDVSRKQLRLYQLYSRTSGKHIQVLGRRISARGEDGDKYAQLLVETDTFGSQVRIKGKETEFYLCMNRKGKLVGKPDGTSKECVFIEKVLENNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQDVHFMKRYPKGQAELQKPFKYTTVTKRSRRIRPTHPG | null | null | angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; cell population proliferation [GO:0008283]; chondrocyte development [GO:0002063]; chondrocyte differentiation [GO:0002062]; endochondral ossification [GO:0001958]; ERK1 and ERK2 cascade [GO:0070371]; fibroblast growth... | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleolus [GO:0005730]; nucleus [GO:0005634] | fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]; type 1 fibroblast growth factor receptor binding [GO:0005105]; type 2 fibroblast growth factor receptor binding [GO:0005111] | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. Required for normal ossification and bone development. Stimulates hepatic and intestinal proliferation (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
O89103 | C1QR1_MOUSE | MAISTGLFLLLGLLGQPWAGAAADSQAVVCEGTACYTAHWGKLSAAEAQHRCNENGGNLATVKSEEEARHVQQALTQLLKTKAPLEAKMGKFWIGLQREKGNCTYHDLPMRGFSWVGGGEDTAYSNWYKASKSSCIFKRCVSLILDLSLTPHPSHLPKWHESPCGTPEAPGNSIEGFLCKFNFKGMCRPLALGGPGRVTYTTPFQATTSSLEAVPFASVANVACGDEAKSETHYFLCNEKTPGIFHWGSSGPLCVSPKFGCSFNNGGCQQDCFEGGDGSFRCGCRPGFRLLDDLVTCASRNPCSSNPCTGGGMCHSVPLS... | null | null | cell migration [GO:0016477]; cell-cell adhesion [GO:0098609] | cell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; external side of plasma membrane [GO:0009897]; extracellular matrix [GO:0031012]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; complement component C1q complex binding [GO:0001849]; extracellular matrix binding [GO:0050840]; extracellular matrix protein binding [GO:1990430] | PF12662;PF07645;PF00059; | 2.10.25.10;3.10.100.10; | null | PTM: N- and O-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Receptor (or element of a larger receptor complex) for C1q, mannose-binding lectin (MBL2) and pulmonary surfactant protein A (SPA). May mediate the enhancement of phagocytosis in monocytes and macrophages upon interaction with soluble defense collagens. May play a role in intercellular adhesion. Marker for ea... | Mus musculus (Mouse) |
O89106 | FHIT_MOUSE | MSFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFRDLHPDEVADLFQVTQRVGTVVEKHFQGTSITFSMQDGPEAGQTVKHVHVHVLPRKAGDFPRNDNIYDELQKHDREEEDSPAFWRSEKEMAAEAEALRVYFQA | 2.7.7.51; 3.6.1.29; 3.6.2.1; 3.9.1.- | null | diadenosine triphosphate catabolic process [GO:0015964]; DNA replication [GO:0006260]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; purine nucleotide metabolic process [GO:0006163] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | adenosine 5'-monophosphoramidase activity [GO:0043530]; adenylylsulfatase activity [GO:0047627]; adenylylsulfate-ammonia adenylyltransferase activity [GO:0047352]; bis(5'-adenosyl)-triphosphatase activity [GO:0047710]; nickel cation binding [GO:0016151]; nucleotide binding [GO:0000166]; ubiquitin protein ligase binding... | PF01230; | 3.30.428.10; | null | PTM: Phosphorylation at Tyr-114 by SRC is required for induction of apoptosis. {ECO:0000250|UniProtKB:P49789}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9699672}. Nucleus {ECO:0000250|UniProtKB:P49789}. Mitochondrion {ECO:0000250|UniProtKB:P49789}. | CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2 H(+); Xref=Rhea:RHEA:13893, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58529, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=3.6.1.29; Evidence={ECO:0000250|UniProtKB:P49789}; CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphos... | null | null | null | null | FUNCTION: Possesses dinucleoside triphosphate hydrolase activity (By similarity). Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP (By similarity). Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP (By similarity). Exhibits adenylylsu... | Mus musculus (Mouse) |
O89107 | DNSL3_RAT | MSLYPASPYLASLLLFILALHGALSLRLCSFNVRSFGESKKENHNAMDIIVKIIKRCDLILLMEIKDSNNNICPMLMEKLNGNSRRSTTYNYVISSRLGRNTYKEQYAFLYKEKLVSVKAKYLYHDYQDGDTDVFSREPFVVWFQAPFTAAKDFVIVPLHTTPETSVKEIDELADVYTDVRRRWKAENFIFMGDFNAGCSYVPKKAWKNIRLRTDPNFVWLIGDQEDTTVKKSTSCAYDRIVLRGQEIVNSVVPRSSGVFDFQKAYELSEEEALDVSDHFPVEFKLQSSRAFTNSRKSVSLKKKKKGSRS | 3.1.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:9665719}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9665719}; | apoptotic DNA fragmentation [GO:0006309]; DNA catabolic process [GO:0006308]; neutrophil activation involved in immune response [GO:0002283]; programmed cell death involved in cell development [GO:0010623]; regulation of acute inflammatory response [GO:0002673]; regulation of neutrophil mediated cytotoxicity [GO:007094... | endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; nucleus [GO:0005634] | deoxyribonuclease I activity [GO:0004530]; DNA binding [GO:0003677]; DNA endonuclease activity [GO:0004520]; endonuclease activity [GO:0004519] | PF03372; | 3.60.10.10; | DNase I family | PTM: Seems to be synthesized as an inactive precursor protein and converted into an active mature enzyme by removal of the N-terminal precursor peptide during apoptosis.; PTM: Poly-ADP-ribosylated by PARP1. ADP-ribosylation negatively regulates enzymatic activity during apoptosis. {ECO:0000250|UniProtKB:Q13609}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9665719}. Secreted {ECO:0000250|UniProtKB:O55070, ECO:0000250|UniProtKB:Q13609}. Note=May first pass through the ER membrane before being imported in the nucleus. Contradictory reports exist about the subcellular localization under normal physiological conditions. Under... | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. Active from pH 6.0 to 9.0. {ECO:0000269|PubMed:9665719}; | null | FUNCTION: Has DNA hydrolytic activity. Is capable of both single- and double-stranded DNA cleavage, producing DNA fragments with 3'-OH ends (PubMed:7957253). Can cleave chromatin to nucleosomal units and cleaves nucleosomal and liposome-coated DNA. Acts in internucleosomal DNA fragmentation (INDF) during apoptosis and ... | Rattus norvegicus (Rat) |
O89109 | KCNN4_MOUSE | MGGELVTGLGALRRRKRLLEQEKRVAGWALVLAGTGIGLMVLHAEMLWFLGCKWVLYLLLVKCLITLSTAFLLCLIVVFHAKEVQLFMTDNGLRDWRVALTRRQVAQILLELLVCGVHPVPLRSPHCALAGEATDAQPWPGFLGEGEALLSLAMLLRLYLVPRAVLLRSGVLLNASYRSIGALNQVRFRHWFVAKLYMNTHPGRLLLGLTLGLWLTTAWVLSVAERQAVNATGHLTDTLWLIPITFLTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLEFNKAEKHVHNFMMDIHYAKEMKESAARLLQEA... | null | null | calcium ion transport [GO:0006816]; cardiac muscle hypertrophy [GO:0003300]; cell volume homeostasis [GO:0006884]; establishment of localization in cell [GO:0051649]; hepatocyte apoptotic process [GO:0097284]; monoatomic anion transport [GO:0006820]; mononuclear cell migration [GO:0071674]; negative regulation of cardi... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytosol [GO:0005829]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; vesicle [GO:0031982] | calcium-activated potassium channel activity [GO:0015269]; calmodulin binding [GO:0005516]; intermediate conductance calcium-activated potassium channel activity [GO:0022894]; inward rectifier potassium channel activity [GO:0005242]; potassium channel activity [GO:0005267]; protein phosphatase binding [GO:0019903]; sma... | PF02888;PF07885;PF03530; | 1.10.287.70; | Potassium channel KCNN family, KCa3.1/KCNN4 subfamily | PTM: Phosphorylation at His-356 by NDKB activates the channel, and conversely it's dephosphorylation by PHPT1 inhibits the channel. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O15554}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15554}. | null | null | null | null | null | FUNCTION: Forms a voltage-independent potassium channel that is activated by intracellular calcium (PubMed:9705284). Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells (PubMed:20884616). Plays... | Mus musculus (Mouse) |
O89110 | CASP8_MOUSE | MDFQSCLYAIAEELGSEDLAALKFLCLDYIPHKKQETIEDAQKLFLRLREKGMLEEGNLSFLKELLFHISRWDLLVNFLDCNREEMVRELRDPDNAQISPYRVMLFKLSEEVSELELRSFKFLLNNEIPKCKLEDDLSLLEIFVEMEKRTMLAENNLETLKSICDQVNKSLLGKIEDYERSSTERRMSLEGREELPPSVLDEMSLKMAELCDSPREQDSESRTSDKVYQMKNKPRGYCLIINNHDFSKAREDITQLRKMKDRKGTDCDKEALSKTFKELHFEIVSYDDCTANEIHEILEGYQSADHKNKDCFICCILSHG... | 3.4.22.61 | null | angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cardiac muscle tissue development [GO:0048738]; execution phase of apoptosis [GO:0097194]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625... | CD95 death-inducing signaling complex [GO:0031265]; cell body [GO:0044297]; cytoplasm [GO:0005737]; death-inducing signaling complex [GO:0031264]; mitochondrion [GO:0005739]; Noc1p-Noc2p complex [GO:0030690]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; ripoptosome [GO:00... | cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic process [GO:0097153]; cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097199]; death ... | PF01335;PF00656; | 3.40.50.1460;1.10.533.10; | Peptidase C14A family | PTM: Generation of the subunits requires association with the death-inducing signaling complex (DISC), whereas additional processing is likely due to the autocatalytic activity of the activated protease (PubMed:31511692). GZMB and CASP10 can be involved in these processing events (By similarity). {ECO:0000250|UniProtKB... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12065591}. Nucleus {ECO:0000269|PubMed:12065591}. Note=Translocates into the nucleus during apoptosis. {ECO:0000269|PubMed:12065591}. | CATALYTIC ACTIVITY: Reaction=Strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala).; EC=3.4.22.61; Evidence={ECO:0000269|PubMed:12065591, ECO:0000269|PubMed:32971525, ECO:0000269|PubMed:9654089, ECO:0000269|PubMed:9837723}; | null | null | null | null | FUNCTION: Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood (PubMed:12065591, PubMed:18455983, PubMed:30361383, PubMed:30381458, PubMed:31511692, Pub... | Mus musculus (Mouse) |
O89112 | LANC1_MOUSE | MAQRAFPNPYADYNKSLAENYFDSTGRLTPEFSHRLTNKIRELLQQMERGLKSADPRDGTGYTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSRRSITFLCGDAGPLAVAAVLYHKMNSEKQAEECITRLIHLNKIDPHVPNEMLYGRIGYIFALLFVNKNFGEEKIPQSHIQQICENILTSGENLSRKRNLAAKSPLMYEWYQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPSGNYPPCLDDTRDLLVHWCHGAPGVIYMLIQAYKVFKEERYLCDAQQCADVIWQYGLLKKGYG... | 2.5.1.18 | null | carbohydrate metabolic process [GO:0005975]; cellular detoxification [GO:1990748]; peptide modification [GO:0031179] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364]; low-density lipoprotein particle receptor binding [GO:0050750]; SH3 domain binding [GO:0017124]; zinc ion binding [GO:0008270] | PF05147; | 1.50.10.10; | LanC-like protein family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43813}. Cell membrane {ECO:0000250|UniProtKB:O43813}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43813}. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:25158856}; CATALYTIC ACTIVITY: Reaction=1-chloro-2,4-dinitr... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.93 mM for 1-chloro-2,4-dinitrobenzene {ECO:0000269|PubMed:25158856}; Vmax=1087 nmol/min/mg enzyme {ECO:0000269|PubMed:25158856}; | null | null | null | FUNCTION: Functions as a glutathione transferase (PubMed:25158856). Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate (PubMed:25158856). Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative... | Mus musculus (Mouse) |
O89116 | VTI1A_MOUSE | MSSDFEGYEQDFAVLTAEITSKIARVPRLPPDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKRSRIAYSDEVRNELLGDAGNSSENQRAHLLDNTERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDREKIQRARDRLRDADANLGKSSRILTGMLRRIIQNRILLVILGIIVVIAILTAIAFFVKGH | null | null | endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; Golgi to vacuole transport [GO:0006896]; intra-Golgi vesicle-mediated transport [GO:0006891]; intracellular protein transport [GO:0006886]; macroautophagy [GO:0016236]; retrograde transport, endosome to Golgi [GO:0042147]; synaptic vesicle to endos... | clathrin-coated vesicle [GO:0030136]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; late endosome membrane [GO:... | SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149] | PF05008;PF12352; | 1.20.5.110;1.20.58.400; | VTI1 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. Involved in vesicular transport from the late endosomes to the t... | Mus musculus (Mouse) |
