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POL1_ARMVN
ID   POL1_ARMVN              Reviewed;        2284 AA.
AC   Q6W8W5;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
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   Arabis mosaic virus (isolate NW) (ArMV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Secoviridae; Comovirinae; Nepovirus.
OX   NCBI_TaxID=282063;
OH   NCBI_TaxID=29760; Vitis vinifera (Grape).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15098112; DOI=10.1007/s00705-003-0277-4;
RA   Wetzel T., Beck A., Wegener U., Krczal G.;
RT   "Complete nucleotide sequence of the RNA 1 of a grapevine isolate of Arabis
RT   mosaic virus.";
RL   Arch. Virol. 149:989-995(2004).
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; AY303786; AAQ73821.1; -; Genomic_RNA.
DR   RefSeq; YP_053925.1; NC_006057.1.
DR   SMR; Q6W8W5; -.
DR   MEROPS; C03.004; -.
DR   GeneID; 2943104; -.
DR   KEGG; vg:2943104; -.
DR   Proteomes; UP000007441; 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; Phosphoprotein; Protease;
KW   RNA-binding; RNA-directed RNA polymerase; Thiol protease; Transferase;
KW   Transmembrane; Transmembrane helix; Viral RNA replication.
FT   CHAIN           1..566
FT                   /note="P1A protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000037040"
FT   CHAIN           567..1216
FT                   /note="Putative ATP-dependent helicase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000037041"
FT   CHAIN           1217..1240
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037042"
FT   CHAIN           1241..1460
FT                   /note="Picornain 3C-like protease"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000037043"
FT   CHAIN           1461..2284
FT                   /note="RNA-directed RNA polymerase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000037044"
FT   TOPO_DOM        567..1172
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1173..1193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1194..1216
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          750..918
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1242..1457
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          1727..1851
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ACT_SITE        1283
FT                   /note="For picornain 3C-like protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1327
FT                   /note="For picornain 3C-like protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1419
FT                   /note="For picornain 3C-like protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   BINDING         780..787
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   MOD_RES         1217
FT                   /note="O-(5'-phospho-RNA)-serine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   2284 AA;  252149 MW;  AFE308312E2E4C12 CRC64;
