ID A0A225AWW1_9EURO Unreviewed; 1241 AA.
AC A0A225AWW1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=UA08_05466 {ECO:0000313|EMBL:OKL58935.1};
OS Talaromyces atroroseus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Trachyspermi.
OX NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL58935.1, ECO:0000313|Proteomes:UP000214365};
RN [1] {ECO:0000313|EMBL:OKL58935.1, ECO:0000313|Proteomes:UP000214365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL58935.1,
RC ECO:0000313|Proteomes:UP000214365};
RA Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA Mortensen U.H., Thrane U.;
RT "Talaromyces atroroseus IBT 11181 draft genome.";
RL Submitted (JUN-2015) 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 -!- 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:OKL58935.1}.
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DR EMBL; LFMY01000008; OKL58935.1; -; Genomic_DNA.
DR RefSeq; XP_020119056.1; XM_020268356.1.
DR AlphaFoldDB; A0A225AWW1; -.
DR STRING; 1441469.A0A225AWW1; -.
DR GeneID; 31005222; -.
DR OrthoDB; 5477821at2759; -.
DR Proteomes; UP000214365; 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; cd17953; DEADc_DDX46; 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; 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:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:OKL58935.1};
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:UP000214365}.
FT DOMAIN 604..632
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 635..813
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 840..990
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 604..632
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 20..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..423
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1241 AA; 137539 MW; 68FC99654AE3D632 CRC64;
MARRGDTRSP SPVGSTYSSS RRSRRDEDRY ERNGRDEGRS HRRSRSPDVS LCQHQSYGYQ
MAYRDVNLTQ SLQHQRRYRD RERDRDRDGY RRRDRSVDRR DRNGYRDEQS YRSTKRDRSR
DRRRSPDRRS DRDYRRRSRE RDRSREKDNR SRRDDSRDRV RRHRDDSTDS RRKSRRDSRD
RSLNRDSDVR SREASKTPAP APVAQTDQEK KAERLAKLEA WKQKQAAERE RKQRELAAAG
GAHSILNEID KRSELATGAP APISPSTPTS TVDYGGKFDP RAIAKKSTGA ATGPSLLGKD
VAVPDSAKAD GITKANKIPV ASSKASGKCF YFGEFVEITG FNAMFSVVPL KASGNVGKFG
FGNKTAIESE KSSAKRTLDF GEEESTRKKL EKLPSLPLED AKDTPDDVVV EDDDSDVDME
TGTEEENAAA ARAAAEKREE RLQSQQTSQS IEPNGDVEMG DAVPTEPTDN GMAVENADEE
EIDPLDAFMS GLTEAAPSKK TSIVKSAKSK QQQPQAIFGD EDEVDMSAVA EGDTDDFLAI
ANKVKKKKDI PAVNHAKVEY EQFRKSFYTE PLDLAEMTEE EVANLRLELD GIKVRGVDPP
KPILKWSQCG LGVQTLDVIG KLGYENPTSI QSQALPAIMS GRDVIGVAKT GSGKTVSFLL
PMFRHIKDQR PLENMEGPIS LIMTPTRELA TQIHKDCKPF LKALNLRAVC AYGGAPIKDQ
IAELKRGAEI VVCTPGRMID LLAANSGRVT NLRRVTYVVL DEADRMFDMG FEPQVMKIMA
NIRPTRQTVL FSATFPRNME ALARKTLTKP VEIIVGGRSV VAPEITQIVE VRNESSKFLR
LLELLGNLYS DEANEDSRTL IFVDRQEAAD SLLRELMRKG YPCMSIHGGK DQIDRDSTIE
DFKAGVFPVL VATSVAARGL DVKQLKLVVN YDAPNHLEDY VHRAGRTGRA GNTGTAVTFL
TEDQERYSVD IAKALKQSGQ EVPAPVQKLV DSFLEKVKAG KEKASASGFG GKGLERLDQE
RDAARNRERK TYRTGEEGEE EEREETKEKK GEDQFAKAAS AIQSATAAAV TPMPGVPKGI
DLDGKITVHK TEKPAAGKPS NDPLDKVGSA VADIHARLNR AGVMRTGVPI DNKGPDAGAF
HATLEINDFP QKARWAVTNR TNVAKILEAT GTSITTKGSY YPAGKEPGPG ENPKLYILVE
GDTELVVTNA MRELMRLLKE GTIAAADSEA RAPTSGRYNV V
//