O89290 | POL_HV193 | MGARASVLSGGKLDAWEKIRLRPGGKKKYRLKHLVWASRELERFALDPGLLETSEGCRKIIGQLQPSLQTGSEELKSLYNTIAVLYYVHQKVEVKDTKEALEKLEEEQNKGRQKTQQATAEKGVSQNYPIVQNLQGQMVHQSLSPRTLNAWVKVIEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKDTINEEAAEWDRLHPTQAGPIPPGQIREPRGSDIAGTTSTLQEQIQWMTGNPPVPVGEMYKRWIILGLNKIVRMYSPVGILDIRQGPKEPFRDYVDRFFKTLRAEQATQEVKGWMTDTLLVQ... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype F1 (isolate 93BR020) (HIV-1) |
O89291 | GAG_HV193 | MGARASVLSGGKLDAWEKIRLRPGGKKKYRLKHLVWASRELERFALDPGLLETSEGCRKIIGQLQPSLQTGSEELKSLYNTIAVLYYVHQKVEVKDTKEALEKLEEEQNKGRQKTQQATAEKGVSQNYPIVQNLQGQMVHQSLSPRTLNAWVKVIEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKDTINEEAAEWDRLHPTQAGPIPPGQIREPRGSDIAGTTSTLQEQIQWMTGNPPVPVGEMYKRWIILGLNKIVRMYSPVGILDIRQGPKEPFRDYVDRFFKTLRAEQATQEVKGWMTDTLLVQ... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype F1 (isolate 93BR020) (HIV-1) |
O89292 | ENV_HV193 | MRVRGMQRNWQHLGKWGLLFLGTLIICNAAENLWVTVYYGVPVWKEATTTLFCASDAKSYEKEAHNVWATHACVPTDPNPQEVVLENVTERFNMWENNMVEQMHTDIISLWDQSLKPCVKLTPLCVTLDCRNIATNGTNDTIAINDTLKEDPEAIQNCSFNTTTEIRDKQLKVHALFYKLDIVQINKDDNRTYRLINCDASTITQACPKVSWDPIPIHYCAPAGYAILKCNEKNFTGTGSCKNVSTVQCTHGIKPVVSTQLLLNGSLAEGEIVIRSQNISDNAKTIIVHLNESVQINCTRPNNNTRKRISLGPGRVFYTT... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype F1 (isolate 93BR020) (HIV-1) |
O89293 | NEF_HV193 | MGGKWSKSSIVGWPAIRERMRRTPPTPPAAEGVGAVSQDLERRGAITSSNTRANNPDLAWLEAQEEDEVGFPVRPQVPLRPMTYKGAVDLSHFLKEKGGLEGLIYSKRRQEILDLWVYHTQGYFPDWQNYTPGPGIRYPLTMGWCFKLVPVDPEEVEKANEGENNCLLHPMSQHGMEDEDKEVLKWEFDSRLALRHIARERHPEYYQD | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype F1 (isolate 93BR020) (HIV-1) |
O89939 | GAG_HV1SE | MGARASVLTGGKLDAWEKIRLRPGGRKSYKIKHLVWASRELERFALNPDLLETAEGCQQIMRQLQPSLQTGTEEIKSLYNAVATLYCVHQRIEVKDTKEALEEVEKIQKKSQEKIQQAAMDKGNSNQVSQNYPIVQNAQGQMVHQAITPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNLMLNTVGGHQAAMQMLKDTINEEAAEWDRMHPQQAGPFPPGQIREPRGSDIAGTTSSLQEQITWMTGNPPIPVGEIYKRWIILGLNKIVRMYSPVSILDIRQGPKEPFRDYVDRFFKCLRAEQASQDVKGWMTDT... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype G (isolate SE6165) (HIV-1) |
O89940 | POL_HV1SE | MGARASVLTGGKLDAWEKIRLRPGGRKSYKIKHLVWASRELERFALNPDLLETAEGCQQIMRQLQPSLQTGTEEIKSLYNAVATLYCVHQRIEVKDTKEALEEVEKIQKKSQEKIQQAAMDKGNSNQVSQNYPIVQNAQGQMVHQAITPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNLMLNTVGGHQAAMQMLKDTINEEAAEWDRMHPQQAGPFPPGQIREPRGSDIAGTTSSLQEQITWMTGNPPIPVGEIYKRWIILGLNKIVRMYSPVSILDIRQGPKEPFRDYVDRFFKCLRAEQASQDVKGWMTDT... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype G (isolate SE6165) (HIV-1) |
O89943 | TAT_HV1SE | MDPVDPNLEPWNHPGSQPKTPCNKCFCKVCCWHCQVCFLNKGLGISYGRKKRKHRRGTPQSSKGHQDPVPKQPLPTTRGNPTGPKESKKEVASKAEADQCD | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype G (isolate SE6165) (HIV-1) |
O89945 | NEF_HV1SE | MGGKWSKSSIVGWPEVRERIRNTPTAAEGVGAVSQDLDRHGAITSSNTAANNPDCAWLEAQEEDSEVGFPVRPQVPLRPMTFKGAFDLSFFLKEKGGLDGLIYSKKRQEILDLWVYNTQGYFPDWQNYTPGPGTRFPLTFGWCFKLVPMDPAEVEEANKGENNSLLHPICQHGMEDEDREVLVWRFDSSLARRHIARELHPEYYKDC | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype G (isolate SE6165) (HIV-1) |
O90304 | SPIKE_BRV1 | MFLCFCTAPILCLWINSGGAVVVSNESLVVCEPVSYPYSLQVLRSFSQRVNLRTKRAVTTDAWSFAYQISTSSLNVNGWYVNFTSPLGWSYPNGKLFGIVLGSDAMMRASVSTFTYDVISYVGQRPNLDCQINDLANGGLESRYSTVRVDNCGNYPCHGGGKPGCSIGHPYMANGVRTRVLLTTQSPGIQYEIYSGQDYAVYQITPYTQYTVTMPSGTSGYCQQTPLYVECGSWTPYRVHAYGCDKATQSCNYTISSDWVVAFKSKASAIILRSQLIVALAQKLSRTVGVNKAVYFWFLKQPYHYLSLVNFSPNYALFSP... | 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 | PF17072; | null | Torovirinae spike protein family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Mediates the binding of virions to the host cell receptor and is involved in membrane fusion. {ECO:0000250}. | Breda virus 1 (BRV-1) |
O90368 | POLN_ONNVS | MDSVYVDIDADSAFLKALQRAYPMFEVEPKQVTPNDHANARAFSHLAIKLIEQEIDPDSTILDIGPAPARRMMSDRKYHCVCPMRSAEDPERLANYARKLASAAGKVTDKNISGKINDLQAVMAVPNMETSTFCLHTDATCKQRGDVAIYQDVYAVHAPTSLYHQAIKGVRVAYWIGFDTTPFMYNAMAGAYPSYSTNWADEQVLKAKNIGLCSTDLSEGRRGKLSIMRGKKLKPCDRVLFSVGSTLYPESRKLLQSWHLPSVFHLKGKLSFTCRCDTIVSCEGYVVKRVTMSPGIYGKTSGYAVTHHADGFLMCKTTDT... | 2.1.1.-; 2.7.7.-; 2.7.7.19; 2.7.7.48; 3.1.3.84; 3.4.22.-; 3.6.1.15; 3.6.1.74; 3.6.4.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03317}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P03317}; Note=For nsP4 adenylyltransferase activity; Mn(2+) supports catalysis at 60% of the levels observed with Mg(2+). {ECO:0000250|UniProtKB:P03317}; COFACTOR:... | 7-methylguanosine mRNA capping [GO:0006370]; DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity [GO:0039523]; viral RNA genome replication [GO:0039694] | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell filopodium [GO:0044176]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type peptidase activity [GO:0008234]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA 5'-phosphatase activity [GO:0140818]; mRNA methyltransferase activity [GO:0008174]; poly(A) RNA polymerase activity [GO:1990817]; polynucleotide 5... | PF01661;PF20852;PF01707;PF00978;PF20896;PF01443;PF01660; | 3.90.70.110;3.40.220.10;3.40.50.300;3.40.50.150; | null | PTM: [Polyprotein P1234]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P1234 is first cleaved in trans through its nsP2 protease activity, releasing P123' and nsP4, which associate to for... | SUBCELLULAR LOCATION: [Polyprotein P1234]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex. {E... | CATALYTIC ACTIVITY: Reaction=GTP + S-adenosyl-L-methionine = N(7)-methyl-GTP + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46948, ChEBI:CHEBI:37565, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87133; Evidence={ECO:0000250|UniProtKB:P27282}; CATALYTIC ACTIVITY: Reaction=L-histidyl-[protein] + N(7)-methyl-GTP = dipho... | null | null | null | null | FUNCTION: [Polyprotein P1234]: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2. {ECO:0000250|UniProtKB:Q8JUX6}.; FUNCTION: [Polyprotein P123']: The early replication complex formed by the polyprotein P123' and nsP4 synthesizes minus-strand RNAs (Probable... | O'nyong-nyong virus (strain SG650) (ONNV) |
O90369 | POLS_ONNVS | MEFIPAQTYYNRRYQPRPWTQRPTIQVIRPKPRRSRPAGQLAQLISAVSRLALRTVPQKPRRTRKTKKQKQVKQEQQSTRNQKKKAPKQKQTQKKKRPGRRERMCMKIENDCIFEVKHEGKITGYACLVGDKVMKPAHVKGTIDNADLAKLAFKRSSKYDLECAQIPVHMKSDASKFTHEKPEGYYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGTRTALSVVTWNKDIVTKITPEGSVEWSLALPVMCLLANTTFPCSQPPCAPCCYEKKPEETLRMLEDNVMQPGYYQLLDSALACSQH... | 3.4.21.90 | null | fusion of virus membrane with host endosome membrane [GO:0039654]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; virion attachment to host cell [GO:0019062] | host cell cytoplasm [GO:0030430]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; virion membrane [GO:0055036] | serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198] | PF01589;PF00943;PF01563;PF00944; | 1.10.287.2230;2.60.40.350;2.60.40.3200;2.60.40.4310;2.60.40.2400;2.60.98.10;2.40.10.10; | null | PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2. The remaining polyprotein is then targeted to the host endoplasmic reticulum, where host signal ... | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000250|UniProtKB:P03316}. Host cytoplasm {ECO:0000250|UniProtKB:P03316}. Host cell membrane {ECO:0000250|UniProtKB:P03316}.; SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein {ECO:000025... | CATALYTIC ACTIVITY: Reaction=Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03316}; | null | null | null | null | FUNCTION: [Capsid protein]: Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedri... | O'nyong-nyong virus (strain SG650) (ONNV) |
O90370 | POLN_ONNVI | MDSVYVDIDADSAFLKALQRAYPMFEVEPKQVTPNDHANARAFSHLAIKLIEQEIDPGSTILGIGSAPARRMMSDRKYHCVCPMRSAEDPERLANYARKLASAAGKVTDKNISGKINDLQAVMAVPNMETSTFCLHTDATCKQRGDVAIYQDVYAVHAPTSLYHQAIKGVHVAYWIGFDTTPFMYNAMAGAYPSYSTNWADEQVLKAKNIGLCSTDLSEGRRGKLSIMRGKKFKPCDRVLFSVGSTLYPESRKLLQSWHLPSVFHLKGKLSFTCRCDTIVSCEGYVVKRVTMSPGIYGKTSGYAVTHHADGFLMCKTTDT... | 2.1.1.-; 2.7.7.-; 2.7.7.19; 2.7.7.48; 3.1.3.84; 3.4.22.-; 3.6.1.15; 3.6.1.74; 3.6.4.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03317}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P03317}; Note=For nsP4 adenylyltransferase activity; Mn(2+) supports catalysis at 60% of the levels observed with Mg(2+). {ECO:0000250|UniProtKB:P03317}; COFACTOR:... | 7-methylguanosine mRNA capping [GO:0006370]; DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity [GO:0039523]; viral RNA genome replication [GO:0039694] | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell filopodium [GO:0044176]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type peptidase activity [GO:0008234]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA 5'-phosphatase activity [GO:0140818]; mRNA methyltransferase activity [GO:0008174]; poly(A) RNA polymerase activity [GO:1990817]; polynucleotide 5... | PF01661;PF20852;PF01707;PF00978;PF20896;PF01443;PF01660; | 3.90.70.110;3.40.220.10;3.40.50.300;3.40.50.150; | null | PTM: [Polyprotein P1234]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P1234 is first cleaved in trans through its nsP2 protease activity, releasing P123 and nsP4, which associate to form... | SUBCELLULAR LOCATION: [Polyprotein P1234]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex. {E... | CATALYTIC ACTIVITY: Reaction=GTP + S-adenosyl-L-methionine = N(7)-methyl-GTP + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46948, ChEBI:CHEBI:37565, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87133; Evidence={ECO:0000250|UniProtKB:P27282}; CATALYTIC ACTIVITY: Reaction=L-histidyl-[protein] + N(7)-methyl-GTP = dipho... | null | null | null | null | FUNCTION: [Polyprotein P1234]: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2. {ECO:0000250|UniProtKB:Q8JUX6}.; FUNCTION: [Polyprotein P123]: The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs (By similar... | O'nyong-nyong virus (strain Igbo Ora) (ONNV) (Igbo Ora virus) |
O90371 | POLS_ONNVI | MEFIPAQTYYNRRYQPRPWTQRPTIQVIRPKPRRRRPAGQLAQLISAVSRLALRTVPQKPRRTRKIKKQKQVKQEQQSTRNQKKKAPKQKQTQKKKRPGRRERMCMKIENDCIFEVKHEGKVTGYACLVGDKVMKPAHVKGTIDNADLAKLAFKRSSKYDLECAQIPVHMKSDASKFTHEKPEGYYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGTRTALSVVTWNKDIVTKITPEGSVEWSLALPVMCLLANTTFPCSQPPCAPCCYEKKPEETLRMLEDNVMQPGYYQLLDSALACSQH... | 3.4.21.90 | null | fusion of virus membrane with host endosome membrane [GO:0039654]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; virion attachment to host cell [GO:0019062] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198] | PF01589;PF00943;PF01563;PF00944; | 1.10.287.2230;2.60.40.350;2.60.40.3200;2.60.40.4310;2.60.40.2400;2.60.98.10;2.40.10.10; | null | PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2 (By similarity). The remaining polyprotein is then targeted to the host endoplasmic reticulum, wh... | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000250|UniProtKB:P03316}. Host cytoplasm {ECO:0000250|UniProtKB:Q8JUX5}. Host cell membrane {ECO:0000250|UniProtKB:P03316}. Host nucleus {ECO:0000250|UniProtKB:Q8JUX5}. Note=Shuttles between the cytoplasm and the nucleus. {ECO:0000250|UniProtKB:Q8JUX5}.; SUBCELLULAR ... | CATALYTIC ACTIVITY: Reaction=Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03315}; | null | null | null | null | FUNCTION: [Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (By similarity). The capsid protein binds to the viral RNA genome at a site adjacent to a ri... | O'nyong-nyong virus (strain Igbo Ora) (ONNV) (Igbo Ora virus) |
O91079 | GAG_HV1YF | MGARASVLTGGKLDQWESIYLRPGGKKKYRMKHLVWASRELERFACNPGLMDTADGCAKLLNQLEPALKTGSEELRSLYNALAVLYCVHSRIQIHNTQEALDKIKEKQEQHKPEPKNPEAGAAAATDSNISRNYPLVQTAQGQMVHQPLTPRTLNAWVKVIEEKAFSPEVIPMFMALSEGATPSDLNTMLNTVGGHQAAMQMLKEVINEEAADWDRTHPVPVGPLPPGQLRDPRGSDIAGTTSTLAEQVAWMTANPPVPVGDIYRRWIVLGLNRIVRMYSPVSILEIKQGPKEPFRDYVDRFYKTLRAEQATQEVKNWMT... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group N (isolate YBF30) (HIV-1) |
O91080 | POL_HV1YF | MGARASVLTGGKLDQWESIYLRPGGKKKYRMKHLVWASRELERFACNPGLMDTADGCAKLLNQLEPALKTGSEELRSLYNALAVLYCVHSRIQIHNTQEALDKIKEKQEQHKPEPKNPEAGAAAATDSNISRNYPLVQTAQGQMVHQPLTPRTLNAWVKVIEEKAFSPEVIPMFMALSEGATPSDLNTMLNTVGGHQAAMQMLKEVINEEAADWDRTHPVPVGPLPPGQLRDPRGSDIAGTTSTLAEQVAWMTANPPVPVGDIYRRWIVLGLNRIVRMYSPVSILEIKQGPKEPFRDYVDRFYKTLRAEQATQEVKNWMT... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group N (isolate YBF30) (HIV-1) |
O91083 | TAT_HV1YF | MEPVDPRLEPWNHPGSQPKTACNNCYCKRCCYHCLYCFTKKGLGISYGRKKRSQRRRTPQSSKSHQDLIPEQPLSQQQGDQTGQKKQKEALESKTEADPCD | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group N (isolate YBF30) (HIV-1) |
