ID B8MMH1_TALSN Unreviewed; 582 AA.
AC B8MMH1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 03-MAY-2023, entry version 62.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=TSTA_099750 {ECO:0000313|EMBL:EED13725.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED13725.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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.
CC {ECO:0000256|RuleBase:RU000492}.
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DR EMBL; EQ962658; EED13725.1; -; Genomic_DNA.
DR RefSeq; XP_002485963.1; XM_002485918.1.
DR AlphaFoldDB; B8MMH1; -.
DR STRING; 441959.B8MMH1; -.
DR GeneID; 8105418; -.
DR VEuPathDB; FungiDB:TSTA_099750; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_1_5_1; -.
DR InParanoid; B8MMH1; -.
DR OMA; HPIMREN; -.
DR OrthoDB; 5480645at2759; -.
DR PhylomeDB; B8MMH1; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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; 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; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF2; DEAD BOX RNA HELICASE-PL10B; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 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, ECO:0000256|RuleBase:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 114..142
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 145..342
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 354..519
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 29..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..142
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 527..542
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 582 AA; 65221 MW; DC73706B3150A731 CRC64;
MDPLSTEDIS CRLEAATLGT RQRLGRAEKY DYSRWAPPTE KPADGIDPRE DVPWASNARK
YEWKEDYGDV GPEDEELEKI LFRNEFLNRV GVKFDNLQSI KVIVEAAEKP DPISRFADAG
LHPIMEKNVA LCGYQIPTPI QAYAIPTILQ GHDLMAIAQT GSGKTAAYLI PVLSKLMGKA
KKLAGPRPKF GEAFDPKVNA VRAEPLVLVI VPTRELACQI FDEARRLCYR SMLRPCVAYG
GGPVSHQRME LQKGCDILIG TPGRLIDFMG QTHVLSLRRV RYTIVDEADE LLNTDWETEF
AQLLSGGDSN EDADHRYMMF SATFNKTCRQ VAKKHLETGY VRIRVGRTGS SHANIEQRII
YAEDQTKMQC LYDLLLSMPP ARTLIFVNTK VQADRLDDYL FNLGLPSTSI HSDRTQRERE
DAMSAFRTGK SPILIATGVS ARGLDIKNVM HVVNFDLPSY DQGGIDEYVH RIGRTARIGN
EGIATSLYNH GRNTDIARDL VKLLLENKQV VPDFLEELKP EGELVFDDDN SDVEEDIDET
NVDADPQSTH SGPVEDAPEL DEFSTPKQEA DITAPTNSDF DW
//
