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Database: UniProt
Entry: A0A367L5J6_9HYPO
LinkDB: A0A367L5J6_9HYPO
Original site: A0A367L5J6_9HYPO 
ID   A0A367L5J6_9HYPO        Unreviewed;      1154 AA.
AC   A0A367L5J6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=L249_3978 {ECO:0000313|EMBL:RCI09694.1};
OS   Ophiocordyceps polyrhachis-furcata BCC 54312.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI09694.1, ECO:0000313|Proteomes:UP000253664};
RN   [1] {ECO:0000313|EMBL:RCI09694.1, ECO:0000313|Proteomes:UP000253664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI09694.1,
RC   ECO:0000313|Proteomes:UP000253664};
RX   PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA   Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA   Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT   "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT   pathogenicity and host specificity in insect fungi.";
RL   BMC Genomics 16:881-881(2015).
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   -!- 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:RCI09694.1}.
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DR   EMBL; LKCN02000014; RCI09694.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367L5J6; -.
DR   STRING; 1330021.A0A367L5J6; -.
DR   Proteomes; UP000253664; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd05684; S1_DHX8_helicase; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; 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; IPR049621; S1_DHX8_helicase.
DR   InterPro; IPR003029; S1_domain.
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; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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.
DR   PROSITE; PS50126; S1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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   Reference proteome {ECO:0000313|Proteomes:UP000253664}.
FT   DOMAIN          190..261
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          499..663
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          688..861
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          77..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1154 AA;  129156 MW;  24CA17B817EE5248 CRC64;
     MDDVSNLELL SLVSKVTSEL QNHAGTSDKT LAEFLIFQRV KSSSLEDFRK WLDTVKNPFP
     ESFVNSLDRL VLTLHPKFKG NAKPSDGDEH RPSRTLEDKE KIFSGLALPD EKNGGGGGGD
     AIDDTLAMLE GLESKTKTGP PSKKRRRSPE DDPTDRRNGH RGSRKARRHR SDARIDRSPE
     PEVDETPQMH KIYKGHVTGI KDFGAFVSLH HVRGKVNGLV HVSRLSAGQR VSHPSDLLSK
     GQQVFVKVFS IEGSRIGLSM KDVEQATGID LEPQSRFSTG ANMEALGGGK RRGFGENVPA
     MPRDGVGPPT RQKKRMTSPE RWEIRQLIAS GVAKASDFPD LEEDYNATLR GDGELELEED
     VDIEVRDEEP PFLAGQTKQS LELSPIRVVK APDGSMNRAA MAGSVIAKER KELKRQEADT
     KEEPKENLSS QWLDPMADPD KRKFASDMRT ARMNPKPEEV PEWKKAVIPR GQSLGKRTNL
     SIKEQRRQLP VYAFRSQLIQ AVKENQILIV VGETGSGKTT QLTQYLAEAG FAGKGGIIGC
     TQPRRVAAMS VAKRVAEEVG CKLGDAVGYT IRFEDCTSPA TKIKYMTDGM LQREILMDPD
     MRRYSVIMLD EAHERTISTD VLFALLKKAL KRRPDLKVIV TSATLDADKF SAYFNECPIF
     TIPGRTFPVE ILYSREPESD YLDVALLTVM QIHLTEPKGD ILLFLTGQEE IDTACETLFD
     RKKALGPSVP DLIILPVYSQ LPTEMQTRIF EPAPPGSRKV VIATNIAETS ITIDEIYYVV
     DPGFVKQNAY DPKLGMDSLV VTPISQAQAN QRAGRAGRTG PGKCFRLYTE AAYQSEMLPT
     TIPEIQRQNL AHTILMLKAM GINDLLHFDF MDPPPVNSML TALEELYALS ALDDEGLLTR
     LGRKMADFPM EPSLAKVLIA AVDRNCSDEM LSLVAMLNVP TIFYRPKDKQ QQADQKKAKF
     HDPHGDHLTL LNVYNAWKRS GFSNPWCHEN FIQARSMRRA KDVRDQLLKI MDRYRHPVVS
     CGRDTQKLRR ALCSGFFRNA ARKDPQEGYK TLIEGTPVYL HPSSALFGKH AEWVVYHTLV
     LTTKEYMHCT TSIEPKWLVE AAPTFFKVAP SDRMSKRKQA ERIQPLYNRF AGENDWRLSA
     QRRGGRGGGG STWG
//
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