ID   1A_CCMV                 Reviewed;         958 AA.
AC   P27752;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 82.
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   Cowpea chlorotic mottle virus (CCMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Bromovirus.
OX   NCBI_TaxID=12303;
OH   NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH   NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1962437; DOI=10.1016/0042-6822(91)90525-g;
RA   Dzianott A.M., Bujarski J.J.;
RT   "The nucleotide sequence and genome organization of the RNA-1 segment in
RT   two bromoviruses: broad bean mottle virus and cowpea chlorotic mottle
RT   virus.";
RL   Virology 185:553-562(1991).
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; M65139; AAA46369.1; -; mRNA.
DR   PIR; B41699; P1BVCC.
DR   RefSeq; NP_613278.1; NC_003543.1.
DR   SMR; P27752; -.
DR   GeneID; 962153; -.
DR   KEGG; vg:962153; -.
DR   Proteomes; UP000008445; 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; IPR002588; Alphavirus-like_MT_dom.
DR   InterPro; IPR022184; CMV_1a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
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   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Host endoplasmic reticulum; Host membrane;
KW   Hydrolase; Membrane; Methyltransferase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..958
FT                   /note="Replication protein 1a"
FT                   /id="PRO_0000083257"
FT   DOMAIN          71..260
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          652..807
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          808..958
FT                   /note="(+)RNA virus helicase C-terminal"
FT   REGION          49..380
FT                   /note="Methyltransferase"
FT   REGION          529..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          680..943
FT                   /note="ATP-dependent helicase"
FT   COMPBIAS        529..548
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         682..689
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   958 AA;  109139 MW;  89AFEF744C2D1D3A CRC64;
     MASSLDLLKL ISERGADSRG ASDIVEQQAV KQLLEQVDYS KRSKKINIRN KLTPDEENAF
     RARYGGAFDL NLTQQYNAPH SLAGALRIAE HYDCLSSFPP LDPIIDFGGS WWHHYSRKDT
     RIHSCCPVLG VRDAARHEER LCRMRKLLQE CDDREDLPDF CIDRAESCSV QADWAICIHG
     GYDMGYTGLC EAMHSHGVRI LRGTIMFDGA MLFDNEGVLP LLKCRWMKSG KGKSEVIKFD
     FMNESTLSYI HSWTNLGSFL TESVHVIGGT TYLLERELLK CNIMTYKIVA TNLKCPKETL
     RHCVWFENIS QYVAVNIPED WNLTHWKPVR VAKTTVREVE EIAFRCFKEN KEWTENMKAI
     ASILSAKSST VIINGQAIMA GERLNIDEYH LVAFALTMNL YQKYENIRNF YSEMEWKGWV
     NHFKTRFWWG GSTATSSTGK IREFLAGKFP WLRLDSYKDS FVFLSKISDV KEFENDSVPI
     SRLRSFFSSE DLMERIELEL ESAQKRRREK KKKEVEKIDE EEFQDAIDIP NDAVRDDAKP
     EKEPKPEVTV GAEPTGPEEA SRHFAIKEFS DYCRRLDCNA VSNLRRLWAI AGCDGRTARN
     KSILETYHRV DDMINLHYPG GQWLYPKKYD YEVGFNDSGL GPKFDDELYV VDKSCICANY
     QVLSKNTDSL KAPSCKISLC DGVAGCGKTT AIKSASNIAE HLVVTANKKS AEDVREALFP
     HNPSSEIAFK VIRTADSALM HGLPRCKRLL VDEAGLLHYG QLLAVAALCK CQSVLAFGDT
     EQISFKSRDA TFRLKYGDLQ FDSRDIVTET WRCPQDVISA VQTLKRGGNR TSKYLGWKSH
     SKVSRSISHK EIASPLQVTL SREKFYLTMT QADKAALVSR AKDFPELDKA WIEKHIKTVH
     EAQGVSVDHA VLVRLKSTKC DLFKTEEYCL VALTRHKITF EYLYVGMLSG DLIFRSIS