POLG_SMSV4
ID POLG_SMSV4 Reviewed; 1214 AA.
AC P36287; Q88193;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Genome polyprotein;
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;
DE Flags: Fragment;
GN ORFNames=ORF1;
OS San Miguel sea lion virus serotype 4 (SMSV-4) (SMSV serotype 4).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Vesivirus.
OX NCBI_TaxID=36407;
OH NCBI_TaxID=9702; Otariidae (fur seals & sea lions).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7769708; DOI=10.1128/jvi.69.7.4484-4488.1995;
RA Neill J.D., Meyer R.F., Seal B.S.;
RT "Genetic relatedness of the caliciviruses: San Miguel sea lion and
RT vesicular exanthema of swine viruses constitute a single genotype within
RT the Caliciviridae.";
RL J. Virol. 69:4484-4488(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1176-1214.
RX PubMed=1529644; DOI=10.1016/0168-1702(92)90008-w;
RA Neill J.D.;
RT "Nucleotide sequence of the capsid protein gene of two serotypes of San
RT Miguel sea lion virus: identification of conserved and non-conserved amino
RT acid sequences among calicivirus capsid proteins.";
RL Virus Res. 24:211-222(1992).
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 -!- 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; M87482; AAA16219.1; -; Genomic_RNA.
DR EMBL; U15302; AAA96500.1; -; Genomic_RNA.
DR SMR; P36287; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase 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: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 InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
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 PRINTS; PR00916; 2CENDOPTASE.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF50494; SSF50494; 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;
KW RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Viral RNA replication.
FT CHAIN <1..1214
FT /note="Genome polyprotein"
FT /id="PRO_0000342017"
FT CHAIN <1..126
FT /note="NTPase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000342018"
FT CHAIN 127..405
FT /note="Protein p30"
FT /evidence="ECO:0000250"
FT /id="PRO_0000342019"
FT CHAIN 406..518
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000342020"
FT CHAIN 519..1214
FT /note="Protease-polymerase p76"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036934"
FT DOMAIN <1..55
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 523..676
FT /note="Peptidase C24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT DOMAIN 926..1051
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 557
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 578
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 640
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT SITE 126..127
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 405..406
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 518..519
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT MOD_RES 428
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 1214 AA; 135088 MW; DB259A357CCFFDAC CRC64;
NKGKTFTSKY VIMTSNTETP VKPTSRRAGA FYRRVMIVDV TNNAVEKWKS DNPGKAVPKW
CFNKDFSHLS LSLRGTEAYC KEYVLDPTGR NHQSRRAPPP QQVTLEQLAQ KMVVQHTTNT
SEFVTQAGDV PVFGFVCQNN EIDTVYNLLA AVKARYGANF NLYKGMVRTA HENSGCGAHV
HVISREDNFR GKVFTVSRSR LESVPHLEGD SFRRSLGVVM SDKDVTTMFY YIKGKVINDQ
VNLTELPANQ HVVTVHTVYD MAWALRRHLK WSGQWQLIKA AFEIMCYPDA AACALRNWMD
STDFSEEHVV TQFIAPGGTI ILESCHGARM WATGKRLIRA GGITEAGGPQ GGVRFAGLGA
RNVPWSEILR EFMTLISHIW SQIKGATVVL TALTFYLKRF RPRIEAKGKN KNKGARKNTG
VALTDDEYDE WRQYRTEKNL DLTVEDFLQL RHRAAMGADD SDAVKFRCWY SERQRNYHDL
EDVTIIGRGG VKRELIRKGP LRPRGNDYYD EPDDWYSEGV IDGVAHKNAI VSVDDVDGMH
KGYAIHIGHG VYISLKHVVS GNARILSEEP KNLTFTGELA TFRLNNILPT AVPVGTSKPI
KDPWGNPVST DWQFKNYNTT SGNIYGACGS SCSLTRQGDC GLPYVDDHGV VVGLHAGSGG
DKCPSRKLIV PYAKVDMRVR DTCTKQCYKD NSPTISYKGL LVKETGEPRT IMKGTRLHVS
PAHTDDYEEC THQPASLGAG DPRCPISLTG IMVNNLQPYT EASPGPDTAT LNRVSKMLTS
HMEGYVQKSQ TEEGYGSAFY MLNHDTSCGP YIGGRKKDHV KDGVLDKNLL DLLSSKWNRA
KLGLALPHEY ALGLKDELRP KDKVAVGKRR LIWGCDVGVS TVCRAAFKRV SESIMANHAL
GFIQVGINMD GPAVEDLFKR LERPKHDRYC VDYSKWDSTQ PPKVTSQSID ILRHFTDKSP
IVDSACATLK SNPIGIFNGV AFKVAGGLPS GMPLTSIINS LNHCLMVGSA VVKALEDSGV
QVSWNIFDSM DLFTYGDDGV YIVPPLISSV MPNVFANLKQ FGLKPTRTDK SDAEITPIPA
DEPVEFLKRT IVRTENGIRA LLDRSSIIRQ FYYIKAENTE NWTIPPKKID TPSRGQQLYN
ACLYASQHGE EFYTNKIIPL VQRAIEFEGL HIEVPEFHHA VAAYNGYFNG TEGQPNQIAF
ASGGLGLSSE VFEN
