DED1_VANPO
ID DED1_VANPO Reviewed; 650 AA.
AC A7TKR8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=ATP-dependent RNA helicase DED1;
DE EC=3.6.4.13;
GN Name=DED1; ORFNames=Kpol_1072p50;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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}.
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DR EMBL; DS480409; EDO17180.1; -; Genomic_DNA.
DR RefSeq; XP_001645038.1; XM_001644988.1.
DR AlphaFoldDB; A7TKR8; -.
DR SMR; A7TKR8; -.
DR STRING; 436907.A7TKR8; -.
DR PRIDE; A7TKR8; -.
DR EnsemblFungi; EDO17180; EDO17180; Kpol_1072p50.
DR GeneID; 5545379; -.
DR KEGG; vpo:Kpol_1072p50; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; A7TKR8; -.
DR OMA; IMRGQPV; -.
DR OrthoDB; 595675at2759; -.
DR PhylomeDB; A7TKR8; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
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 Gene3D; 3.40.50.300; -; 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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 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..650
FT /note="ATP-dependent RNA helicase DED1"
FT /id="PRO_0000310183"
FT DOMAIN 191..380
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 391..551
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 160..188
FT /note="Q motif"
FT MOTIF 324..327
FT /note="DEAD box"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 204..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 650 AA; 70089 MW; 1AA9D83262EBB451 CRC64;
MADLQEQVQN LNINDDDKNA SSYVPPHLRN QRRGPPRHDS PSDGSENNND FGFGFNNRRG
GYNGGSGYRG GNNSYNRRGN YQGGQNNSNN NNNGGGFNRI PGRGSWTNGK HVPGAKNQNL
EVQLFGTPED PQFQSSGINF DNYDDIPVDA SGTDVPEAIT EFTSPPLDAL LLENIILARF
TKPTPVQKYS VPIVSRGRDL MACAQTGSGK TGGFLFPVLS ESFKNGPSPM PESARKSFVK
KAYPTALVLA PTRELATQIY DEAKKFTYRS WVRPTVVYGG SDIGSQIRDL SRGCDLLVAT
PGRLSDLLER GRVSLANVKY LVLDEADRML DMGFEPQIRQ IVDGCDMPPV GERQTLMFSA
TFPDDIQHLA RDFLSDYIFL SVGKVGSTSE NITQRILYVE DMDKKSTLLD LLSASNDGLT
LIFVETKRMA DELTDFLIMQ DFRATAIHGD RTQSERERAL AAFKNGNANL LVATAVAARG
LDIPNVTHVV NYDLPSDIDD YVHRIGRTGR AGNTGVATAF FNRGNRNIVK GMYELLAEAN
QEIPPFLNDV MRESGRGGRT SGFSSRNNSN RDYRRSGSNN GGSWGNSRSN SNSGAGGWGS
SRSGGAGGAG GAGGAGGAGG SSWGRSGSSG WGNSSSSNAG AGSNAKSSWW
