ID A0A2W1E466_9PLEO Unreviewed; 841 AA.
AC A0A2W1E466;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PtrM4_07453 {ECO:0000313|EMBL:PWO12113.1}, PtrM4_092790
GN {ECO:0000313|EMBL:KAF7571779.1};
OS Pyrenophora tritici-repentis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=45151 {ECO:0000313|EMBL:KAF7571779.1, ECO:0000313|Proteomes:UP000245464};
RN [1] {ECO:0000313|EMBL:KAF7571779.1, ECO:0000313|Proteomes:UP000245464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M4 {ECO:0000313|EMBL:KAF7571779.1,
RC ECO:0000313|Proteomes:UP000245464};
RX PubMed=29685100; DOI=10.1186/s12864-018-4680-3;
RA Moolhuijzen P., See P.T., Hane J.K., Shi G., Liu Z., Oliver R.P.,
RA Moffat C.S.;
RT "Comparative genomics of the wheat fungal pathogen Pyrenophora tritici-
RT repentis reveals chromosomal variations and genome plasticity.";
RL BMC Genomics 19:279-279(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 {ECO:0000256|ARBA:ARBA00008792}.
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:KAF7571779.1}.
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DR EMBL; NQIK02000004; KAF7571779.1; -; Genomic_DNA.
DR EMBL; NQIK01000005; PWO12113.1; -; Genomic_DNA.
DR Proteomes; UP000245464; 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; cd17982; DEXHc_DHX37; 1.
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; 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:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 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 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:KAF7571779.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 13..190
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 213..459
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 841 AA; 93024 MW; 34305F370600E7C7 CRC64;
MQLPIVAEEQ KIMEAIHNHD VVVVWGATGS GKTTQVPQFL LESGYGAADG PTPGMIGVTQ
PRRVAAVSMA KRVGDELGDQ SSKVAYQIRF DTSTNAKTAV KFMTDGVLLR EITQDFVLTK
YSAIVIDEAH ERSVNTDILI GMLSRIVDLR AQMAREDPKN KPLKLVIMSA TLRISDFTEN
KRLFRGEPPP LIKAEGRQYT VVNHFARRTQ RDYVDEMYRK VCRGHRKLPK GGMLIFLTGQ
NEISQLAKQL KQAFPSTQGK DIKAGKVVVS PTETPLEVED IELGAPSQNK TYEDDDGSDS
EGSVIMGLDD EDDKEFEIED EKPEETVMNV HVLPLYSQLP TNQQLRVFDP PPDGSRLIVL
ATNVAETSLT IPGIRYVFDC GRAKEKKYDL VTGVQSFEVG WISKASANQR AGRAGRTGPG
HCYRLYSSAV FERDFEEYAA PEISRTPLEG VVLQLKSMGA PVVSFPFPTP PDRESLQKAE
NLLSYLGALS VDGKVTKLGH ELSLYPLNPR FARMVAMGVA QNLTAETIAL VAALSVPELI
IPENKLGLRE PVKDPEAIRT EQDNVEAEER SRLRKAYNAA QAKMSINAKQ SDCIKLSNAI
CAYAYEPNSQ GFCEDMFLNA KAMNEASQLR HQLTNIVRAH RPTAIGGYQA KLPAPSERSI
NLLTQICAAG FIDQIAMRAD LAPIPPELPR KPKTAIDVPY VTLFSSQSER SDDPHAQYVY
LHPSSILART PPAKMPGYII YSHLQRAATS TINGSRTPKT RMHPLTPVTR PQIINIALNT
PLLQASKPKG KIVELSKDKR ECEVEMSLMG EKGSQGWGLG IRKVVQRKES DGRWVIERIL
G
//
