1A_CMVY
ID 1A_CMVY Reviewed; 993 AA.
AC Q83264;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 66.
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 Y) (CMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Bromoviridae; Cucumovirus.
OX NCBI_TaxID=12312;
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].
RA Kataoka J., Masuta C., Takanami Y.;
RT "Complete nucleotide sequence of RNA1 of cucumber mosaic virus Y strain and
RT evolutionary relationships among genome RNAs of the virus strains.";
RL Nihon Shokubutsu Byori Gakkaiho 56:501-507(1990).
RN [2]
RP INTERACTION WITH ARABIDOPSIS TIP1-1; TIP1-2; TIP1-3; TIP2-1; TIP2-2 AND
RP TIP2-3.
RC STRAIN=Isolate Kor;
RX PubMed=17030879; DOI=10.1099/vir.0.82252-0;
RA Kim M.J., Kim H.R., Paek K.-H.;
RT "Arabidopsis tonoplast proteins TIP1 and TIP2 interact with the cucumber
RT mosaic virus 1a replication protein.";
RL J. Gen. Virol. 87:3425-3431(2006).
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 (By similarity).
CC Interacts with Arabidopsis TIP1-1, TIP1-2, TIP1-3, TIP2-1, TIP2-2 and
CC TIP2-3. {ECO:0000250, ECO:0000269|PubMed:17030879}.
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; D12537; BAA02105.1; -; Genomic_RNA.
DR PIR; JQ2169; JQ2169.
DR SMR; Q83264; -.
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 1: Evidence at protein level;
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_0000083264"
FT DOMAIN 72..290
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 683..839
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 840..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 713..976
FT /note="ATP-dependent helicase"
FT COMPBIAS 543..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 715..722
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 993 AA; 111468 MW; 20F9EA0F3A63D0FF CRC64;
MATSSFNINE LVASHGDKGL LATALVDKTT HEQLEEQLQH QRRGRKVYIR NVLGVKDSEV
IRNRYGGKYD LHLTQQEFAS QGLAGALRLC GTLDCLDSFP SSGLRQDLVL DFGGSWVTHY
LRGHNVHCCS PCLGIRDKMR HSERLMNMRK 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 VCGKEREVSE LDSLSAQTRS PITRVAERAT AMLEYAAYEK
HLHDTTVSNL KRIWNMAGGD DKRSFLEGNL KFVFDSYFTV DPMVNIHFST GRWVRPVPEG
IVYPVGYNER GLGPKSDGEL YIVNSECVIC NSESLSTVYG RSLQTPTGTI SQVDGVAGCG
KTMPIKSIFE PSTDMIVTAN KKSAQDVRMA LFKSSDSKEA CTFVRTADSV LLNECPTVSR
VLEDEVVLLH FGQLCAVMSK LKAVRAICFG DAEQIAFSSR DASFDMRFSK IIPDETSDAD
TTFRSPQDVV PLVRLMATKA LPKGTHSKYT KWVSQSKVRR SVTSRAIASV TLVDLDSSRF
YITMTQADKA SLISRAKEMN LPKTFWNERI KTVHESQGIS EDHVTLVRLK STKCDLFKQF
SYCLVALTRH KVTFRYEYCG VLNGDLIASV ARA
