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Database: UniProt
Entry: W9X259_9EURO
LinkDB: W9X259_9EURO
Original site: W9X259_9EURO 
ID   W9X259_9EURO            Unreviewed;       795 AA.
AC   W9X259;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=ATP-dependent RNA helicase DRS1 {ECO:0000256|ARBA:ARBA00044078};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE   AltName: Full=ATP-dependent RNA helicase drs1 {ECO:0000256|ARBA:ARBA00044094};
GN   ORFNames=A1O7_00916 {ECO:0000313|EMBL:EXJ64579.1};
OS   Cladophialophora yegresii CBS 114405.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1182544 {ECO:0000313|EMBL:EXJ64579.1, ECO:0000313|Proteomes:UP000019473};
RN   [1] {ECO:0000313|EMBL:EXJ64579.1, ECO:0000313|Proteomes:UP000019473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114405 {ECO:0000313|EMBL:EXJ64579.1,
RC   ECO:0000313|Proteomes:UP000019473};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora yegresii CBS 114405.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-binding RNA helicase involved in ribosome assembly.
CC       {ECO:0000256|ARBA:ARBA00043881}.
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   -!- SUBUNIT: Associates with pre-ribosomal particles.
CC       {ECO:0000256|ARBA:ARBA00044029}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX27/DRS1
CC       subfamily. {ECO:0000256|ARBA:ARBA00043999}.
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:EXJ64579.1}.
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DR   EMBL; AMGW01000001; EXJ64579.1; -; Genomic_DNA.
DR   RefSeq; XP_007753146.1; XM_007754956.1.
DR   AlphaFoldDB; W9X259; -.
DR   STRING; 1182544.W9X259; -.
DR   GeneID; 19175531; -.
DR   VEuPathDB; FungiDB:A1O7_00916; -.
DR   eggNOG; KOG0338; Eukaryota.
DR   HOGENOM; CLU_003041_3_1_1; -.
DR   OrthoDB; 149428at2759; -.
DR   Proteomes; UP000019473; Unassembled WGS sequence.
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:UniProtKB-EC.
DR   CDD; cd17947; DEADc_DDX27; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   PANTHER; PTHR47959:SF14; DEAD-BOX ATP-DEPENDENT RNA HELICASE 28; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019473}.
FT   DOMAIN          269..297
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          300..474
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          485..685
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          707..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          650..681
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           269..297
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        10..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..80
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..174
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..206
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..764
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..795
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   795 AA;  88157 MW;  918CCE5791EE964E CRC64;
     MAPNKQEDEF VLTLSDREAD LSVSESDIEA IQPQKGIKRK REVKKDAKNK RQKNGPDGEL
     ETASAYSDPN DDDVDEQGIK DDALDPEFEF DIGTNTVLQD IEEFDGWGQD ITTAKNRDRR
     GVDIDAIIAR RAGKKSKPSK HEEEVEAADP EAEDAMSNGD DEDDDVELPD LGDDELLAAD
     VFGAEAESEG EEQVSDADEE QPPHEEADDQ VSDTDSVASP TAHPDDIASD YSDAASQTSV
     EEDAEEAAKR AAFFAPEEKD TQPNVKSMSS FQQFSLSRPI LRGLAGLSFT TPTPIQVRAI
     PIALQGLDVV GSAVTGSGKT AAFLLPILER LLYRPRKVPT TRVAILMPTR ELAVQCYNVA
     TALARYTDIT FAQVVGGFSL REQETILKKR PDVVIATPGR FIDHMRNSAS FAVENIEILV
     LDEADRMLET GFEDELNEIL KTIPQGRQTM LFSATMTDSV DKLVRVGMNR PVRLSVDAKK
     STTAGLTQEF VRLRQGREDR RLATLCVLCQ KFFAERTIVF FRQKKEAHRV RIVFGLLGLR
     AGELHGSMTQ EQRISAVNAF RDGKTTHLLA TDLASRGLDI KNVATVVNYE APQTHEIYLH
     RVGRTARAGR SGRACTIAAE PDRKIVKAAV KSARQQGAKV VSRVVDGKDV DDMALHLDDL
     ESEIEEILKE EKEEKQLATT EAELQRGVNL IKHQDEIMAR PKRTWFETEK EKRDAQSKGR
     LELNGPNGVV KIKGEKKKLS NKDKKRLDDA RERKEGKMWR KGKGSEQAAR MAIKARKKSS
     KAGKAKAKGK AKGKR
//
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