ID   F2PSH5_TRIEC            Unreviewed;       763 AA.
AC   F2PSH5;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=TEQG_03927 {ECO:0000313|EMBL:EGE04754.1};
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN   [1] {ECO:0000313|Proteomes:UP000009169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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}.
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DR   EMBL; DS995735; EGE04754.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2PSH5; -.
DR   VEuPathDB; FungiDB:TEQG_03927; -.
DR   eggNOG; KOG0925; Eukaryota.
DR   HOGENOM; CLU_001832_5_11_1; -.
DR   Proteomes; UP000009169; 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:EGE04754.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          102..267
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          292..474
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   763 AA;  86548 MW;  208AE56A712C70F0 CRC64;
     MAARSDSENA SRAKRLKTTA EWDPRSNPYL AHMYENEDAS SGINDESPLA AFRRHETTAE
     MANEVESGSL NPFTGKPFSS RYVSILKTRR DLPVHQQRNE FLKLYQESQI LVFVGETGSG
     KTTQIPQFVL YDDLPQFRGK LVACTQPRRV AAMSVAERVA NEMDVKLGEE VGYSIRFEDK
     TSSKTILKYM TDGMLLREAM HDHDLKRYST IILDEAHERT MATDVLMGLL KEVVLRRPDM
     KLIIMSATLD AQKFQRYFSD APLLAVPGRT HPVEIFYTPE PEQDYVEAAI RTVLQIHATE
     PEGDILLFLT GEEEIEDAVR KISLEVDEMI REVDAGPMKV YPLYGSLPPA MQQRIFEPPP
     PPRKPKGRPG RKCIISTNIA ETSLTIDGIV YVVDPGFSKQ KVYNPRIRVE SLLVSPISKA
     SAQQRAGRAG RTRPGKCFRL YTEGAFKKEL IEQTYPEILR SNLSSTVLDL KKLGIDDLVH
     FDLMDPPAPE TLMRALEELN YLACLDDDGN LTALGRLASE FPLDPALAVM LISSPEFYCS
     NEILSITSLL SVPQIFVRPV AQRKRADEMK ALFSHPDGDH LTLLNAYHAF KGPEAQANPR
     QWCHDHFLSL RSLQSADNVR LQLQRIMERE EIELVSTPFE DKKYYENIRR ALVAGFFMQV
     AKKESQGKNL YRTVKDNNEP VLLHPSTVLG YEAEWVLYNE FVLTTKSFIR TVTAVKGEWL
     LDISPAYYDI SSFPKGEIRS ALIRAGERLS RKEKMRSDAS KKR
//