ID   1A_CMVII                Reviewed;         993 AA.
AC   Q83270;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 62.
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 Iizuka) (CMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Cucumovirus.
OX   NCBI_TaxID=117113;
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].
RA   Karasawa A., Ito A., Okada I., Hase S., Ehara Y.;
RT   "A possible role of RNA 2 of cucumber mosaic cucumovirus as a determinant
RT   of infection phenotype on cowpea.";
RL   Nihon Shokubutsu Byori Gakkaiho 63:289-297(1997).
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; D16403; BAA03887.1; -; Genomic_RNA.
DR   SMR; Q83270; -.
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_0000083259"
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          51..409
FT                   /note="Methyltransferase"
FT   REGION          544..575
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;  111480 MW;  BCD95906008B1CA7 CRC64;
     MATSSFNINE LVASHGDKGL LATALVDKTA HEQLEEQLQH QRRGRKVYIR NVLGVKDSEV
     IRNRYGGKYD LHLTQQEFAP HGLAGVLRLC ETLDCLDSFP SSGLRQDLVL DFGGSWVTHY
     LRGHNVHCCS PCLGIRDKMR HAERLMNMRK IILNDPQQFD GRQPDFCTQP AEDCKVQAHF
     AISIHGGYDM GFRGLCEAMN AHGTTILKGT MMFDGAMMFD DQGVIPELNC QWRKIRSAFS
     ETEDVTPLSG KLNSTVFSRV RKFKTMVAFD FINESTMSYV HDWENIKSFL TDQTYSYRGM
     TYGIERCVIH AGIMTYKIIG VPGMCPPELI RHCIWFPSIK DYVGLKIPAS QDLVEWKTVR
     ILMSTLRETE EIAMRCYNDK KAWMEQFKVI LGVLSAKSST IVINGMSMQS GERIDINDYH
     HIGFAILLHT KMKYEQLGKM YDMWNASSIS KWFAALTRPL RVFFSSVVHA LFPTLRPREE
     KEFLIKLSTF VTFNEECSFD GGEEWDVISS AAYVATQAVT DGKILAAQKA EKLAEKLAQP
     VIEVSDSPEA SSQTPDDTAE VCGKEREVSE LDSLSAQTRS PITRVAERAT AMLEYAAYEK
     QLHDTTVSNL KRIWNMAGGD DKRNSLEGNL KFVFDTYFTV DPMVNIHFST GRWMRPVPEG
     VVYSVGYNER GLGPKSDGEL YIVNSECVIC NSESLSTVTR SLQAPTGTIS QVDGVAGCGK
     TTAIKSIFEP STDMIVTANK KSAQDVRMAL FKSSDSKEAC TFVRTADSVL LNECPTVSRV
     LVDEVVLLHF GQLCAVMSKL KAVRAICFGD SEQIAFSSRD ASFDMRFSKI IPDETSDADT
     TFRSPQDVVP LVRLMATKAL PKGTHSKYTK WVSQSKVTRS VTSRAIVSVT LVDLDSSRFY
     ITMTQADKAS LISRAKEMNL PKTFWNERIK TVHESQGISE DHVTLVRLKS TKCDLFKQFS
     YCLVALTRHK VTFRYEYCGV LNGDLIAECV ARA