ID A0A436ZUA4_9PEZI Unreviewed; 1119 AA.
AC A0A436ZUA4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=DFL_006954 {ECO:0000313|EMBL:RVD82531.1};
OS Arthrobotrys flagrans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Arthrobotrys.
OX NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD82531.1, ECO:0000313|Proteomes:UP000283090};
RN [1] {ECO:0000313|EMBL:RVD82531.1, ECO:0000313|Proteomes:UP000283090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD82531.1,
RC ECO:0000313|Proteomes:UP000283090};
RA Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT "Intercellular communication is required for trap formation in the
RT nematode-trapping fungus Duddingtonia flagrans.";
RL Submitted (JAN-2019) 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:RVD82531.1}.
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DR EMBL; SAEB01000009; RVD82531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A436ZUA4; -.
DR STRING; 97331.A0A436ZUA4; -.
DR VEuPathDB; FungiDB:DFL_006954; -.
DR Proteomes; UP000283090; 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; 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:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 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};
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:UP000283090}.
FT DOMAIN 481..645
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 670..843
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 67..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 127953 MW; A871508DFABB5F35 CRC64;
MSDLRGWISD NLLKLSGAAD STIIDFVLAT ASSSKSSSAL ADKLSSFIDG DTSSTRDFAE
ELYRRTGKKS NGALVASNGG STAVKKVEKK KYGFVAMEDD DELMSMPPPP VPREKGDRSR
DKDRKKRDSD EKQSRNEKER ERERDRDKER DQDRDRGKDK DRRTRKSRRR DEGEDVWGDV
EVEPEDYPEE EYEMPPSKRP RIEDGDEGEP GIQEEELNEE EKAELQRLRD LEERDEFAER
LKKKDKDRTN KLVEDRSSTK EGREATERRR LADNPAAREA AVSDLRLRSR QSYLQKREIE
QVALLRKRVA EEQQELRENP NLSQREKAEF EKNRKLLEAH EARARIDDHR DGYALPEDYI
TEKGKIDRKR KEEALYKRYV DRDETGHERF VTEHEEWERE QTAKAKAQVN RSEREDDGNY
EYVFDDTQKI NFLMENTQAG TPASKEQRFI EEQLKAAEKK ALSMEETRKS LPIYAFRDDL
LAAVEQYQVL IIVGETGSGK TTQIPQYLHE AGYTKNGQKV GCTQPRRVAA MSVAARVADE
MGVKIGKEVG YSIRFEDQTS DKTVLKYMTD GMLLREFLTE PDLGGYSALM IDEAHERTLH
TDILFGLVKD IARFRPELKL LISSATMDAQ KFAAYFDDAP IFNIPGRRYP VDIHYTSQPE
ANYLHAAITT IFQIHISAPK GDILVFLTGQ DEIEAAQQNL EETARKLGSK IRELIVAPIY
ANLPSELQSK IFEPTPENAR KVVLATNIAE TSITIDGIVY VIDPGFVKEN VYNPKSGMES
LVVTPCSRAS ANQRSGRAGR VGPGKCFRLY TKWAYYNELE ENTTPEIQRT NLNSVVLLLK
SLGINDLIGF DFMDPPPAET LIRALEQLYA LGALNDKGEL TKIGRQMAEF PTDPMLAKAI
LAADKYGCVE EVLSIISMLG EASALFYRPK DKKLYADQAR NRFTNKQGGD HLTLLNIWNQ
WVDTDFSYVW ARENYLQHRS LTRARDVRDQ LSRLCDRVEV TLSSCGSSDV VPIQKAITAG
FFPNAARLQR GGDSYRTVKN AQTVYIHPSS TLFEVNPKWV IYYELVLTSK EFMRNVLPLQ
PEWLVEVAPH YHKKKDLDTL GIDKKMPKQQ AQQQQQQKS
//
