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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_FCVF4              Reviewed;        1763 AA.
P27408; Q66913;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-JUL-2008, sequence version 2.
10-MAY-2017, entry version 93.
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 Japanese F4) (FCV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Caliciviridae; Vesivirus.
NCBI_TaxID=11980;
NCBI_TaxID=9681; Felidae (cat family).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7696398; DOI=10.1292/jvms.56.1093;
Oshikamo R., Tohya Y., Kawaguchi Y., Tomonaga K., Maeda K., Takeda N.,
Utagawa E., Kai C., Mikami T.;
"The molecular cloning and sequence of an open reading frame encoding
for non-structural proteins of feline calicivirus F4 strain isolated
in Japan.";
J. Vet. Med. Sci. 56:1093-1099(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1383-1763.
PubMed=1853578; DOI=10.1016/0042-6822(91)91016-A;
Tohya Y., Taniguchi Y., Takahashi E., Utagawa E., Takeda N.,
Miyamura K., Yamazaki S., Mikami T.;
"Sequence analysis of the 3'-end of feline calicivirus genome.";
Virology 183:810-814(1991).
[3]
ACTIVE SITES, AND MUTAGENESIS OF HIS-1079; HIS-1093; HIS-1099;
HIS-1102; HIS-1110; GLU-1121; ASP-1125; GLU-1131; ASP-1155; GLU-1164;
CYS-1193 AND HIS-1208.
PubMed=17459935; DOI=10.1128/JVI.02840-06;
Oka T., Yamamoto M., Yokoyama M., Ogawa S., Hansman G.S., Katayama K.,
Miyashita K., Takagi H., Tohya Y., Sato H., Takeda N.;
"Highly conserved configuration of catalytic amino acid residues among
calicivirus-encoded proteases.";
J. Virol. 81:6798-6806(2007).
-!- FUNCTION: NTPase presumably plays a role in replication. Despite
having similarities with helicases, does not seem to display any
helicase activity (By similarity). {ECO:0000250}.
-!- 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}.
-!- 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 (By
similarity). {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- DOMAIN: Protease-polymerase is composed of two domains displaying
two different catalytic activity. These activities may act
independently (By similarity). {ECO:0000250}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
Pro-Pol is first autocatalytically cleaved, then processes the
whole polyprotein.
-!- 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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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D31836; BAA06622.2; -; Genomic_RNA.
EMBL; D90357; BAA14370.1; -; Genomic_RNA.
ProteinModelPortal; P27408; -.
SMR; P27408; -.
MEROPS; C24.002; -.
OrthoDB; VOG090000KB; -.
Proteomes; UP000008668; Genome.
Proteomes; UP000173772; 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; 4.
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;
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; RNA-directed RNA polymerase; Thiol protease; Transferase;
Viral RNA replication.
CHAIN 1 1763 Genome polyprotein.
/FTId=PRO_0000341991.
CHAIN 1 46 Protein p5.6.
/FTId=PRO_0000341992.
CHAIN 47 331 Protein p32.
/FTId=PRO_0000341993.
CHAIN 332 685 NTPase.
/FTId=PRO_0000341994.
CHAIN 686 960 Protein p30.
/FTId=PRO_0000341995.
CHAIN 961 1071 Viral genome-linked protein.
/FTId=PRO_0000341996.
CHAIN 1072 1763 Protease-polymerase p76.
/FTId=PRO_0000036899.
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:0000269|PubMed:17459935}.
ACT_SITE 1131 1131 For protease activity.
{ECO:0000269|PubMed:17459935}.
ACT_SITE 1193 1193 For protease activity.
{ECO:0000269|PubMed:17459935}.
SITE 46 47 Cleavage; by Pro-Pol. {ECO:0000250}.
SITE 331 332 Cleavage; by Pro-Pol. {ECO:0000250}.
SITE 685 686 Cleavage; by Pro-Pol. {ECO:0000250}.
SITE 960 961 Cleavage; by Pro-Pol. {ECO:0000250}.
SITE 1071 1072 Cleavage; by Pro-Pol. {ECO:0000250}.
MOD_RES 984 984 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
MUTAGEN 1079 1079 H->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1093 1093 H->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1099 1099 H->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1102 1102 H->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1110 1110 H->A: Complete loss of protease activity
in vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1121 1121 E->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1125 1125 D->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1131 1131 E->A: Complete loss of protease activity
in vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1155 1155 D->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1164 1164 E->A: No effect on protease activity in
vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1193 1193 C->A: Complete loss of protease activity
in vitro. {ECO:0000269|PubMed:17459935}.
MUTAGEN 1208 1208 H->A: Complete loss of protease activity
in vitro. {ECO:0000269|PubMed:17459935}.
