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Genome polyprotein [Cleaved into: Protein p5.6; Protein p32; NTPase (EC 3.6.1.15) (p39); Protein p30; Viral genome-linked protein (VPg) (p13); Protease-polymerase p76 (Pro-Pol) (EC 2.7.7.48) (EC 3.4.22.66)]

 POLG_FCVUR              Reviewed;        1763 AA.
Q66914;
09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-MAY-2017, entry version 103.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Protein p5.6;
Contains:
RecName: Full=Protein p32;
Contains:
RecName: Full=NTPase;
EC=3.6.1.15;
AltName: Full=p39;
Contains:
RecName: Full=Protein p30;
Contains:
RecName: Full=Viral genome-linked protein;
AltName: Full=VPg;
AltName: Full=p13;
Contains:
RecName: Full=Protease-polymerase p76;
Short=Pro-Pol;
EC=2.7.7.48;
EC=3.4.22.66;
ORFNames=ORF1;
Feline calicivirus (strain Cat/United States/Urbana/1960) (FCV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Caliciviridae; Vesivirus.
NCBI_TaxID=292349;
NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7618275; DOI=10.1006/viro.1995.1354;
Sosnovtsev S.V., Green K.Y.;
"RNA transcripts derived from a cloned full-length copy of the feline
calicivirus genome do not require VpG for infectivity.";
Virology 210:383-390(1995).
[2]
PROTEIN SEQUENCE OF 686-695, PROTEOLYTIC PROCESSING OF POLYPROTEIN,
AND MUTAGENESIS OF GLU-46; GLU-331; GLU-683; GLU-685; GLU-960;
GLU-1071; GLU-1345 AND GLU-1419.
PubMed=12072506; DOI=10.1128/JVI.76.14.7060-7072.2002;
Sosnovtsev S.V., Garfield M., Green K.Y.;
"Processing map and essential cleavage sites of the nonstructural
polyprotein encoded by ORF1 of the feline calicivirus genome.";
J. Virol. 76:7060-7072(2002).
[3]
PROTEIN SEQUENCE OF 961-969 AND 1072-1080, PROTEOLYTIC PROCESSING OF
POLYPROTEIN, AND MUTAGENESIS OF CYS-1193.
PubMed=10400760;
Sosnovtseva S.A., Sosnovtsev S.V., Green K.Y.;
"Mapping of the feline calicivirus proteinase responsible for
autocatalytic processing of the nonstructural polyprotein and
identification of a stable proteinase-polymerase precursor protein.";
J. Virol. 73:6626-6633(1999).
[4]
PROTEIN SEQUENCE OF 961-980.
PubMed=11062050; DOI=10.1006/viro.2000.0579;
Sosnovtsev S.V., Green K.Y.;
"Identification and genomic mapping of the ORF3 and VPg proteins in
feline calicivirus virions.";
Virology 277:193-203(2000).
[5]
FUNCTION OF PROTEASE-POLYMERASE P76.
PubMed=15254188; DOI=10.1128/JVI.78.15.8172-8182.2004;
Kuyumcu-Martinez M., Belliot G., Sosnovtsev S.V., Chang K.O.,
Green K.Y., Lloyd R.E.;
"Calicivirus 3C-like proteinase inhibits cellular translation by
cleavage of poly(A)-binding protein.";
J. Virol. 78:8172-8182(2004).
[6]
FUNCTION OF PROTEASE-POLYMERASE P76.
PubMed=15105529; DOI=10.1099/vir.0.19564-0;
Willcocks M.M., Carter M.J., Roberts L.O.;
"Cleavage of eukaryotic initiation factor eIF4G and inhibition of
host-cell protein synthesis during feline calicivirus infection.";
J. Gen. Virol. 85:1125-1130(2004).
[7]
INTERACTION IN VIRAL REPLICATION COMPLEX.
PubMed=16432023; DOI=10.1099/vir.0.81456-0;
Kaiser W.J., Chaudhry Y., Sosnovtsev S.V., Goodfellow I.G.;
"Analysis of protein-protein interactions in the feline calicivirus
replication complex.";
J. Gen. Virol. 87:363-368(2006).
-!- FUNCTION: NTPase presumably plays a role in replication. Despite
having similarities with helicases, does not seem to display any
helicase activity.
-!- FUNCTION: Viral genome-linked protein is covalently linked to the
5'-end of the positive-strand, negative-strand genomic RNAs and
subgenomic RNA. Acts as a genome-linked replication primer. May
recruit ribosome to viral RNA thereby promoting viral proteins
translation (By similarity). {ECO:0000250,
ECO:0000269|PubMed:15105529, ECO:0000269|PubMed:15254188}.
