ID C3U5A5_SAFV Unreviewed; 2318 AA. AC C3U5A5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 02-JUN-2021, entry version 80. DE RecName: Full=Capsid protein VP0 {ECO:0000256|ARBA:ARBA00018989}; DE EC=3.4.22.28 {ECO:0000256|ARBA:ARBA00012631}; DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552}; DE AltName: Full=Capsid protein VP1 {ECO:0000256|ARBA:ARBA00018984}; DE AltName: Full=Capsid protein VP2 {ECO:0000256|ARBA:ARBA00018985}; DE AltName: Full=Capsid protein VP3 {ECO:0000256|ARBA:ARBA00018981}; DE AltName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; DE AltName: Full=Leader protein {ECO:0000256|ARBA:ARBA00016334}; DE AltName: Full=P1C {ECO:0000256|ARBA:ARBA00015466}; DE AltName: Full=P1D {ECO:0000256|ARBA:ARBA00015464}; DE AltName: Full=Picornain 3C {ECO:0000256|ARBA:ARBA00019475}; DE AltName: Full=Protease 3C {ECO:0000256|ARBA:ARBA00021011}; DE AltName: Full=Protein 2C {ECO:0000256|ARBA:ARBA00019346}; DE AltName: Full=Protein 3A {ECO:0000256|ARBA:ARBA00019289}; DE AltName: Full=RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022412}; DE AltName: Full=VPg {ECO:0000256|ARBA:ARBA00019035}; DE AltName: Full=Virion protein 1 {ECO:0000256|ARBA:ARBA00017124}; DE AltName: Full=Virion protein 3 {ECO:0000256|ARBA:ARBA00017121}; DE AltName: Full=protein 2B {ECO:0000256|ARBA:ARBA00019290, ECO:0000256|ARBA:ARBA00019353}; DE Flags: Fragment; GN Name=gp1 {ECO:0000313|EMBL:ACO92355.1}; OS Saffold virus (SafV) (Human TMEV-like virus-Saffold). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Picornavirales; Picornaviridae; Cardiovirus. OX NCBI_TaxID=434309 {ECO:0000313|EMBL:ACO92355.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:ACO92355.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Pak5152 {ECO:0000313|EMBL:ACO92355.1}; RX PubMed=19193786; DOI=10.1128/JVI.02085-08; RA Blinkova O., Kapoor A., Victoria J., Jones M., Wolfe N., Naeem A., RA Shaukat S., Sharif S., Alam M.M., Angez M., Zaidi S., Delwart E.L.; RT "Cardioviruses are genetically diverse and cause common enteric infections RT in South Asian children."; RL J. Virol. 83:4631-4641(2009). CC -!- FUNCTION: Affects membrane integrity and causes an increase in membrane CC permeability. {ECO:0000256|ARBA:ARBA00004017}. CC -!- FUNCTION: Forms a primer, VPg-pU, which is utilized by the polymerase CC for the initiation of RNA chains. {ECO:0000256|ARBA:ARBA00002520}. CC -!- FUNCTION: Forms an icosahedral capsid of pseudo T=3 symmetry with CC capsid proteins VP2 and VP3. Together they form an icosahedral capsid CC composed of 60 copies of each VP1, VP2, and VP3, with a diameter of CC approximately 300 Angstroms.VP4 lies on the inner surface of the CC protein shell formed by VP1, VP2 and VP3. All the three latter proteins CC contain a beta-sheet structure called beta-barrel jelly roll. VP1 is CC situated at the 12 fivefold axes, whereas VP2 and VP3 are located at CC the quasi-sixfold axes. {ECO:0000256|ARBA:ARBA00002469}. CC -!