ID   A0A2V1CSC9_9HELO        Unreviewed;       903 AA.
AC   A0A2V1CSC9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=DL98DRAFT_509335 {ECO:0000313|EMBL:PVH88629.1};
OS   Cadophora sp. DSE1049.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiales incertae sedis; Cadophora.
OX   NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH88629.1, ECO:0000313|Proteomes:UP000244409};
RN   [1] {ECO:0000313|EMBL:PVH88629.1, ECO:0000313|Proteomes:UP000244409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSE1049 {ECO:0000313|EMBL:PVH88629.1,
RC   ECO:0000313|Proteomes:UP000244409};
RX   PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA   Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA   Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA   Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT   "Comparative genomics provides insights into the lifestyle and reveals
RT   functional heterogeneity of dark septate endophytic fungi.";
RL   Sci. Rep. 8:6321-6321(2018).
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};
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DR   EMBL; KZ804110; PVH88629.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1CSC9; -.
DR   STRING; 1485229.A0A2V1CSC9; -.
DR   Proteomes; UP000244409; 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   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; 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:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PVH88629.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244409}.
FT   DOMAIN          152..342
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          467..641
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   903 AA;  99610 MW;  8300FBB5A3294A19 CRC64;
     MPEKVHVKFG DSAASQQEQD TNAPVHTQKL KQSSLKNGVK RMRDGSLKAI SRPGPKGGPE
     QAKSDETHKT VTGSTQAAHT PVSGTVRQNG GSEPFARSAF TKSLSNGIRS SKHKRNSSGT
     EHEDRQKLHR IAQQHENTRK LLPIWPKKAD IRCALRNNDV LLINGETGSG KSTQVPQFLY
     TESWCRRQMV QIQKDGGKTV EESVGGIIAI TQPRRVAATT LARRVASEMG SPFSGEVGEV
     GYAVRFDSFL PKGTKIKFVT EGMLLQEMLH DPYLRKYSAV IVDEIHERSV DVDLIAGFLR
     NLVHGDKKGR GGVPLKVIIM SATLDLGGIE AFFARPTSAS RYTPGKNHGR ILAPNLLEDE
     VDGDVELEQQ KLFHGSSSWG GLSDSDNEIS NGDKVMPASA EDIALARNAN RSTQSHISDL
     VPKSSAQLSE PEHNGVAVEY VRGRQYEVEI MYEVKPTQDY LHTILQTVLQ LHVTEPLPGD
     ILVFLTGQDE IESLRSALSD HAEKIVKTLP RMKIMPLYGA LPAAAQQEAF EKVKEKFTRK
     IVLATNIAET SITVSGVRFV VDCGKSKVKQ YRPRLGMESL LAKPISRVSA IQRAGRAGRE
     AKGKCFRIYT EEDYLKFDQD EFPEILRSDV LEAVLKMKSR GVGDVSDFPL MDSPDIMAIQ
     NALKQLHMMG AVDDVGNITT VGKKMATFPL PATYGRVLIA AAEPRSDMLL EVIDVISCLT
     TDSEIFNQPK SEDDQENIIE ARKDLLSPDG DIVTLLAVIG KYASVAHADR LDWCRQRLIA
     PRAMKMALQI RQQLRQICRQ QKLLSAAPPT DSEPYEPLSP ERVVLLLKTF LTAFAAKTAL
     LAPDGSYVMA VGRNPIAVHP SSVLFGQKKS EAIMFLEHVF TTKNYAKKVS PVQANWIEEA
     FTL
//