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POL1_GCMV
ID   POL1_GCMV               Reviewed;        2252 AA.
AC   P13025;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=RNA1 polyprotein;
DE   AltName: Full=P1;
DE   Contains:
DE     RecName: Full=P1A protein;
DE              Short=1A;
DE     AltName: Full=Protease cofactor;
DE   Contains:
DE     RecName: Full=Putative ATP-dependent helicase;
DE              EC=3.6.4.-;
DE     AltName: Full=1B;
DE     AltName: Full=Membrane-binding protein;
DE     AltName: Full=NTP-binding protein;
DE              Short=NTB;
DE   Contains:
DE     RecName: Full=Viral genome-linked protein;
DE     AltName: Full=1C-VPg;
DE   Contains:
DE     RecName: Full=Picornain 3C-like protease;
DE              Short=3C-like protease;
DE              EC=3.4.22.-;
DE     AltName: Full=1D-PRO;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE     AltName: Full=1E-POL;
OS   Grapevine chrome mosaic virus (GCMV) (Hungarian grapevine chrome mosaic
OS   virus).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Secoviridae; Comovirinae; Nepovirus.
OX   NCBI_TaxID=12273;
OH   NCBI_TaxID=4045; Apium graveolens (Celery).
OH   NCBI_TaxID=29760; Vitis vinifera (Grape).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2798128; DOI=10.1093/nar/17.19.7795;
RA   le Gall O., Candresse T., Brault V., Dunez J.;
RT   "Nucleotide sequence of Hungarian grapevine chrome mosaic nepovirus RNA1.";
RL   Nucleic Acids Res. 17:7795-7807(1989).
CC   -!- FUNCTION: Picornain 3C-like protease is a thiol protease that cleaves
CC       the P1 and P2 polyproteins. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: [Viral genome-linked protein]: Host endoplasmic
CC       reticulum lumen {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Putative ATP-dependent helicase]: Host
CC       endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages by picornain 3C-like protease in vivo
CC       yield mature proteins. Picornain 3C-like protease is autocatalytically
CC       processed (By similarity). {ECO:0000250}.
CC   -!- PTM: VPg is uridylylated by the polymerase and is covalently linked to
CC       the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC       peptide primer for the polymerase (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the nepoviruses RNA1 polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; X15346; CAA33405.1; -; Genomic_RNA.
DR   PIR; S06188; S06188.
DR   RefSeq; NP_619705.1; NC_003622.1.
DR   SMR; P13025; -.
DR   MEROPS; C03.025; -.
DR   PRIDE; P13025; -.
DR   GeneID; 956641; -.
DR   KEGG; vg:956641; -.
DR   Proteomes; UP000008624; Genome.
DR   GO; GO:0044166; C:host cell endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR   InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR   InterPro; IPR044067; PCV_3C_PRO.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF00910; RNA_helicase; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51874; PCV_3C_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; Helicase;
KW   Host endoplasmic reticulum; Host membrane; Hydrolase; Membrane;
KW   Nucleotide-binding; Nucleotidyltransferase; Protease; RNA-binding;
KW   RNA-directed RNA polymerase; Thiol protease; Transferase; Transmembrane;
KW   Transmembrane helix; Viral RNA replication.
FT   CHAIN           1..564
FT                   /note="P1A protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000037070"
FT   CHAIN           565..1187
FT                   /note="Putative ATP-dependent helicase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000037071"
FT   CHAIN           1188..1216
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037072"
FT   CHAIN           1217..1426
FT                   /note="Picornain 3C-like protease"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000037073"
