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Database: UniProt
Entry: A0A178EZ12_TRIRU
LinkDB: A0A178EZ12_TRIRU
Original site: A0A178EZ12_TRIRU 
ID   A0A178EZ12_TRIRU        Unreviewed;      1988 AA.
AC   A0A178EZ12;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=ATP-dependent RNA helicase DHX8 {ECO:0000313|EMBL:OAL64613.1};
GN   ORFNames=A7C99_4047 {ECO:0000313|EMBL:OAL64613.1};
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551 {ECO:0000313|EMBL:OAL64613.1, ECO:0000313|Proteomes:UP000243015};
RN   [1] {ECO:0000313|EMBL:OAL64613.1, ECO:0000313|Proteomes:UP000243015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCC(F)T1i {ECO:0000313|Proteomes:UP000243015};
RA   Zhan P., Tao Y., Liu W.;
RT   "Genome sequencing of Trichophyton rubrum CMCC(F)T1i isolated from hair.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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:OAL64613.1}.
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DR   EMBL; LHPM01000015; OAL64613.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:TERG_04997; -.
DR   VEuPathDB; FungiDB:TERG_04998; -.
DR   Proteomes; UP000243015; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd17913; DEXQc_Suv3; 1.
DR   CDD; cd21691; GH2-like_DHX8; 1.
DR   CDD; cd05684; S1_DHX8_helicase; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   CDD; cd18805; SF2_C_suv3; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 1.20.272.40; -; 1.
DR   Gene3D; 1.20.58.1080; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003029; S1_domain.
DR   InterPro; IPR022192; SUV3_C.
DR   InterPro; IPR044774; Suv3_DEXQc.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 2.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF00575; S1; 1.
DR   Pfam; PF12513; SUV3_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 2.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 2.
DR   PROSITE; PS50126; S1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000313|EMBL:OAL64613.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243015}.
FT   DOMAIN          360..517
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1019..1090
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          1333..1496
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1514..1694
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          852..873
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          924..1009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1968..1988
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1230..1257
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        939..953
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        964..1009
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1988 AA;  223624 MW;  9178FBF96F9E5AEE CRC64;
     MQPWQRPARG LCLRCALRAP TTPTGRSFSG SVQHNRARIT ALNRPLEQLS FDWVSGRKGK
     NDQKEGRDFK PWKAQGPRTK IRKVGRVSFD ERFQSALLES SDIVRKELEQ TKLELAHWDK
     FFASIVHACK SSLIDDGDEA HFGQRFTLRR TFGKMGREGI VDYLRRQYRN HKLDTAFSST
     ATKSDSLADF RYPAEWYPVA RSMQRKIHLH VGPTNSGKTY HALQRLEKAK SGFYGGPLRL
     LAHEIYSRLN KKGISCALIT GDEVRVPENG PVKVYSNTVE MVPIGQEVEV GVIDEIQMIA
     DPHRGWAWTR AVLGCQAQEL HLCGEERAVP LIQRLVSLMG DTLEIHNYKR LNPLKTMASS
     LKGDIRRLEK GDCIVAFSRV GIHSLKQEIE KVTGRRAAIV YGSLPAEIRA QQADLFNDPN
     NDYDFLVASD AIGMGLNLSC KRIIFESVIK RLPTGIQRLS ISEIKQIGGR AGRYRSAAQS
     SSSRIANEKE NVGLVTCLDE ADLPYIRAAM MAEAEPLDAA GILPLDSVID NYSNMFPPDT
     PFGYIYQRLE RVSRTDPPFF MCKIQDTEAT FGLLDNIQGL NVIDKMVFMS APLRATDPVM
     ARVIKAFAEC VGQQKSGRLL DIPELDLEIL DRPVSGDDKE YLRSLEALHR SLILYLWLGY
     RFGGVFTDRT LATHAKEMAE VKMDRTLTEF SANSKLRKQA LRKKRIKGAK DKFLDSPEPT
     GVMDTIPDIP ELDTTLSDED EIEFEDPNSA LESTHIRAPV PFAQHTSPST PITSMDDLES
     LELLSLISRV TTELQNHLGV NEKTLAEFVI DQHLKCKSLD EFKSSLKAVG AEFPQSLVES
     VDRLVLTMHP KYKSKRTKPD EQEKKHIGQD GVDDIEKKAR VFKGLAVPDD KAPHWEEHEP
     EPERNTNAEA MDDTFAMLEG LAGKAKAEQN GYSNSRKRSR SPEINDYDRN RPRRGRYKSR
     SRSRSGSPNR DRYGNRHSHR IRKYPDEPRE RGRSGRNYNY DDDLKRPPAS ELDDRPILFK
     IYDGRVTGIK DFGVFVNLQG VRGRVDGLVH VSAMQEGARV NHPSDLVSRG QQVKVKIVSI
     QDSRIGLSMK EVDQVSGHDL APQRRIASGA NMERLDGTGA DDRYGNLGSS VPVIERDSDA
     KRSKKRLNSP ERWEIKQLIA SGAVSAADYP DLDEEYHATL RGEGDFEEEE DIDIEVREEE
     PPFLAGQTKQ SLELSPIRVV RAPDGSLNRA AMAGANLAKE RREIRQQEAQ DKAAEKAAQV
     DLNAQWQDPM VAPEQRKFAS ELRTATTEKS SESLPEWKRA AQNKDVSYGK RTNLSMKEQR
     ESLPVFKFRK QLLEAVRENQ LLIVVGDTGS GKTTQVTQYL AEGGFTNNGM IGCTQPRRVA
     AVSVAKRVSE EVGCQLGQEV GYTIRFEDCS SPNTKIKYMT DGILQREILL DPDLKKYSAI
     MLDEAHERTI ATDILFGLLK KTIKRRPDLK LIVTSATLDA DKFSEYFNGC PIFSIPGRTY
     PVEIMYSKEP ESDYLDAALV TVMQIHLTEP PGDILLFLTG KEEIDTSAEI LYERMKALGP
     NVPELVILPV YSALPSEMQS RIFEPAPPGG RKVVIATNIA ETSITIDQIY YVIDPGFVKQ
     NAYDPKLGMD SLVITPISQA QAKQRAGRAG RTGPGKCFRL YTEAAYQSEM LPTSIPDIQR
     QNLTQTILML KAMGINDLLH FDFMDPPPTN TMLTALEELY ALSALDDEGL LTRLGRKMAD
     FPMDPGLAKV LIASVDMGCS DEVLTIVAML SVAQGIFYRP KEKQQQADQK KAKFHDPHGD
     HLTLLNVYNA WKQSRFSTPW CFENFIQARQ IRRAQDVRQQ LVTIMDRYHH KIVSCGRDTT
     RVRQAFCSGF FRNAARKDPQ EGYKTLIEGT PVYMHPSSAL FGKAAEHVIF DTLVLTTKEY
     MQCATTIEPK WLVEAAPTFY KQASTNKLSK RKRAERIQPL HNKFAGEDDW RLSAQRRQGR
     GGGGGTWG
//
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