POLG_VESVA
ID POLG_VESVA Reviewed; 1881 AA.
AC Q9DUN3;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Protein p16;
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 p76;
DE Short=Pro-Pol;
DE EC=2.7.7.48;
DE EC=3.4.22.66;
GN ORFNames=ORF1;
OS Vesicular exanthema of swine virus serotype A48 (isolate Swine/United
OS States/A48/1948) (VESV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Vesivirus.
OX NCBI_TaxID=85617;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9660070; DOI=10.1016/s0168-1702(98)00013-6;
RA Neill J.D., Meyer R.F., Seal B.S.;
RT "The capsid protein of vesicular exanthema of swine virus serotype A48:
RT relationship to the capsid protein of other animal caliciviruses.";
RL Virus Res. 54:39-50(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Neill J.D., Seal B.S., Ridpath J.F.;
RT "Complete nucleotide sequence of the genomic RNA of vesicular exanthema of
RT swine virus A48.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
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 p76 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 -!- SUBUNIT: [Protein p32]: Homodimer, interacts with NTPase, protein p30
CC and Pro-Pol. {ECO:0000250}.
CC -!- SUBUNIT: [Viral genome-linked protein]: Interacts with capsid protein
CC and Pro-Pol. {ECO:0000250}.
CC -!- SUBUNIT: [Protease-polymerase p76]: Homooligomers, interacts with Vpg,
CC protein p32 and may interact with capsid protein (By similarity).
CC {ECO:0000250}.
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; U76874; AAG13641.1; -; Genomic_RNA.
DR RefSeq; NP_066255.1; NC_002551.1.
DR SMR; Q9DUN3; -.
DR GeneID; 911834; -.
DR KEGG; vg:911834; -.
DR Proteomes; UP000007661; Genome.
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; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR016024; ARM-type_fold.
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; SSF48371; SSF48371; 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; Hydrolase; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
KW RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Viral RNA replication.
FT CHAIN 1..1881
FT /note="Genome polyprotein"
FT /id="PRO_0000402456"
FT CHAIN 1..148
FT /note="Protein p16"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402457"
FT CHAIN 149..435
FT /note="Protein p32"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402458"
FT CHAIN 436..791
FT /note="NTPase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402459"
FT CHAIN 792..1070
FT /note="Protein p30"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402460"
FT CHAIN 1071..1183
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402461"
FT CHAIN 1184..1881
FT /note="Protease-polymerase p76"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402462"
FT DOMAIN 564..720
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1188..1341
FT /note="Peptidase C24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT DOMAIN 1593..1718
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1222
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1243
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1305
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT BINDING 590..597
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 148..149
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 435..436
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 791..792
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 1070..1071
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 1183..1184
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT MOD_RES 1093
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1881 AA; 208813 MW; 6E487A72523AFE4F CRC64;
MAQTLSKISN KENASSGLRP KRFKPHQPIP TWMVRCEPLD HDSRRGRDPV RASPQAKRVR
TPTPYPRHLK PAASAVVRSG NNPSHLKPAS TDVVRSGPQP LCCEAKDGGV VRSCKTYNLK
PAHESKAVAF SLPKTDGPTG NEPEFIAEAC PSCALYDTCP NCTSKVINDD GSTDGTIPSW
DQIETTPAFL SLLSNTDEEM SADELTNLAA HLRKAFETGS HPANVDYSKD QLQGLLEMAE
AAVPPARRQT LPFYQQRLEA RRTWREKIFN QPLEEINKIL TTSKDRFQRC AAWKVILEKA
VLAKEYGEEA YAYAQQALKN INSFDVNLVL KMAAATFIDH IRMMTVDNPD LVSYIPKLIV
KLKPLTLKMI IDNHENTKEG WLVTLTSLAE LYGMVEVAID FVPTVVGKLF DLLMKTTSKM
YSMFKSVVLA TFTSESLDFT NPFWYAIAAI LCFLITGAIP HNGKMKIHKN ILSNATGIVA
GIKAIQALAA MFSTWSNERL VNDLSSRTIA LTELNNPTIT ADIDAVINLQ RLAEVLRDEV
KSHTLNPLMQ PYNPILRNLM SALDKVISCC TRRKAIATKR TAPVAVILTG PPGCGKTTAA
FALAKRLSQQ KPSIISLDVD HHDTYTGNEV CIIDEFDSSD KVDYANFVVN MVNTNPMVLN
CDLIENKGKT FTSKYVIMTS NTETPVKPTS RRAGAFYRRV MIVDVTNNAV DKWKSDNPGK
AVPKWCFNKD FSHLSLSLRG TEPYSKEYVL DPTGRNHQSR RAPPPQQITL EQLAQKMVVQ
HTTNTSEFVT QAGDVPVFGF VCQNNEIDTV YNLLAAVKAR YGANFNLYKG MVRTAHENSG
CGAHVHVISR EDNFRGKAFT VNRSRLESVP HLEGDSFRRS LGVVMSDKDV TTMFYYIKGK
VINDQVSLTE LPANQHVVTV HTVYDMAWAL RRHLKWSGQW QLIKAAYEIM CYPDTAACAL
RNWMDSTDFS EEHVVTQFIA PGGTIILESC YGARMWATGQ RLIRAGGLTE AGGPQGGVRF
AGLGARNVPW SEILREFMTL ISHIWSQIKG ATVVLTALTF YLKRFRPRVE AKGKNKNKGP
RKNTGVALTD DEYNDWKQSK AEKNLDLTVK DFLQLRHRAA MGADNTDAVK FRYWYSKKQK
IYHDLENFPI IGRGGLKREL IRKGPLRPRG NDFYDEPDDW YSEGVIDGVT HKNAIVSVDD
VDGMHKGYAI HIGHGVYISL KHVLTGNARI LSEEPKGITI SGELATFRLN NILPTAVPVG
TNKPIKDPWG NPVSTDWQFK NYNTTSGNIY GACGSSCSLT RQGDCGLPYV DDHGVVVGLH
AGSGGDKCPS RKLIVPYVKV DMRIRDTCTK ESPTKTHKPT FSYRGLLGKE TGEPRTIMKG
TRLHVSPAHV DDYEECTHQP ASLGAGDPRC PISLTGIMVN NLQPYTEASP GPDTATLNRV
SKMLTSHMEG YVPKVHKTEE DSISAFYMLN HDTLCGPYIG ARKKDHVKDG VLDKNLLDLL
SSKWNRAKLG LALPHEYALG LKDELRPKDK VAVGKRRLIW GCDVGVSTVC AAAFKRVSES
IMANHALGFI QVGINMDGPA VEDLFKRLER PKHDRYCVDY SKWDSTQPPK VTSQSIDILR
HFTDKSPIVD SACATLKSNP IGIFNGVAFK VAGGLPSGMP LTSIINSLNH CLMVGSAVVK
ALEDSGVRVT WNIFDSMDLF TYGDDGVYIV PPLISSVMPK VFANLRQFGL KPTRTDKSDA
EITPIPADEP VEFLKRTIVR TENGVRALLD RSSIIRQFYY IKAENTENWT VPPKRIDTPS
RGQQLYNACL YASQHGEEFY TSKIVPLIER AVKLEGLHIE VPEFHQAVAA YNGYFNGTEG
QPNQIAHASG GLGLSGEVFE N
