ID E3RCX9_PYRTT Unreviewed; 814 AA.
AC E3RCX9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PTT_01261 {ECO:0000313|EMBL:EFQ96421.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ96421.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ96421.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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 ---------------------------------------------------------------------------
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; GL531946; EFQ96421.1; -; Genomic_DNA.
DR RefSeq; XP_003295484.1; XM_003295436.1.
DR AlphaFoldDB; E3RCX9; -.
DR STRING; 861557.E3RCX9; -.
DR EnsemblFungi; EFQ96421; EFQ96421; PTT_01261.
DR KEGG; pte:PTT_01261; -.
DR eggNOG; KOG0922; Eukaryota.
DR HOGENOM; CLU_001832_5_11_1; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR CDD; cd17917; DEXHc_RHA-like; 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; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT DOMAIN 157..331
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 382..555
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 814 AA; 90814 MW; 8B8A895BC21ADA23 CRC64;
MSKEKSSVPK VEQTDGKIAE LKKGKKRKRA QPANDGWSGK KGAGQLTKFD NSDDETSKPV
PERETQIEKP KEPENVSEPS AERPEKSHKR KKSEVAPEST KPNLKPDQKV KPRSKQPEKP
RSSQQNVMVP PHLLKKRDEL RLVRKTLPIW PQADAIRAAL QRNNVLVLTG ETGSGKSTQV
PQFLVNESWC TGCIAITQPR RVAAISLARR VADEMGSLIG DKGPAAKVGY SVRFDNAAGK
HTKVKFLTEG MLLQEMLRDP TMSQYSAVVV DEVHERSVNV DLILGFLRNL LSDKENLKTR
KHPLKVVVMS ATADVESLVK FFGDSQPTPN PEQATEKPTK KDASKSDTGK ISTCYVKGRQ
YPVKTVYLPQ PTQDWVESAL KLVFQIHYKE PLPGDILVFL TGQDTIEGLE KLINDYAEGM
DEEVPKLIVL PLFAALPQQA QQRIFHPTPY RTRRVILATN IAETSVTVPG VRFVIDCGKS
KIKQFRNRLG LESLLVKPIS KSAAIQRKGR AGREAPGQCY RLYTEEGYKT MEERTIPEIL
RCDLSQAILT MKARGIDDVL SFPFLDRPPR EALEKALLQL LHLQALTETG AISPTGLAIA
KFPLTPTLGR VLVEAAKPER DCLLDIIDVI AALSVENVFL NLVSEERKEE AEEARRDLFR
REGDHITLLV TVQRFAAEEK SLRKAWCEKH FVSHRAMDNV MKIRTQLLEQ CKQQKLLASD
ATASEGAPDE ARSEAILKCL LRGFIGNTAR LMPDASYKTL MGNQTVAIHP SSVLFGKKVE
AVVFTEFVFT GRAWARGVSV VQLGWVEEVV EGIM
//