-!- FUNCTION: Protease-polymerase p76 processes the polyprotein: Pro-
Pol is first released by autocleavage, then all other proteins are
cleaved. Cleaves host translation initiation factor eIF4G1, eIF4G2
and PABP1 thereby inducing a shutdown of host protein synthesis.
This shutdown may not prevent viral mRNA from being translated
since viral Vpg replaces the cap. May cleave host polyadenylate-
binding protein thereby inhibiting cellular translation. It is
also an RNA-directed RNA polymerase which replicates genomic and
antigenomic viral RNA by recognizing specific signals. Transcribes
also a subgenomic mRNA by initiating RNA synthesis internally on
antigenomic RNA. This sgRNA codes for structural proteins.
Catalyzes the covalent attachment VPg with viral RNAs.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: Endopeptidase with a preference for cleavage
when the P1 position is occupied by Glu-|-Xaa and the P1' position
is occupied by Gly-|-Yaa.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- SUBUNIT: Protein p32: homodimer, interacts with NTPase, protein
p30 and Pro-Pol. Viral genome-linked protein interacts with capsid
protein and Pro-Pol. Protease-polymerase p76: Homooligomers,
interacts with Vpg, protein p32 and may interact with capsid
protein. {ECO:0000269|PubMed:16432023}.
-!- DOMAIN: Protease-polymerase is composed of two domains displaying
two different catalytic activity. These activities may act
independently.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
Pro-Pol is first autocatalytically cleaved, then processes the
whole polyprotein. {ECO:0000269|PubMed:10400760,
ECO:0000269|PubMed:12072506}.
-!- PTM: VPg is uridylylated by the polymerase and is covalently
attached to the 5'-end of the polyadenylated genomic and
subgenomic RNAs. This uridylylated form acts as a nucleotide-
peptide primer for the polymerase (By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; L40021; AAA79323.1; -; Genomic_RNA.
RefSeq; NP_783196.1; NC_001481.2.
ProteinModelPortal; Q66914; -.
SMR; Q66914; -.
MEROPS; C24.002; -.
GeneID; 1502252; -.
KEGG; vg:1502252; -.
OrthoDB; VOG0900025Y; -.
BRENDA; 3.4.22.66; 8732.
Proteomes; UP000001098; Genome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000317; Peptidase_C24.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF03510; Peptidase_C24; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00910; RNA_helicase; 1.
PRINTS; PR00916; 2CENDOPTASE.
PRINTS; PR00918; CALICVIRUSNS.
SMART; SM00382; AAA; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Covalent protein-RNA linkage;
Direct protein sequencing;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus;
Host gene expression shutoff by virus; Host-virus interaction;
Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Protease; Reference proteome; RNA-directed RNA polymerase;
Thiol protease; Transferase; Viral RNA replication.
CHAIN 1 1763 Genome polyprotein.
/FTId=PRO_0000341636.
CHAIN 1 46 Protein p5.6.
/FTId=PRO_0000036907.
CHAIN 47 331 Protein p32.
/FTId=PRO_0000036908.
CHAIN 332 685 NTPase.
/FTId=PRO_0000036909.
CHAIN 686 960 Protein p30.
/FTId=PRO_0000036910.
CHAIN 961 1071 Viral genome-linked protein.
/FTId=PRO_0000036911.
CHAIN 1072 1763 Protease-polymerase p76.
/FTId=PRO_0000036912.
DOMAIN 458 614 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1095 1199 Peptidase C24.
DOMAIN 1478 1603 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 484 491 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
ACT_SITE 1110 1110 For protease activity. {ECO:0000250}.
ACT_SITE 1131 1131 For protease activity. {ECO:0000250}.
ACT_SITE 1193 1193 For protease activity.
SITE 46 47 Cleavage; by Pro-Pol.
SITE 331 332 Cleavage; by Pro-Pol.
SITE 685 686 Cleavage; by Pro-Pol.
SITE 960 961 Cleavage; by Pro-Pol.
SITE 1071 1072 Cleavage; by Pro-Pol.
MOD_RES 984 984 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
MUTAGEN 46 46 E->A: Complete loss of proteolytic
processing between P5.6 and P32; Complete
loss of infectious clone recovery.
{ECO:0000269|PubMed:12072506}.
MUTAGEN 331 331 E->A: Complete loss of infectious clone
recovery. {ECO:0000269|PubMed:12072506}.
MUTAGEN 683 683 E->A: Complete loss of infectious clone
recovery. {ECO:0000269|PubMed:12072506}.
MUTAGEN 685 685 E->A: Complete loss of infectious clone
recovery. {ECO:0000269|PubMed:12072506}.
MUTAGEN 960 960 E->A: Complete loss of infectious clone
recovery. {ECO:0000269|PubMed:12072506}.
MUTAGEN 1071 1071 E->A: Complete loss of infectious clone
recovery. {ECO:0000269|PubMed:12072506}.
