ID   ALPHA_BSMV              Reviewed;        1139 AA.
AC   P17595;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Replication protein alpha-A;
DE   Includes:
DE     RecName: Full=Methyltransferase;
DE              EC=2.1.1.-;
DE   Includes:
DE     RecName: Full=NTPase/helicase;
DE              EC=3.6.4.13;
OS   Barley stripe mosaic virus (BSMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Virgaviridae; Hordeivirus.
OX   NCBI_TaxID=12327;
OH   NCBI_TaxID=4513; Hordeum vulgare (Barley).
OH   NCBI_TaxID=4565; Triticum aestivum (Wheat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=ATCC PV43;
RX   PubMed=2728343; DOI=10.1016/0042-6822(89)90427-3;
RA   Gustafson G., Armour S.L., Gamboa G.C., Burgett S.G., Shepherd J.W.;
RT   "Nucleotide sequence of barley stripe mosaic virus RNA alpha: RNA alpha
RT   encodes a single polypeptide with homology to corresponding proteins from
RT   other viruses.";
RL   Virology 170:370-377(1989).
RN   [2]
RP   FUNCTION.
RX   PubMed=2209552; DOI=10.1002/j.1460-2075.1990.tb07553.x;
RA   Petty I.T., French R., Jones R.W., Jackson A.O.;
RT   "Identification of barley stripe mosaic virus genes involved in viral RNA
RT   replication and systemic movement.";
RL   EMBO J. 9:3453-3457(1990).
RN   [3]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH THE SUPPRESSOR OF RNA SILENCING
RP   GAMMA-B.
RX   PubMed=28388677; DOI=10.1371/journal.ppat.1006319;
RA   Zhang K., Zhang Y., Yang M., Liu S., Li Z., Wang X., Han C., Yu J., Li D.;
RT   "The Barley stripe mosaic virus gammab protein promotes chloroplast-
RT   targeted replication by enhancing unwinding of RNA duplexes.";
RL   PLoS Pathog. 13:e1006319-e1006319(2017).
CC   -!- FUNCTION: Probably contains methyltransferase and helicase activities
CC       (PubMed:2209552). Methyltransferase displays a cytoplasmic capping
CC       enzyme activity (Probable). This function is necessary since all viral
CC       RNAs are synthesized in the cytoplasm, and host capping enzymes are
CC       restricted to the nucleus (Probable). Helicase region probably exhibits
CC       NTPase and RNA unwinding activities (Probable).
CC       {ECO:0000269|PubMed:2209552, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Interacts with the suppressor of RNA silencing Gamma-B (via C-
CC       terminus). {ECO:0000269|PubMed:28388677}.
CC   -!- SUBCELLULAR LOCATION: Host chloroplast envelope
CC       {ECO:0000269|PubMed:28388677}. Note=The viral replication sites are
CC       located at the host chloroplast membrane.
CC       {ECO:0000269|PubMed:28388677}.
CC   -!- MISCELLANEOUS: The genome of this virus consists of three linear,
CC       positive, single-stranded RNAs encapsidated in separate virions
CC       designated RNA-alpha, RNA-beta and RNA-gamma. Three proteins (alpha-A,
CC       beta-A and gamma-A) are translated directly from these genomic RNAs and
CC       the remaining proteins encoded on RNA-beta (beta-B, beta-C and beta-D)
CC       and RNA-gamma (gamma-B) are expressed via three subgenomic messenger
CC       RNAs. {ECO:0000305}.
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DR   EMBL; J04342; AAA46336.1; -; Genomic_RNA.
DR   PIR; JA0109; PAVBBS.
DR   RefSeq; NP_604474.1; NC_003469.1.
DR   SMR; P17595; -.
DR   GeneID; 962673; -.
DR   KEGG; vg:962673; -.
DR   Proteomes; UP000001667; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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; IPR027417; P-loop_NTPase.
DR   Pfam; PF01443; Viral_helicase1; 1.
DR   Pfam; PF01660; Vmethyltransf; 1.
DR   PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Hydrolase; Methyltransferase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..1139
FT                   /note="Replication protein alpha-A"
FT                   /id="PRO_0000222492"
FT   DOMAIN          81..305
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          805..969
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          970..1139
FT                   /note="(+)RNA virus helicase C-terminal"
FT   REGION          60..438
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000255"
FT   REGION          611..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          835..1109
FT                   /note="Helicase"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        614..637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         838..845
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1139 AA;  129628 MW;  24B1500FD05362D9 CRC64;
     MASDEIVRNL ISREEVMGNL ISTASSSVRS PLHDVLCSHV RTIVDSVDKK AVSRKHEDVR
     RNISSEELQM LINAYPEYAV SSSACESGTH SMAACFRFLE TEYLLDMVPM KETFVYDIGG
     NWFSHMKFRA DREIHCCCPI LSMRDSERLE TRMMAMQKYM RGSKDKPLRL LSRYQNILRE
     QAARTTAFMA GEVNAGVLDG DVFCENTFQD CVRRVPEGFL KTAIAVHSIY DIKVEEFASA
     LKRKGITQAY GCFLFPPAVL IGQKEGILPS VDGHYLVENG RIKFFFANDP NAGYSHDLKD
     YLKYVEKTYV DIEDGVFAIE LMQMRGDTMF FKITDVTAAM YHMKYRGMKR DETFKCIPLL
     KNSSVVVPLF SWDNRSLKIT SGLLPRTLVE QGAAFIMKNK EKDLNVAVLK NYLSAVNNSY
     IFNGSQVRDG VKIAPDLISK LAVTLYLREK VYRQRENSII SYFEQEMLHD PNLKAMFGDF
     LWFVPNTLSS VWKNMRKSLM EWFGYAEFDL TTFDICDPVL YVEIVDRYKI IQKGRIPLGE
     FFDCHEECEN YELREKEKND LAVKMAQKVT GTVTECEKDL GPLVQPIKEI LVQLVMPNLV
     RALCRPRSPT SPLDLKSIPG STPSHSSSDS EHSMTEEASC TIAGSVPTWE IATRKDLTFQ
     RIDEDMSRRT GMPPRPKVTS SYNMNARAEF LYYQLCSVIC ERAQILSVIE DFRQNLIFSD
     KVAVPLNARF YSFQSLRPGW VFKTPSHSEV GHSYAVHFDF KTIGTDLEES LAFCRMVPIS
     WDKSGKYIAT TPHFPERHGY YVICDNTKLC NNWLIYNKLV DVYALVADRP LRFELIDGVP
     GCGKSTMILN SCDIRREVVV GEGRNATDDL RERFKRKKNL NSKTANHRVR TLDSLLLAEG
     PCVPQADRFH FDEALKVHYG AIMFCADKLG ASEILAQGDR AQLPMICRVE GIELQFQSPD
     YTKTIINPKL RSYRIPGDVA FYLSAKEFYK VKGIPQKVIT SNSVKRSLYA RGETTPERFV
     SLLDVPVRKD THYLTFLQAE KESLMSHLIP KGVKKESIST IHEAQGGTYE NVILVRLQRT
     PNEIYPGGPR SAPYIVVGTS RHTKTFTYCS VTDDKLLLDI ADVGGIAHTP IRTFESHIV