CONFLICT 1417 1417 V -> M (in Ref. 2; BAA14370).
{ECO:0000305}.
CONFLICT 1485 1487 YSK -> FSN (in Ref. 2; BAA14370).
{ECO:0000305}.
SEQUENCE 1763 AA; 194988 MW; 173626D6C862E46C CRC64;
MSQTLSFVLK THSVRKDFVH SVKVTLARRR DLQYLYNKLA RTMRAEACPS CSSYDVCPNC
TSSDIPDNGS STTSIPSWED VTKTSTYSLL LSEDTSDELC PDDLVNVAAH IRKALSTQAH
PANTEMCKEQ LTSLLVMAEA MLPQRSRASI PLHQQHQAAR LEWREKFFSK PLDFLLERIG
VSKDILQITA IWKIILEKAC YCKSYGEQWF CAAKQKLREM RTFESDTLKP LVGAFIDGLR
FMTVDNPNPM GFLPKLIGLV KPLNLAMIID NHENTLSGWV VTLTAIMELY NITECTIDVI
TSLVTGFYDK ISKATKFFSQ VKALFTGFRS EDVANSFWYM AAAILCYLIT GLIPNNGRFS
KIKACLSGAT TLVSGIIATQ KLAAMFATWN SESIVNELSA RTVAISELNN PTTTSDTDSV
ERLLELAKIL HEEIKVHTLN PIMQSYNPIL RNLMSTLDGV ITSCNKRKAI ARKRQVPVCY
ILTGPPGCGK TTAAQALAKK LSDQEPSVIN LDVDHHDTYT GNEVCIIDEF DSSDKVDYAN
FVIGMVNSAP MVLNCDMLEN KGKLFTSKYI IMTSNSETPV KPSSKRAGAF YRRVTIIDVT
NPLVESHKRA RPGTSVPRSC YKKNFSHLSL AKRGAECWCK EYVLDPKGLQ HQTIKAPPPT
FLNIDSLAQT MKQDFVLKNM AFEAEDGCSE HRYGFICQQS EVETVRRLLN AIRARLNATF
TVCVGPEASH SIGCTAHVLT PDEPFNGRRF IVSRCNEASL AALEGNCVQS ALGVCMSNKD
LTHLCHFIRG KIVNDSVRLD ELPANQHVVT VNSVFDLAWA LRRHLTLTGQ FQAIRAAYDV
LTVPDKVPAM LRHWMDETSF SDEHVVTQFV TPGGVVILES CGGARIWALG HNVIRAGGVT
ATPTGGCVRL VGLSAQTLPW SEIFRELFTL LGRIWSSIKV STLVLTALGM YASRFRPKSE
AKGKTKSKIG PYRGRGVALT DDEYDEWREH NANRKLDLSV EDFLMLRHRA ALGADDADAV
KFRSWWNSRT RPGDGFEDVT VIGKGGVKHE KIRTSTLRAV DRGYDVSFAE ESGPGTKFHK
NAIGSVTDVC GEHKGYCVHM GHGVYASVAH VVKGDSYFLG ERIFDVKTNG EFCCFRSTKI
LPSAAPFFSG KPTRDPWGSP VATEWKPKAY TTTSGKIVGC FATTSTETHP GDCGLPYIDD
NGRVTGLHTG SGGPKTPSAK LVVPYIHIDM KNKSVTPQKY DETKPNISYK GLVCKQLDEI
RIIPKGTRLH VSPAHVDDFE ECSHQPASLG SGDPRCPKSL TAIVVDSLKP YCDRVEGPPH
DVLHRVQKML IDHLSGFVPM NISSETSMLS AFHKLNHDTS CGPYLGGRKK DHMVNGEPDK
QLLDLLSSKW KLATQGIALP HEYTIGLKDE LRPIEKVQEG KRRMIWGCDV GVATVCAAAF
KGVSDAITAN HQYGPIQVGI NMDSPSVEVL YQRIKSAAKV FAVDYSKWDS TQSPRVSAAS
IDILRYFSDR SPIVDSAANT LKSPPIAIFN GVAVKVASGL PSGMPLTSVI NSLNHCMYVG
CAILQSLEAR QIPVTWNLFS SFDMMTYGDD GVYMFPTMFA SVSDQIFGNL SAYGLKPTRV
DKSVGAIESI DPESVVFLKR TITRTPNGIR GLLDRSSIIR QFFYIKGENS DDWKTPPKTI
DPTSRGQQLW NACLYASQHG VEFYNKVLKL AMRAVEYEGL HLKPPSYSSA LEHYNSQFNG
VEARSDQINM SDVTALHCDV FEV


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