MUTAGEN 1193 1193 C->G: Complete loss of proteolytic
processing.
{ECO:0000269|PubMed:10400760}.
MUTAGEN 1345 1345 E->A: No effect on infectious clone
recovery. {ECO:0000269|PubMed:12072506}.
MUTAGEN 1419 1419 E->A: No effect on infectious clone
recovery. {ECO:0000269|PubMed:12072506}.
SEQUENCE 1763 AA; 194911 MW; 7F105592DF0BF821 CRC64;
MSQTLSFVLK THSVRKDFVH SVKRTLQRRR DLQYLYNKLS RPIRAEACPS CASYDVCPNC
TSGSIPDDGS SKGQIPSWED VTKTSTYSLL LSEDTSDELH PDDLVNVAAH IRKALSTQSH
PANVDMCKEQ LTSLLVMAEA MLPQRSRSTL PLHQKYVAAR LEWREKFFSK PLDFLLEKIG
TSRDILQITA VWKIIIEKAC YCKSYGEHWF EAAKQKLREI KSYEHNTLKP LIGAFIDGLR
LMTIDNPNPM GFLPKLIGLI KPLNLAMIID NHENTLSGWV ITLTAIMELY NITECTIDVI
TSIITGFYDK IGKATKFYSQ IKALFTGFRS EDVANSFWYM AAAILCYLIT GLIPNNGRLS
KIKACLAGAT TLVSGIVATQ KLAAMFATWN SESIVNELSA RTVAISELNN PTTTSDTDSV
ERLLELAKIL HEEIKIHTLN PIMQSYNPIL RNLMSTLDGV ITSCNKRKAI AKKRPVPVCY
ILTGPPGCGK TTAALALAKK LSDQEPSVIN LDVDHHDTYT GNEVCIVDEF DSSDKVDYAN
FVIGMVNSAP MVLNCDMLEN KGKLFTSKYI IMTSNSETPV KPSSRRAGAF YRRVTIIDVA
NPLAESHKRA RPGTSVPRSC YKKNFSHLSL AKRGAECWCK EYVLDPKGLQ HQSIKAPPPT
FLNIDSLAQT MKQDFTLKNM AFEAENGHSE HRYGFVCQQG EVETVRRLLN AVRTRLNATF
TVCVGSEASS SIGCTAHVLT PDEPFNGKKY VVSRCNEASL SALEGNCVQS ALGVCMSTKD
LTHLCHFIRG KIVNDSVRLD ELPANQHVVT VNSVFDLAWA LRRHLTLAGQ FQAIRAAYDV
LTAPDKVPAM LRHWMDETSF SDEHVVTQFV TPGGIVILES CGGARIWALG HNVIRAGGVT
ATPTGGCIRF MGLSAQTMPW SEIFRELFSL LGRIWSSIKV STLVLTALGM YASRFRPKSE
AKGKTKSKVG PYRGRGVALT DDEYDEWREH NATRKLDLSV EDFLMLRHRA ALGADDADAV
KFRSWWNSRS RLADDYEDVT VIGKGGVKHE KIRTNTLRAV DRGYDVSFAE ESGPGTKFHK
NAIGSVTDVC GEHKGYCVHM GHGVYATVAH VAKGDSFFLG ERIFDLKTNG EFCCFRSTKI
LPSAAPFFPG KPTRDPWGSP VATEWKPKPY TTTSGKIVGC FATTSTETHP GDCGLPYIDD
NGRVTGLHTG SGGPKTPSAK LVVPYVHIDM KTKSVTAQKY DVTKPDISYK GLICKQLDEI
RIIPKGTRLH VSPAHTEDFE ECSHQPASLG SGDPRCPKSL TAIVVDSLKP YCDKVEGPPH
DILHRVQKML IDHLSGFVPV NISSETSMLS AFHKLNHDTS CGPYLGGRKK DHMTNGEPDK
PLLDLLSAKW KLATQGIALP HEYTIGLKDE LRPVEKVAEG KRRMIWGCDV GVATVCAAAF
KGVSDAITAN HQYGPVQVGI NMDSPSVEAL HQRIKSAAKV YAVDYSKWDS TQSPRVSAAS
IDILRYFSDR SPIVDSAANT LKSPPIAIFN GVAVKVSSGL PSGMPLTSVI NSLNHCLYVG
CAILQSLEAR GVPVTWNLFS TFDMMTYGDD GVYMFPMMFA SVSDQIFANL SAYGLKPTRV
DKSVGSIEPI DPESVVFLKR TITRTPQGIR GLLDRSSIIR QFYYIKGENS DDWKTPPKSI
DPTSRGQQLW NACLYASQHG VEFYNKIYKL AQKAVEYEEL HLEPPTYHSA LEHYNNQFNG
VEARSDQIDS SGMTALHCDV FEV


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