ID   1A_CMVO                 Reviewed;         993 AA.
AC   P20122;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 70.
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 O) (CMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Cucumovirus.
OX   NCBI_TaxID=12309;
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.
RX   PubMed=2628183; DOI=10.1016/0378-1119(89)90448-4;
RA   Hayakawa T., Mizukami M., Nakamura I., Suzuki M.;
RT   "Cloning and sequencing of RNA-1 cDNA from cucumber mosaic virus strain
RT   O.";
RL   Gene 85:533-540(1989).
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   PIR; JQ0379; P1VXCM.
DR   SMR; P20122; -.
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; Transferase.
FT   CHAIN           1..993
FT                   /note="Replication protein 1a"
FT                   /id="PRO_0000083262"
FT   DOMAIN          72..290
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          687..838
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          839..993
FT                   /note="(+)RNA virus helicase C-terminal"
FT   REGION          50..409
FT                   /note="Methyltransferase"
FT   REGION          537..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..975
FT                   /note="ATP-dependent helicase"
FT   BINDING         714..721
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   993 AA;  111266 MW;  8FDEC1F3C66EBB4C CRC64;
     MATSSFNINE LVASHGDKGL LATALVDKAA HEQLEEQLQH QRRGRKVYVR NVLSVKDSEV
     IRNRYGGKYD LHLTQQEFAP HGLAGALRLC ETLDCLDSFP SSGLRQDLVL DFGGSWVTHY
     LRGHNVHCCS PCLGIRDKMR HTERLMNMRK IILNDPQQFD GRQPDFCTHP AADCKVQAHF
     AISIHGGYDM GFRGLCEAMN AHGTTILKGT MMFDGAMMFD DQGIIPELNC QWRKIRNAFS
     ETEDVTPLVG KLNSTVFSRV RKFKTLVAFD FINESTMSYV HDWENIKSFL TDQTYSYKGM
     TYGIERCVIN AGIMTYKIIG VPGMCPPELI RHCIWFPSIK DYVGLKIPAS QDLVEWKTVR
     ILTSTLRETE EIAMRCYNDK KAWMEQFKVI LGVLSAKSST IVINGMSMQS GERIDINDYH
     YIGFAILLHT KMKYEQLGKM YDMWNASSIS KWFAALTRPV RVFFSSAVHA LFPTLRPREE
     KEFLIKLSTF VTFNEECSFD GGEEWDVISS AAYVATQAVT DGKVLAAQKA EKLAEKLAQP
     VDEVSDSPEV PSSTPDDTAD VCGKEQEVSE LDSLSAQTRS PITRVAERAT AMLEYAAYEK
     QLHDTTVSNL KRIWNMAGGD DKRNSLEGNL KFVFDTYFTV DPMVNIHFST GRWMRPVPEG
     IVYSVGYNER GLGPKSDGEL FIVNSECVIC NSESLSAVTR SLQAPTGTIS QVDGVAGCGK
     TTAIKSIFEP STDMIVTANK KSAQDVRMAL FKSSDSKEAC AFVRTADSVL LNECPTVSRV
     LVDEVVLLHF GQLCAVMSKL KAVRAICFGD SEQIAFSSRD ASFDMRFSKI IPDETSDADT
     TFRSPQDVVP LVRLMATKAL PKGTHSKYTK WVSQSKVKRS VTSRSIASVT LVDLDSSRFY
     ITMTQADKAS LISRAKEMNL PKTFWNERIK TVHESQGISE DHVTLVRLKS TKCDLFKQFS
     YCLVALTRHK VTFRYEYCGV LNGDLIAECI ARA