ID   C3U5A5_SAFV             Unreviewed;      2318 AA.
AC   C3U5A5;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   22-FEB-2023, entry version 87.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
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; Caphthovirinae; 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: Cytoplasmic vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004180}. 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   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC       {ECO:0000256|ARBA:ARBA00008303}.
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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: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-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
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   CDD; cd01699; RNA_dep_RNAP; 1.
DR   Gene3D; 1.20.960.20; -; 1.
DR   Gene3D; 2.60.120.20; -; 3.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 4.10.90.10; Capsid protein VP4 superfamily, Picornavirus; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51874; PCV_3C_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51218; SF3_HELICASE_2; 1.
PE   3: Inferred from homology;
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   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW   Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870};
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   Membrane {ECO:0000256|ARBA:ARBA00023136};
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
//