O91086 | ENV_HV1YF | MGMKSGWLLFYLLVSLIKVIGSEQHWVTVYYGVPVWREAETTLFCASDAKAHSTEAHNIWATQACVPTDPNPQEVLLPNVTEKFNMWENKMADQMQEDIISLWEQSLKPCVKLTPLCVTMLCNDSYGEERNNTNMTTREPDIGYKQMKNCSFNATTELTDKKKQVYSLFYVEDVVPINAYNKTYRLINCNTTAVTQACPKTSFEPIPIHYCAPPGFAIMKCNEGNFSGNGSCTNVSTVQCTHGIKPVISTQLILNGSLNTDGIVIRNDSHSNLLVQWNETVPINCTRPGNNTGGQVQIGPAMTFYNIEKIVGDIRQAYCN... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group N (isolate YBF30) (HIV-1) |
O91087 | NEF_HV1YF | MGKIWSKSSLVGWPEIRERMRRQTQEPAVEPAVGAGAASQDLANRGAITIRNTRDNNESIAWLEAQEEEEEVGFPVRPQVPLRPITYKQAFDLSFFLKDKGGLEGLVWSRKRQDILDLWMYHTQGILPDWHNYTPGPGIRYPVTFGWCFKLVPLSAEEVEEANEGDNNALLHPICQHGADDDHKEVLVWRFDSSLARRHVARELHPEFYKNC | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group N (isolate YBF30) (HIV-1) |
O91464 | POLG_AIVA8 | MAATRVSRSVLAAVAHSAAHRTYHTVLDCYDRLYLNTNPHLSYPLPKNSSFPCPFCQYDEQNEVLSPESLRGEGAEPCWKCSQDKPRRKYNTTPPEDWLYDSDVQSWFYPETYYSDLQQKFFDKLALLSLPGAYQAKTPEERALAGALTQLLNFPSTPPLTLPTTNLQRQGNSVTNIYGNGNNVTTDVGANGWAPTVSTGLGDGPVSASADSLPGRSGGASSEKTHTVSGSSNKVGSRFSKWWEPAAARASESATDSAIEGIDAAGKAASKAITRKLDRPAAPSSTANPQPSLIALNPSATQSGNASILTGSTAPSLLAY... | 2.7.7.48; 3.4.22.28; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral RNA genome replicati... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198] | PF00548;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;3.40.50.300;2.40.10.10; | null | PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (PubMed:22226945). The leader protein-VP0 junction is cleaved by 3C proteinase (PubMed:14512530). The VP1/2A junction is cleaved by the protein 3CD in association with protein 2A (PubM... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion {ECO:0000269|PubMed:27595320, ECO:0000269|PubMed:27681122}. Host cytoplasm {ECO:0000250|UniProtKB:P12296}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000269|PubMed:27595320, ECO:0000269|PubMed:27681122}. Host cytoplasm {ECO:0000250|UniProtKB:P12296}.; SU... | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) ... | null | null | null | null | FUNCTION: [Leader protein]: Inhibits the integrated stress response (ISR) in the infected cell by preventing the sequestration of eIF2B by phosphorylated EIF2S1/eIF-2alpha (PubMed:32690955). Stress granule formation in response to EIF2S1/eIF-2alpha phosphorylation is thus inhibited, which allows protein synthesis and v... | Aichi virus (strain Human/A846/88/1989) (AiV) (Aichi virus (strain A846/88)) |
O91532 | HBEAG_HBVA7 | MQLFHLCLIISCTCPTVQASKLCLGWLWGMDIDPYKEFGATVELLSFLPSDFFPSVRDLLDTASALYREALESPEHCSPHHTALRQAILCWVELMTLATWVGNNLQDPASRDLVVNYVNTNMGLKIRQLLWFHISCLTFGRETVLEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRDRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC | 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... | Hepatitis B virus genotype A2 (isolate Japan/11D11HCCW/1998) (HBV-A) |
O91534 | HBSAG_HBVA7 | MGGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPAFGANSNNPDWDFNPIKDHWPAANQVGVGAFGPGFTPPHGGILGWSPQAQGILTTVSTIPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTAFHQTLQDPRVRGLYLPAGGSSSGTVNPAPNIASHISSISARTGDPVTNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGSPVCLGQNSQSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSTTTSTGPCKTCTTPAQGNSMFPSCCCTKPTDGN... | 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 (isolate Japan/11D11HCCW/1998) (HBV-A) |
O91734 | POLG_EC01F | MGAQVSTQKTGAHETSLSATGNSIIHYTNINYYKDAASNSANRQDFTQDPGKFTEPMKDVMIKTLPALNSPTVEECGYSDRVRSITLGNSTITTQECANVVVGYGEWPEYLSDNEATAEDQPTQPDVATCRFYTLDSVQWENGSPGWWWKFPDALRDMGLFGQNMYYHYLGRAGYTIHVQCNASKFHQGCILVVCVPEAEMGSAQTSGVVNYEHISKGEIASRFTTTTTAEDHGVQAAVWNAGMGVGVGNLTIFPHQWINLRTNNSATIVMPYVNSVPMDNMYRHHNFTLMIIPFVPLDFSAGASTYVPITVTVAPMCAE... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence... | caveolin-mediated endocytosis of virus by host cell [GO:0075513]; DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:0... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.80.10;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms t... | Echovirus 1 (strain Human/Egypt/Farouk/1951) (E-1) |
O91936 | POLG_HCVSA | MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARQPTGRSWGQPGYPWPLYANEGLGWAGWLLSPRGSRPNWGPNDPRRKSRNLGKVIDTLTCGFADLMGYIPLVGGPVGGVARALAHGVRVLEDGVNYATGNLPGCSFSIFILALLSCLTVPTSAVPYRNASGVYHVTNDCPNSSIVYEAEDLILHAPGCVPCVRQGNVSRCWVQITPTLSAPSLGAVTAPLRRAVDYLAGGAALCSALYVGDACGAVFLVGQMFTYSPRRHNVVQDCNCSIYSGHITGHRMAW... | 2.7.7.48; 3.4.21.98; 3.4.22.-; 3.6.1.15; 3.6.4.13 | COFACTOR: [Protease NS2]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P26663}; Note=Activity of protease NS2 is dependent on zinc ions and completely inhibited by EDTA. This is probably due to the fact that NS2 protease activity needs NS3 N-terminus that binds a zinc atom (active region NS2-3).... | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host cell cycle G1/S transiti... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell lipid droplet [GO:0044186]; host cell mitochondrial membrane [GO:0044191]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; ribonucleoprotein complex [GO... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:000425... | PF07652;PF01543;PF01542;PF01539;PF01560;PF01538;PF01006;PF01001;PF01506;PF08300;PF08301;PF12941;PF02907;PF00998; | 2.40.10.120;3.30.70.270;6.10.250.1610;6.10.250.1750;6.10.250.2920;2.20.25.210;3.30.160.890;2.30.30.710;1.20.1280.150;2.20.25.220;3.40.50.300;1.10.820.10;2.40.10.10; | Hepacivirus polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membran... | SUBCELLULAR LOCATION: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the c... | CATALYTIC ACTIVITY: [Serine protease/helicase NS3]: Reaction=Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.; EC=3.4.21.98; Evidence={ECO:0000250|UniProtKB:P27958}; CATALYTIC ACTIVITY: [Serine protease/helicase NS3... | null | null | null | null | FUNCTION: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA struc... | Hepatitis C virus genotype 5a (isolate SA13) (HCV) |
O91940 | L_BRSVA | MDTLIHENSTNVYLTDSYLKGVISFSECNALGSYLLDGPYLKNDYTNIISRQKPLIEHINLKKLSIIQSFVTKYNKGELGLEEPTYFQSLLMTYKSLSTSELITTTTLFKKIIRRAIEISDVKVYAILNKLGLKEKGKVDRCDDTNTTLSNIVRDNILSVISDNTPSTKKPNNSSCKPDQPIKTTILCKLLSSMSHPPTWLIHWFNLYTKLNDILTQYRTNEARNHGYILIDTRTLGEFQFILNQYGCIVYHKKLKKITITTYNQFLTWKDISLSRLNVCMITWISNCLNTLNKSLGLRCEFNNVTLSQLFLHGDCILKL... | 2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P28887}; Note=For RNA-directed RNA polymerase activity. Mn(2+) can stimulate de novo initiation but it is inefficient at supporting elongation of de novo initiated RNA. {ECO:0000250|UniProtKB:P28887}; | null | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | ATP binding [GO:0005524]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA-dependent RNA polymerase activity [GO:0003968] | PF14314;PF14318;PF00946; | null | Paramyxovirus L protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P28887}. Host cytoplasm {ECO:0000250|UniProtKB:P28887}. Note=Localizes in cytoplasmic inclusion bodies. {ECO:0000250|UniProtKB:P28887}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=GTP + H2... | null | null | null | null | FUNCTION: Responsible for RNA synthesis (replicase and transcriptase), cap addition, and cap methylation. Performs also the polyadenylation of subgenomic mRNAs by a stuttering mechanism at a slipery stop site present at the end of viral genes. The template is composed of the viral RNA tightly encapsidated by the nucleo... | Bovine respiratory syncytial virus (strain A51908) (BRS) |
O92446 | VP91_NPVBM | MMSGVMLLVFAIFLIIAFTLIYLAIYFKFDETTYTKRLQVMIEYIKRTNADEPTPNVIGYVSDITQNTYTVTWFNTVDLSTYQESVHDDRNEIFDFLNQKLQPVDRIVHDRVRANDENPNEFILSGDKDDVTMKCPAYFNFDYAQLKCVPVPPCDNKPAGRYPMDERLLDTLVLNQHLDKDYSSNEHLYHPTFYLRCFANGAHAVEECPDNYTFDAKTRQCKVNELCENRPDGYILSYFPSNLLVNQFMQCVSGRHVVRECPANKIFDRNLMSCVEAHPCTFNGAGHTYITADISDAQYFKCLNNNESQLMTCINRIRNS... | null | null | null | extracellular region [GO:0005576]; virion component [GO:0044423] | chitin binding [GO:0008061]; metal ion binding [GO:0046872] | PF08475;PF01607; | null | null | null | SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=In virions, associates with the capsid and maybe also with the envelope surrounding the capsid. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Probable capsid-associated protein. {ECO:0000250}. | Bombyx mori nuclear polyhedrosis virus (BmNPV) |
O92529 | POLG_HCVT5 | MSTLPKPQRKTKRNTNRRPMDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARPSQGRTWGQPGYPWPLYGNEGCGWAGWLMSPRGSRPSWGPNDPRRRSRNLGKVIDTLTCGLADLMGYIPVVGGPLGGVAAALAHGVRAIEDGINYATGNLPGCSFSIFILALLSCLTTPASALTYGNSSGLYHLTNDCPRSSIVLEAEAMILHLAGCVPCVRAGNISRCWHPVSPTLAVPNASVPASGFRKHVDLLAGAAVVCSSMYIGDLCGAVFLAGQLATFSPRIHDITQDCNCSVYTGHVTGHRMAW... | 2.7.7.48; 3.4.21.98; 3.4.22.-; 3.6.1.15; 3.6.4.13 | COFACTOR: [Protease NS2]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P26663}; Note=Activity of protease NS2 is dependent on zinc ions and completely inhibited by EDTA. This is probably due to the fact that NS2 protease activity needs NS3 N-terminus that binds a zinc atom (active region NS2-3).... | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host cell cycle G1/S transiti... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell lipid droplet [GO:0044186]; host cell mitochondrial membrane [GO:0044191]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; ribonucleoprotein complex [GO... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:000425... | PF07652;PF01543;PF01542;PF01539;PF01560;PF01538;PF01006;PF01001;PF01506;PF08300;PF08301;PF12941;PF02907;PF00998; | 2.40.10.120;3.30.70.270;6.10.250.1610;6.10.250.1750;6.10.250.2920;2.20.25.210;3.30.160.890;2.30.30.710;1.20.1280.150;2.20.25.220;3.40.50.300;1.10.820.10;2.40.10.10; | Hepacivirus polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membran... | SUBCELLULAR LOCATION: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the c... | CATALYTIC ACTIVITY: [Serine protease/helicase NS3]: Reaction=Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.; EC=3.4.21.98; Evidence={ECO:0000250|UniProtKB:P27958}; CATALYTIC ACTIVITY: [Serine protease/helicase NS3... | null | null | null | null | FUNCTION: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA struc... | Hepatitis C virus genotype 6b (isolate Th580) (HCV) |
O92530 | POLG_HCVVN | MSTLPKPQKRNQRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRQTGRTWAQPGYPWPLYGNEGCGWMGWLLSPRGSRPHWGPNDPRRRSRNLGKVIDTLTCGFADLMGYIPVVGAPLGGVAAALAHGVRAVEDGINYATGNLPGCSFSIFLLALLSCLTTPASAVHYANKSGIYHLTNDCPNSSIVYEAEDFIMHLPGCVPCIKSGNGSSCWLPATLTIAVPNASIPVRGFRRHVDLMVGAAAFCSAMYVGDLCGGIFLVGQLFSFNPRRHWVVQDCNCSIYVGHITGHRMAW... | 2.7.7.48; 3.4.21.98; 3.4.22.-; 3.6.1.15; 3.6.4.13 | COFACTOR: [Protease NS2]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P26663}; Note=Activity of protease NS2 is dependent on zinc ions and completely inhibited by EDTA. This is probably due to the fact that NS2 protease activity needs NS3 N-terminus that binds a zinc atom (active region NS2-3).... | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host cell cycle G1/S transiti... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell lipid droplet [GO:0044186]; host cell mitochondrial membrane [GO:0044191]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; ribonucleoprotein complex [GO... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:000425... | PF07652;PF01543;PF01542;PF01539;PF01560;PF01538;PF01006;PF01001;PF01506;PF08300;PF08301;PF12941;PF02907;PF00998; | 2.40.10.120;3.30.70.270;6.10.250.1610;6.10.250.1750;6.10.250.2920;2.20.25.210;3.30.160.890;2.30.30.710;1.20.1280.150;2.20.25.220;3.40.50.300;1.10.820.10;2.40.10.10; | Hepacivirus polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membran... | SUBCELLULAR LOCATION: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the c... | CATALYTIC ACTIVITY: [Serine protease/helicase NS3]: Reaction=Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.; EC=3.4.21.98; Evidence={ECO:0000250|UniProtKB:P27958}; CATALYTIC ACTIVITY: [Serine protease/helicase NS3... | null | null | null | null | FUNCTION: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA struc... | Hepatitis C virus genotype 6d (isolate VN235) (HCV) |
