ID A0A1B6QEE4_SORBI Unreviewed; 1285 AA.
AC A0A1B6QEE4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=SORBI_3002G313400 {ECO:0000313|EMBL:KXG36287.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG36287.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:KXG36287.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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 Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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; CM000761; KXG36287.1; -; Genomic_DNA.
DR STRING; 4558.A0A1B6QEE4; -.
DR EnsemblPlants; KXG36287; KXG36287; SORBI_3002G313400.
DR Gramene; KXG36287; KXG36287; SORBI_3002G313400.
DR eggNOG; KOG0924; Eukaryota.
DR InParanoid; A0A1B6QEE4; -.
DR OMA; VDVMFHR; -.
DR OrthoDB; 5488182at2759; -.
DR Proteomes; UP000000768; Chromosome 2.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768}.
FT DOMAIN 598..761
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 783..963
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1285 AA; 144438 MW; 34084DEDD059959A CRC64;
MEGNGNAEVD LDATMTTLGP EDDTSQGLIL TNKQRVMYRP PAGKSVLGLD TLADKKRAAG
GGSVFKPPPP NVAVAADSID EDEKPGPTEN DAPSLSTAIR SNSSRRYRGS GSDDKTSLNE
PTVTDDNQRA PTPSHRDETH RQETHISGSS QGSRPHGTPR GSDYYDDRGS RDKYGDRERS
ASIGYSSSGR RRYHDDRESH TRRDERGRST SIEYTNKRSR HEHSSRSSRT PARSDWDDGR
WEWEDTPRRD YRDNRPGSRR QHPTRSPMLA AASPDARLVS PWLGGSTPRS AASPWDNVSP
SPAPIRASGS SKGSSYSHSS GRSHQLSFSS TTSSNIFDAD RSPSNPDRNY EITEEMMQEM
DYNADRAWYD CEEHTTMFDG DNSMYLGDDN SYKKKEAEMP KKLTRRDGSL MTLAQSKKLS
QMTADNAQWE DRQLLRSGAV KGTEVQTEFD DEEERKVILL VHDTKPPFLD GRVVFTKQAE
PVMPLKDPTS DMAIIARKGS SLVREIREKQ SMNKSRQRFW ELAGSKLGNI LGVEKTAEQV
DADTAVVGDQ GEINFKEEAK FSQHLKDKAE AVSDFAKSKS LSQQRQYLPI FTVRDDLLQV
VRENQVVVVV GETGSGKTTQ LTQYLHEDGY TTTGVVGCTQ PRRVAAMSVA KRVSEEMETD
LGDKVGYAIR FEDVTGPNTI IKYMTDGVLL RETLKDADLD KYRVIVMDEA HERSLNTDVL
FGILKKVVAR RRDFKLIVTS ATLNADKFSK FFGGVPVFHI PGRTFPVNIM FSKTPCEDYV
EAAVKQAMTI HITSGPGDIL IFMTGQEEIE ATCYALAERM EQLISSSTKT VPKLEILPIY
SQLPADLQAK IFQKAEEGAR KCIVATNIAE TSLTVDGIFY VIDTGYGKMK VYNPRMGMDA
LQVFPVSRAA ADQRAGRAGR TGPGTCYRLF TESAYQNEML PNPVPEIQRT NLGNVVLLLK
SLRVENLLDF DFMDPPPQEN ILNSMYQLWV LGALNNVGGL TEIGWKMVEF PLDPTLAKML
LMGEQLECLD EVLTIVSMLS VPSVFFRPKD RAEESDAARE KFFVPESDHL TLLNVYLQWK
SNQYRGDWCN DHFLHVKGLR KAREVRSQLL DILKTLKIPL TSCHMEWDVV RKAICSAYFH
NSARLKGVGE YVNCRNGMPC HLHPSSALYG LGYTPDYVVY HELVLTTKEY MQCVTAVDPQ
WLAEMGPMFF SVKETDTSLL DHKKRQKEEK TAMEEEMEKL RQEQAEAARM EKEKEREKRA
KQQQQVAMPG LKKGATYLRP RKMGL
//