FT   CHAIN           1427..2252
FT                   /note="RNA-directed RNA polymerase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000037074"
FT   TOPO_DOM        565..1140
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1141..1161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1162..1187
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          733..899
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1213..1422
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          1697..1825
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ACT_SITE        1256
FT                   /note="For picornain 3C-like protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1294
FT                   /note="For picornain 3C-like protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1386
FT                   /note="For picornain 3C-like protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   BINDING         763..770
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
SQ   SEQUENCE   2252 AA;  249867 MW;  DDFB0DCF7E94171B CRC64;
     MMDSTIILPY AKYNYSLNKY LFYNSNLDID LDSFNFYKKY NNTLSLLKRK FLDLFCIPVS
     SSSPPAIQKN GLLSASNPKH LFAFANFVLD CGVNPFLQIW EETLANWPLF QGQSLLACCR
     TTAEVRREAA EASAEILRLK QVEREHAFQA EVKSLIAAGA LPACAEGLAR KIWSAGKDQR
     KVRVAIRTKL TKANALGAAH RSAVATAQAK AEVLREFEPS PAHIQIAVKA HIFAEKLSRK
     YADLTAQVRA RRAAARDLRA KEIYLEIVDL LGAPLLSIPQ QIKIKGKYLR RSVAAEVEVP
     HTRNPMAELV PYKGLGAVSA DPRCWVVAQC GKFSATHANL CSEIYSMVIG PWVQLTDFSS
     IRQFVMNISF LKDFYPEDAL IASLKEVNTE AQLAVAAIVT QEEVSKMEAN ARSANCRANI
     FKRIASRITS AACSVKNAFL DGCELTGKRL SEGVFSVVIG HFREALTTIK FELGVAMELV
     EVLIARVKSW FDTLLAKIDH ALASLGKWAC YALGILLGIG LCNLIETIIG GHGMLVSLFC
     TGVFATMAIK CAGGWDAAQR EMVAMITTLA QSIFGRRKGL DSTDLNTRSI PLLTNVITAM
     TTFGTGLCKF QSSSIIEIGK LAGACHQMRM GKEALKEFAA MIMHYLGRIA DKITGRETIF
     FDELSTLVSV DVRGWIRCAQ GAILESYHTD PGCETFQDVI GRLVQEGQKL QVGVNGIPRK
     ISADYASLIG QIMKDLLELQ KRMMRCGTVT GRRKEPVWIY LWGPSHCGKS NFMDVLGMAL
     CKHFDLPYTV CGRNVKDSFF SGYMGQTIME IDDLSSIKTD PPMEGELINL VSCKDYPLNM
     ADVADKPIYF KSQFVISSSN QEDVPAGAGV RDISSYRSRK AALIEVRRKP GVIFDPDNAM
     AASQARFKDP MTHMLLNGQN DENSWMEMDD VITECINISA RHRAAQEKLQ NASLRAKASL
     DPVTLASQEF LRKEVNSVYL EIPTLEIEKA GISGVRGGRC LYADGILYTL GTEFQLIPHP
     VENEGYQKLW AQRMKNMYLP AVTTGRYLNA SSMIVTGFLR SLVNGDCAVL SVDALSTTAT
     FTQKRIFESL NLAERVYLRA LQCQIDAYTL DIPENPYSNV CWVKMLKALG QGREFIVSNG
     GGILMIAAAI ILVLVCGWGF WKAFVGLFTG SMSLGAALAG CQEAEVKAHS VYSADGGDRG
     YRSRNIPINH RYSYARSQAG NGLLPASRLC VAIYGPRGVF ISGMQYKNKC VMMTRHQAQS
     LNEGDELSVV FASTGESMMI RFHAYHIREN VGSEVVCWLA PSLPQLPCDL KGLFLEDAEV
     ELPSNFKSMG YVLRQDSNAF HYDTLDTYAA VDKTPLVLKG VNGDDLYIHE IPEKIVFHYE
     SRNNDCGMLL TCQLSGKMKV VGMLVAGKDK TSWACILPNP HLAELKSQIE YIPEFGEAEE
     GYFKVGHVSP KEAPTMPKKT NSVQVPQALR VPCDLPIKEP SIISKNDPRC PANVDPPKAA
     MKKKFQQPML DLDQKCLDEI AGDMLETWYD CEDSILSDIP LATAINGIPA GCEDAELENF
     VMKTSPGYPY FKNKGLGKGK HPYFEECEDG SLKLKEGSQA AELYENMAQF AKEEVPELVV
     IECPKDELLP ARKIKVGPCR LFEIMPLHYN LLLRVKTCAF TAFLQHNRHR LPCQVGTNPY
     SREWGHLLNR LRRVKTNEAI NCDYSGFDGL LTPQLVEMMA KMINRLYLRS GESEVMQAQR
     LNMIMALCGR YALVGTQVYK VNCGLPSGFA LTVVMNSIFN EILIRYAYKT LAPTPEKNSF
     GINVCLLVYG DDNLISVSPA VASWFTGEAI RVTLAEKRIK ITDGSDKDAP TIEAKPFSEL
     DFLKRKFYVH PEHGQVWAPL DKSAIFSCLH WLTPQKSKFA LQEKACDYLG EVDVVEELII
     NVNVSLVELY LHNDKEEFNR VRSFYIARLP MQVDQFRTWA FCEAFHSAQQ TGMLRHDPAK
     ILDSLAGPEF PRFMRCSGEG DKAHFYTPIL GVCGPHYKPK EQDFLVSTLP IKQGEGVHIP
     IKIGGGVGGL PTHQWVKNFG RPSQLKNNDG YACYKLLCEQ IEQGKRLVFM SAAPYVAGNA
     ALISFGSSRK ILKEQMPLCH YRNSIPESVD GLTGYFDAPL PAATIGKSYF ANGETYAALC
     EFKNGEVLDI VGPTNVQILN GAVRQGKVPC LAAHSVGTKF KVSLVCNKTM CPHHHHTGPT
     FEQAFRTCWL SKCKTKETQV SPWFGTKFLG IS
 
 
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