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Genome polyprotein [Cleaved into: Protein p18; Protein p32; NTPase (EC 3.6.1.15) (p39); Protein p30; Viral genome-linked protein (VPg) (p13); Protease-polymerase (Pro-Pol) (EC 2.7.7.48) (EC 3.4.22.66)]

 POLG_CACV4              Reviewed;        1929 AA.
Q8V736; O72119;
09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
10-MAY-2017, entry version 86.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Protein p18;
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;
Short=Pro-Pol;
EC=2.7.7.48;
EC=3.4.22.66;
ORFNames=ORF1;
Canine calicivirus (strain 48) (CaCV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Caliciviridae; Vesivirus; unclassified Vesivirus.
NCBI_TaxID=292348;
NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=12206310; DOI=10.1023/A:1020174225622;
Matsuura Y., Tohya Y., Nakamura K., Shimojima M., Roerink F.,
Mochizuki M., Takase K., Akashi H., Sugimura T.;
"Complete nucleotide sequence, genome organization and phylogenic
analysis of the canine calicivirus.";
Virus Genes 25:67-73(2002).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1571-1929.
PubMed=10211962;
Roerink F., Hashimoto M., Tohya Y., Mochizuki M.;
"Organization of the canine calicivirus genome from the RNA polymerase
gene to the poly(A) tail.";
J. Gen. Virol. 80:929-935(1999).
-!- 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 processes the polyprotein: Pro-Pol
is first released by autocleavage, then all other proteins are
cleaved. Cleaves host translation initiation factor eIF4G1 and
eIF4G2 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}.
-!- 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 (By similarity). {ECO:0000250}.
-!- 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; AB070225; BAB83601.1; -; Genomic_RNA.
EMBL; AF053720; AAC16445.1; -; Genomic_RNA.
RefSeq; NP_777373.1; NC_004542.1.
ProteinModelPortal; Q8V736; -.
SMR; Q8V736; -.
GeneID; 956316; -.
KEGG; vg:956316; -.
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: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.
3: Inferred from homology;
ATP-binding; Covalent protein-RNA linkage; Host-virus interaction;
Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Protease; RNA-directed RNA polymerase; Thiol protease; Transferase;
Viral RNA replication.
CHAIN 1 1929 Genome polyprotein.
/FTId=PRO_0000341984.
CHAIN 1 176 Protein p18.
/FTId=PRO_0000341985.
CHAIN 177 468 Protein p32. {ECO:0000250}.
/FTId=PRO_0000036886.
CHAIN 469 825 NTPase. {ECO:0000250}.
/FTId=PRO_0000036887.
CHAIN 826 1112 Protein p30. {ECO:0000250}.
/FTId=PRO_0000036888.
CHAIN 1113 1232 Viral genome-linked protein.
{ECO:0000250}.
/FTId=PRO_0000036889.
CHAIN 1233 1879 Protease-polymerase. {ECO:0000250}.
/FTId=PRO_0000036891.
DOMAIN 597 753 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1256 1361 Peptidase C24.
DOMAIN 1643 1768 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 623 630 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
ACT_SITE 1271 1271 For protease activity. {ECO:0000250}.
ACT_SITE 1292 1292 For protease activity. {ECO:0000250}.
ACT_SITE 1355 1355 For protease activity. {ECO:0000250}.
SITE 176 177 Cleavage; by Pro-Pol. {ECO:0000250}.
SITE 468 469 Cleavage; by Pro-Pol. {ECO:0000250}.
SITE 825 826 Cleavage; by Pro-Pol. {ECO:0000250}.
SITE 1111 1112 Cleavage; by Pro-Pol. {ECO:0000250}.
SITE 1232 1233 Cleavage; by Pro-Pol. {ECO:0000250}.
