POLG_CACV4
ID POLG_CACV4 Reviewed; 1929 AA.
AC Q8V736; O72119;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Protein p18;
DE Contains:
DE RecName: Full=Protein p32;
DE Contains:
DE RecName: Full=NTPase;
DE EC=3.6.1.15;
DE AltName: Full=p39;
DE Contains:
DE RecName: Full=Protein p30;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=VPg;
DE AltName: Full=p13;
DE Contains:
DE RecName: Full=Protease-polymerase;
DE Short=Pro-Pol;
DE EC=2.7.7.48;
DE EC=3.4.22.66;
GN ORFNames=ORF1;
OS Canine calicivirus (strain 48) (CaCV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Vesivirus; unclassified Vesivirus.
OX NCBI_TaxID=292348;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12206310; DOI=10.1023/a:1020174225622;
RA Matsuura Y., Tohya Y., Nakamura K., Shimojima M., Roerink F., Mochizuki M.,
RA Takase K., Akashi H., Sugimura T.;
RT "Complete nucleotide sequence, genome organization and phylogenic analysis
RT of the canine calicivirus.";
RL Virus Genes 25:67-73(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1571-1929.
RX PubMed=10211962; DOI=10.1099/0022-1317-80-4-929;
RA Roerink F., Hashimoto M., Tohya Y., Mochizuki M.;
RT "Organization of the canine calicivirus genome from the RNA polymerase gene
RT to the poly(A) tail.";
RL J. Gen. Virol. 80:929-935(1999).
CC -!- FUNCTION: NTPase presumably plays a role in replication. Despite having
CC similarities with helicases, does not seem to display any helicase
CC activity (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Viral genome-linked protein is covalently linked to the 5'-
CC end of the positive-strand, negative-strand genomic RNAs and subgenomic
CC RNA. Acts as a genome-linked replication primer. May recruit ribosome
CC to viral RNA thereby promoting viral proteins translation (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Protease-polymerase processes the polyprotein: Pro-Pol is
CC first released by autocleavage, then all other proteins are cleaved.
CC Cleaves host translation initiation factor eIF4G1 and eIF4G2 thereby
CC inducing a shutdown of host protein synthesis. This shutdown may not
CC prevent viral mRNA from being translated since viral Vpg replaces the
CC cap. May cleave host polyadenylate-binding protein thereby inhibiting
CC cellular translation. It is also an RNA-directed RNA polymerase which
CC replicates genomic and antigenomic viral RNA by recognizing specific
CC signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis
CC internally on antigenomic RNA. This sgRNA codes for structural
CC proteins. Catalyzes the covalent attachment VPg with viral RNAs (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase with a preference for cleavage when the P1
CC position is occupied by Glu-|-Xaa and the P1' position is occupied by
CC Gly-|-Yaa.; EC=3.4.22.66; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU01242};
CC -!- DOMAIN: Protease-polymerase is composed of two domains displaying two
CC different catalytic activity. These activities may act independently
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. Pro-
CC Pol is first autocatalytically cleaved, then processes the whole
CC polyprotein (By similarity). {ECO:0000250}.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently attached
CC to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This
CC uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase (By similarity). {ECO:0000250}.
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DR EMBL; AB070225; BAB83601.1; -; Genomic_RNA.
DR EMBL; AF053720; AAC16445.1; -; Genomic_RNA.
DR SMR; Q8V736; -.
DR PRIDE; Q8V736; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; 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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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; IPR000317; Peptidase_C24.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF03510; Peptidase_C24; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00916; 2CENDOPTASE.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51894; CV_3CL_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Covalent protein-RNA linkage; Host-virus interaction;
KW Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW Protease; RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Viral RNA replication.
FT CHAIN 1..1929
FT /note="Genome polyprotein"
FT /id="PRO_0000341984"
FT CHAIN 1..176
FT /note="Protein p18"
FT /id="PRO_0000341985"
FT CHAIN 177..468
FT /note="Protein p32"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036886"
FT CHAIN 469..825
FT /note="NTPase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036887"
FT CHAIN 826..1112
FT /note="Protein p30"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036888"
FT CHAIN 1113..1232
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036889"
FT CHAIN 1233..1879
FT /note="Protease-polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036891"
FT DOMAIN 597..753
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1235..1391
FT /note="Peptidase C24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT DOMAIN 1643..1768
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 1271
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1292
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1355
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT BINDING 623..630
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 176..177
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 468..469
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 825..826
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 1111..1112
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 1232..1233
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT MOD_RES 1137
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
SQ 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
