ID A0A0D2DBW5_9EURO Unreviewed; 961 AA.
AC A0A0D2DBW5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PV07_00082 {ECO:0000313|EMBL:KIW33214.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW33214.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW33214.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW33214.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits and is required for the normal formation of 25S and
CC 5.8S rRNAs. {ECO:0000256|ARBA:ARBA00003706}.
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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC subfamily. {ECO:0000256|ARBA:ARBA00010379}.
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DR EMBL; KN847040; KIW33214.1; -; Genomic_DNA.
DR RefSeq; XP_016253430.1; XM_016386502.1.
DR AlphaFoldDB; A0A0D2DBW5; -.
DR STRING; 569365.A0A0D2DBW5; -.
DR GeneID; 27339276; -.
DR VEuPathDB; FungiDB:PV07_00082; -.
DR HOGENOM; CLU_003041_5_2_1; -.
DR OrthoDB; 5475716at2759; -.
DR Proteomes; UP000054466; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17959; DEADc_DDX54; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR012541; DBP10_C.
DR InterPro; IPR033517; DDX54/DBP10_DEAD-box_helicase.
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:SF8; RNA HELICASE; 1.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 109..137
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 140..312
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 371..532
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 359..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 109..137
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 719..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 961 AA; 106102 MW; 31314FBDE5EBB6BB CRC64;
MTRDGTFSYG DHYILLTSAE QGSNSTMPHR AGSPARSENE FDIGSALFGH DSEVTHDTLH
EQNGALQRND LDVMADDSEV DEEAIIAAQQ AASNRKGANL KGRTVKKGGG FQAMGLNANL
LKAITRKGFS VPTPIQRKTI PLLLGDKDVV GMARTGSGKT AAFVIPMIEK LKVHSTKVGA
RALILAPSRE LALQTLQVVK ELGRGTDLRS ILLVGGDSLE DQFAAMSNNP DIIIATPGRF
LHLKVEMNLD LLSIKYVVFD EADRLFEMGF AAQLTEILHA LPASRQTLLF SATLPKSLVE
FARAGLQEPM LVRLDADSKI SPDLQSAFFT LKSSEKEGAL LHILQDIIKM PTGSQLITST
TTSTIADKPN NKKRKRQETE ENSSNASGTN PFSTIVFTAT KHHVEYVASL LRLAGYAVSY
VYGSLDQTAR KSQVQAFRTG QTNILVVTDV AARGIDIPVL ANVINYDFPS QPKIFVHRVG
RTARAGQRGW SYSLVRDADA PYLLDLQLFL ARKLVLGRAA SNELVNFAQD VVVGSFRREA
IQTSCEWVTK SLESDSDLSA LRNVALKGEK LYQRTRNSAS SESAKRSKQL VSSSAWTELH
SLFNDETDDM EVERERMLAR VGGFRPQESI FEIGARRGGR KNNEDAVDAI RKIRSGFESR
KQKSVDASQA LREAGNDDAV DPTNSPYDPA EDEAHPGFID GSNDVDRMSE ASLSDLEITF
SQPYSKKSQT PKSPKPGLRT TEGDFRDPEN FMSYHPTAHD LTSDRAYGVH SGSNTNASAS
FVESARTATM DLGADESSKT FGENRAIMRW DKRHKKYVRR DNDEDGSKTG KRLVKGESGA
KIAASFRSGR FDRWMKANRV NRLGRVGEEE KSSNANADGM GVGGGRGRKF QHKSQRTPKQ
PDKLRGDYEK QMKKVKGAKE REEQAGGKAK GELRNVDRMV KERRLKEKRR EKNARPRRRK
A
//