- FUNCTION: Serves as membrane anchor via its hydrophobic domain. CC {ECO:0000256|ARBA:ARBA00003704}. CC -!- FUNCTION: VP0 precursor is a component of immature procapsids. CC {ECO:0000256|ARBA:ARBA00002982}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CC Evidence={ECO:0000256|ARBA:ARBA00001556}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004180}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004180}; CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004180}. Host cytoplasm CC {ECO:0000256|ARBA:ARBA00004192}. Host cytoplasmic vesicle membrane CC {ECO:0000256|ARBA:ARBA00004295}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004295}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004295}. Host nucleus, host nucleolus CC {ECO:0000256|ARBA:ARBA00004307}. Membrane CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004287}. Virion CC {ECO:0000256|ARBA:ARBA00004328}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FJ463616; ACO92355.1; -; Genomic_RNA. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW. DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR CDD; cd00205; rhv_like; 3. DR Gene3D; 2.40.10.10; -; 1. DR Gene3D; 2.60.120.20; -; 3. DR Gene3D; 3.30.70.270; -; 2. DR Gene3D; 4.10.90.10; -; 1. DR InterPro; IPR015031; Capsid_VP4_Picornavir. DR InterPro; IPR037080; Capsid_VP4_sf_Picornavirus. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ. DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir. DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR044067; PCV_3C_PRO. DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001676; Picornavirus_capsid. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR033703; Rhv-like. DR InterPro; IPR001205; RNA-dir_pol_C. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR029053; Viral_coat. DR Pfam; PF00548; Peptidase_C3; 1. DR Pfam; PF00680; RdRP_1; 1. DR Pfam; PF00073; Rhv; 2. DR Pfam; PF00910; RNA_helicase; 1. DR Pfam; PF08935; VP4_2; 1. DR PRINTS; PR00918; CALICVIRUSNS. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF56672; SSF56672; 1. DR PROSITE; PS51874; PCV_3C_PRO; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51218; SF3_HELICASE_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Capsid protein {ECO:0000256|ARBA:ARBA00022561}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Helicase {ECO:0000256|ARBA:ARBA00022806}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200}; KW Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Ion channel {ECO:0000256|ARBA:ARBA00023303}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}; KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484}; KW T=pseudo3 icosahedral capsid protein {ECO:0000256|ARBA:ARBA00022706}; KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transport {ECO:0000256|ARBA:ARBA00022448}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804}; KW Viral ion channel {ECO:0000256|ARBA:ARBA00023039}; KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}; KW Virion {ECO:0000256|ARBA:ARBA00022844}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}. FT