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DED1_COCIM
ID   DED1_COCIM              Reviewed;         665 AA.
AC   Q1DJF0; A0A0D6K9M7; J3K0D9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=ATP-dependent RNA helicase DED1;
DE            EC=3.6.4.13;
GN   Name=DED1; ORFNames=CIMG_09563;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704915; EAS28359.2; -; Genomic_DNA.
DR   RefSeq; XP_001239942.2; XM_001239941.2.
DR   AlphaFoldDB; Q1DJF0; -.
DR   SMR; Q1DJF0; -.
DR   STRING; 246410.Q1DJF0; -.
DR   EnsemblFungi; EAS28359; EAS28359; CIMG_09563.
DR   GeneID; 4558926; -.
DR   KEGG; cim:CIMG_09563; -.
DR   VEuPathDB; FungiDB:CIMG_09563; -.
DR   InParanoid; Q1DJF0; -.
DR   OMA; CYRSWVR; -.
DR   OrthoDB; 595675at2759; -.
DR   Proteomes; UP000001261; 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   CDD; cd17967; DEADc_DDX3_DDX4; 1.
DR   Gene3D; 3.40.50.300; -; 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   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..665
FT                   /note="ATP-dependent RNA helicase DED1"
FT                   /id="PRO_0000255986"
FT   DOMAIN          212..405
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          416..576
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           181..209
FT                   /note="Q motif"
FT   MOTIF           349..352
FT                   /note="DEAD box"
FT   BINDING         225..232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   665 AA;  71139 MW;  513D5C022649C51F CRC64;
     MADSLKMAGL SLEDSQHAPS HATGRAPYIP PHLRGQQRAG PTMPVDGAAP QGRPPMNPGS
     WGPNGAPPNN WAPRGANNIN GAPAWGAAGG GGARFDPNAY GHPGHRGGQS HGGAGSGAAR
     GSGDGQWRDG KHIPGPPNAR LERELFGVPN DPSKQHTGIN FANYDDIPVE ASGHDVPEPV
     TTFTNPPLDD HLISNIKLAT YKTPTPVQKY SIPIVMGGRD LMACAQTGSG KTGGFLFPIL
     SQAFKNGPSA VPTQNANQFS YGRQRKAYPT SLILAPTREL VSQIYDEARK FAYRSWVRPC
     VVYGGADIGS QLRQIERGCD LLVATPGRLV DLIERGRISL CNIKYLVLDE ADRMLDMGFE
     PQIRRIVEGE DMPPVNGRQT LMFSATFPRD IQMLARDFLK DYVFLSVGRV GSTSENITQK
     VEYVEDADKR SVLLDILHTH GTGLTLIFVE TKRMADSLSE FLINQNFPAT AIHGDRTQRE
     RERALEYFRN GRCPILVATA VAARGLDIPN VTHVVNYDLP TDIDDYVHRI GRTGRAGNTG
     LSTAFFNRGN RGVVRDLIEL LKEAHQEVPA FLENIAREGS GYGGRGGGRG GGRGRGANAT
     RDMRRMGGGG PPMSGTPSYS GGYGGGANNY GGSYSSAPSY GGYGGGYGGG SYGNPSGPTG
     PSSWW
 
 
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