     MWQISEGSQC CCTGKTWSNA EAKEARYVCN CILSCRLVKV EVVPQLPKSR IAPAQDKAER
     ITPLCNSNGG AAPTIPKSKR AFEPRTPLIK QRCDVVVRVG PPADLDLVYP ALVQEEVAIP
     PTEKVLQPTL KAEVRVPIFC APKRMVAFPK PPTKIASKRD ALQFPAGAVA FNGINFIDAK
     GKVVLSEGAK RILKGIRVAK QQRQRTARRS AACKKVRKAR DLALFKRLSE ECTFQDLPGG
     FAGEIPAGHA CYRKVAAPTT SFKKEVSKGK KAKKPSTPVL PAQDFSCVDS FDWGEKSSPV
     EIEDDWVLIE KPVLQRQAAH SAQGRATEAL TRFAASGGFT VKAHQKVEEL ASSGEAGHLI
     AGEFAELCLR SLVYNDAPVL SASIEELITE QDFKDAIELF NIELAELPTD STTCGQFNDW
     ASAAKKMAKG VGSIVGDFAR MSGAGVLITF DRCIEYLQKK ALTFCQKVFN ATMAPYLSHL
     AEASNIISKI WKKLAEWMES LKGKAGLALE VLAQHAIFAL GAIVVGGVVV LVEKVLVACK
     VIPNCGIVLG AFLTLFFASL GLTALECTAE EIFRMHQCCK GAIYSMYSVK EPMNEAEGSS
     VTMGVLQGLD NAISALTRVG QSMISFKLGS FSYYAKIAQG FDQLARGKKA IGELTGWLID
     LVGGVYSKVS GQESTFFDEL STIVCLDVRS WLLKSKRVRL QVETMAIGDR ITLDTISKPT
     GMQGHKILIT AAGVPRKTSA DFTMCIKEEV SKLEEVHQRT ACAGINEGMR QFPFWVYIFG
     ASQSGKTTIA NSVIIPSLLE EMNLPKTSVY SRPKTGGFWS GYARQACVKV DDFYAIEQTP
     SLASSMIDVV NSEPYPLDMA YLHEKGMSMD SPLVVTTANT VKPPTNAGIT DEASFFNRRA
     AVIEVRRKDN THFTPRAYDN CIEVRFLHNK CAYVDSEGIP QGPAVNTPME EGWISPSEAV
     ATLKNLLGEH VLAEEEKLLD YRERIGNDHP IYNAAQEFIG NMHYPGQWLT TEQKNTYGIN
     EEGFSFLAVD GKMYKYNVLG KLNPCETVPP HPNVIPWLEE KTLSIVHWDA HKHIATGPRN
     ALVSCFLQGL VQDQSRVQSV DLMGKDSSPE QQAFFKRLTL SERIYLRLCQ IRIDAVKKEQ
     LSSVSRGALD VLRDCMYKSK AKLVENYSLL LTLVAILVLI ATAYSLISTL IGLAGCSSFA
     GGMVALNHVS NASIPCSEPR LEEGYIPRNK FVSRISRTRG DGPAQGQGDH EELVTELYYY
     FDGVKRLISC CWFKGRSLLL TRHQAMAIPI GNEIQVIYAD GTERKLVWPG RQEDRSCKGY
     IEFPDNELVV FEHARLLTMP IKYEKFFVDD PDHQISPNVA VKCCVARLED GIPQFHFWNK
     YASARSDVHT IKDEGGSAVY QNKIRRYIIY AHEAKRNDCG AIAVAEIQRT PKVLAMLVSG
     IGNVTYSSVI PSYSSSFVRG DVPYVPEDGI KTNGYRKVGY LMAKDAPHVP SKTAFMKVPD
     EICFPYPNPK QPAILSAEDE RLIGTVHEGY TPIREGMKKF AEPMHLLDAQ LLDEVAGDMV
     HTWFDAGEIL EDVPLSIAIN GDVEEEYFDP IAMDTSEGYP EVLQRKNGEK GKARFFVGEP
     GAREFVPGCG PERAYLSLEE ECKTRIPSLV SIETPKDERL KRSKIETPGT RLFSVLPLAY
     NLLLRVKFLS FSRLLMKKRS HLPCQVGINP YSREWTDLYH RLAEKSDVGY NCDYKGFDGL
     ITEQILAVVA TMINAGFRNP VSNQQRSNLL MAISGRLSIC GSQVYETEAG IPSGCALTVV
     INSIFNELLM RYCYKKIVPP IYRECFDRCV VLITYGDDNV FTVSQSIMTS FTGDALKAEM
     ANLGVTITDG KDKSLATIPA RPLLELEFLK RGFKKGNGGL IYAPLEKLSI MSSLVYIRSD
     GSDMLQKLVD NVNTALVELY LHQDREYSES VRDFYLEKLP PGSYKELTTW YEAQIFHECQ
     LSGESGWKPQ GLIEVSHGAS FASFVQQNGT ELERHDICPG LAISGSKYIA REEEILMSLS
     SLLPGDINAV KLTLKCGDGI GRLPSKASVL SQRKPGIVMQ LCARAIKEKK TLVIRDERPY
     IGGWAMACIC GESFGFSIKD TLALYANLMG PNRKNGLATY FTDFDSPVHV KKIHAITNGE
     EGVAMLKDSF AFCEPTTIAA TSCDTRKEMV SHLPTSFPNI VLIGGISYPK EGGEPGALYS
     PTDVVMSKKL QGVYVSEAVL KCCLRCPGAA VKTVLQTSSP GSSLSQAHFR SLRRVQSHRC
     MRKS
 
 
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