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Database: UniProt
Entry: G3ARW0_SPAPN
LinkDB: G3ARW0_SPAPN
Original site: G3ARW0_SPAPN 
ID   G3ARW0_SPAPN            Unreviewed;       918 AA.
AC   G3ARW0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=ATP-dependent RNA helicase DBP10 {ECO:0000256|ARBA:ARBA00019117};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE   AltName: Full=ATP-dependent RNA helicase dbp10 {ECO:0000256|ARBA:ARBA00021760};
GN   ORFNames=SPAPADRAFT_140104 {ECO:0000313|EMBL:EGW31377.1};
OS   Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN   [1] {ECO:0000313|EMBL:EGW31377.1, ECO:0000313|Proteomes:UP000000709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC       subfamily. {ECO:0000256|ARBA:ARBA00010379}.
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DR   EMBL; GL996503; EGW31377.1; -; Genomic_DNA.
DR   RefSeq; XP_007376155.1; XM_007376093.1.
DR   AlphaFoldDB; G3ARW0; -.
DR   STRING; 619300.G3ARW0; -.
DR   GeneID; 18870268; -.
DR   KEGG; spaa:SPAPADRAFT_140104; -.
DR   eggNOG; KOG0337; Eukaryota.
DR   HOGENOM; CLU_003041_5_1_1; -.
DR   InParanoid; G3ARW0; -.
DR   OMA; EDQFGMM; -.
DR   OrthoDB; 5475716at2759; -.
DR   Proteomes; UP000000709; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0030684; C:preribosome; IEA:UniProt.
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:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProt.
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:EGW31377.1};
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:UP000000709};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          102..130
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          133..304
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          371..531
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          826..918
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           102..130
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        20..44
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..877
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        903..918
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   918 AA;  105018 MW;  8761ADC966463773 CRC64;
     MSDDEDFDIA GSLGLNQEEE EDYSSSDNES EQEIQDEIIS SDEEEQADEP PKKKTKPTKK
     QESFPSLELS DNEQDREDAD DDSQLNSYFI ANNPATKKAK AGSFASFGLS KFLLTNIAKK
     GFRQPTPIQR KTIPLVMENR DVVGMARTGS GKTAAFVLPL IEKLKVRSAS GVRAIILSPS
     RELALQTYKQ VKEFGHGTNL QTTVLIGGDT LEEDFSKMVS KPDIIVCTPG RFLHLKVEMD
     YDLSTIQYIV FDEADRLFEM GFAIQLNELL ASLPPNRQSL LFSATLPRSL VDFAKAGLTN
     PVLVRLDAET KISDQLQMAY FTTKKNEREA NLLYILQEVI KLPLGSPEQI KKLKDMDKRQ
     VESDEENEED GKKKKYKFKK ERMPAANQLP SEFSTIVFVP TKHHVEYVTR MLRDAGYLVS
     YIYGTLDQHA RKNQLYQFRI GLTHIMVVTD VAARGIDIPV LANVINFTLP GSSKIFIHRV
     GRTARAGNKG WAYSIVNEKE LPYLLDLELF LGKKILLTSM HETKCEVLKR KQGDAYVPPK
     VNYTERLVLG SIPRLDLEGC QELYENLLRN DYELKVLRDV AAKGEKLYHR TRQAASPESL
     KRSKEIMETG SWDEQHVLFG PNLEKQKQDF LAKLQNRNVK ETVFEFNKKG NDKDENSLVE
     FMHRRRRQIA PIQRRAKERR ELLQKERNAG LTHGIEDEIL HEEGETGYNA DEQELEQVFE
     DADKISSKKK TYRDPNFFLS HYAPASVIQD QQLSISSSFA NDAQAATFDL DNDDKIQKNK
     QTMAWDKKKG KYVNSKSTDV KYIIGESGQK IPATFRSGKF DEWKKKRGAN LTTESTGESD
     NKRFKHKKVQ TPKLPDKFRD DYHKQKKKVE KAVEGGMKVR GYNKPGHQQE IKSTEQIRKA
     RMVKEQRRAK NARPSRRK
//
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