ID A0A166SNA5_9PEZI Unreviewed; 772 AA.
AC A0A166SNA5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=CT0861_01955 {ECO:0000313|EMBL:KZL70963.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL70963.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL70963.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL70963.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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 DDX15/PRP43 sub-subfamily. {ECO:0000256|ARBA:ARBA00024333}.
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:KZL70963.1}.
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DR EMBL; LFIV01000081; KZL70963.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166SNA5; -.
DR STRING; 708197.A0A166SNA5; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000076552; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR CDD; cd17973; DEXHc_DHX15; 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; IPR044756; DHX15_DEXHc.
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:SF109; ATP-DEPENDENT RNA HELICASE DHX15 HOMOLOG; 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; 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:KZL70963.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT DOMAIN 115..280
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 305..487
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 772 AA; 87436 MW; B54DA4422CB35ECE CRC64;
MADADPKGSK RSSADRDGSS RKKVKKEESD SEEPKYNPYL AHMKEENGFK SEEGVIDSSS
PFAGFKKRAT TAKQAEKVED LDTNAFTGRP HSQKYFQILQ SRRDLPVQKQ RQEFLDKYHS
TQILVFVGET GSGKTTQIPQ YVVYDELPQL NRKMVACTQP RRVAAMSVAQ RVSDEMDVEL
GEEVGYSIRF EDRTGPNTIL KYMTDGMLLR EAIHDHEMSR YSCIILDEAH ERTLATDILM
ALLKQIAARR PDLKIIVMSA TLDAQKFQRY FNDAPLLAVP GRTHPVEIFY TPEPERDYVE
AAIRTVLQIH ASEGEGDVLL FLTGEEEIED ACRKISLEAD EMTREIDAGP LAVYPLYGTL
PPHQQQKIFD KPPAPYKKGG RPGRKVIVAT NIAETSLTID GIVYVVDPGF SKQKIYNPRI
RVESLLVSPI SKASAQQRAG RAGRTKPGKC FRLYTENAFK KELIEQTHPE ILRSNLANTV
LELKKLGVED LVHFDLMDPP APETMMRALE ELNYLACLDD DGELTTLGSL ASEFPLDPAL
AVMLISSPEF YCSNEILSIT SLLSVPQIWV RPAAQRKRAD EMKAQFSHPE GDHLTLLNAY
HAFKGTASQP GVDPKKWCHE HFLSFRHLSS ADNVRAQLKR IMETHGLELI STPFEDKNYY
TNIRRALLSG FFMQVAMKES SGKVYRTIKD DQAVMMHPST VLKTDYEWVL YNEFVLTSKQ
YIRTCTGIRP EWLLEIAPVY YDLSSFEKGD VKTALTRAAE KKRRKEAMKN GR
//
