ID   1A_TAV                  Reviewed;         993 AA.
AC   P28931;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 75.
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   Tomato aspermy virus (TAV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Cucumovirus.
OX   NCBI_TaxID=12315;
OH   NCBI_TaxID=4627; Canna.
OH   NCBI_TaxID=41568; Chrysanthemum morifolium (Florist's daisy) (Dendranthema grandiflorum).
OH   NCBI_TaxID=4688; Lilium.
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=V;
RX   PubMed=1895056; DOI=10.1099/0022-1317-72-9-2191;
RA   Bernal J.J., Moriones E., Garcia-Arenal F.;
RT   "Evolutionary relationships in the cucumoviruses: nucleotide sequence of
RT   tomato aspermy virus RNA 1.";
RL   J. Gen. Virol. 72:2191-2195(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; D10044; BAA00936.1; -; Genomic_RNA.
DR   PIR; JQ1370; P1VXTA.
DR   RefSeq; NP_620760.1; NC_003837.1.
DR   SMR; P28931; -.
DR   GeneID; 962652; -.
DR   KEGG; vg:962652; -.
DR   Proteomes; UP000007399; 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_0000083266"
FT   DOMAIN          72..289
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          682..838
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          839..993
FT                   /note="(+)RNA virus helicase C-terminal"
FT   REGION          50..408
FT                   /note="Methyltransferase"
FT   REGION          525..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          711..975
FT                   /note="ATP-dependent helicase"
FT   COMPBIAS        561..581
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;  112062 MW;  516926DD910FF4EA CRC64;
     MAASAFNIHK LVASHGDKGL LASALVDKLA HEQLEEQVQH QRRGLKVYIR NALDVKDSEI
     IRDRYGGKYD LHLTQQEQAP HGLAGALRLC ELLDCLDSFP RTGLRQDLVL DFGGSWVTHY
     LRGHNVHCCS PCLGIRDKMR HTERLMTMRK VIVNDPDTFE SRVPDFCTLP AEDCKVQAHF
     VISIHGGYDM GFKGLCRAMH AHGTTFLKGT MMFDGAMLFD TEGYLADLKC KWKKIKPRTY
     ESEDQTPLLS RISDNLTTTI KDHTLIAFDF VDESTLSYVH KWENVKSFLT DQTYSYKGMT
     YGLERCLIQH GIMTYKIIAV PGTCPPELIR HCIWFTSLKD YVGLKIPVSQ DLVEWKTVRI
     LISTLRETEE IAMRCYSDKK NWLEQFKVIL GVLSSKSSTI VINGMAMQAG ERIDTSDYHY
     IGLAILLHTR MKYEQLGRMY DMWNSTFIRK FFASLTRPMR VFLSACVKTL FPTLRPRDEK
     EFLVKLSTFV TFNEVCQVDL DAEWDVISSA AFTAEMAVED GKRLAEDRKQ KAEAASQIPV
     DEIPDDTAES SDDTPREADT NQKSEPSSPE LETLSTQTRS PITRLAQRAS SMLEYSAYEA
     QLHDNAVSNL DRMWCMAGGD KKNNRLESNV KFVFETYHIV DPLVNVHFPT GRWLYRVPEG
     ISYSVGFNEH GIGPKADGEL YIVNADCVIS NSKCLADTTL QYLAPTGTIS LVDGVAGCGK
     TTAIKKMFNP ATDVIVTANK KSALDVRQAL FNCTDSKEAT TFVRTADSIL MNDTNEVQRV
     LVDEVVLLHF GQLCAVMSKL KAVRAICFGD SEQIAFCSRD ASFDMRHSTI IPDETDTADT
     TFRSPQDVIK VVKCMASKAL KKGTHSKYAS WVSQSKVQRS VSSKAVASVT MVDLTEDRFY
     ITMTQADKTA LRTRARELNM SNDFIEHRIK TTHESQGVSE DHVTLVRLKT TKCDLFKAFK
     YCLVAVTRHK KTFRYEHVGK LDGDLIAECL ARV