ID A0A0F4YXP7_TALEM Unreviewed; 825 AA.
AC A0A0F4YXP7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=T310_3111 {ECO:0000313|EMBL:KKA22855.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA22855.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA22855.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA22855.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-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:KKA22855.1}.
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DR EMBL; LASV01000121; KKA22855.1; -; Genomic_DNA.
DR RefSeq; XP_013329467.1; XM_013474013.1.
DR AlphaFoldDB; A0A0F4YXP7; -.
DR STRING; 1408163.A0A0F4YXP7; -.
DR GeneID; 25315461; -.
DR OrthoDB; 5487240at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd17945; DEADc_DDX23; 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 PRINTS; PR01217; PRICHEXTENSN.
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:KKA22855.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KKA22855.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958}.
FT DOMAIN 382..410
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 413..618
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 629..792
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 382..410
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 12..82
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 91125 MW; 92D453930CB72B48 CRC64;
MDGILTNGNG EVRPPEPPPE PVERPPTPPP APPADSAPPP PPPPPPMDDD AAAPPPPADT
DVAAPPPPPE EAPPPPPPAA DVPKKKKGWG SSSSAPKPLS VEELLRKKRE ADAAAAKPKF
LSKAERERIA LEKRAKEVEA ERRAKAERDL PTNDVDRNGT TANGNANGDA KSIPTGPRAL
RNGEIPTAPA AMRKEQANKD YDMSPPQPPK PIAFGKEDSK GEKRSAEEEA EAALIRQRYM
GADQTSSFSA KKKRKRTTER KFNFEWSVDE DTSGDYNPLY QNRQEANFYG RGRLAGFGDD
VADNLTRRYA KALEDRDREA GSIRAREILE MERRRKEESS RNAIDKHWSE KRLDQMRERD
WRIFKEDFNI STKGGSIPNP MRSWEESGLP RRLLDLIYKV GYTEPTPIQR AAIPIALQSR
DLIGVAVTGS GKTAAFLLPL LVYISELPRL DEFEWRKNDG PYAIILAPTR ELAQQIEIEA
KKFADPLGFT VVSIVGGHSL EEQAYSLRNG AEIIIATPGR LVDCLERRML VLAQCCYVIM
DEADRMIDLG FEEPVNKILD ALPVSNEKPD TEEAEDSRAM SQHIGGKERY RQTMMYTATM
PPAVERIARR YLRRPAIVTI GNVGQAVDTV EQRVEFIAGE DKRKKRLAEI LMSGEFQPPI
IVFVNIKRNC DVIAREIKQW GFSAVTLHGS KTQEQREAAL ASVRNGTTDV LVATDLAGRG
IDVPDVSLVV NFNMATNIES YTHRIGRTGR AGKSGVAITF LGNEDADVMY DLKQMLMKSS
VSRVPEELRK HEAAQSKPTR GAGAAAKQQK VEESGAFGGK GGGLW
//