DOMAIN 1310..1475 FT /note="SF3 helicase" FT /evidence="ECO:0000259|PROSITE:PS51218" FT DOMAIN 1660..1853 FT /note="Peptidase C3" FT /evidence="ECO:0000259|PROSITE:PS51874" FT DOMAIN 2095..2213 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT COILED 1553..1580 FT /evidence="ECO:0000256|SAM:Coils" FT NON_TER 2318 FT /evidence="ECO:0000313|EMBL:ACO92355.1" SQ SEQUENCE 2318 AA; 259535 MW; 639293B2F85610EC CRC64; MCFTPSLWFK NCHSFSKPSG LGFLILLTGN MACKHGYPFL CPLCTAIDVS SDGSFALLFD NEWYPTDLLT VDLDDDVFYP LDCLMDWTDL PLIQDVLMEP QGNSNSSDKN NSQSSGNEGV IINNYYSNQY QNSIDLSANA NGVGKENSKP QGQLMNILGS AADAFKNIAP LLMDQDTEEM TNLSDRVASD TAGNTATNTQ STVGRLFGYA SRHRGKHPTS CADRATDKVL AAERYYTIKL ATWDTTLKAF DHIRVPFPHI LSGKEGGVFG ATLRRHYLCK CGWRIQVQCN ASQFHAGSLL IFMAPEFDTS PYESETEPDK NKVFTMDTTW QSGTKCLRGH SFESKTNQSL RPLSLNHQNT WQWTIYPHQI LNLRTNTTCD IEVPYVNICP TSSWTQHANW TLVVAVLTPL QCPTGSAPDV EITASIQPVK PVFNGLRHSV LEPDSPFPGT IREHAGTFYS TTPDTTVPVY GKTISTPANY MCGEFTDLLS LCKIPTFIGN NLDSKWNPYF SSTNSVNENV SLVTYQVTLS SINLANTMLS SVARNFNQYR GSLNFLFVFT GSAMVKGKFL ISYTPPGADK PKNRNQAMQA TYAIWDLGLN SSYNFTVPFI SPTHFRQTSY TTSTITSVDG WISVWQLTPL TYPANTPTHS DILTLVSGGD DFTLRMPVTP TKYVPHGVDN AEKGKVADDN ASTDFVAEPV KLPENQTEVG FFYDRAVQAC VLKSSQNFSD TFQLQSSDTL LNQTILTPLP NYKVDQSKEE LVEQYRWLES AGTSTQPPYK TKQDWNFVMF SPFTYYKCDL EVTLTALNNN GQGALVRYSP CGAPADITTQ TMSSTPSLAD TRDPHMWFVG PGTTNQVSFV LPFTSPLSVL PAVWFNGYAN FDNSSRYGVA PNADFGRLFV QGSGTFSVHF RYKKMRVFCP RPTVYFPWPS NPQRTKIHAE NPVPILELQN PISIYRVDLF INFSDEIIQF TYKVHGRTVC QYEIPGFGLS RSGRLLVCMG EKPCQLPIST PKCFYHIVFT GSRNSFGVSI YKARYRPWKQ PLHDELFDYG FSTFTDFFKA VRDYHASYYK QRLQHDIETN PGPVQSVFQL QGGVLTKSQA PMSGLQSMLL RAIGIEADCT EFTRAVNLIT DLCNTWESAK TTLSSPEFWT KMVMRIVKMV AASVLYLHNP DLTTTVCLSL MAGIDILTND SVFNWLSSKL SKFFHTPAPP IVPLLQQQSP IREANDNFNL AKNIEWAIKT IKRIVEWITS WFKQEETSPQ AKLDKMLADF PEHCASILAM RNGRKAYTDC AGAFKYFEQL YNLAVQCKRI PLATLCEKFK NKHDHAVARP EPVVVVLRGN AGQGKSVTSQ IIAQAVSKLS FGRQSVYSLP PDSDYLDGYE NQYSVIMDDL GQNPDGEDFK VFCQMVSSTN FLPNMAHLEK KGTPFTSNFI IATTNLPKFR PVTVAHYPAV DRRITFDLTV EAGDECVTHN GMLDVEKAFE EIPGKPQLDC FNTDCRLLHK RGVRFVCNRT KNVYNLQQVV KMVKNTIDNK VENLKKMNTL VAQSPGNDMD YVLTCLRQTN AALQDQIDEL QEAFNQAQER QNFLSDWLKV SAIVFASIAS LSAVCKLVSR FKNLVCPAPV QIQLSEGEQA AYSGGKKGEK QTLQVLDVQG GGKIVAQAGN PVMDYEVNIA KNMVTPITFF YADKAQVTQS CLLIKGHLFV VNRHVAETDW CAFELKGTRH ERDSVQMRSV NKSGMEVDLT FVKVVKGPLF KDNSKKFCSK DDDFPARNET VIGIMNTGVP FVFTGKFLIG NQPVNTTTGA CFNHCIHYRA TTHRGWGGSA LICHVNGKKA VYAMHSAGGG GIAAATIITQ EMIEAAEKAL DCLTPQGAIV EIGIDTVVHV PRKTKLRRTV AHPCFQPKFE PAVLSRYDPR TTKDVDQVAF SKHTTNLEEL PPVFTVVAKE YANRVFTTLG KENQILTPEQ AILGLSGMDP MEKDTSPGLP YTQQGLKRAQ LVNFEQGTMA QNLKEAHTKL TKGNYEDILY QSFLKDEIRP IEKIHEAKTR IVDVPPFHHC IWGRQLLGRF ASKFQTNPGL DLGSAIGTDP DTDWTAFAFQ LLQYKYVYDV DYSNFDASHS TAMFEILIEN FFTVENGFDE RIGDYLRSLA VSRHAFEERR VLVRGGLPSG CAATSMLNTI INNIVIRAAL DLTYSNFEFD DIKVLSYGDD LLIATNYQIN FNLVKQRLAP FNYKITPANK TVEFPETSNL YEVTFLKRKF VRHNSCLFKP QMDTENLKAM VSYCRPGTLK EKLNSIALLA VHSGKSVYDE IFDPFRRIGI IVPEHSTM //