ID DED1_PICST Reviewed; 647 AA.
AC A3LQ01;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 3.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=ATP-dependent RNA helicase DED1;
DE EC=3.6.4.13;
GN Name=DED1; ORFNames=PICST_55603;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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 (By similarity).
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABN65127.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000496; ABN65127.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001383156.2; XM_001383119.1.
DR AlphaFoldDB; A3LQ01; -.
DR SMR; A3LQ01; -.
DR STRING; 322104.A3LQ01; -.
DR GeneID; 4837080; -.
DR KEGG; pic:PICST_55603; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; A3LQ01; -.
DR OrthoDB; 5480645at2759; -.
DR Proteomes; UP000002258; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; 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:0003723; F:RNA binding; 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; 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: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; Cytoplasm; Helicase; Hydrolase; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..647
FT /note="ATP-dependent RNA helicase DED1"
FT /id="PRO_0000285137"
FT DOMAIN 199..388
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 399..559
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 168..196
FT /note="Q motif"
FT MOTIF 332..335
FT /note="DEAD box"
FT COMPBIAS 1..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 212..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 647 AA; 68899 MW; 66B8DA2EBA0085C7 CRC64;
MTDITQKMNE LSVQDGGSGA GNSPGAGNGP SGGNGSRRSQ YVPPHLRNRN TSSGSGFGGN
GGGRGRGSFG GSNYNNAGNR DNTIFGGSGR SRDRGFGGRG GFRSNQSRPG VGRWVDGKHE
PSARNERIEL ELFGTAEDTS FQSSGINFDN YDDIPVEASG DGVPDPITSF TAPPLDELLV
ENITMSRFTK PTPVQKYSVP IVAGGRDLMA CAQTGSGKTG GFLFPVLSES YINGPAPIAE
STGAFSSHKV HPTILVMAPT RELVSQIYDE AKKFAYRSWV KPAVVYGGAD IGQQIRNLDK
GCDLLVATPG RLKDLLERGR VSLANIKYLV LDEADRMLDM GFEPQIRHIV QECDMPDVQD
RQTLMFSATF PTDIQMLARD FLKDYIFLSV GRVGSTSENI TQKILYVEDE EKKSVLLDLL
SAGDAGLTII FTETKRMADN LADFLYDQGF PATAIHGDRS QYEREKALAA FKSGAAPILV
ATAVAARGLD IPNVAHVINY DLPSDIDDYV HRIGRTGRAG NVGIATAFFN RNNKNVVKGL
IDLLSEANQE VPDFLAKIGR ESAFGGKTGG MRGGRGGSRG PVRDFRRGAS GGSSGGWGNS
SGSAGGWGAA PSGGNSYNSG YSSRSNSYNS SYGSSGYGNP TSTNSWW
//
