ID A0A2C5XL49_9HYPO Unreviewed; 778 AA.
AC A0A2C5XL49;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=CDD81_221 {ECO:0000313|EMBL:PHH66158.1};
OS Ophiocordyceps australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH66158.1, ECO:0000313|Proteomes:UP000226192};
RN [1] {ECO:0000313|EMBL:PHH66158.1, ECO:0000313|Proteomes:UP000226192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map64 {ECO:0000313|EMBL:PHH66158.1,
RC ECO:0000313|Proteomes:UP000226192};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) 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:PHH66158.1}.
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DR EMBL; NJET01000010; PHH66158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5XL49; -.
DR STRING; 1399860.A0A2C5XL49; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000226192; 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:InterPro.
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:UP000226192}.
FT DOMAIN 252..280
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 283..457
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 487..636
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 633..673
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 252..280
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 40..54
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..179
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 86313 MW; E8F40A81C910CCC5 CRC64;
MASHKRKVEA QDFVYTLSDN DDDDGALVET DVPRQPPKKK SKTTSSKKSK RTKKGPITKQ
EDDGEAENDS ENMWGPKEED DGAMNSDFEF IVDAGELGGE EDFEGWGFDN AKKGITVEKK
NIDIDDIIRR RREKSDKVED EIGQDEEDLD NVQVSMDDDD DQVLADDAFG MGAESEDEPS
QEEVSNKESD SPAEDDEPAS DNDSVATPVS HPEDDMSDDG EDEREDADEQ AKRDAFFAPE
QREEKDAKVD VSSFMALSLS RPILRGLAAV GFSKPTPIQS KTVPIALMGK DVVGGAVTGS
GKTAAFMIPI LERLLYRPNK LPTTRVVVLT PTRELAMQCH AVAIKLASHT DIKFSLAVGG
LSLKVQESEL RRRPDVVIAT PGRFIDHLRN SASFNVDTVE ILVLDEADRM LEDGFADELN
EILTTIPKSR QTMLFSATMT STVDRLIRLG MDKPVRIMVD SKKKTVGTLV QEFVRLRPGR
EDKRMGYLAC LCKSLYTERV IIFFRQKKEA HRARIIFGLL NLSCAELHGS MNQTQRIESV
EAFRDGKVSF LLATDLASRG LDIKGIDTVI NYEAPQSLEI YVHRVGRTAR AGRKGTAVTL
AAEPDRKVVK AAVRAAKSQG AKIVSRAVPA TEVDQFQAKI DGFEDEIEGI IKEEKEEKQM
AAAEMQVKKG ENMILHEREI KARPKRTWFE TEHEKSKAKE AGRSELNGVR EAMKKKTGGK
LSNKDKKRLD VKALRSEGTL WRKGKAPDTA EKTKKKPARG GSRGAAKASR GRSRGGKR
//
