1A_BMV
ID 1A_BMV Reviewed; 961 AA.
AC P03588;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Brome mosaic virus (BMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Bromoviridae; Bromovirus.
OX NCBI_TaxID=12302;
OH NCBI_TaxID=15371; Bromus inermis (Smooth brome grass) (Bromopsis inermis).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6694215; DOI=10.1016/s0022-2836(84)80012-1;
RA Ahlquist P., Dasgupta R., Kaesberg P.;
RT "Nucleotide sequence of the brome mosaic virus genome and its implications
RT for viral replication.";
RL J. Mol. Biol. 172:369-383(1984).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNA-DIRECTED RNA
RP POLYMERASE 2A, AND MUTAGENESIS OF 396-LEU--LEU-407; LEU-400; LYS-403 AND
RP LYS-406.
RX PubMed=19325881; DOI=10.1371/journal.ppat.1000351;
RA Liu L., Westler W.M., den Boon J.A., Wang X., Diaz A., Steinberg H.A.,
RA Ahlquist P.;
RT "An amphipathic alpha-helix controls multiple roles of brome mosaic virus
RT protein 1a in RNA replication complex assembly and function.";
RL PLoS Pathog. 5:E1000351-E1000351(2009).
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. {ECO:0000269|PubMed:19325881}.
CC -!- SUBUNIT: Interacts with RNA-directed RNA polymerase 2a.
CC {ECO:0000269|PubMed:19325881}.
CC -!- INTERACTION:
CC P03588; P03594: ORF2a; NbExp=2; IntAct=EBI-15874242, EBI-15874357;
CC P03588; Q04947: RTN1; Xeno; NbExp=4; IntAct=EBI-15874242, EBI-38020;
CC P03588; Q12443: RTN2; Xeno; NbExp=4; IntAct=EBI-15874242, EBI-32591;
CC P03588; Q12402: YOP1; Xeno; NbExp=4; IntAct=EBI-15874242, EBI-37092;
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19325881}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19325881}.
CC -!- SIMILARITY: Belongs to the bromoviridae replication protein 1a family.
CC {ECO:0000305}.
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DR EMBL; X02380; CAA26228.1; -; Genomic_RNA.
DR PIR; A04196; P1BVA.
DR RefSeq; NP_041196.1; NC_002026.1.
DR BMRB; P03588; -.
DR SMR; P03588; -.
DR DIP; DIP-59378N; -.
DR IntAct; P03588; 4.
DR PRIDE; P03588; -.
DR GeneID; 962143; -.
DR KEGG; vg:962143; -.
DR Proteomes; UP000001649; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
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:0039690; P:positive stranded viral RNA replication; IDA:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Helicase; Host endoplasmic reticulum; Host membrane;
KW Hydrolase; Membrane; Methyltransferase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..961
FT /note="Replication protein 1a"
FT /id="PRO_0000083256"
FT DOMAIN 71..260
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 655..810
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 811..961
FT /note="(+)RNA virus helicase C-terminal"
FT REGION 48..380
FT /note="Methyltransferase"
FT REGION 392..409
FT /note="Membrane association"
FT REGION 503..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..946
FT /note="ATP-dependent helicase"
FT BINDING 685..692
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 396..407
FT /note="LTLNLYQKYEKL->ATLNAYQKYEKA: Complete loss of
FT membrane-rearranging capacity, viral RNA template
FT recruitment, and replication. Increase in 1a mediated 2aPol
FT accumulation."
FT /evidence="ECO:0000269|PubMed:19325881"
FT MUTAGEN 396
FT /note="L->A: Reduces 1a membrane association."
FT MUTAGEN 400
FT /note="L->A: Reduces 1a membrane association."
FT /evidence="ECO:0000269|PubMed:19325881"
FT MUTAGEN 403
FT /note="K->E: Slightly reduces 1a membrane association."
FT /evidence="ECO:0000269|PubMed:19325881"
FT MUTAGEN 403
FT /note="K->R: No effect on membrane association; 5- to 8-
FT fold increase in the number of 1a-induced membrane
FT invaginations. Enhances viral RNA template recruitment.
FT Complete loss of RNA replication. 50% loss of 1a mediated
FT 2aPol accumulation."
FT /evidence="ECO:0000269|PubMed:19325881"
FT MUTAGEN 406
FT /note="K->E: No effect on 1a membrane association."
FT /evidence="ECO:0000269|PubMed:19325881"
SQ SEQUENCE 961 AA; 109210 MW; 4F315CB2E2F4EFBC CRC64;
MSSSIDLLKL IAEKGADSQS AQDIVDNQVA QQLSAQIEYA KRSKKINVRN KLSIEEADAF
RDRYGGAFDL NLTQQYHAPH SLAGALRVAE HYDCLDSFPP EDPVIDFGGS WWHHFSRRDK
RVHSCCPVLG VRDAARHEER MCRMRKILQE SDDFDEVPNF CLNRAQDCDV QADWAICIHG
GYDMGFQGLC DAMHSHGVRV LRGTVMFDGA MLFDREGFLP LLKCHWQRDG SGADEVIKFD
FENESTLSYI HGWQDLGSFF TESVHCIDGT TYLLEREMLK CNIMTYKIIA TNLRCPRETL
RHCVWFEDIS KYVGVSIPED WSLNRWKCVR VAKTTVREVE EIAFRCFKES KEWTENMKAV
ASILSAKSST VIINGQAIMA GERLDIEDYH LVAFALTLNL YQKYEKLTAL RDGMEWKGWC
HHFKTRFWWG GDSSRAKVGW LRTLASRFPL LRLDSYADSF KFLTRLSNVE EFEQDSVPIS
RLRTFWTEED LFDRLEHEVQ TAKTKRSKKK AKVPPAAEIP QEEFHDAPES SSPESVSDDV
KPVTDVVPDA EVSVEVPTDP RGISRHGAMK EFVRYCKRLH NNSESNLRHL WDISGGRGSE
IANKSIFETY HRIDDMVNVH LANGNWLYPK KYDYTVGYNE HGLGPKHADE TYIVDKTCAC
SNLRDIAEAS AKVSVPTCDI SMVDGVAGCG KTTAIKDAFR MGEDLIVTAN RKSAEDVRMA
LFPDTYNSKV ALDVVRTADS AIMHGVPSCH RLLVDEAGLL HYGQLLVVAA LSKCSQVLAF
GDTEQISFKS RDAGFKLLHG NLQYDRRDVV HKTYRCPQDV IAAVNLLKRK CGNRDTKYQS
WTSESKVSRS LTKRRITSGL QVTIDPNRTY LTMTQADKAA LQTRAKDFPV SKDWIDGHIK
TVHEAQGISV DNVTLVRLKS TKCDLFKHEE YCLVALTRHK KSFEYCFNGE LAGDLIFNCV
K
