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Database: UniProt
Entry: A0A024GB94_9STRA
LinkDB: A0A024GB94_9STRA
Original site: A0A024GB94_9STRA 
ID   A0A024GB94_9STRA        Unreviewed;       838 AA.
AC   A0A024GB94;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=BN9_043910 {ECO:0000313|EMBL:CCI43607.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI43607.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI43607.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI43607.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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:CCI43607.1}.
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DR   EMBL; CAIX01000052; CCI43607.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024GB94; -.
DR   STRING; 65357.A0A024GB94; -.
DR   InParanoid; A0A024GB94; -.
DR   OrthoDB; 5475716at2759; -.
DR   Proteomes; UP000053237; 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; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          29..57
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          60..233
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          264..407
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          785..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           29..57
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        785..812
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..838
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   838 AA;  94813 MW;  28634D18B6375E38 CRC64;
     MASAMPTDDG SNATKAPQNN NSKKNKKGGG FQHLGLSNPV YRAVMAMGYK VPTPIQRKSL
     PLILSGKDVV GMARTGSGKS AAFLIPLIEK LKEHSTRVGL RGLVLAPTRE LALQTLQFTK
     GLAKYTSLRI SLIVGGEGME QQFSALASNP DILVATPGRL MHHLQEIPDF NLKSVEYVVF
     DEADRLFEMG FADQLHEILS QMPLNRQTLL FSATLPSVLA QFARAGLNEP AMIRLDVENK
     MSENLKMAFF TVRSDDKPAV FVHLVRDFLP KSDQTIIFTA TRHHVELLHQ LLNANNIESS
     CVYGEMDQTS RKLNIAKFRA GKTNLLLVTD VAARGIDIPL LNNVINYSFP PTAKLFVHRV
     GRAARAGKSG TAFSLLDPTE YPFLVDLHLY IGRRLEDSSP VNSEPYSLKE MQVQHIHYGS
     FPCEITDREN EQIQYLLKHH PIVSPLVKVC DNASKLYQRT RADPSKLSIK RAKGLQIQCH
     PLFKKDFLDH DRAEKEECLA KIQTFRPTQT IFEVASSRAV PGTKKSNTTS AMSVMASKRN
     AHSKIIEKHA SKDAEVSHIS IPIERYTTPT CFPAQVVAQT EPKKGRYLSK HARKQLRRRV
     AAGESQSDVL ENLLAAQDQR NEPTSDTMEI RQTQVKPEFK DQDNYIDTAK SERELMDGSF
     FNQVDDQNAF SNRLDASTLD LNPDDALQMN RKRRIVHWDT RKKKYVRTMA QDLTKQGTVR
     KKPPAHEYIR TESGIKIKAK KQQWGELYKK WQQKQNRSIR PGLEEDERAG NIDYRHKRVK
     LKGVKNELQS EQMIRKEQAR KGRSQSNYKT DKTSHKPRRK GGSHGAPTRS KSIIRKRR
//
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