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Database: UniProt
Entry: A0A0H1BK75_9EURO
LinkDB: A0A0H1BK75_9EURO
Original site: A0A0H1BK75_9EURO 
ID   A0A0H1BK75_9EURO        Unreviewed;       786 AA.
AC   A0A0H1BK75;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   ORFNames=EMPG_13283 {ECO:0000313|EMBL:KLJ11528.1};
OS   Blastomyces silverae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ11528.1, ECO:0000313|Proteomes:UP000053573};
RN   [1] {ECO:0000313|Proteomes:UP000053573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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   -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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         ECO:0000256|RuleBase:RU365068};
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC       {ECO:0000256|RuleBase:RU365068}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC       subfamily. {ECO:0000256|ARBA:ARBA00037933}.
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:KLJ11528.1}.
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DR   EMBL; LDEV01001501; KLJ11528.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H1BK75; -.
DR   STRING; 2060906.A0A0H1BK75; -.
DR   OrthoDB; 149428at2759; -.
DR   Proteomes; UP000053573; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd17949; DEADc_DDX31; 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; IPR025313; DUF4217.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24031:SF89; ATP-DEPENDENT RNA HELICASE DDX31-RELATED; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365068};
KW   Helicase {ECO:0000256|RuleBase:RU365068, ECO:0000313|EMBL:KLJ11528.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365068};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU365068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053573};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT   DOMAIN          201..407
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          434..644
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          39..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          729..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..753
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   786 AA;  86301 MW;  947438553E513E67 CRC64;
     MADDGMLLNF NLGDGIIQTQ QKFKGGTWKD RLSVKKIALH RQNKSKFPNS EDQDRAGRKD
     GAVNPNRVEI TSPRPPKRQR VDGDFKPSSS SSHRASGHTP TSTNVGSSND RGNTQGNQAR
     KNQNQPREII SSLFSFNPAP VSAVEPPKPE EGAEPSKPSN APLIDGIDTF TSLGLSPMLA
     AHLLTKLELK APTAVQKSAI SQLLKEECDA FIQAQTGSGK TLAYLLPLVQ RLITLSSTNG
     KAFERTSDGS DNAAVHRDSG LFAIILAPTR ELCKQISVVL EQLLRCAHWI VAGTVIGGEK
     KKSEKARLRK GLNILVATPG RLADHLENTK VLDVSNVRWL VLDEGDRLMD LGFEEEIQGI
     VKKLDERQKS KGIPGLPAKR VTILCSATLK MNVQRLGEIS LKDAVHVQAD PEDEDDETKT
     KNTGTNSEFS VPAQLKQSYA VVAAKLRLVT LTALMKRTFA RKGSVMKAII FVSCADSVDF
     HFEAFSRQDS ENKSEEKEPK NTEASLPTKP APIHGTVAKA TAFSNPTNPV TIYKLHGSLP
     QHVRTSTLSA FSRQGEAAVL ICTDVAARGL DLPNVDFVVE YDPAFSSDDH LHRIGRTARL
     GRDGRAHIFL LPGNEEKYVE ILKRGYRDGG AKVSCIDVNE SLKRGFGGNT ESTSKGWEEK
     TTEWQLDIER WALENPTILE MARRAYQSHI RAYATHIASE RDMFNIKDLH LGHLAKSFAL
     RDRPAKINVP GLRPGKEDTK KEFKADRKGA RDGAQASKGT NTSDAARKMR AKMKEHMAGA
     NEFNIA
//
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