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RDRP_WCMVO
ID   RDRP_WCMVO              Reviewed;        1294 AA.
AC   P15402;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=RNA replication protein;
DE   AltName: Full=147 kDa protein;
DE   AltName: Full=ORF1 protein;
DE   Includes:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE   Includes:
DE     RecName: Full=Helicase;
DE              EC=3.6.4.13;
OS   White clover mosaic virus (strain O) (WCMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Alphaflexiviridae; Potexvirus.
OX   NCBI_TaxID=12190;
OH   NCBI_TaxID=3898; Trifolium.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2353451; DOI=10.1016/0042-6822(90)90469-8;
RA   Beck D.L., Forster R.L.S., Bevan M.W., Boxen K.A., Lowe S.C., Gardner R.C.;
RT   "Infectious transcripts and nucleotide sequence of cloned cDNA of the
RT   potexvirus white clover mosaic virus.";
RL   Virology 177:152-158(1990).
CC   -!- FUNCTION: RNA replication. The central part of this protein possibly
CC       functions as an ATP-binding helicase (Probable). {ECO:0000305}.
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=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SIMILARITY: Belongs to the potexvirus/carlavirus RNA replication
CC       protein family. {ECO:0000305}.
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DR   EMBL; X16636; CAA34628.1; -; Genomic_RNA.
DR   PIR; A46350; A46350.
DR   Proteomes; UP000007628; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR002588; Alphavirus-like_MT_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR   Pfam; PF00978; RdRP_2; 1.
DR   Pfam; PF01443; Viral_helicase1; 1.
DR   Pfam; PF01660; Vmethyltransf; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT   CHAIN           1..1294
FT                   /note="RNA replication protein"
FT                   /id="PRO_0000222559"
FT   DOMAIN          59..224
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          541..698
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          699..832
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1071..1178
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   BINDING         570..577
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1294 AA;  147571 MW;  CE7342AA0D9992DF CRC64;
     MAKVRAALDR ITDPSVKAVL NEEAYSHIRP VLRESLTNNP YAIAPDAADT LEKYGIATNP
     FAVKVHSHGA VKSIENTLLE RVGFNLPKEP CTFLFLKRSK LRYLRRGPSN NDIFINLAIE
     PRDLQRYEED TLVESWTRIT TRYAYISDTF HFFTRKMLAD LFFHNPALDV LYATLVLPPE
     ALHKHPSIEP DLYTINYNFN GFQYIPGNHG GGSYSHEFKQ LEWLKVGHLK SPELCLTFQM
     IESIGANHLF MITRGIKITP RVRTFTKDSY VLFPQIFHPR NLNPSKPFPK VKAMQLFTYV
     KSVKNPTERD IYAKIRQLIK TSELSDYHPD EIVHIVNYFV FISKLDSINS YSDILSLPIW
     SKALLPIKTK ITQLWEKLTG ARAFNQLLDA LQWKTFTYPL EVVDSPQPLQ TRDCFIEDER
     LEIDTLEDEI PPNPNDNTSM SPQSIEEAVK NNPDLPWAPW LLILQAHNAD CTEKQYDPEN
     NLILPIQEIN TLPKHQHPDI PTDLLTLLTK LHREPTTVSL DNHRARAYGS DVKNLRIGAL
     LKKQSKDWLA SFALKTENIE REVLMSVIHG AGGSGKSHAI QTWMRSLNRR DRHVTIILPT
     TDLRNDWTNK VPNLEQANFK TFEKALCQPC GKIIVFDDYS KLPQGYIEAF LAINQNVILA
     ILTGDSKQSF HHESNEDAYT ATLEPSIITY QPFCRYYLNI THRNKPDLAN KLGVYSCSSG
     TTSFTMSSQA LKGMPILSPS IMKKTALGEM GQKSMTYAGC QGLTTKAVQI LLDTNTPLCS
     SNVIYTALSR AVDHIHFINT GPNSTDFWEK LDSTPYLKTF LDCVREEKMN EIIAAEEPPT
     PVQAPTTHFP KVNPTTVIES YVHDLPEKHD REIFSETHGH SNAIQTDNPV VQLFPHQQAK
     DETLYWATIE ARLQCTSSEE NLKEFHLKHD IGDILFLNYK QAMNLPQDPI PFNPDLWTLC
     RQEIENTYLK KSAAALVNAA TRQSPDFDSH AIALFLKSQW VKKTEKIGCL KIKAGQTIAA
     FMQQTVMIYG TMARYMRKFR NQYCPRKIFV NCETTPADFN SFILDEWNFN RTCFSNDFTA
     FDQSQDGSIL QFEVIKAKFH NIPEDVIEGY IQIKTHAKIF LGTLSIMRLS GEGPTFDANT
     EANIAYTHTK FNIPCDAAQV YAGDDMSIDY VASVKPSFNM IEHLMKLKGK PVFNTQTQGD
     FAEFCGWTIS PKGIIKKPEK MNMSIELQKN INKFHEVKRS YALDHAFAYQ LGDELHELYN
     ENEAEHHQLA TRSLILAGQA TALDILDYGL RDLK
 
 
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