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1A_OLV2I
ID   1A_OLV2I                Reviewed;         908 AA.
AC   Q83943;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 75.
DE   RecName: Full=Replication protein 1a;
DE   Includes:
DE     RecName: Full=ATP-dependent helicase;
DE              EC=3.6.4.-;
DE   Includes:
DE     RecName: Full=Methyltransferase;
DE              EC=2.1.1.-;
GN   ORFNames=ORF1a;
OS   Olive latent virus 2 (isolate Italy) (OLV-2).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Oleavirus.
OX   NCBI_TaxID=650489;
OH   NCBI_TaxID=4145; Olea.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8887501; DOI=10.1099/0022-1317-77-10-2637;
RA   Grieco F., Dell'Orco M., Martelli G.P.;
RT   "The nucleotide sequence of RNA1 and RNA2 of olive latent virus 2 and its
RT   relationships in the family Bromoviridae.";
RL   J. Gen. Virol. 77:2637-2644(1996).
RN   [2]
RP   SEQUENCE REVISION.
RA   Grieco F.;
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the virus replication. Contains a helicase domain
CC       and a methyltransferase domain. The methyltransferase domain is
CC       probably involved in viral RNA capping. Involved in the formation of ER
CC       membrane spherular invaginations in which RNA replication complexes
CC       form (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RNA-directed RNA polymerase 2a. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bromoviridae replication protein 1a family.
CC       {ECO:0000305}.
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DR   EMBL; X94346; CAA64072.1; -; Genomic_RNA.
DR   RefSeq; NP_620042.1; NC_003673.1.
DR   SMR; Q83943; -.
DR   GeneID; 991141; -.
DR   KEGG; vg:991141; -.
DR   Proteomes; UP000000412; Genome.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; 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; IPR027417; P-loop_NTPase.
DR   Pfam; PF01443; Viral_helicase1; 1.
DR   Pfam; PF01660; Vmethyltransf; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Host endoplasmic reticulum; Host membrane;
KW   Hydrolase; Membrane; Methyltransferase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..908
FT                   /note="Replication protein 1a"
FT                   /id="PRO_0000402414"
FT   DOMAIN          66..304
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          599..755
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          756..908
FT                   /note="(+)RNA virus helicase C-terminal"
FT   REGION          47..341
FT                   /note="Methyltransferase"
FT   REGION          629..887
FT                   /note="ATP-dependent helicase"
SQ   SEQUENCE   908 AA;  102756 MW;  4E749369ACCD4DA6 CRC64;
     MDSAALEKMT GAKFPAVQGV IEEFSRDRVQ NVLGDMRSRQ VIKYAVGLSE ASVQELRFNW
     PCFTWEEESV PLPPHPFAAY SRRAFTRWAI AQCGPVPIKD FGGNWFLHWQ WQTGVHSCCP
     LLNPRDGAHQ TRRELNMESY LRTHGPKYDK FNELSRPDLC HHRAEDCSVR AKAALSVDSA
     YDMGLKNTCK AMHRAGIELL HGNILFDPDM LIEAKMEGFV AGMNYHWKKT RRSTGLMSSF
     LEMGSSLFGV SNSSKEGEGH HDLKIKMGSS STHMVPADWE ISYHFRDDCV LGYTHNLADV
     LSIATGSYVK VGNTFYELER TGLKSGMLMY TITACKGLYD RASARSTPLS AKASTVIING
     MSYQVGEKLD PISFPYLAAS FYMQAQKAVF EVQQVVDLHT PNRNLWSWFK KKFELKAHAF
     LFALGLRDSH DEWLLDQIEF ELNETVCTLP GEFLEPVSEV ERLDAALEDW RRDRERLNGK
     SVENLKTLTV LVELAKKLGI SAYEVLNSHQ NESERPKDQW HVEAALFEAV ELERAHWKML
     TAEAQAMSLQ DPLSREAKSK GWSYESSDSL PCAYAYVFSE GRFVKPADLK KKTRVLVSPS
     MQIMNQIRMA ESLEKAIAMN VKSCKKTWID GVAGCGKTYE IVHTADIFKK DDLILTANKK
     SQEDIFSQLK PGTDCAKRIR TVDSYLLKPD VQAKRLFIDE AGLVHPGKLL AAMRFAECDD
     CLLFGDSEQI PFVNIVESLQ PAKFLKLEVD AREVRETTYR CPADVTATLA TLYKKKKIVT
     KSKVLKSVTS KSLASASAVS GLDPHSWHLT MYQADKAELV RVARTNQMDD VWIKEHIKTV
     HEAQGISVPH VKLYRFKTFD QPLFDAAHAE AYRLVAISRH TQSFTYIGVN QHLCKADRML
     KFVICQIP
 
 
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