ID   1A_PSVJ                 Reviewed;        1005 AA.
AC   P28726;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 78.
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   Peanut stunt virus (strain J) (PSV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Cucumovirus.
OX   NCBI_TaxID=12314;
OH   NCBI_TaxID=4045; Apium graveolens (Celery).
OH   NCBI_TaxID=3818; Arachis hypogaea (Peanut).
OH   NCBI_TaxID=53860; Coronilla.
OH   NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH   NCBI_TaxID=3873; Lupinus luteus (European yellow lupine).
OH   NCBI_TaxID=3879; Medicago sativa (Alfalfa).
OH   NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
OH   NCBI_TaxID=3914; Phaseolus angularis (Azuki bean) (Vigna angularis).
OH   NCBI_TaxID=47097; Tephrosia.
OH   NCBI_TaxID=3898; Trifolium.
OH   NCBI_TaxID=3904; Vicia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1545224; DOI=10.1099/0022-1317-73-3-701;
RA   Karasawa A., Nakaho K., Kakutani T., Minobe Y., Ehara Y.;
RT   "Nucleotide sequence analyses of peanut stunt cucumovirus RNAs 1 and 2.";
RL   J. Gen. Virol. 73:701-707(1992).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D11126; BAA01900.1; -; Genomic_RNA.
DR   PIR; JQ1451; P1VXPJ.
DR   SMR; P28726; -.
DR   PRIDE; P28726; -.
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..1005
FT                   /note="Replication protein 1a"
FT                   /id="PRO_0000083265"
FT   DOMAIN          72..285
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          695..846
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          847..1005
FT                   /note="(+)RNA virus helicase C-terminal"
FT   REGION          51..404
FT                   /note="Methyltransferase"
FT   REGION          719..983
FT                   /note="ATP-dependent helicase"
FT   BINDING         722..729
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1005 AA;  112018 MW;  42C73BA334E630F9 CRC64;
     MAVSSSNLNE LVASHGSSGL IASALVDKVA SEQLEEQLNH QRRGLKVYIR NRLDVKESEV
     IRNRYGGKYD LHLSQQEHAP HGLAGALRLC ETLDCLDAFP RTGLRQDLVL DFGGSWVTHF
     LRGHNVHCCS PCLGVRDKMR HTERLLSMRK AIINDPQTFE GRQPNFCTNP AEKCDVQAHY
     AISIHGGYDM GFEGLCRAMN AHGTTFLKGT MMFDGAMLFD DSGFIPELKC HWRKIKNAFS
     EKENASTFTS KLNLAVSGKT LIAFDFENES TMSYIHEWKN IKSFLTDQTF SYNGYTYGIE
     RCVIYAGILT YKIIGVPGEC PPEVIRHCVW FPSLKDYVGL KIPVSADLVE WKTVRLPLST
     LRDTEEIAMR CYNDKKTWQD QFKIILGVLS SKSSTIVING MAMQAGERVD INDYPYIGFA
     IMLHTKMKYD KLSLMYDAWG ASIISQWWKA MTKPIRTFVR LVARTLFPTL RPRSESEFLV
     KLSTFVTFND ECITDMGEVW DVTANAAAVA AWAVSDGKQL VAEKEKALEL ANQQPVQNDS
     QPLTTVNLST QDPPRSVTAI LDPENPVVGQ AELPEPPELK ALSFQTRSPD TRLAERASAM
     LEYVAYEQQL HQNVISNLQR IWCSAGGDFV TNRLEGNLKF VFDTYFLTDP LVNVHFPSGR
     WMRPVPAGTK YMVGFNEKGL GPKMDSELYI VNADCVICNS DGLSSAVKAL TAPTGTISLV
     DGVAGCGKTT AIKKLFQPAT DLIVTANKKS AQDVRMALFG ASDSKEACTF VRTADSILLN
     DVPEVSRVLV DEVVLLHFGQ LCAVMSKLKA VRAICFGDSE QIAFGSRDAS FDMRRSTILP
     DESSTSDTTF RSPQDVVPLV TRMAGKALPR GAKSKYSRWL SQSKVLNSVS QRCIPSVALV
     DMDESRFYIT MTQADKAALI TRAKELQMPS SFYDNKIKTV HESQGISEDH VTLVRLKSTK
     CDLFKSFPYC LVALTRHKVS FRYEFCGELK GDLIALVLAT HSPLI