ID   1A_CMVIX                Reviewed;         993 AA.
AC   Q66121;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 67.
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 Ixora) (CMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Cucumovirus.
OX   NCBI_TaxID=117114;
OH   NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH   NCBI_TaxID=3562; Spinacia oleracea (Spinach).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7561763; DOI=10.1099/0022-1317-76-9-2257;
RA   McGarvey P.B., Tousignant M., Geletka L., Cellini F., Kaper J.M.;
RT   "The complete sequence of a cucumber mosaic virus from Ixora that is
RT   deficient in the replication of satellite RNAs.";
RL   J. Gen. Virol. 76:2257-2270(1995).
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; U20220; AAC54620.1; -; Genomic_RNA.
DR   PIR; E71392; E71392.
DR   SMR; Q66121; -.
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_0000083260"
FT   DOMAIN          72..290
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          684..838
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          839..993
FT                   /note="(+)RNA virus helicase C-terminal"
FT   REGION          51..409
FT                   /note="Methyltransferase"
FT   REGION          543..576
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;  111440 MW;  8C6448DE2EFA9DCA CRC64;
     MATSSFNINE LVASHGDKGL LATALVDKTA HEQLEEQLQH QRRGRKVYIR NVLGVKDSEV
     IRNRYGGKYD LHLTQQEFAP HGLAGALRLC ETLDCLDSFP SSGLRQDLVL DFGGSWVTHY
     LRGHNVHCCS PCLGIRDKMR HAERLMNMRK IILNDPQQFD GRQPDFCTHP AAECDVQAHF
     AISIHGGYDM GFRGLCEAMN AHGTTILKGT MMFDGAMMFD DQGVIPELNC QWRKIRSAFS
     ETEDVTPLSG KLNSTVFSRV RKFKTMVAFD FINESTMSYV HDWENIRSFL TDQTYSYRGM
     TYGIERCVIH AGIMTYKIIG VPGMCPPELI RHCIWFPSIK DYVGLKIPAS QDLVEWKTVR
     YLTSTLRETE EIAMRCYNDK KAWMEQFKVI LGVLSAKSST IVINGMSMQS GERIDINDYH
     YIGLAILLHT KMKYEQLGKM YDMWNASSIS KWFAALTRPL RVFFSSVVHA LFPTLRPREE
     KEFLIKLSTF VTFNEECSFD GGEEWDVISS AAYVATQAVT DGKVLAAQKA EKLAEKLAQP
     VIEVSDRPEA PSPTPDDPAD VCGKEQEVSE LDSLSAQTRS PITRVAERAT AMLEYAAYEK
     QLHDTTVSNL KRIWNMAGGD DKRNSLEGNL KFVFDTYFTV DPMVNIHFST GKWMRPVPEG
     IVYSVGFNEH GLGPKSDGEL YIVNSECVVC NNESLSNVTR SLQAPTGTIS QVDGVAGCGK
     TTAIKSIFEP STDMVVTANK KSAQDVRMAL FKSSDSKEAC TFVRTADSVL LNECPTVSRV
     LVDEVVLLHF GQLCAVMSKL KAVRAICFGD SEQIAFSSRD ASFDMRFSKI IPDETSDADT
     TFRSPQDVVP LVRLMATKAL PRGTHSKYTK WVSQSKVKRS VTSRAISSVT LVDLDSSRFY
     ITMTQADKAS LISRAKEMNL PKTFWNERIK TVHESQGISE DHVTLVRLKS TKCDLFKQFS
     YCLVALTRHK VTFRYEHCGI LNGDLIAECI ARA