ID   1A_CMVQ                 Reviewed;         991 AA.
AC   P06011;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 79.
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   Cucumber mosaic virus (strain Q) (CMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Cucumovirus.
OX   NCBI_TaxID=12310;
OH   NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH   NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=4018086; DOI=10.1111/j.1432-1033.1985.tb09025.x;
RA   Rezaian M.A., Williams R.H.V., Symons R.H.;
RT   "Nucleotide sequence of cucumber mosaic virus RNA. 1. Presence of a
RT   sequence complementary to part of the viral satellite RNA and homologies
RT   with other viral RNAs.";
RL   Eur. J. Biochem. 150:331-339(1985).
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; X02733; CAA26515.1; -; Genomic_RNA.
DR   PIR; A25480; P1BVCV.
DR   SMR; P06011; -.
DR   Proteomes; UP000008454; 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; IPR021002; 1a_necrotic_phenotyp-det_dom.
DR   InterPro; IPR002588; Alphavirus-like_MT_dom.
DR   InterPro; IPR022184; CMV_1a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF12467; CMV_1a; 1.
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..991
FT                   /note="Replication protein 1a"
FT                   /id="PRO_0000083263"
FT   DOMAIN          72..290
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          686..837
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          838..991
FT                   /note="(+)RNA virus helicase C-terminal"
FT   REGION          52..409
FT                   /note="Methyltransferase"
FT   REGION          711..973
FT                   /note="ATP-dependent helicase"
FT   BINDING         713..720
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   991 AA;  110918 MW;  9EE5F708B80E9A39 CRC64;
     MATSSFNINE LVASHGDKGL LATALVDKTA HEQLEEQLQH QRRGLKVYIR NVLDVKDSEV
     IRTRYGGKYD LHLAQQELAP HGLAGALRLC ETLDCLDFFP RSGLRQDLVL DFGGSWVTHY
     LRGHNVHCCS PCLGIRDKMR HTERLMSMRK VILNDPQQFD GRQPDFCTKS AAECKVQAHF
     AISIHGGYDM GFRGLCEAMN AHGTTILKGT MMFDGAMMFD DQGFIPELKC QWRKIKSAFS
     EEEDATCSAA KLNSSVFSRV RNGKTLIAFD FVEESTMSYV HDWDNIKSFM TDQTYSFNGM
     TYGIERCVIY AGVMTYKIVG VPGMCPPELI RHCIWFPSMK DYVGLKIPAS DDLVKWKTVR
     ILLSTLRETE EIAMRCYNDK KNWMDLFKII LGVLSSKSST IVINGMSMQS GERIDLNDYH
     YIGFAILLHT KLKYEQLGKM YDMWNASFIW KWFASMSRPF RVFFSTVVKT LFPTLRPREE
     KEFLVKLSTF VTFNEECSFD GGKEWDVISS AAFVATQAVA DGTILAEEKA KKLADRLAVP
     VEEVTAIPEV SPTPVDQGTA CGLETETSEL DSLSAQTRSP IARIAERATA MLEYSAYEKQ
     LHDTTVSNLQ RIWCMAGGDN KRNSLESNLK FVFDTYFSVD ALVNVHFPTG RWMHPVPEGV
     VYSVGYNEKG LGPKLDSELY IVNGDCVISN SHDLFSITKS LLAPTGTISQ VDGVAGCGKT
     TAIKSMFNPS TDIIVTANKK SAQDVRYALF KSTDSKEACA FVRTADSILL NDCPTVSRVL
     VDEVVLLHFG QLCAVMSKLH AVRALCFGDS EQIAFSSRDA SFDMRFSKLI PDETSDADTT
     FRSPQDVVPL VRLMATKALP KGTRTKYSDG AQSKVRKSVT SRAVASVSLV ELDPTRFYIT
     MTQADKASLI TRAKELNLPK AFYTDRIKTV HESQGISEDH VTLVRLKSTK CDLFKKFSYC
     LVAVTRHKVT FRYEYCGVLG GDLIANCIPL V