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RDRP_NCBVS
ID   RDRP_NCBVS              Reviewed;        1925 AA.
AC   Q9YRB3;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Methyltransferase/helicase/RNA-directed RNA polymerase;
DE            EC=2.1.1.-;
DE            EC=2.7.7.48;
DE            EC=3.6.4.13;
OS   Nudaurelia capensis beta virus (isolate Pine emperor moth/South Africa)
OS   (NbetaV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Hepelivirales; Alphatetraviridae; Betatetravirus.
OX   NCBI_TaxID=652108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=10329566; DOI=10.1006/viro.1999.9677;
RA   Gordon K.H., Williams M.R., Hendry D.A., Hanzlik T.N.;
RT   "Sequence of the genomic RNA of nudaurelia beta virus (Tetraviridae)
RT   defines a novel virus genome organization.";
RL   Virology 258:42-53(1999).
CC   -!- FUNCTION: RNA-dependent RNA polymerase replicates the viral genome.
CC       {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;
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 ssRNA positive-strand viruses RNA-directed
CC       RNA polymerase family. {ECO:0000305}.
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DR   EMBL; AF102884; AAC97509.1; -; Genomic_RNA.
DR   RefSeq; NP_048059.1; NC_001990.1.
DR   PRIDE; Q9YRB3; -.
DR   GeneID; 1450472; -.
DR   KEGG; vg:1450472; -.
DR   Proteomes; UP000000831; 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   Gene3D; 3.40.50.300; -; 2.
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; 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; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; RNA-directed RNA polymerase;
KW   Transferase.
FT   CHAIN           1..1925
FT                   /note="Methyltransferase/helicase/RNA-directed RNA
FT                   polymerase"
FT                   /id="PRO_0000402485"
FT   DOMAIN          45..252
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          533..693
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          694..834
FT                   /note="(+)RNA virus helicase C-terminal"
FT   REGION          737..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1310..1445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1468..1636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1666..1727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1806..1847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1905..1925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1313..1329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1331..1356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1357..1433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1478..1528
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1543..1564
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1581..1616
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1671..1686
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1700..1727
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1925 AA;  215612 MW;  49A1354A777E9A1A CRC64;
     MEDASKQLRV LDAQERAKAA FQLDFIASVE TLEDAQEKYE GMMFRSGTKL PSTHIKLAID
     LRVAEKDLRR HVKNVPTVLE IGPSVESVRY AVQTRDKERV HGCTFSDARD NLRHNKIGYE
     AHYDRKIGPD AALLAAGIPT DTFCVDGFSN CEYQSPLAIA CHSLYPDGES NSIMDVAKGM
     ALHGTHVIYA WMHLPVELLT LTDADNIFEG YSIRFEETGA LPCTKRRKAI FSGYNDFGSA
     YVHDAHHWAG WLKHRGVDTP YGFSILIDIQ QRFGMHTKLK ITRGHSSGSI TTVFPLSKLG
     LIWVPNIVKI MYPKAKHEPE YIVTDKKKYE GVCVYVGTRV QSSGKSITLA EIVQYIRTRL
     TRIILNGTVH EKTWTIAEQD IERLAVSIMF RKNVERAVSE KALMRAQKKC KSAEKQALLP
     VWMRRIANWF QDKFQIDEEV VRKRYLECLK AQPWIHADKV VNCETKRYNP TVAEVGPKNH
     LLATTGLREL QREIPSANEP QDRGAKAWHS AHADLDIYAE GLRLDSAKEA AAGKQSLAIT
     LQQAFQVLGK TKCEGCNNIE IEYWTGPPGS GKSRAAKPRF ADLQGGVLYC APTRTLRDAL
     DESVVHPSRV CTYHNALHVA AKESGNRPFD VIVIDEAETT PACYVGTMHH ASPSSRIVCL
     GDPHQIGYID FSDRKDDLKP FSIIAAECRT RRFNTTYRCP QDVLNLPIFK TLYPDAISFS
     KQLTSIRYLT RARSVTRTRH AQTLTQDQKP HSEPPVTAHE PQARRTDVIV HYAGTLPERA
     LLEKVRHINV ALTRHTNALY IRDESEKGEL VPSLMTPPSW STYRCTPVDK QMVPDPVAVE
     RENGSSGPCD SHHIGAITIL QELGKLTDTK GVRVFESEAV PTAHRRVVLD GNLDSGPDRY
     PMYQFTNLRG TKYTNIKDNQ QALHTLVGRY ARKINSSSRE DAEFDVKRIT ARLKEWIPFR
     TAEPEQVDSC FADAMQKIAE RGHGVDDIED FWSNEGQRIS YHLKGQQKVM DPTKLKLGQG
     ISAHEKCANI ALSAWVRIIQ DQMSTSEKFI FANGQSDRDT MSIIEARLQE KAREFKSIDI
     KEFDTVHNWV SILVFSWRCD RGCPEHLIEY FEKRSKSRTL SSRIGSVDVS FMLDSGAVWT
     IARNTLFASG LMLALFVGVD FIAAKGDDVF LAGNNLYLDA ERLRMGSYLA ANNLKIEKTA
     VVSFIGFIVS QAAVTADVVR LATRTYGRSY KNADDLAKYK IAIADHCKLF RSPRTRLMTA
     INCATLYGTS KECINYLMDA LDAFGHTKMS DLHLDPGFVM RVTPMKVDER VYSGQDGCQR
     ADKTREKQPE PGQPGPQQQQ QASTQEAGSK TSPRSRTDYQ PRPDGRTREP REHPGQPRSD
     TREGVKASDD GESHGSDIRG MDSRLSRPGR RIQDEPGRRE NSRRRDTSVN MRSISRDRGR
     QIPGTEFYDA TAGWRDLAST SDASPVLQAS VVVHHHHQQH GSRSDERRSG CVRERLEQQD
     GLDRSDVPKL GASRERVLHG RPDRSADGRT TPDSTGCIRV TRELPSDIER RHSVLQRTHS
     RESGSGGDRA VPTGQRTPEG EPGHSSRDHP NGRNVTARRF RAELHIDDDD RGPGRVRGRS
     NPATHGVDGA DAGVGAAGVP DCEPDIRRRK HNHHHDHAAT RVGDGNVAIH SQQRDGHRDR
     GRGSATVRVR SEFGRLGTES AGHQLNQDST NEHEPNDAGN AQDHSVPTQR NEGLLYAPEG
     VPTRVRNDNG DVLWTGAMED TEDNCGRLPP GNWWTPGYHR QQLRDRRCRD DRYVYINRTL
     LQGVPTLRSD TGGGEPLGPL RQCDTSEGRR GANSGSNLDR SAPIRIPGTI QRIRGPIRDG
     GQDHSPDTSL CAISSRSGEC GDGLHRERDR ECSLEFHLGE AATKSETCWR NRSRSPQSCG
     PHREP
 
 
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