ID A0A2B7ZMJ8_9EURO Unreviewed; 943 AA.
AC A0A2B7ZMJ8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=GX50_02574 {ECO:0000313|EMBL:PGH34591.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH34591.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH34591.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH34591.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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}.
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:PGH34591.1}.
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DR EMBL; PDND01000037; PGH34591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7ZMJ8; -.
DR STRING; 73230.A0A2B7ZMJ8; -.
DR VEuPathDB; FungiDB:EMCG_07449; -.
DR OrthoDB; 5475716at2759; -.
DR Proteomes; UP000226031; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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, ECO:0000313|EMBL:PGH34591.1};
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:UP000226031};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 88..116
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 119..291
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 351..507
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 28..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 88..116
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 28..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 943 AA; 104493 MW; E6E728C25FE8DE5A CRC64;
MAMPHRDVSP AASENEFDIS KLLVKGDDDL SDLERPSKKR KPQQTLNLDV MGDDDDGADG
DEAFIAAQQA AANRKASNLK GRTVKKGGGF QSMGLNATLL KAIARKGFSV PTPIQRKTIP
LLLDDQDVVG MARTGSGKTA AFVIPMIEKL KSHSAKFGSR ALILSPSREL ALQTLKVVKE
LGRGTDLKCV LLVGGDSLEE QFEHMAGNPD IMIATPGRFL HLKVEMSLDL SSIRYVVFDE
ADRLFEMGFA AQLTEILHGL PSSRQTLLFS ATLPKSLVEF ARAGLQEPTL IRLDAESKIS
PDLQNAFFTV KSSEKEGALL HLLHEVIKIP TGETETHKRA KEEANNPKKR KRSEFASKPY
KESPTEHSTI IFTATKHHVD YLTSVLRISG FAVSYAYGSL DQTARKIEVQ NFRSGITHIL
VVTDVAARGI DIPILSNVIN YDFPSQPKIF VHRVGRTARA GKTGWSYSLI RESDAPYLLD
LQLFLGRPLI LGRGSGQQVN YAEDVVVGSL PRDQVSRYSE WMTKLLDEDV DVELQREVAM
KGEKLYMRTR NSASSESAKR AKNVVGSDEW MMVHPLFNDE SSRLEEEREK MIARVGGYKP
QETIFEIGGR RGGKKGNDEA IDMMRKIRST FESKRARKES EGKSTHPTDD SGVANYPSNG
NDDDDDELAD VGDENDNVIT AENMSLASDS ELEVTFSYPQ SGKSKSRNDR NNSKPGEVFH
NPEYFMSYTP ASNSLVEDRA YGVHSGSNTN FVEASRGATM DLAGDESTSR SFGEPRSIMR
WDKRQKKYVS RRNDEDGSKG GKGDLLVRGE SGTKIAASFR SGRFDAWKKG KRIGRMPRVG
EAEAPGLSSG APGGKKYRHR KEQAPKTPDK FRDDYEKKKK KVEAANQRET EKAFDPSSGA
NKVGVKGRGK SELKSVEDIR KARKVKEMRK EKNARPSKKG KGR
//
