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1A_BBMV
ID   1A_BBMV                 Reviewed;         966 AA.
AC   Q00020;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 85.
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   Broad bean mottle virus.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Bromovirus.
OX   NCBI_TaxID=12301;
OH   NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Bawden;
RX   PubMed=1962437; DOI=10.1016/0042-6822(91)90525-g;
RA   Dzianott A.M., Bujarski J.J.;
RT   "The nucleotide sequence and genome organization of the RNA-1 segment in
RT   two bromoviruses: broad bean mottle virus and cowpea chlorotic mottle
RT   virus.";
RL   Virology 185:553-562(1991).
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.
CC   -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC       {ECO:0000250}; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the bromoviridae replication protein 1a family.
CC       {ECO:0000305}.
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DR   EMBL; M65138; AAA42740.1; -; Genomic_RNA.
DR   PIR; A41699; P1BVBB.
DR   RefSeq; NP_659000.1; NC_004008.1.
DR   SMR; Q00020; -.
DR   GeneID; 962140; -.
DR   KEGG; vg:962140; -.
DR   Proteomes; UP000007448; 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:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
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; IPR022184; CMV_1a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF12503; CMV_1a_C; 1.
DR   Pfam; PF01443; Viral_helicase1; 1.
DR   Pfam; PF01660; Vmethyltransf; 1.
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..966
FT                   /note="Replication protein 1a"
FT                   /id="PRO_0000083255"
FT   DOMAIN          71..261
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          660..815
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          816..966
FT                   /note="(+)RNA virus helicase C-terminal"
FT   REGION          49..381
FT                   /note="Methyltransferase"
FT   REGION          687..951
FT                   /note="ATP-dependent helicase"
FT   BINDING         690..697
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   966 AA;  109622 MW;  DF592681D7231C8D CRC64;
     MSSFVNLESL ISERGANCRG ADEIVNNETT RILTSQIEHS QRSKKVNIRN KLSVAECDAF
     RARYGGAFDV NLTHEYTAPH SLAGALRVAE HYDCIDSFPP EDKIIDFGGS WLHHYSRGDS
     RVHSCCPILG PRDATRHEER MCRLRKMVQT SDRFVDVPDF CLNKAEDCNV QADWAICIHG
     GYDMGFQGLC KAMHAPLERG ILQGTIMFDG AMLFDRQGEL PLLQCRWQRV GTGSKEQIKF
     DFINESTLSY VHDWKNLGSF LTESTYSIGG TTYLLERMLL KCSIMTYKII ATNVRCPPES
     LRHCIWFENI SQYLAVQIPI GYNLNDWKTV RVARATVREV EEISFRCFKE NKDWTENMRS
     VASILSAKSS TVIINGQSIM SGERLDVLEY HLVAFSLTLN LYQKYEKLRN FQGELEWKGW
     ANHFKTRLWW CGRTVSTEGG FLRNFLADKI PWLKLNTYAD SLDFITKISE VESFEVDSVP
     TSRLRSFFQK EENIVERAAS EIMSANARRI AKKAEMSKEF DDFVDAPEEF APEDVVEEVI
     NTPVTQDVKL RQSKPETARS IVLDPDAVLK NGAINEFADY SKRLHENTVS NLRHLWTLMG
     CRGNEIHNKS VAETYHRVDD MVNVHFPNGH WMYPLKYEYT VGYNDGGLGE KFENELYVVD
     KTCSCANAKA IADACKKVSA PTCSVVMVDG VAGCGKTTAI KETFRFEKDI IVTANRKSAE
     DVRKAIFGDA SDSEVALKVV RTADSAIMHG LPECHRLLVD EAGLLHYGQL LAVADLCKCS
     EVLAFGDTEQ ISFKSRDATF RMKYCNIEYD KRDIVSKTFR CPQDVVSAVK ILKRKCANRS
     SKYNGWVSSS KVEKSLSKSR IVSINQVSME KHKFYLTMTE ADKAALCSRA KDVGLDKTWV
     ESNMETVHEA QGKAVDHVVL VRLKSTKCDL FKSEEYCLVA LTRHKRTFEY LYNGDLGGDL
     ISFYVT
 
 
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