1A_CMVFN
ID 1A_CMVFN Reviewed; 993 AA.
AC P17769; Q9WA94;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 76.
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 FNY) (CMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Bromoviridae; Cucumovirus.
OX NCBI_TaxID=12307;
OH NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
OH NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2732682; DOI=10.1099/0022-1317-70-1-1;
RA Rizzo T.M., Palukaitis P.;
RT "Nucleotide sequence and evolutionary relationships of cucumber mosaic
RT virus (CMV) strains: CMV RNA 1.";
RL J. Gen. Virol. 70:1-11(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 EMBL; D00356; BAA00264.1; -; Genomic_RNA.
DR PIR; JA0074; JA0074.
DR RefSeq; NP_049323.1; NC_002034.1.
DR SMR; P17769; -.
DR GeneID; 962641; -.
DR KEGG; vg:962641; -.
DR Proteomes; UP000002502; 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..993
FT /note="Replication protein 1a"
FT /id="PRO_0000083258"
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 538..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..975
FT /note="ATP-dependent helicase"
FT COMPBIAS 543..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 714..721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 993 AA; 111433 MW; 27F80E979F767960 CRC64;
MATSSFNINE LVASHGDKGL LATALVDKTA HEQLEEQLQH QRRGRKVYIR NVLGVKDSEV
IRNRYGGKYD LHLTQQEFAP HGLAGALRLC ETLDCLDSFP SSGLRQDLVL DFGGSWVTHY
LRGHNVHCCS PCLGIRDKMR HAERLMNMRK IILNDPQQFD GRQPDFCTQP AADCKVQAHF
AISIHGGYDM GFRGLCEAMN AHGTTILKGT MMFDGAMMFD DQGVIPELNC QWRKIRSAFS
ETEDVTPLVG KLNSTVFSRV RKFKTMVAFD FINESTMSYV HDWENIKSFL TDQTYSYRGM
TYGIERCVIH AGIMTYKIIG VPGMCPPELI RHCIWFPSIK DYVGLKIPAS QDLVEWKTVR
ILTSTLRETE EIAMRCYNDK KAWMEQFKVI LGVLSAKSST IVINGMSMQS GERIDINDYH
YIGFAILLHT KMKYEQLGKM YDMWNASSIS KWFAALTRPL RVFFSSVVHA LFPTLRPREE
KEFLIKLSTF VTFNEECSFD GGEEWDVISS AAYVATQAVT DGKILAAQKA EKLAEKLAQP
VSEVSDSPET SSQTPDDTAD VCGREREVSE LDSLSAQTRS PITRVAERAT AMLEYAAYEK
QLHDTTVSNL KRIWNMAGGD DKRNSLEGNL KFVFDTYFTV DPMVNIHFST GRWMRPVPEG
IVYSVGYNER GLGPKSDGEL YIVNSECVIC NSESLSTVTR SLQAPTGTIS QVDGVAGCGK
TTAIKSIFEP STDMIVTANK KSAQDVRMAL FKSSDSKEAC TFVRTADSVL LNECPTVSRV
LVDEVVLLHF GQLCAVMSKL KAVRAICFGD SEQIAFSSRD ASFDMRFSKI IPDETSDADT
TFRSPQDVVP LVRLMATKAL PKGTHSKYTK WVSQSKVKRS VTSRAIASVT LVDLDSSRFY
ITMTQADKAS LISRAKEMNL PKTFWNERIK TVHESQGISE DHVTLVRLKS TKCDLFKQFS
YCLVALTRHK VTFRYEYCGV LNGDLIAECV ARA