O92531 | POLG_HCVVO | MSTLPKPQRKTKRNTNRRPMDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARQSQGRHWAQPGYPWPLYGNEGCGWAGWLLSPRGSRPNWGPNDPRRRSRNLGKVIDTLTCGFADLMGYIPVVGAPLGGVAAALAHGVRAIEDGINYATGNLPGCSFSIFLLALLSCLTTPASAVHYRNISGIYHLTNDCPNSSIIYEADNIIMHTPGCVPCVKTGNKSQCWVPVAPTLAVANASVPIRGFRSHVDLLVGSAAACSALYIGDLCGGVFLVGQLFTFRPRQHTTVQECNCSIYTGHITGHRMAW... | 2.7.7.48; 3.4.21.98; 3.4.22.-; 3.6.1.15; 3.6.4.13 | COFACTOR: [Protease NS2]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P26663}; Note=Activity of protease NS2 is dependent on zinc ions and completely inhibited by EDTA. This is probably due to the fact that NS2 protease activity needs NS3 N-terminus that binds a zinc atom (active region NS2-3).... | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host cell cycle G1/S transiti... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell lipid droplet [GO:0044186]; host cell mitochondrial membrane [GO:0044191]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; ribonucleoprotein complex [GO... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:000425... | PF07652;PF01543;PF01542;PF01539;PF01560;PF01538;PF01006;PF01001;PF01506;PF08300;PF08301;PF12941;PF02907;PF00998; | 2.40.10.120;3.30.70.270;6.10.250.1610;6.10.250.1750;6.10.250.2920;2.20.25.210;3.30.160.890;2.30.30.710;1.20.1280.150;2.20.25.220;3.40.50.300;1.10.820.10;2.40.10.10; | Hepacivirus polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membran... | SUBCELLULAR LOCATION: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the c... | CATALYTIC ACTIVITY: [Serine protease/helicase NS3]: Reaction=Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.; EC=3.4.21.98; Evidence={ECO:0000250|UniProtKB:P27958}; CATALYTIC ACTIVITY: [Serine protease/helicase NS3... | null | null | null | null | FUNCTION: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA struc... | Hepatitis C virus genotype 6k (isolate VN405) (HCV) |
O92532 | POLG_HCVVP | MSTLPKPQRKTKRNTNRRPMDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARQPIGRSWGQPGYPWPLYGNEGCGWAGWLLSPRGSRPNWGPNDPRRRSRNLGKVIDTLTCGLADLMGYIPVLGGPLGGVAAALAHGVRAIEDGVNYATGNLPGCSFSIFLLALLSCLTTPASAIQVRNASGIYHLTNDCSNNSIVFEAETIILHLPGCVPCIKVGNGSRCWLSVSPTLAVPNSSVPIHGFRRHVDLLVGAAAFCSAMYIGDLCGSVFLVGQLFTFRPKHHQVTQDCNCSIYAGHITGHRMAW... | 2.7.7.48; 3.4.21.98; 3.4.22.-; 3.6.1.15; 3.6.4.13 | COFACTOR: [Protease NS2]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P26663}; Note=Activity of protease NS2 is dependent on zinc ions and completely inhibited by EDTA. This is probably due to the fact that NS2 protease activity needs NS3 N-terminus that binds a zinc atom (active region NS2-3).... | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host cell cycle G1/S transiti... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell lipid droplet [GO:0044186]; host cell mitochondrial membrane [GO:0044191]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; ribonucleoprotein complex [GO... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:000425... | PF07652;PF01543;PF01542;PF01539;PF01560;PF01538;PF01006;PF01001;PF01506;PF08300;PF08301;PF12941;PF02907;PF00998; | 2.40.10.120;3.30.70.270;6.10.250.1610;6.10.250.1750;6.10.250.2920;2.20.25.210;3.30.160.890;2.30.30.710;1.20.1280.150;2.20.25.220;3.40.50.300;1.10.820.10;2.40.10.10; | Hepacivirus polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membran... | SUBCELLULAR LOCATION: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the c... | CATALYTIC ACTIVITY: [Serine protease/helicase NS3]: Reaction=Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.; EC=3.4.21.98; Evidence={ECO:0000250|UniProtKB:P27958}; CATALYTIC ACTIVITY: [Serine protease/helicase NS3... | null | null | null | null | FUNCTION: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA struc... | Hepatitis C virus genotype 6h (isolate VN004) (HCV) |
O92815 | POL_WDSV | MGNSSSTPPPSALKNSDLFKTMLRTQYSGSVKTRRINQDIKKQYPLWPDQGTCATKHWEQAVLIPLDSVSEETAKVLNFLRVKIQARKGETARQMTAHTIKKLIVGTIDKNKQQTEILQKTDESDEEMDTTNTMLFIARNKRERIAQQQQADLAAQQQVLLLQREQQREQREKDIKKRDEKKKKLLPDTTQKVEQTDIGEASSSDASAQKPISTDNNPDLKVDGVLTRSQHTTVPSNITIKKDGTSVQYQHPIRNYPTGEGNLTAQVRNPFRPLELQQLRKDCPALPEGIPQLAEWLTQTMAIYNCDEADVEQLARVIFP... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. {ECO:0000250}; COFACT... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural constituent of virion [GO:0039660]; zinc ion binding ... | PF18697;PF00075;PF17919;PF00665;PF00077;PF00078;PF00098; | 2.30.30.850;3.10.20.370;3.30.70.270;2.40.70.10;3.10.10.10;3.30.420.10;4.10.60.10; | null | PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p25]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 for protease p14.; | null | FUNCTION: [Matrix protein p10]: Targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the pre-integration complex (By similarity). {ECO:0000250}.; FUNCTION: Capsid protein p25 forms the sp... | Walleye dermal sarcoma virus (WDSV) |
O92920 | HBEAG_HBVD7 | MQLFHLCLIISCSCPTVQASKLCLGWLWDMDIDPYKEFGATVQLLSFLPHDFFPSVRDLLDTASALFRDALESPEHCSPHHTALRQAILCWGELMTLATWVGANLQDPASRELVVTYVNINMGLKFRQLLWFHISCLTFGRETVIEYLVSFGVWIRTPQAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC | 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... | Hepatitis B virus genotype D (isolate Germany/1-91/1991) (HBV-D) |
O92921 | HBSAG_HBVD7 | MGQNLSTSNPLGFFPDHQLDPAFRANTANPDWDFNPNKDTWPDANKVGAGAFGLGFTPPHGGLLGWSPQAQGIIQTLPANPPPASTNRQTGRQPTPLSPPLRNTHPQAMQWNSTTFHQTLQDPRVRGLYFPAGGSSSGTVNPVPTTASPISSIFSRIGDPALNMENITSGLLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQSPTSNHSPTSCPPTCPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSVGPCRTCTTTVQGTSMYPSCCCTKPSDGNCTCIPIPSSWA... | 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 (isolate Germany/1-91/1991) (HBV-D) |
O92954 | GAG_RSVSB | MEAVIKVISSACKTYCGKTSPSKKEIGAMLSLLQKEGLLMSPSDLYSPGSWDPITAALSQRAMVLGKSGELKTWGLVLGALKAAREEQVTSEQAKFWLGLGGGRVSPPGPECIEKPATERRIDKGEEVGETTVQRDAKMAPEETATPKTVGTSCYHCGTAIGCNCATASAPPPPYVGSGLYPSLAGVGEQQGQGGDTPRGAEQPRAEPGHAGLAPGPALTDWARIREELASTGPPVVAMPVVIKTEGPAWTPLEPKLITRLADTVRTKGLRSPITMAEVEALMSSPLLPHDVTNLMRVILGPAPYALWMDAWGVQLQTVI... | 3.4.23.- | null | proteolysis [GO:0006508]; viral procapsid maturation [GO:0046797] | host cell nucleolus [GO:0044196]; host cell nucleoplasm [GO:0044095]; viral capsid [GO:0019028] | aspartic-type endopeptidase activity [GO:0004190]; nucleic acid binding [GO:0003676]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF00607;PF02813;PF00077;PF00098; | 1.10.1200.30;2.40.70.10;1.10.375.10;1.10.150.90;4.10.60.10; | null | PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. The cleavage at the C-terminus of the Capsid protein p27 is slowly trimmed by the viral protease, sometimes being cut internally thereby generating the short version of the capsid protein and a capsid protein C-terminally extended by 3 ... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03322}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 1]: Virion {ECO:0000250|UniProtKB:P03322}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 2]: Virion {ECO:0000250|UniProtKB:P03322}.; SUBCELLULAR LOCATION: [Nuc... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: The p10 domain folds back and interacts with the capsid protein domain during Gag polyprotein assembly in the immature particle (before the maturation cleavage that splits the 2 domains). {ECO:0000250|UniProtKB:P03322}.; FUNCTION: [Capsid protein p27, alternate cleaved 1]: Self-associates t... | Rous sarcoma virus subgroup B (strain Schmidt-Ruppin) (RSV-SR-B) |
O92955 | ENV_RSVSB | MEAVIKAVLTGYPGETSKKDSKKKPPATSKKDPEKTPLLPTRVNYILIIGVLVLCEVTGVRADVHLLEQPGNLWITWASRTGQTDFCLSTQSATSPFQTCLIGIPSPISEGDFKGYVSDNCTTLEPHRLVSRGIPGGPENSTTLTYQKVSCLLLKLNVSLLDEPSELQLLGSQSLPNITNITRIPSVAGGCIGFTPYDSPAGVYGWDRREVTHILLTDPGNNPFFDKASNSSKPFTVVTADRHNLFMGSEYCGAYGYRFWEMYNCSQMRQNWSICQDVWGRGPPENWCTSTGGTWVNQSKEFNETEPFSFTVNCTGSNLG... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | null | PF03708;PF00429; | 1.10.287.210; | Alpharetroviruses envelope glycoprotein family | PTM: [Envelope glycoprotein gp95]: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000303|PubMed:31151254}. Host cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000303|PubMed:31151254}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000305}; P... | null | null | null | null | null | FUNCTION: [Surface protein]: The surface protein (SU) attaches the virus to the host cell entry receptor TVB-S3/CAR1 (PubMed:8945512). This interaction triggers the refolding of the transmembrane protein (TM) thereby unmasking its fusion peptide and the formation of a reactive thiolate on Cys-100 to activate its fusoge... | Rous sarcoma virus subgroup B (strain Schmidt-Ruppin) (RSV-SR-B) |
O92956 | POL_RSVSB | MEAVIKVISSACKTYCGKTSPSKKEIGAMLSLLQKEGLLMSPSDLYSPGSWDPITAALSQRAMVLGKSGELKTWGLVLGALKAAREEQVTSEQAKFWLGLGGGRVSPPGPECIEKPATERRIDKGEEVGETTVQRDAKMAPEETATPKTVGTSCYHCGTAIGCNCATASAPPPPYVGSGLYPSLAGVGEQQGQGGDTPRGAEQPRAEPGHAGLAPGPALTDWARIREELASTGPPVVAMPVVIKTEGPAWTPLEPKLITRLADTVRTKGLRSPITMAEVEALMSSPLLPHDVTNLMRVILGPAPYALWMDAWGVQLQTVI... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | COFACTOR: [Reverse transcriptase alpha-subunit]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255|PROSITE-ProRule:PRU00405}; COFACTOR: [Reverse transcriptase alpha-subunit]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; N... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826] | virion component [GO:0044423] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; zinc ion binding [GO:0008270] | PF00607;PF00552;PF02022;PF02813;PF00665;PF00077;PF00078;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;4.10.60.10; | null | PTM: [Isoform Gag-Pol polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000250|UniProtKB:P03354}.; PTM: Capsid protein p27: The cleavage at the C-terminus is slowly trimmed by the viral protease, sometimes being cut internally thereby generating the short version of the capsid protein and ... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03354}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 1]: Virion {ECO:0000250|UniProtKB:P03354}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 2]: Virion {ECO:0000250|UniProtKB:P03354}.; SUBCELLULAR LOCATION: [Nuc... | CATALYTIC ACTIVITY: [Reverse transcriptase alpha-subunit]: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:P... | null | null | null | null | FUNCTION: Capsid protein p27: Self-associates to form the irregular polyhedron core composed of hexamers and pentamers, that encapsulates the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro. Binds to inositol hexakisphosphate (IP6), which allows the assembly of the polyhedral capsid. {ECO:0000250|UniProt... | Rous sarcoma virus subgroup B (strain Schmidt-Ruppin) (RSV-SR-B) |
O92972 | POLG_HCVJ4 | MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKASERSQPRGRRQPIPKARRPEGRAWAQPGYPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTIPASAYEVRNVSGIYHVTNDCSNSSIVYEAADVIMHTPGCVPCVREGNSSRCWVALTPTLAARNASVPTTTIRRHVDLLVGTAAFCSAMYVGDLCGSIFLVSQLFTFSPRRHETVQDCNCSIYPGHVSGHRMAW... | 2.7.7.48; 3.4.21.98; 3.4.22.-; 3.6.1.15; 3.6.4.13 | COFACTOR: [Protease NS2]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17239391}; Note=Activity of protease NS2 is dependent on zinc ions and completely inhibited by EDTA. This is probably due to the fact that NS2 protease activity needs NS3 N-terminus that binds a zinc atom (active region NS2-3). ... | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host cell cycle G1/S transiti... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell lipid droplet [GO:0044186]; host cell mitochondrial membrane [GO:0044191]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; ribonucleoprotein complex [GO... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; molecular adaptor activity [GO:0060090]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; seri... | PF07652;PF01543;PF01542;PF01539;PF01560;PF01538;PF01006;PF01001;PF01506;PF08300;PF08301;PF12941;PF02907;PF00998; | 2.40.10.120;3.30.70.270;6.10.250.1610;6.10.250.1750;6.10.250.2920;2.20.25.210;3.30.160.890;2.30.30.710;1.20.1280.150;2.20.25.220;3.40.50.300;1.10.820.10;2.40.10.10; | Hepacivirus polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membran... | SUBCELLULAR LOCATION: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the c... | CATALYTIC ACTIVITY: [Serine protease/helicase NS3]: Reaction=Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.; EC=3.4.21.98; Evidence={ECO:0000250|UniProtKB:P27958}; CATALYTIC ACTIVITY: [Serine protease/helicase NS3... | null | null | null | null | FUNCTION: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA struc... | Hepatitis C virus genotype 1b (strain HC-J4) (HCV) |
O93182 | GAG_HV190 | MGARASVLSGGKLDAWEKIRLRPGGKKKYRLKHLVWASRELERFALNPGLLETPEGCLQIIEQIQPAIKTGTEELKSLFNLVAVLYCVHRKIDVKDTKEALDKIEEIQNKSQQKTQQAAADKEKDNKVSQNYPIVQNAQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNAMLNTVGGHQAAMQMLKDTINEEAAEWDRVHPVHAGPIPPGQMREPRGSDIAGTTSTLQEQIAWMTGNPAIPVGDIYKRWIILGLNKIVRMYSPVSILDIKQGPKEPFRDYVDRFFKTLRAEQATQDVKNWMTET... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype H (isolate 90CF056) (HIV-1) |
