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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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