MOD_RES 1137 1137 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
SEQUENCE 1929 AA; 214806 MW; 9F8A92FC0657A623 CRC64;
MASAIALSSS TAQNKITLKS VASRLQQTDD PDIRVWSQSV GFHLQFSNWK CANAFCRFVT
DAYNLTPYKE CARSITRQLT SLSNYLSAQT GVSVSGTQFL LSPSDVEVPV AKTGESVSDI
MVPSYSVNGT SMEFDSMAQL AQALTTGFTF SVNDAQIGNA PAQTGESVSG TGFIAEACPS
CALYDKCPNC TSELINDDGS SQSPGDIPHW THHKIASGIV NILSSDMSSM EDDDFANIAA
HVKKALGTNS HPANNDMSKD QLNWLLNIAE ASLIRKADRT ALPMNAARIA ARRGWREKLF
NEPADKLYTL LRKSKDSFQK SAIWGILFEK ASNAKHYTEI VFQDIVKLIK EECNPSNNFY
FKVMAQSFLD HFRMLVIDNP DPVANLPKFI LKLKPLNLKM IIENHENTAE GWIVTLTAVA
ELYGWLEFAV DLVPKIVSEL YDLLTSATQK CFSMVRELLT NLNILKAESF DFTNPFWYAL
AALLSYFVTG FLPNNAKCSA IKQTLNGATT LVAGITAIQK LAAMFSAWSN ESVVDDLSTK
VIGLTEADNP TVTQDIDAVT NLQIMAEQLK DQIKLKTLDP TFQPYLPVLR NLMSTTDSVI
SHCAKRKALA TQRTAPVCII LTGPAGCGKT TLAYAIANRL SAQKPSVLNL NIDHHDAYTG
NEVCIIDEFD SNPDSKFVEF VVEMVNTNPM LLNCDLIENK GKTFSSKYVI MTSNNETPVK
PNSTRAPPFY RRVRIIDVTN PGVMSFKYEN PGQEVPSYLF SNDFNHLSMS MRGFGAFSKT
RVIDPEGRKT CGLEGPPGQR VDVDDIVRYM QRMYRENQMN FKSEAGNNRL KTPRFAFVTQ
RKHVDTVYKI LAAAKTTYNG YYSLTKDSFD VNEGHNIGSS VFVVGDDKEI PHNCKIFRCN
HLAMFRHPEL AHIEGDNFRA ALGVTMSDQD VTLMFYHIRG KHIQDEVRLD ELPANHHIVT
VHSVYDMAWA LNRHLSLTGK WQALKAVYDL YMTPDILPAA LRHWMDNTKF SSDHVVTQFI
VPGGTIILET CNGARMWATS RRLIRAGGIS NNNGPEGGFR FGSIAPRDIP WSEILREFLN
LISLIWSRVK GATIVLTALL LYMKRYKPRS EAKGKTKGGR GAIRHGGKGI VLSDDEYDEW
REFNMEKRMD MSVDEFLMLK HRAALGSDDT GAIQFRSWWT ARQMRESTGL DHDDVTVIGK
GGVRHEVHRT EIMKAPKQKK KSFAWGEDMY AEGDGKIVNH VNAIVPVTGL CGEHIGYAVH
IGHGKCISLK HVLKTGSYVF NQKPIDVTFD GELAHFQIQQ PPSSAAPVTF SSKPTRDPWG
RSVSTEWKHD TYNTTAGKMY GSICWTATRT QPGDCGLPYV DRAGQVVGLH AGSGGDSAPG
RKIVIPVTKF KLPSNTVLSN RFWKEEAPTI SYKGLTVQET GVNKAVLKGT NYHVSPAHVD
DYQDCTHQPA NLGAQDERYP VSLTSIVINN LEPYKQPTQG PPTEVLNKAY NMLVQHYEPL
IPKATTHLEM GDAFAALNVK TSCGPYITGR KKDHIDPETG KWDETLRNHI NARWSLATQG
VPIPHEYQLG LKDELRPKDK IAVGKRRLIW GCDVGVAVVA ASAFKEVSSA IMAMSEFDFI
QVGINMDGTA VETLYKRLYT PGTHRYCVDY SKWDSTQPPN VTRMSLELLR HFTDKSPVVD
SAVATLSSPS IAVFGGVSFK TNGGLPSGMP LTSILNSLNH CLLVGSAIIQ VLESKGVDVN
WNIYDTIDLF TYGDDGVYIV PNFVHSVMPE VFSCLSSYGL KPTRTDKSSA PITEIPLSEP
IEFLKRQFVR NQFGVRALLD RSSLIRQFYY IKGKNTMEWT KPPEQIDLTS RTAQLQVVML
YASQHGREFY KKCLDYYQLA MEYEGIKLDA PTYDEALAKY NANFNGVEDC DLLPAGYDEH
RLDKIVFEN


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