O93209 | POL_FFV | MDLLKPLTVERKGVKIKGYWDSQADITCVPKDLLQGEEPVRQQNVTTIHGTQEGDVYYVNLKIDGRRINTEVIGTTLDYAIITPGDVPWILKKPLELTIKLDLEEQQGTLLNNSILSKKGKEELKQLFEKYSALWQSWENQVGHRRIRPHKIATGTVKPTPQKQYHINPKAKPDIQIVINDLLKQGVLIQKESTMNTPVYPVPKPNGRWRMVLDYRAVNKVTPLIAVQNQHSYGILGSLFKGRYKTTIDLSNGFWAHPIVPEDYWITAFTWQGKQYCWTVLPQGFLNSPGLFTGDVVDLLQGIPNVEVYVDDVYISHDSE... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826]; viral penetration into host nucleus [GO:0075732] | host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; virion component [GO:0044423] | aspartic-type endopeptidase activity [GO:0004190]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523] | PF17921;PF00075;PF17919;PF00665;PF00078;PF18103;PF03539; | 1.10.340.70;2.30.30.140;3.30.70.270;6.10.20.110;2.40.70.10;3.10.10.10;3.30.420.10; | null | PTM: Specific enzymatic cleavages in vivo by viral protease yield mature proteins. The protease is not cleaved off from Pol. Since cleavage efficiency is not optimal for all sites, long and active p65Pro-RT, p87Pro-RT-RNaseH and even some Pr125Pol are detected in infected cells (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [Integrase]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000305}. Note=Nuclear at initial phase, cytoplasmic at assembly. {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease/Reverse transcriptase/ribonuclease H]: Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000305}. Note... | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; 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:CH... | null | null | null | null | FUNCTION: The aspartyl protease activity mediates proteolytic cleavages of Gag and Pol polyproteins. The reverse transcriptase (RT) activity converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell (early reverse transcription) or after proviral DNA transcription (late reverse ... | Feline foamy virus (FFV) (Feline syncytial virus) |
O93215 | POL_HV190 | MGARASVLSGGKLDAWEKIRLRPGGKKKYRLKHLVWASRELERFALNPGLLETPEGCLQIIEQIQPAIKTGTEELKSLFNLVAVLYCVHRKIDVKDTKEALDKIEEIQNKSQQKTQQAAADKEKDNKVSQNYPIVQNAQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNAMLNTVGGHQAAMQMLKDTINEEAAEWDRVHPVHAGPIPPGQMREPRGSDIAGTTSTLQEQIAWMTGNPAIPVGDIYKRWIILGLNKIVRMYSPVSILDIKQGPKEPFRDYVDRFFKTLRAEQATQDVKNWMTET... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype H (isolate 90CF056) (HIV-1) |
O93235 | CIRBA_XENLA | MSDEGKLFIGGLNFETNEDCLEQAFTKYGRISEVVVVKDRETKRSRGFGFVTFENVDDAKDAMMAMNGKSVDGRQIRVDQAGKSSGERRGGYRGGSSGGRGFFRGGRGRGGGDRGYGSSRFDNRSGGYGGSSGSRDYYGSGRSQGSYGDRSGGSYRDSYDSYATHE | null | null | cell migration [GO:0016477]; embryo development ending in birth or egg hatching [GO:0009792]; gastrulation [GO:0007369]; kidney field specification [GO:0072004]; mRNA stabilization [GO:0048255]; negative regulation of nuclear-transcribed mRNA poly(A) tail shortening [GO:0060212]; neurogenesis [GO:0022008]; positive reg... | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681] | enzyme binding [GO:0019899]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; ribosome binding [GO:0043022]; small ribosomal subunit rRNA binding [GO:0070181]; translation repressor activity [GO:0030371] | PF00076; | 3.30.70.330; | null | PTM: Methylated on arginine residues within RGG motifs. Methylation by prmt1 promotes cytoplasmic accumulation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shuttles between the nucleus and cytoplasm. Predominantly cytoplasmic in oocytes. Translocates from the nucleus to the cytoplasm upon arginine methylation (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Cold-inducible mRNA binding protein. Acts cooperatively with elavl1/elrA to stabilize AU-rich sequence (ARE)-containing mRNAs by binding to them and inhibiting their deadenylation (By similarity). Essential for embryonic gastrulation and neural development, acting to maintain the expression of a set of adhesi... | Xenopus laevis (African clawed frog) |
O93248 | OPA1_ONCMA | MLRVGRAVACVACNNLASKNMGVRFRMPLQKLHPLSRAIHHRYNASANAQRPPHCSAARHFTSMSRLPMRPPKPSPGGHGGWRYQQHRSFWMLRLASRLLKLRYIVLGSAVGGGYTAKKTYEEWKDMLPDMSAYNWVIPDFVWELSDQIDLDKLTKILPELEEIAKLLPELPDFDKIGENFTFLKSILFTAEAPGDTPVKAATEAPVTATPEASDKQFKKSSDKEKVDQLQEELLRTQMKYQRMLERLEKENKDLRKVVLQKDEKGIHQRKIKKSLIDMYSEVLDILSDFDSNYNTQDHLPRVVVVGDQSAGKTSVLEMI... | 3.6.5.5 | null | apoptotic process [GO:0006915]; GTP metabolic process [GO:0046039]; inner mitochondrial membrane organization [GO:0007007]; membrane tubulation [GO:0097749]; mitochondrial fusion [GO:0008053]; negative regulation of apoptotic process [GO:0043066]; visual perception [GO:0007601] | dendrite [GO:0030425]; microtubule [GO:0005874]; mitochondrial crista [GO:0030061]; mitochondrial intermembrane space [GO:0005758]; mitochondrial outer membrane [GO:0005741] | cardiolipin binding [GO:1901612]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; microtubule binding [GO:0008017]; phosphatidic acid binding [GO:0070300] | PF00350;PF19434; | 3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family | PTM: Cleaved by OMA1 or YME1L downstream of the transmembrane region in response to different signals to generate soluble forms. Cleaved by OMA1 at position S1 following stress conditions, generating the short soluble form (Dynamin-like GTPase OPA1, short form; S-OPA1). {ECO:0000250|UniProtKB:O60313}. | SUBCELLULAR LOCATION: [Dynamin-like GTPase OPA1, long form]: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O60313}; Single-pass membrane protein {ECO:0000255}. Note=Detected at contact sites between endoplasmic reticulum and mitochondrion membranes. {ECO:0000250|UniProtKB:O60313}.; SUBCELLULAR LOCATION: [Dynamin-... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; Evidence={ECO:0000250|UniProtKB:O60313}; | null | null | null | null | FUNCTION: Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function. Exists in two forms: the transmembrane, long form (Dynamin-like GTPase OPA1, long form; L-OPA1), whic... | Oncorhynchus masou (Cherry salmon) (Masu salmon) |
O93257 | XRCC6_CHICK | MEMWVLGEVGMAVLSAAAMADWVSYYRGDGPDEEEDGEQQEEEGPEAVADYRFSGRDSLIFLVDASKAMFEPYENEEAATPFDMTMQCIRNVYTSKIISSDKDLLSVVFYGMENNKNSADFKHIYVLQELDNPGAKRILELDQYRGDEGRVLFRETFGHNADYSLGEALWACSNLFSDVRVRLSHKRIMLFTNEDNPHANDSAKAKLARTRAGDLRDTGIILDLMHLKKPGGFDISLFYRDIINVAEDEDLGIQPDESGKLEHLMKKVRAKETRKRALSRLNLYLNKDLSFSVGVYNLIQKAYKPYPVKLYRETNEPVKT... | 3.6.4.-; 4.2.99.- | null | cellular response to gamma radiation [GO:0071480]; DNA recombination [GO:0006310]; double-strand break repair via nonhomologous end joining [GO:0006303]; negative regulation of DNA-templated transcription [GO:0045892]; telomere maintenance [GO:0000723] | chromosome [GO:0005694]; Ku70:Ku80 complex [GO:0043564]; nonhomologous end joining complex [GO:0070419]; nucleoplasm [GO:0005654]; ribonucleoprotein complex [GO:1990904] | 5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; ATP binding [GO:0005524]; damaged DNA binding [GO:0003684]; DNA helicase activity [GO:0003678]; double-stranded DNA binding [GO:0003690]; hydrolase activity [GO:0016787]; RNA binding [GO:0003723]; telomeric DNA binding [GO:0042162] | PF02735;PF03730;PF03731;PF02037; | 1.10.1600.10;2.40.290.10;4.10.970.10;1.10.720.30;3.40.50.410; | Ku70 family | PTM: Phosphorylated on serine residues. {ECO:0000250|UniProtKB:P12956}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12956}. Chromosome {ECO:0000250|UniProtKB:P12956}. | null | null | null | null | null | FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase that plays a key role in DNA non-homologous end joining (NHEJ) by recruiting DNA-PK to DNA. Required for double-strand break repair and V(D)J recombination. Also has a role in chromosome translocation. Has a role in chromosome translocation. The DNA helicas... | Gallus gallus (Chicken) |
O93274 | FZD8_XENLA | MESLSLSLLLLVSWLQGSQCAAAKELSCQEITVPLCKDIGYNYTYMPNQFNHDTQDEAGMEVHQFWPLVVIHCSPDLKFFLCSMYTPICLEDYKKPLPPCRSVCERARAGCAPLMRQYGFAWPDRMRCDRLPEQGNPDTLCMDYYNRTEQTTAAPSHPEPPKPPARSVPKGRTRVEPPRSRSRATGCESGCQCRAPMVQVSNERHPLYNRVRTGQIPNCAMPCHNPFFSPEERTFTEFWIGLWSVLCFASTFATVSTFLIDMERFKYPERPIIFLSACYLLVSTGYLIRLIAGHEKVACSRGELDLEHIIHYETTGPALC... | null | null | canonical Wnt signaling pathway [GO:0060070]; non-canonical Wnt signaling pathway [GO:0035567]; positive regulation of DNA-binding transcription factor activity [GO:0051091] | plasma membrane [GO:0005886] | G protein-coupled receptor activity [GO:0004930]; Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147] | PF01534;PF01392; | 1.10.2000.10;1.20.1070.10; | G-protein coupled receptor Fz/Smo family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10097073}; Multi-pass membrane protein {ECO:0000269|PubMed:10097073}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC... | Xenopus laevis (African clawed frog) |
O93279 | A4_TAKRU | MGETTAFVLLLVATLTRSSEIPADDTVGLLTEPQVAMFCGKLNMHINVQNGKWESDPSGTKSCLNTKEGILQYCQEVYPELQITNVVEANQPVSIQNWCKKGRKQCRSHTHIVVPYRCLVGEFVSDALLVPDKCKFLHQERMNQCESHLHWHTVAKESCGDRSMNLHDYGMLLPCGIDRFRGVKFVCCPAETEQETDSSEVEGEESDVWWGGADPEYSENSPPTPSRATYVAGDAFERDENGDGDEDEEDDEDVDPTDEQESDERTANVAMTTTTTTTTESVEEVVRAVCWAQAESGPCRAMLERWYFNPKKRRCVPFLF... | null | null | axonogenesis [GO:0007409]; central nervous system development [GO:0007417] | cell surface [GO:0009986]; early endosome [GO:0005769]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle [GO:0005798]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037] | heparin binding [GO:0008201]; serine-type endopeptidase inhibitor activity [GO:0004867]; signaling receptor activator activity [GO:0030546]; signaling receptor binding [GO:0005102]; transition metal ion binding [GO:0046914] | PF10515;PF12924;PF12925;PF02177;PF03494;PF00014; | 6.10.250.1670;1.20.120.770;3.30.1490.140;3.90.570.10;4.10.410.10;2.30.29.30; | APP family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Functional neuronal receptor which couples to intracellular signaling pathway through the GTP-binding protein G(O). {ECO:0000250}. | Takifugu rubripes (Japanese pufferfish) (Fugu rubripes) |
O93308 | SMC1A_XENLA | MGFLKLIEIENFKSYKGRQIIGPFHRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEDSGEEKVFSRVIVGGSSEYKINNKVVQLSEYSDSLEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEAERYQRLKDEVARAQIQLQLFKLYHNESEIEKLNKELSVKNKGIEKDKKHMDKVEEELKDKKKELGKMMREQQAIEKEIKEKDAELNQKLPQYIKAKENPSHKIKKFRAAKKSLQ... | null | null | cell division [GO:0051301]; DNA repair [GO:0006281]; meiotic cell cycle [GO:0051321]; response to DNA damage checkpoint signaling [GO:0072423]; response to radiation [GO:0009314]; sister chromatid cohesion [GO:0007062] | kinetochore [GO:0000776]; meiotic cohesin complex [GO:0030893]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; DNA binding [GO:0003677] | PF06470;PF02463; | 1.20.1060.20;3.30.70.1620;3.40.50.300; | SMC family, SMC1 subfamily | null | SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain... | null | null | null | null | null | FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped.... | Xenopus laevis (African clawed frog) |
O93309 | SMC3_XENLA | MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKRDKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSSKRETSGEKSRQLRDAQQDARDKMEEIERQVRELKSKISAMKEEKEQLSSERQEQIKQRTKLELKTKDLQDELAGNS... | null | null | cell division [GO:0051301]; DNA repair [GO:0006281]; meiotic cell cycle [GO:0051321]; mitotic sister chromatid cohesion [GO:0007064]; regulation of DNA replication [GO:0006275] | chromatin [GO:0000785]; chromosome, centromeric region [GO:0000775]; meiotic cohesin complex [GO:0030893]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cohesin loader activity [GO:0061775]; double-stranded DNA binding [GO:0003690] | PF06470;PF02463; | 1.10.287.1490;1.20.1060.20;3.30.70.1620;3.40.50.300; | SMC family, SMC3 subfamily | PTM: Acetylation at Lys-113 and Lys-114 by ESCO1 is important for genome stability and S phase sister chromatid cohesion. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9649503}. Chromosome {ECO:0000269|PubMed:9649503}. Chromosome, centromere {ECO:0000269|PubMed:9649503}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably b... | null | null | null | null | null | FUNCTION: Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Co... | Xenopus laevis (African clawed frog) |
