ID A0A446BH49_9PEZI Unreviewed; 666 AA.
AC A0A446BH49;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=TT172_LOCUS4187 {ECO:0000313|EMBL:SPQ21768.1};
OS Thermothielavioides terrestris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ21768.1, ECO:0000313|Proteomes:UP000289323};
RN [1] {ECO:0000313|EMBL:SPQ21768.1, ECO:0000313|Proteomes:UP000289323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Huttner S., Dainat J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC subfamily. {ECO:0000256|ARBA:ARBA00024358}.
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DR EMBL; OUUZ01000008; SPQ21768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A446BH49; -.
DR SMR; A0A446BH49; -.
DR Proteomes; UP000289323; 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:InterPro.
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 187..215
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 218..408
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 419..579
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 187..215
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ SEQUENCE 666 AA; 70903 MW; 9E8D3861F82B9528 CRC64;
MADQLSGSMG NLSLDSAPPA AQLSNQQPVT RSYIPPHLRA KMAAANAPPA NGPPMGPGPM
NGPGPVNGLN NSAWAGNNNF DVRAGGGNWG AYDQSPHPWG GRQGGFNRNA YRGPASGGGG
AMGGGAGRGE GRWIDGKHVI GSGDPRLERE LFGTADDPSK QHTGINFEKY DDIPVTPSGR
DVPEPILTFS NPPLDPHLLS NIELARYKIP TPVQKYSIPI VINGRDLMAC AQTGSGKTGG
FLFPILHQSF TQGPSPVPAQ GGGYGRQRKA YPTALILAPT RELVSQIYDE ARKFAYRSWV
RPCVVYGGAD IGSQLRQIER GCDLLVATPG RLVDLIERGR ISLCNIKYLV LDEADRMLDM
GFEPQIRRIV QGEDMPPTGQ RQTLMFSATF PRDIQMLAQD FLSDYVFLSV GRVGSTSENI
TQKIEYVEDI DKRSVLLDIL HTHAGGLTLI FVETKRMADS LSDFLINQNF PATSIHGDRT
QRERERALEL FRNGKCPILV ATAVAARGLD IPNVTHVINY DLPTDIDDYV HRIGRTGRAG
NTGIATAFFN RGNRGIVREL IDLLKEANQE IPSFLETIAR ESSYGGGRGG RGGGRGRGRG
GNTDFRKYGG GGGGFGGGFG GPQHSSGGGG GYGGYGGPQS GGYGGGYGGY GGGYGNPGGA
GGQSWW
//
