ID D4D6W9_TRIVH Unreviewed; 677 AA.
AC D4D6W9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=ATP-dependent RNA helicase DED1 {ECO:0000256|ARBA:ARBA00024397};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=ATP-dependent RNA helicase ded1 {ECO:0000256|ARBA:ARBA00024405};
GN ORFNames=TRV_02846 {ECO:0000313|EMBL:EFE42407.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE42407.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- FUNCTION: ATP-binding RNA helicase involved in translation initiation.
CC Remodels RNA in response to ADP and ATP concentrations by facilitating
CC disruption, but also formation of RNA duplexes.
CC {ECO:0000256|ARBA:ARBA00025161}.
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. DDX3/DED1
CC subfamily. {ECO:0000256|ARBA:ARBA00024358}.
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:EFE42407.1}.
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DR EMBL; ACYE01000147; EFE42407.1; -; Genomic_DNA.
DR RefSeq; XP_003023025.1; XM_003022979.1.
DR AlphaFoldDB; D4D6W9; -.
DR GeneID; 9583045; -.
DR KEGG; tve:TRV_02846; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR OrthoDB; 5480645at2759; -.
DR Proteomes; UP000008383; 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:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd17967; DEADc_DDX3_DDX4; 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; IPR044763; Ded1/Dbp1_DEADc.
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:SF32; RNA HELICASE; 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 Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022540}.
FT DOMAIN 198..226
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 229..422
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 433..593
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 198..226
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 8..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 72107 MW; F5D3A79AE5E725B7 CRC64;
MADNLKIGNL SLNDSQHAPN QTGRSAYIPP HLRGQARQAA AAESAAGPTV DGPDGPAPGQ
NGRPAGMNAS AWAPGAPNNA PGWGAGDYGP RGGPAVNGNS GWGQPAGSRR TFDPHAYGHP
GHQGQQGGNY GGGGAARGSG DGQWRDGKHI PGPSNARLER ELFGIPNDPS KQHTGINFAN
YDDIPVEASG QNVPEPVSTF TNPPLDDHLI SNIKLASYKV PTPVQKYSIP IVMGGRDLMA
CAQTGSGKTG GFLFPILSQA FQNGPSPAPT QQGGQFSYGR QRKAYPTSLI LAPTRELVSQ
IYDEARKFAY RSWVRPCVVY GGADIGSQLR QIERGCDLLV ATPGRLVDLI ERGRISLCNI
KYLVLDEADR MLDMGFEPQI RRIVEGEDMP PVAGRQTLMF SATFPRDIQM LARDFLKDYV
FLSVGRVGST SENITQKVEY VEDNDKRSVL LDILHTHGAG LTLIFVETKR MADSLSEFLI
NQHFPATAIH GDRTQRERER ALEYFRNGRC PILVATAVAA RGLDIPNVTH VVNYDLPTDI
DDYVHRIGRT GRAGNTGIST AFFNRGNRGV VRDLIELLKE AHQEVPSFLE NIAREGSGYG
GRGGRGRGRG SAGANRDMRR MGGGMGGPPS YGGGGNYAAP QSYGGGGGNY GGGPYGGGYG
GGGYGNPSGP TGPSSWW
//