O93310 | RAD21_XENLA | MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIICPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFSLNQSRVEEITMREEVSNINILQDNDFGDFGMDDREMMREGSAFEDDMLTTNASNLKLEPEQSTSQLNEKSNHLEYDDQYKDDNFGEGNEGGILDDKLLSNDAGGIFDDPPAMPEEGVAMPEQPVHDDLDDDDNVSMGAPDSPDSVDPVEPLPTMTDQTTLVPNEEEAFALEPIDITVKETKAKRKR... | null | null | apoptotic process [GO:0006915]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; protein localization to chromatin [GO:0071168]; replication-born double-strand break repair via sister chromatid exchange [GO:1990414]; sister chromatid cohesion [GO:0007062] | chromosome, centromeric region [GO:0000775]; cohesin complex [GO:0008278]; cytosol [GO:0005829]; nuclear matrix [GO:0016363]; spindle pole [GO:0000922] | chromatin binding [GO:0003682] | PF04824;PF04825; | 1.10.10.580; | Rad21 family | PTM: Cleaved by separase/ESPL1 at the onset of anaphase; this cleavage is required for sister chromatid separation and cytokinesis (By similarity). Cleaved by caspases at the beginning of apoptosis (By similarity). {ECO:0000250|UniProtKB:O60216}.; PTM: Phosphorylated; becomes hyperphosphorylated in M phase of cell cycl... | SUBCELLULAR LOCATION: [Double-strand-break repair protein rad21 homolog]: Nucleus {ECO:0000250|UniProtKB:O60216}. Nucleus matrix {ECO:0000250|UniProtKB:O60216}. Chromosome {ECO:0000269|PubMed:11931760}. Chromosome, centromere {ECO:0000250|UniProtKB:O60216}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O... | null | null | null | null | null | FUNCTION: [Double-strand-break repair protein rad21 homolog]: As a member of the cohesin complex, involved in sister chromatid cohesion from the time of DNA replication in S phase to their segregation in mitosis, a function that is essential for proper chromosome segregation, post-replicative DNA repair, and the preven... | Xenopus laevis (African clawed frog) |
O93327 | H2AY_CHICK | MSSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAIITPPPAKKAKSPSQKKTVSKKTGGKKGARKSKKKQGEVSKSASADSTTEGTPADGFTVLSTKSLFLGQKLQVVQADIATIDSDAVVHPTNSDFYTGGEVGSTLEKKGGKEFVEAVIELRKKNGPLDIAGAVVSAGHGLPAKFVIHCNSPGWGSDKCEELLEKTVKNCLALADEKKLKSIAFPSIGSGRNGFPK... | null | null | heterochromatin organization [GO:0070828]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription of nucleolar large rRNA by RNA polymerase I [GO:1901837]; nucleosome assembly [GO:0006334]; regulation ... | nucleosome [GO:0000786]; nucleus [GO:0005634] | ADP-D-ribose binding [GO:0072570]; ADP-D-ribose modification-dependent protein binding [GO:0160002]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211;PF01661; | 1.10.20.10;3.40.220.10; | Histone H2A family | PTM: ADP-ribosylated. {ECO:0000305, ECO:0000305|PubMed:15718235}.; PTM: Monoubiquitinated at either Lys-116 or Lys-117. May also be polyubiquitinated. Ubiquitination is mediated by the CUL3/SPOP E3 complex and does not promote proteasomal degradation. Instead, it is required for enrichment in inactive X chromosome chro... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75367}. Chromosome {ECO:0000250|UniProtKB:O75367}. | null | null | null | null | null | FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regula... | Gallus gallus (Chicken) |
O93344 | AL1A2_CHICK | MTSSKIEMPGEVKADPAALMASLHLLPSPTLNLEIKHTKIFINNEWQNSESGRVFPVYNPATGEQICEIQEADKVDTDKAVRAARLAFSLGSVWRRMDASERGQLLDKLADLVERDRAVLATMESLNSGKPFLQAFYVDLQGVIKTLRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVVNILPGFGPIVGAAIASHVGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCC... | 1.2.1.36 | null | heart looping [GO:0001947]; heart morphogenesis [GO:0003007]; positive regulation of gene expression [GO:0010628]; protein homotetramerization [GO:0051289]; response to retinoic acid [GO:0032526]; retinoic acid biosynthetic process [GO:0002138]; retinoic acid metabolic process [GO:0042573]; retinol metabolic process [G... | cytoplasm [GO:0005737] | aldehyde dehydrogenase (NAD+) activity [GO:0004029]; NAD-retinol dehydrogenase activity [GO:0004745]; retinal dehydrogenase activity [GO:0001758] | PF00171; | null | Aldehyde dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + retinal = 2 H(+) + NADH + retinoate; Xref=Rhea:RHEA:16177, ChEBI:CHEBI:15035, ChEBI:CHEBI:15036, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.36; Evidence={ECO:0000250|UniProtKB:Q62148}; PhysiologicalDirection=left-to-right; Xref=Rhea:R... | null | PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000250|UniProtKB:Q63639}. | null | null | FUNCTION: Catalyzes the NAD-dependent oxidation of aldehyde substrates, such as all-trans-retinal and all-trans-13,14-dihydroretinal, to their corresponding carboxylic acids, all-trans-retinoate and all-trans-13,14-dihydroretinoate, respectively. Retinoate signaling is critical for the transcriptional control of many g... | Gallus gallus (Chicken) |
O93348 | HBB1_PAGBO | MVEWTDKERSIISDIFSHLDYEDIGPKALSRCLIVYPWTQRHFSGFGNLYNAESIIGNANVAAHGIKVLHGLDRGLKNMDNIEATYADLSTLHSEKLHVDPDNFKLLADCITIVLAAKMGQAFTAEIQGAFQKFLAVVVSALGKQYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues. | Pagothenia borchgrevinki (Bald rockcod) (Trematomus borchgrevinki) |
O93349 | HBB2_TRENE | MVEWTDKERTIISDIFSHMDYDDIGPKALSRCLIVYPWTQRHFSGFGNLYNAEAIIGNANVAAHGIKVLHGLDRGMKNMDNIADAYTDLSTLHSEKLHVDPDNFKLLSDCITIVLAAKMGHAFTAETQGAFQKFLAAVVSALGKQYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues. | Trematomus newnesi (Dusky notothen) |
O93351 | HBB_TREHA | MVEWTDKERSIISDIFSHMDYDDIGPKALSRCLVVYPWTQRYFSGFGNLYNAEGIMSNANVAAHGIKVLHGLDRGVKNMDNIAATYADLSTLHSEKLHVDPDNFKLLSDCITIVLAAKMGHAFTAETQGAFQKFLAVVVSALGKQYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues. | Trematomus hansoni (Striped rockcod) (Notothenia hansoni) |
O93364 | OXLA_CROAD | MNVFFMFSLLFLAALGSCAHDRNPLEECFRETDYEEFLEIAKNGLTATSNPKRVVIVGAGMAGLSAAYVLAGAGHQVTVLEASERVGGRVRTYRKKDWYANLGPMRLPTKHRIVREYIKKFDLKLNEFSQENENAWYFIKNIRKRVREVKNNPGLLEYPVKPSEEGKSAAQLYVESLRKVVEELRSTNCKYILDKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVGGMDQLPTSMYEAIKEKVQVHFNARVIEIQQNDREATVTYQTSANEMSSVTADYVIVCTTSRAARRI... | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:6067195}; | amino acid catabolic process [GO:0009063]; apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | L-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family, FIG1 subfamily | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9703950}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:6067195}; CATALYTIC ACTIVITY: Reaction=H2O ... | null | null | null | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:6067195). Is active on L-Arg, L-Phe, L-Met, and L-Leu and is weakly active on L-Val (PubMed:6067195). Exhibits di... | Crotalus adamanteus (Eastern diamondback rattlesnake) |
O93383 | NRG1_XENLA | MAEKKKVKEGKGRKGKGKKDRKGKKAEGSDQGAAASPKLKEIKTQSVQEGKKLVLKCQAVSEQPSLKFRWFKGEKEIGAKNKPDSKPEHIKIRGKKKSSELQISKASSADNGEYKCMVSNQLGNDTVTVNVTIVPKPTYNHLLLMKIYLKVTSVEKSVEPSTLNLLESQKEVIFATTKRGDTTAGPGHLIKCSDKEKTYCVNGGECYVLNGITSSNQFMCKCKPGFTGARCTETDPLRVVRSEKHLGIEFMEAEELYQKRVLTITGICIDLLVVGDMCVVDAYCKTKKQRKKLNDRLRQSLRERNKNITNKDNRPHNPKN... | null | null | animal organ development [GO:0048513]; cell differentiation [GO:0030154]; intracellular signal transduction [GO:0035556]; nervous system development [GO:0007399] | extracellular space [GO:0005615]; plasma membrane [GO:0005886] | chemorepellent activity [GO:0045499]; growth factor activity [GO:0008083]; protein tyrosine kinase activator activity [GO:0030296] | PF07679;PF02158; | 2.60.40.10;2.10.25.10; | Neuregulin family | PTM: Proteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form.; PTM: Extensive glycosylation precedes the proteolytic cleavage. {ECO:0000250}. | SUBCELLULAR LOCATION: [Pro-neuregulin-1, membrane-bound isoform]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Does not seem to be active. {ECO:0000250}.; SUBCELLULAR LOCATION: [Neuregulin-1]: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Direct ligand for the ERBB tyrosine kinase receptors. Induces expression of acetylcholine receptor in synaptic nuclei. | Xenopus laevis (African clawed frog) |
O93385 | PITX2_CHICK | MSCMKDPLSLERLGAGNNKLCSSSPSSSSSSSSCHHQQPALAMATALAPGQARSSLEAAKHRLEVHTISDTSSPEAAEKEKSQQGKSEDAGPEDPSKKKRQRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRERNQQAELCKNGFGPQFNGLMQPYDDMYPGYSYNNWAAKGLTSASLSTKSFPFFNSMNVNPLSSQSMFSPPNSISSMSMSSSMVPSAVTGVPGSGLNSLNNLNNLSNPSLNSAVPTPACPYAPPTPPYVYRDTCNSSLASLRLKAKQHSSFGYASVQNPAS... | null | null | anatomical structure morphogenesis [GO:0009653]; determination of left/right symmetry [GO:0007368]; embryonic limb morphogenesis [GO:0030326]; embryonic organ morphogenesis [GO:0048562]; heart looping [GO:0001947]; heart morphogenesis [GO:0003007]; positive regulation of dermatome development [GO:0061184]; positive reg... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046;PF03826; | 1.10.10.60; | Paired homeobox family, Bicoid subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:P97474}. | null | null | null | null | null | FUNCTION: May play a role in myoblast differentiation. May be involved in the establishment of left-right asymmetry in the developing embryo (By similarity). May play a role in vasculogenesis during avian embryogenesis. {ECO:0000250|UniProtKB:P97474}. | Gallus gallus (Chicken) |
O93409 | MLRSA_DANRE | MAPKKAKRRAAGGEGSSNVFSMFEQSQIQEYKEAFTIIDQNRDGIISKDDLRDVLASMGQLNVKNEELEAMIKEASGPINFTVFLTMFGEKLKGADPEDVIVSAFKVLDPEGTGSIKKEFLEELLTTQCDRFTAEEMKNLWAAFPPDVAGNVDYKNICYVITHGEEKEE | null | null | actin-myosin filament sliding [GO:0033275]; muscle contraction [GO:0006936]; muscle tissue morphogenesis [GO:0060415]; skeletal muscle tissue development [GO:0007519] | cytoplasm [GO:0005737]; myosin complex [GO:0016459] | calcium ion binding [GO:0005509] | PF13405; | 1.10.238.10; | null | null | null | null | null | null | null | null | FUNCTION: Myosin regulatory subunit that plays a role to maintain muscle integrity during early development (PubMed:32707087). Plays a role in muscle contraction (PubMed:32707087). {ECO:0000269|PubMed:32707087}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
O93430 | GLRA1_DANRE | MFALGIYLWETIVFFSLAASQQAAARKAASPMPPSEFLDKLMGKVSGYDARIRPNFKGPPVNVTCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPSMLDSIWKPDLFFANEKGANFHEVTTDNKLLRISKNGNVLYSIRITLVLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWDEKGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEARFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFS... | null | null | cellular response to amino acid stimulus [GO:0071230]; cellular response to ethanol [GO:0071361]; cellular response to zinc ion [GO:0071294]; central nervous system development [GO:0007417]; chloride transmembrane transport [GO:1902476]; monoatomic ion transport [GO:0006811]; neuropeptide signaling pathway [GO:0007218]... | chloride channel complex [GO:0034707]; dendrite [GO:0030425]; membrane [GO:0016020]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | extracellularly glycine-gated chloride channel activity [GO:0016934]; extracellularly glycine-gated ion channel activity [GO:0016933]; glycine binding [GO:0016594]; ligand-gated monoatomic ion channel activity [GO:0015276]; neurotransmitter receptor activity [GO:0030594]; transmembrane signaling receptor activity [GO:0... | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Glycine receptor (TC 1.A.9.3) subfamily, GLRA1 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q64018}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q64018}. Synapse {ECO:0000250|UniProtKB:Q64018}. Perikaryon {ECO:0000250|UniProtKB:Q64018}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q64018}. Cell membrane {ECO:0000269|PubMed:1018... | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:10188956, ECO:0000269|PubMed:26344198}; | null | null | null | null | FUNCTION: Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:10188956, PubMed:26344198). Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents. Channel activity is potent... | Danio rerio (Zebrafish) (Brachydanio rerio) |
O93507 | TAL1_DANRE | MMEKLKSEQFPLSPSAEGCASPPRGDGDARGKQEGTTAETGEHRLPEELNGVAKETAHHATELKKEVAVIELSRRGGSADIKGRELKAELSHKVQTTELCRPPIPLPLPPRDPLSDTRMVQLSPPAFPLPARAMLYSNMTTPLATINSGFAGDAEQYGMYPSNRVKRRPAPYEVEINDGSQPKIVRRIFTNSRERWRQQNVNGAFAELRKLIPTHPPDKKLSKNEILRLAMKYINFLAKLLNDQDDMVGGEAPARANRDSRDATLVRDDLLQEMLSPNSSCGSLLDGDASPESFTEDQDSSVESRPSARGLHHSSLPLDG... | null | null | angiogenesis [GO:0001525]; artery morphogenesis [GO:0048844]; blood vessel development [GO:0001568]; definitive hemopoiesis [GO:0060216]; embryonic heart tube development [GO:0035050]; embryonic hemopoiesis [GO:0035162]; endocardium formation [GO:0060214]; endocardium morphogenesis [GO:0003160]; erythrocyte differentia... | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P22091, ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Transcription factor that plays a pivotal role in hemopoietic and endothelial development, acting synergistically with lmo2 and downstream of clo. Specifies mesodermal precursors to a hemangioblast cell fate. Hemangioblasts are bipotential precursors of blood and endothelium, and in the absence of hemopoietic... | Danio rerio (Zebrafish) (Brachydanio rerio) |
