ID L8WKH7_THACA Unreviewed; 1274 AA.
AC L8WKH7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=AG1IA_09112 {ECO:0000313|EMBL:ELU36859.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU36859.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU36859.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELU36859.1}.
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DR EMBL; AFRT01003028; ELU36859.1; -; Genomic_DNA.
DR AlphaFoldDB; L8WKH7; -.
DR STRING; 983506.L8WKH7; -.
DR HOGENOM; CLU_001832_6_2_1; -.
DR OMA; VDVMFHR; -.
DR Proteomes; UP000011668; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; 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; PS00690; DEAH_ATP_HELICASE; 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 Helicase {ECO:0000313|EMBL:ELU36859.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000011668}.
FT DOMAIN 579..761
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 786..958
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 140..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1274 AA; 141920 MW; 87B148E3B0B9F3A4 CRC64;
MDRSAGHEKS PDSSEVDPFV HNIAIKLSRA LNIVNPNDLL ATRVINIVKS NSPDGFIKGV
LCDLTAARAF GKFQDSFLQD IHSEISIHLD QQKDGHVPQP IAGIEVHDSE VLEPEAPRAG
GLMRPDGTVC SFSLVAESPH ADHNTQRHTF RAPAKLEPPT PRTSVLGLDR LAREKRINAT
LEAARKKPRL DMPADGDVNQ SVFKVPALPA RLQNQNPRQR AEETPSHGGG LSDAARKRLD
DYRRSRDQQH DGVAAPRESR DDAPRGLGDF QQRANKDRRR GRYDRSQFAE PPTPSASVRV
PNVGWDSTPR VGGGSNEGGW GRVKEQRWDA TPMAKRKGDE DEDEFGGALE TREWEEEQVR
LDRDWYMTGE EGGVVGNEEY NPLAQYEDLD AVKQAEIATK QVNADNDLWE ANRMVTSGIA
SRKQLDLDFA EDDSESTVHV LVHDLKPPFL DGRTVFTKQL EPINPLRDAT SDMAVFAKKG
SALVKEKREQ AERARAAAKM AALGGTALGN IMGVKDEEAE AENEAEKNAA GKKEEDYKGD
SKFASHLKTN AATSSFAKSR TLKEQREYLP AFACREDLMK TIRENQVIVV VGETGSGKTT
QLAQFLYEDG YCKHGIIGCT QPRRVAAMSV AKRVSEEMEV SSSIPPPKMG VGLDNLIGHS
RFDCRIRNPF RRLYLQRNKD QVYMTDGVLL RESLNEGDLD RYSVIILDEA HERSLSTDVL
MGLLRKILSR RRDLKLIVTS ATMNAEKFSD FYGQAPCFTI PGRTFPVEMF HSKSPCEDYV
DSAVKQVLQI HLSLPPGDIL VFMTGQEDIE VTCQVVTERL SQLDDPAPLA VLPIYSQMPA
DLQAKIFEAT SDGRRKVIVA TNIAETSLTV DGILYVVDSG YSKLKVYNPK VGMDALQITP
VSQANANQRT GRAGRTGAGF CYRLYTEMAF RNEMFPNTIP EIQRTNLANT VLLLKSLGVK
NLLEFDFMDP PPQANILNSM YQLWVLGALD NVGDLTPVGR KMSEFPMEPS MAKMLITSVE
YKCSAEIGRK KPMPRARSSQ SMRATTSPFS MCSKCGKPMG GYRDDWCMKH FLHPKLLRKA
REVRQQLEDI MKMQKMEIIS AGTDFDVVRK AICSGYFHQA ARVKGIGEFV NIRSGLPTHL
HPTSALYGLG CKYTPSYVIY HELIMTSKEY MTQVTAVDAY WLAELGSVFY SVKEKNFDER
GARRKADREF SKRAELESEM ARQRDEVAKK QAESEASSNE RKSSARIAVP GTPRHVGIGA
GARVGQTPRR RVGL
//
