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Database: UniProt
Entry: A7TKR8
LinkDB: A7TKR8
Original site: A7TKR8 
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   16-OCT-2019, entry version 62.
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)
OS   (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
OC   Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M.,
RA   Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two
RT   yeast 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
CC       initiation. Remodels RNA in response to ADP and ATP concentrations
CC       by facilitating disruption, but also formation of RNA duplexes (By
CC       similarity). {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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC       subfamily. {ECO:0000305}.
DR   EMBL; DS480409; EDO17180.1; -; Genomic_DNA.
DR   RefSeq; XP_001645038.1; XM_001644988.1.
DR   SMR; A7TKR8; -.
DR   STRING; 36033.XP_001645038.1; -.
DR   PRIDE; A7TKR8; -.
DR   EnsemblFungi; EDO17180; EDO17180; Kpol_1072p50.
DR   GeneID; 5545379; -.
DR   KEGG; vpo:Kpol_1072p50; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   eggNOG; ENOG410XNTI; LUCA.
DR   InParanoid; A7TKR8; -.
DR   KO; K11594; -.
DR   OMA; GPDWWGQ; -.
DR   OrthoDB; 595675at2759; -.
DR   PhylomeDB; A7TKR8; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033592; F:RNA strand annealing activity; IEA:EnsemblFungi.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0000390; P:spliceosomal complex disassembly; IEA:EnsemblFungi.
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; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   Initiation factor; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; RNA-binding.
FT   CHAIN         1    650       ATP-dependent RNA helicase DED1.
FT                                /FTId=PRO_0000310183.
FT   DOMAIN      191    380       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      391    551       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     204    211       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       160    188       Q motif.
FT   MOTIF       324    327       DEAD box.
FT   COMPBIAS     47     98       Asn-rich.
FT   COMPBIAS    555    648       Gly/Ser-rich.
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
//
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