O93523 | VM3BP_BOTJA | MIEVLLVTICLAAFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSKDYSETHYSPDGREITTYPAVEDHCYYHGRIENDADSTASISACNGLKGHFKLQRETYFIEPLKLSNSEAHAVFKYENVEKEDEAPKMCGVTQNWKSYEPIKKASQLVVTAEQQKYNPFRYVELFIVVDQGMVTKNNGDLDKIKARMYELANIVNEILRYLYMHAALVGLEIWSNGDKITVKPDVDYTLNSFAEWRKTDLLTRKKHDNAQLLTAIDFNGPTIGYAYIGSMCHPKRSVAIVED... | 3.4.24.49 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:18831982}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18831982}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF08516;PF00200;PF01562;PF01421; | 3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIb sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 in insulin B chain.; EC=3.4.24.49; Evidence={ECO:0000269|PubMed:6819660}; | null | null | null | null | FUNCTION: [Zinc metalloproteinase-disintegrin-like bothropasin]: Has caseinolytic activity. Causes hemorrhage on rabbit skin and causes myonecrosis in mouse tibialis anterior muscle.; FUNCTION: [Disintegrin-like bothropasin]: Inhibits platelet aggregation. | Bothrops jararaca (Jararaca) (Bothrops jajaraca) |
O93529 | FOXB1_XENLA | MPRPGRNTYSDQKPPYSYISLTAMAIQGSQEKMLPLSEIYKFIMDRFPYYRENTQRWQNSLRHNLSFNDCFIKIPRRPDQPGKGSFWALHPRCGDMFENGSFLRRRKRFKVMKSDHLAPSKASDAAQYLQQQAKLRLSALAASGTHLPPMSTYNLGVSPTSSFKHPFAIENIIAREYKMPGGLAFSTMQPMPAAYPLHNQLTTVGGSIGTGWPHMYSSSMLDSTTPISMANSDYSVSAYGVPIKPICHGAQTLLPAIPVPIKPTAALPALPTHIPAILSNSSPSMSPTSPQTATSQSSPATPSDTLTNPSTALLSVAVH | null | null | axon target recognition [GO:0007412]; cell migration in diencephalon [GO:0061381]; ectoderm development [GO:0007398]; floor plate development [GO:0033504]; hypothalamus cell migration [GO:0021855]; inferior colliculus development [GO:0061379]; mammillary body development [GO:0021767]; mammillothalamic axonal tract deve... | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; 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] | PF00250; | 1.10.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}. | null | null | null | null | null | FUNCTION: Probable transcription factor. May be involved in the early anteroposterior patterning of the neuroectoderm. {ECO:0000269|PubMed:11404077, ECO:0000269|PubMed:15656969}. | Xenopus laevis (African clawed frog) |
O93530 | WRN_XENLA | MTSLQRKLPEWMSVKQQEDRIDDAKKSFCKKNILEDNLPFMKFNGSIVYSYESNDCSLLSEDIRSSLLEEDVLGFDIEWPPVYTKGKTGKVALIQVCVSEKKCYLFHISPMAGFPKGLKRLLEDESVRKVGVGIEGDQWKLMSDYELKLKGFIELSEMANQKLRCKEKWTFNGLIKHLFKEQLYKRKSYRCSNWDIFLLTEDQKLYAATDAYAGLLIYKKLEGMDAHESDSFRVGREGVADCKGVKRQLTDLSKGLMDLVNQVPNSFGCYTEAVRAVDILEDLSEKLEELRNIMKEASKAEGNGLHFQNSEDCSKKDKSI... | 3.1.-.-; 5.6.2.4 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:Q14191}; Note=Binds 2 divalent metal cations in the exonuclease domain; in human Mg(2+) and Mn(2+) give high activity, in mouse Mn(2+) and Zn(2+) give high activity. {ECO:0000250|UniProtKB:O09053, ECO:0000250|UniProtKB:Q1419... | DNA metabolic process [GO:0006259]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via homologous recombination [GO:0000724]; G-quadruplex DNA unwinding [GO:0044806]; telomere maintenance [GO:0000723] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654] | 3'-5' DNA helicase activity [GO:0043138]; 3'-5' exonuclease activity [GO:0008408]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; four-way junction helicase activity [GO:0009378]; isomerase activity [GO:0016853]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:00... | PF00270;PF01612;PF00271;PF00570;PF14493;PF16124;PF09382; | 1.10.150.80;3.40.50.300;3.30.420.10;1.10.10.10; | Helicase family, RecQ subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9697700}. Note=Associates with probable replication foci (PubMed:9697700). {ECO:0000269|PubMed:9697700}. | 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:0000250|UniProtKB:Q14191, ECO:0000305|PubMed:9697700}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:... | null | null | null | null | FUNCTION: Multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alte... | Xenopus laevis (African clawed frog) |
O93574 | RELN_CHICK | TNGLNTTTASVLQFSLGSGSCRFSYSDPSITVSYSKNSSADWTQLEKISAPSNVSTIIHILYLPEDAKGENVHFQWKQDYLHAGEVYEACWALDNILIINAAHRKVVLEDNLDPVDTGNWLFFPGATVKHSCQSDGNSIYFHGTEGSEFNFATTRDVDLSTEDAQEQWAEEFESQPKGWDILGAVIGTECGTLESGSSMVFLRDGERKICTPYMDTTGYGNLRFYFSMGGNCDSGESHENDVILYAKIEGRREHIALDTLTYAAYKVPSLVSVVISPDLQTPATKFCLKQKSHQGHNRNVWAVDYFHVLPVLPSTVTHMI... | 3.4.21.- | null | axon guidance [GO:0007411]; brain development [GO:0007420]; cell adhesion [GO:0007155]; cell morphogenesis [GO:0000902]; central nervous system development [GO:0007417]; cerebral cortex tangential migration [GO:0021800]; glial cell differentiation [GO:0010001]; neuron migration [GO:0001764]; peptidyl-tyrosine phosphory... | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; extracellular space [GO:0005615]; neuron projection [GO:0043005] | lipoprotein particle receptor binding [GO:0070325]; metal ion binding [GO:0046872]; serine-type peptidase activity [GO:0008236] | PF07974;PF18720;PF21471; | 2.60.120.260; | Reelin family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: Extracellular matrix serine protease that plays a role in layering of neurons in the cerebral cortex and cerebellum. Regulates microtubule function in neurons and neuronal migration. Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migra... | Gallus gallus (Chicken) |
O93627 | RBL_THEKO | MVEKFDTIYDYYVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESSTGTWTTLYPWYEQERWADLSAKAYDFHDMGDGSWIVRIAYPFHAFEEANLPGLLASIAGNIFGMKRVKGLRLEDLYFPEKLIREFDGPAFGIEGVRKMLEIKDRPIYGVVPKPKVGYSPEEFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERAEIMAKIIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKHAMVDVVITGWGALRYIRDLAADYGLAIHGHRAMHAAFTRNPYHGISMFVLAKLYRLIGIDQLHVGTAGA... | 4.1.1.39 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:11435112, ECO:0000269|PubMed:20926376}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:11435112, ECO:0000269|PubMed:20926376}; | AMP catabolic process [GO:0006196]; carbon fixation [GO:0015977] | null | magnesium ion binding [GO:0000287]; oxidoreductase activity [GO:0016491]; ribulose-bisphosphate carboxylase activity [GO:0016984] | PF00016;PF02788; | 3.20.20.110;3.30.70.150; | RuBisCO large chain family, Type III subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:9988755}; CATALYTIC A... | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 90 degrees Celsius (PubMed:9988755). Highly thermostable, has a half-life of 220 minutes at 90 degrees Celsius (PubMed:9988755). {ECO:0000269|PubMed:20926376, ECO:0000269|PubMed:9988755}; | FUNCTION: Catalyzes the addition of molecular CO(2) and H(2)O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA) (PubMed:10512715, PubMed:9988755). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase (PubMed:17303759). {ECO:000025... | Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
O93715 | GLCDH_SACSO | MKAIIVKPPNAGVQVKDVDEKKLDSYGKIKIRTIYNGICGTDREIVNGKLTLSTLPKGKDFLVLGHEAIGVVEESYHGFSQGDLVMPVNRRGCGICRNCLVGRPDFCETGEFGEAGIHKMDGFMREWWYDDPKYLVKIPKSIEDIGILAQPLADIEKSIEEILEVQKRVPVWTCDDGTLNCRKVLVVGTGPIGVLFTLLFRTYGLEVWMANRREPTEVEQTVIEETKTNYYNSSNGYDKLKDSVGKFDVIIDATGADVNILGNVIPLLGRNGVLGLFGFSTSGSVPLDYKTLQEIVHTNKTIIGLVNGQKPHFQQAVVHL... | 1.1.1.120; 1.1.1.359; 1.1.1.47; 1.1.1.48 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16556607}; Note=Binds 2 Zn(2+) ions per subunit. One of the zinc atoms is essential for catalytic activity while the other has a structural function. {ECO:0000269|PubMed:16556607}; | galactose catabolic process via D-galactonate [GO:0033498]; non-phosphorylated glucose catabolic process [GO:0019595]; protein tetramerization [GO:0051262] | null | aldose 1-dehydrogenase activity [GO:0047640]; galactose 1-dehydrogenase (NADP+) activity [GO:0047910]; galactose 1-dehydrogenase activity [GO:0019151]; galactose binding [GO:0005534]; glucose 1-dehydrogenase (NAD+) activity [GO:0047934]; glucose 1-dehydrogenase (NADP+) activity [GO:0047935]; glucose 1-dehydrogenase [NA... | PF08240;PF16912; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family, Glucose 1-dehydrogenase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH; Xref=Rhea:RHEA:14293, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16217, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.47; Evidence={ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812}; CATALYTIC ACTIVITY: Reaction=D-gluco... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 mM for D-glucose (in the presence of NAD(+), at 70 degrees Celsius and pH 8) {ECO:0000269|PubMed:3827812}; KM=1.5 mM for D-glucose (in the presence of NAD(+), at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170}; KM=0.44 mM for D-glucose (in the presen... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. {ECO:0000269|PubMed:3827812}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 77 degrees Celsius. At 37 degrees Celsius, shows about 20% activity as compared with the maximal value. {ECO:0000269|PubMed:3827812}; | FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Displays broad substrate specificity since it is able to catalyze the oxidation of a number of alternative aldose sugars, such as D-galactose, D-xylose and L-arabinose, to the corresponding glyconate. Can utilize both ... | Saccharolobus solfataricus (Sulfolobus solfataricus) |
O93845 | DPOE_EMENI | MPSRKPSKYGNKFRSGAASFNPKRTKTVEFSSLRSSEATSQDEKFEAIRLANSIDESLGFPRFEAGEKRVGWLINMHSTSIEDPNVPGGRAGVDYYFLDDDGGSFKATVEYDPYFLIAVKTGHEAEVEEWCRRMFEGLIKKIKRVVKEDLKLPNHLLGHRRTFLQLDFANVSHLLEVRKTLLPLAEKNRKNARPNGTTNASDFIIDIREYDVPYHVRVAIDKDIRIGKWYTVEATHGIISLTCLEERLTRADPVVLAFDIETTKLPLKFPDSVIDQIMMISYMIDGQGFLITNREIVSEDIDDFEYTPKPEYSGPFMIFN... | 2.7.7.7 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P15436}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P15436}; | base-excision repair, gap-filling [GO:0006287]; CENP-A containing chromatin assembly [GO:0034080]; CMG complex assembly [GO:0140529]; DNA replication proofreading [GO:0045004]; double-strand break repair via nonhomologous end joining [GO:0006303]; error-prone translesion synthesis [GO:0042276]; gene conversion [GO:0035... | chromosome, telomeric repeat region [GO:0140445]; epsilon DNA polymerase complex [GO:0008622]; nuclear replication fork [GO:0043596] | 4 iron, 4 sulfur cluster binding [GO:0051539]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; double-stranded DNA binding [GO:0003690]; nucleotide binding [GO:0000166]; single-stranded DNA 3'-5' DNA exonuclease activity [GO:0008310]; single-stranded DNA binding [GO:0003697]; SUMO binding [... | PF00136;PF03104;PF08490; | 1.10.132.60;3.30.342.10;3.90.1600.10;3.30.420.10; | DNA polymerase type-B family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | 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:0000250|UniProtKB:P15436}; | null | null | null | null | FUNCTION: DNA polymerase II participates in chromosomal DNA replication. {ECO:0000250}. | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
O93852 | ALO1_CANAL | MTDIPESLKPFVTKKVIHSTWAGTFLCKPQAIFQPRNVEEIQELIKQARLHGKTIMTVGSGHSPSDLTMTTEWLCNLDKFNHVLLEEPYYAPKSPTDDTPEIKFVDLTVEAGTRIFELNEYLKRNNLAIQNLGSISDQSIAGLISTGTHGSTQYHGLVSQQVVSVKFLNSAGELITCSSVDKPEYFRAILLSLGKIGIITHVTLRTCPKYTIKSKQEIINFETLLNNWDNLWLESEFIRIWWFPYTNKCVLWRANKSTDPLSDPRPSWYGTKLGRFFYESLLWVSVHLFPRLTPFVEKFVFGQQYGEVETLGKGDIAVQN... | 1.1.3.37; 1.1.3.8; 1.3.3.12 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; | cellular detoxification [GO:1990748]; cellular response to oxidative stress [GO:0034599]; cellular response to starvation [GO:0009267]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; filamentous growth of a population of unicellular organisms in response to st... | mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | D-arabinono-1,4-lactone oxidase activity [GO:0003885]; FAD binding [GO:0071949]; L-galactonolactone oxidase activity [GO:0050024]; L-gulono-1,4-lactone dehydrogenase activity [GO:0080049]; L-gulonolactone oxidase activity [GO:0050105] | PF04030;PF01565; | 3.30.465.10;3.30.70.2520;3.30.43.10; | Oxygen-dependent FAD-linked oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=D-arabinono-1,4-lactone + O2 = dehydro-D-arabinono-1,4-lactone + H(+) + H2O2; Xref=Rhea:RHEA:23756, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16292, ChEBI:CHEBI:58277; EC=1.1.3.37; Evidence={ECO:0000269|PubMed:7957197}; PhysiologicalDirection=left-to-right; Xref=R... | null | PATHWAY: Cofactor biosynthesis; D-erythroascorbate biosynthesis; dehydro-D-arabinono-1,4-lactone from D-arabinose: step 2/2. {ECO:0000269|PubMed:7957197}. | null | null | FUNCTION: D-arabinono-1,4-lactone oxidase that catalyzes the final step of biosynthesis of D-erythroascorbic acid, an important antioxidant and one of the virulence factors enhancing the pathogenicity (PubMed:11349062, PubMed:7957197). Is also able to oxidize L-galactono-1,4-lactone, L-xylono-1,4-lactone and L-gulono-1... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
