位置:首页 > 蛋白库 > DED1_NEUCR
DED1_NEUCR
ID   DED1_NEUCR              Reviewed;         688 AA.
AC   Q9P6U9; Q7S7K7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=ATP-dependent RNA helicase ded1;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box RNA helicase 9;
GN   Name=drh-9; Synonyms=ded1; ORFNames=15E6.040, NCU01369;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL353822; CAB88635.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA31690.3; -; Genomic_DNA.
DR   PIR; T48796; T48796.
DR   RefSeq; XP_960926.3; XM_955833.3.
DR   AlphaFoldDB; Q9P6U9; -.
DR   SMR; Q9P6U9; -.
DR   STRING; 5141.EFNCRP00000004089; -.
DR   EnsemblFungi; EAA31690; EAA31690; NCU01369.
DR   GeneID; 3877087; -.
DR   KEGG; ncr:NCU01369; -.
DR   VEuPathDB; FungiDB:NCU01369; -.
DR   HOGENOM; CLU_003041_16_3_1; -.
DR   InParanoid; Q9P6U9; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0002183; P:cytoplasmic translational initiation; IEA:EnsemblFungi.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:EnsemblFungi.
DR   GO; GO:1990625; P:negative regulation of cytoplasmic translational initiation in response to stress; IEA:EnsemblFungi.
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..688
FT                   /note="ATP-dependent RNA helicase ded1"
FT                   /id="PRO_0000232161"
FT   DOMAIN          225..416
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          427..587
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           194..222
FT                   /note="Q motif"
FT   MOTIF           360..363
FT                   /note="DEAD box"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         238..245
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   688 AA;  72055 MW;  9656D45DCDE6097B CRC64;
     MADQLSSGMG NLSIDQQPPS GPQMGGQGQM RRSYIPPHLR GKMGDAAPPM AGPNGLNNSA
     WAGNNNYDAR GPGGGGNWPA PGGPPGPGFE GQQGAGWGGP RPQGGFNPNA YRGNAGAGAG
     AGAGGGGGSF SNRGSGDGQW RDGKHIPGPA NPRVERELFG TPDDPSKQHT GINFEKYDDI
     PVEASGDNVP EPVLTFSNPP LDNHLISNIQ LARYNVPTPV QKYSIPIVMG GRDLMACAQT
     GSGKTGGFLF PILSQSFHTG PSPIPASAAG AYGRQRKAYP TALILAPTRE LVSQIYDEAR
     KFAYRSWVRP CVVYGGADIG SQLRQIERGC DLLVATPGRL VDLIERGRIS LCNIKYLVLD
     EADRMLDMGF EPQIRRIVEG EDMPKVNDRQ TLMFSATFPR DIQILARDFL KDYIFLSVGR
     VGSTSENITQ KVEYVEDIDK RSVLLDILHT HAGGLTLIFV ETKRMADSLS DFLINQNFPA
     TSIHGDRTQR ERERALEMFR NGRCPILVAT AVAARGLDIP NVTHVINYDL PTDIDDYVHR
     IGRTGRAGNT GIATAFFNRG NRGVVRELLE LLKEANQEVP AFLETIARES SFGGGRGGRG
     GGRGGGRGRT QTADYRKFGG SGGGGFGGGF GGAPASGGYG GGGYGGGGPP AGGYGGGGGA
     GYGGGGGGGG YGGGGYGNPG GAGGQSWW
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024