O93875 | ERG3_CANAX | MDIVLEICDYYLFDKVYADVFPKDGAVHEFLKPAIQSFSQIDFPSLPNLDSFDTNSTLISSNNFNISNVNPATIPSYLFSKIASYQDKSEIYGLAPKFFPATDFINTSFLARSNIFRETLSLFIITTIFGWLLYFIVAYLSYVFVFDKKIFNHPRYLKNQMSLEIKRATTAIPVMVLLTIPFFLLELNGYSFLYLDINECTGGYKAILWQIPKFILFTDCGIYFLHRWLHWPSVYKVLHKPHHKWIVCTPFASHAFHPVDGFFQSLPYHLYPLLFPLHKVLYLFLFTFVNFWTVMIHDGSYWSNDPVVNGTACHTVHHLY... | 1.14.19.20 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:P53045}; | cholesterol biosynthetic process via lathosterol [GO:0033490]; ergosterol biosynthetic process [GO:0006696]; sphingolipid biosynthetic process [GO:0030148] | endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789] | C-4 methylsterol oxidase activity [GO:0000254]; C-5 sterol desaturase activity [GO:0000248]; delta7-sterol 5(6)-desaturase activity [GO:0050046]; iron ion binding [GO:0005506]; sphingolipid delta-4 desaturase activity [GO:0042284]; sphingosine hydroxylase activity [GO:0000170] | PF04116; | null | Sterol desaturase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a Delta(7)-sterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a Delta(5),Delta(7)-sterol + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:54320, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI... | null | PATHWAY: Steroid metabolism; ergosterol biosynthesis; ergosterol from zymosterol: step 3/5. | null | null | FUNCTION: C-5 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathwa (PubMed:10433965, PubMed:20733039, PubMed:9000517). ERG3 catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol (PubMed:10433965). The third module... | Candida albicans (Yeast) |
O93922 | ATG7_PICPA | MTSMDIPYSQISSFVNSSFFQKVSQLKLNKYRLDDTDKAIVGSVDFKFIGKNQPTSLSVDESSFNDNITYTHAQFPVKGILKNLNTVEDFRKVDKNEFLQSQGLVVHKSIQDRSCLKDLSKLTQFFILSFSDLKGFKFIYWFGFPSLVSRWKVNKLSGLTESQIEPYESKLNEWLNARLPIEQKQAFIIDNLEFKPFEQLSSFSPDDQLNIGFIDTSSILNKCSTQLRNILYMLAYYGFENIKVYNFRFNNTTSFTLDITLAEPLTSEPKTTGWERTAQGKLGPKLADIGALVDPARLADQSVDLNLKLMKWRVMPELDL... | null | null | autophagosome assembly [GO:0000045]; cellular response to nitrogen starvation [GO:0006995]; micropexophagy [GO:0000426]; pexophagy [GO:0000425]; piecemeal microautophagy of the nucleus [GO:0034727]; protein modification by small protein conjugation [GO:0032446]; protein transport [GO:0015031] | phagophore assembly site [GO:0000407] | Atg12 activating enzyme activity [GO:0019778]; Atg8 activating enzyme activity [GO:0019779] | PF16420;PF00899; | 3.40.50.720;3.40.140.100;3.40.140.70; | ATG7 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal structure {ECO:0000250}. | null | null | null | null | null | FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for its conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and aut... | Komagataella pastoris (Yeast) (Pichia pastoris) |
O93927 | FKS1_CRYNH | MSYPNPPPPPKGSASFSSSSSDPFNQTNQLPYDSQFPPQHAFAHPSAPNPGAGGAGVAPPGQGGQYAPYYDNEPEMGGRWEGGGMGRETWASESGWSQNEPNYPPSDYHGGPGYLPSRASTPTFEGSNAGHRPRDPYPAWTVDANIPLSKEEIEDVLIDLANKFGFQKDSSRNVYDFLMIQLDSRASRMSPNQALLTLHADYIGGEHANYRKWYFAAQLDLDDAIGAVQNPGLNRVRSVARRGGKTKNPLATAQEKSLESATSRWRTAMNNMSQYDRLRQVALYLLCWGEAAQVRFMPECLCFIFKCADDYYRSPECQNR... | 2.4.1.34 | null | (1->3)-beta-D-glucan biosynthetic process [GO:0006075]; cell wall biogenesis [GO:0042546]; cell wall organization [GO:0071555]; fungal-type cell wall polysaccharide biosynthetic process [GO:0051278] | 1,3-beta-D-glucan synthase complex [GO:0000148]; perinuclear endoplasmic reticulum [GO:0097038]; plasma membrane [GO:0005886] | 1,3-beta-D-glucan synthase activity [GO:0003843]; alpha-1,3-glucan synthase activity [GO:0047657] | PF14288;PF02364; | null | Glycosyltransferase 48 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P38631}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378, ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34; Evidence={ECO:0000269|PubMed:15980360}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.21 mM for UDP-glucose (at pH 7.75) {ECO:0000269|PubMed:15980360}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.75. {ECO:0000269|PubMed:15980360}; | null | FUNCTION: Catalytic subunit of the 1,3-beta-glucan synthase (GS) complex (PubMed:15980360). Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall (PubMed:15980360). Involved in cell wall synthesis, maintenance and remodeling (By similarity). {ECO:0000250|UniProtKB:P38631, ECO:0000269|PubMed:1... | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
O93937 | PYR1_EMENI | MPETVGHEEPALPSSPQAGGAVAYNAISKELQPLPPTETANGGIIPPASSRIEGSTGRLCALELEDGTVYQGYNFGAEKSVAGELVFQTGMVGYPESITDPSYRGQILVITFPLVGNYGVPSRETMDELLKTLPKHFESTEIHIAALVVATYAGENYSHFLAESSLGQWLKEQGVPAIHGVDTRALTKRIRQKGSMLGRLLLHKADVAETDAALAQDTWKSSFEQIDWVDPNTKNLVSEVSIREPKLFSPPENVALKHPSSRPIRVLCLDVGLKFNQLRCLVARGVEVLVVPWDYDFPTLAGKDYDGLFVSNGPGDPATM... | 2.1.3.2; 3.5.1.2; 6.3.4.16; 6.3.5.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; amino acid metabolic process [GO:0006520]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; nitrogen compound metabolic process [GO:0006807]; UTP biosynthetic proces... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | amino acid binding [GO:0016597]; aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; glutaminase activity [GO:000435... | PF02786;PF02787;PF00988;PF00117;PF02142;PF00185;PF02729; | 3.40.50.20;3.40.50.880;3.40.50.1370;3.30.1490.20;3.30.470.20;3.50.30.20;1.10.1030.10;3.20.20.140;3.40.50.1380; | Metallo-dependent hydrolases superfamily, DHOase family, CAD subfamily; CarA family; CarB family; Metallo-dependent hydrolases superfamily, DHOase family, CAD subfamily; Aspartate/ornithine carbamoyltransferase superfamily, ATCase family | null | null | CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI... | null | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000250|UniProtKB:P07259}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000250|UniProtKB:P07259}. | null | null | FUNCTION: Multifunctional protein that encodes the first 2 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5) and aspartate transcarbamylase (ATCase; EC 2.1.3.2). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (G... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
O94168 | SNF1_CANTR | MSEQNQGQPDQQHSGDHQHHHHHHHHHHHSQQPAQPIPIDPNVNPANRIGRYQIIKTLGEGSFGKVKLAQHVGTGQKVALKIINRKTLAKSDMQGRVEREISYLRLLRHPHIIKLYDVIKSKDEIIMVIEFAGKELFDYIVQRGKMPEDEARRFFQQIIAAVEYCHRHKIVHRDLKPENLLLDDQLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSSGVILYVMLCGRLPFDDEFIPALFKKISNGVYTLPNYLSPGAKHLLTRMLVVNPLNRITIHEIMEDEWFKQDMPDYLLPPDLSKIK... | 2.7.11.1 | null | CAMKK-AMPK signaling cascade [GO:0061762]; establishment of mitotic spindle orientation [GO:0000132]; fungal-type cell wall assembly [GO:0071940]; invasive growth in response to glucose limitation [GO:0001403]; negative regulation of TORC1 signaling [GO:1904262]; negative regulation of translation [GO:0017148]; phospho... | cellular bud neck septin ring [GO:0000144]; nuclear envelope lumen [GO:0005641]; nuclear membrane [GO:0031965]; nucleotide-activated protein kinase complex [GO:0031588]; vacuolar membrane [GO:0005774] | AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; guanyl-nucleotide exchange factor activity [GO:0005085]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310] | PF16579;PF00069;PF08587; | 3.30.310.80;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily | null | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8 (By similarity). {ECO:0000250}. | Candida tropicalis (Yeast) |
O94200 | PFKA2_CANAX | MISIVNGTSTLSLVAGSVETLNQAINFYTNILGLSVHSEQNDWTYLSNDDNKMIVKIQLDTKSGLSLDQVNDRRTEIIAKLNVTDWRSLDTTSVLKVQNLVALIETLTTFNYTLQITPNELYPNEVYCVGPIGYIIGFTACDEPLTLVPPLQKSHPKPGLVSNLMSKSGSQSRNIEETKAVRRNIAVMTSGGDSQGMNAAVRAVVRATIFHGSKAFAVQEGYAGLVKGGPEYIKEMKWQDVRGFLSEGGTNIGTARCMEFKERWGRLKGCKNLIDAGIDGLIVCGGDGSLTGADLFRHEWPSLIQELKDKGEITNEQFER... | 2.7.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03184}; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; vacuolar acidification [GO:0007035]; vacuolar proton-transporting V-type ATPase complex assembly [GO:0070072] | 6-phosphofructokinase complex [GO:0005945]; membrane [GO:0016020]; mitochondrion [GO:0005739] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029]; mRNA binding [GO:0003729]; proton-transporting ATPase activity, rotatio... | PF00365; | 3.40.50.450;3.10.180.10;3.40.50.460; | Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Eukaryotic two domain clade 'E' sub-subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}. | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03184}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03184}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. | Candida albicans (Yeast) |
O94201 | PFKA1_CANAX | MPSSSDAINRISYISLVTSDNDKFNQTFQFYSQLGFRLTKSFSKVSSYGSGLGANHPEFQLGVSHDSLKEVWLESYPLQNVDSNGNLRPWQEMEVYDGDNCERLNESTVIKVRLLGETPLKSISQKQFVFFTTQLNKIEKILTDANVKYGKVVDNVILAEDPLNNIISFSNTQNELCKTRFQSPEEYVEKTTAEILAKRKKSQLGSKFGSFEEISPSEVGGGNGLRKKKIGVMTSGGDAPGMNPAVRAVVRAGIYYGCDVYAVYEGYEGLVKGGDLLKKMEWSDVRSYMSLGGTSIGTARCKEFRERAGRLQGAYNMIKN... | 2.7.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03184}; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; regulation of intracellular pH [GO:0051453] | 6-phosphofructokinase complex [GO:0005945]; mitochondrion [GO:0005739] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029]; proton-transporting ATPase activity, rotational mechanism [GO:0046961] | PF00365;PF18468; | 3.10.180.90;3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Eukaryotic two domain clade 'E' sub-subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}. | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03184}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03184}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. | Candida albicans (Yeast) |
O94220 | INU2_ASPFI | MLNPKVAYMVWMTCLGLTLPSQAQSNDYRPSYHFTPDQYWMNEPNGLIKIGSTWHLFFQHNPTANVWGNICWGHATSTDLMHWAHKPTAIADENGVEAFTGTAYYDPNNTSGLGDSANPPYLAWFTGYTTSSQTQDQRLAFSVDNGATWTKFQGNPIISTSQEAPHDITGGLESRDPKVFFHRQSGNWIMVLAHGGQDKLSFWTSADTINWTWQSDLKSTSINGLSSDITGWEVPDMFELPVEGTEETTWVVMMTPAEGSPAGGNGVLAITGSFDGKSFTADPVDASTMWLDNGRDFDGALSWVNVPASDGRRIIAAVMN... | 3.2.1.7 | null | polysaccharide catabolic process [GO:0000272]; sucrose catabolic process [GO:0005987] | cytoplasm [GO:0005737]; extracellular region [GO:0005576] | inulinase activity [GO:0051670]; sucrose alpha-glucosidase activity [GO:0004575] | PF08244;PF00251; | null | Glycosyl hydrolase 32 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24251113}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (2->1)-beta-D-fructosidic linkages in inulin.; EC=3.2.1.7; Evidence={ECO:0000269|PubMed:22750808, ECO:0000269|PubMed:24251113}; | null | null | null | null | FUNCTION: Endo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60. {ECO:0000269|PubMed:24251113}. | Aspergillus ficuum |
O94235 | MPH1L_SCHPO | MSKRNPPVTNIADLVSDSSLDEDSLSFLEELQDPELYFKNDTFSSKSSHSDGTVTGDTLRRQSSGATALERLVSHPRTKNFDLQGNGGQNSALKEVNTPAYQSMHHFEHLITPLPSTNASHSEVSLSAGVNDLNSNSEHDLLPKSVNKTPGSLSISRRRRIGRIGLGPPKRAEYTLTDPSKTSDTKNSTEADEDIEMKSREVSPASNSVAATTLKPLQLHNTPLQTSQEHPKPSFHPSQFESSFSPRVQFDHDVERRASELHSRPVTVFQEPQRSASQPYESHALSPKVAPLFDNSQATPIPKRQQDVVTVANLQFIKLG... | 2.7.12.1 | null | cell division [GO:0051301]; chromosome segregation [GO:0007059]; meiosis I [GO:0007127]; meiotic centromeric cohesion protection in anaphase I [GO:1990813]; meiotic spindle assembly checkpoint signaling [GO:0033316]; mitotic spindle assembly checkpoint signaling [GO:0007094]; phosphorylation [GO:0016310]; protein local... | cytosol [GO:0005829]; kinetochore [GO:0000776]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Involved in the regulation of the onset of mitosis. Involved in a pathway that coordinates cell proliferation and differentiation. {ECO:0000269|PubMed:9601094}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
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