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DED1_CRYNB
ID   DED1_CRYNB              Reviewed;         637 AA.
AC   P0CQ75; Q55YR5; Q5KN36;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=ATP-dependent RNA helicase ded1;
DE            EC=3.6.4.13;
GN   Name=DED1; OrderedLocusNames=CNBA7700;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AAEY01000005; EAL23003.1; -; Genomic_DNA.
DR   RefSeq; XP_777650.1; XM_772557.1.
DR   AlphaFoldDB; P0CQ75; -.
DR   SMR; P0CQ75; -.
DR   EnsemblFungi; AAW41314; AAW41314; CNA07860.
DR   EnsemblFungi; EAL23003; EAL23003; CNBA7700.
DR   GeneID; 4934036; -.
DR   KEGG; cnb:CNBA7700; -.
DR   VEuPathDB; FungiDB:CNBA7700; -.
DR   HOGENOM; CLU_003041_16_3_1; -.
DR   Proteomes; UP000001435; Chromosome 1.
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; RNA-binding.
FT   CHAIN           1..637
FT                   /note="ATP-dependent RNA helicase ded1"
FT                   /id="PRO_0000410248"
FT   DOMAIN          191..384
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          395..556
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          15..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           160..188
FT                   /note="Q motif"
FT   MOTIF           328..331
FT                   /note="DEAD box"
FT   COMPBIAS        39..68
FT                   /note="Pro 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   637 AA;  68050 MW;  D3BD775D690B0958 CRC64;
     MAATDVNGLA SQMNSVNLNG ASQKPQKPAY VPPHLRNRAA PPAAVPPAAP AAYRPSPTGL
     PTPATTPPTR HIVPAAVAED DVGGWGAQPR VRKTFEHGAP PGFGSWKNGQ HVVGARNTRM
     EKEMYGEVGD GLHQATGINF DKYADIPVEV SGKGVPEPVT EFTNPPINPV LLENVKYARY
     ATPTPVQKYS IPIVADGRDL MACAQTGSGK TGGFLFPILS ALFTYGPSTP PVEQDTGYGY
     RRTKKVYPTA LVLAPTRELV SQIHEEARKF AYRSWVRPAV VYGGADIGSQ MRALDRGCDL
     LSATPGRLVD LIERGKISLA NVKYLVLDEA DRMLDMGFEP QIRRIVDEED MPGVLERQTL
     MFSATFPREI QNLARSFLKE YIFLTVGRVG STSENITQRV EYVDDQDKRS LLLDLLLAEQ
     SGGLILVFVE TKRMADTLCD FLCSRRHNAT SIHGDRTQRE REAALYAFKS GRAPILVATA
     VAARGLDIPN VTHVILYDLP NDVAEYTHRI GRTGRAGNVG TSTAFFNRGN TNIGKDLIEL
     LKEANQEVPQ WLVEISSERS YGGGGGGGYK GSRGRSTGGG GGARLGGRDM RQGGGGYGGG
     GRTSGYGGGY GGGGGGAGWG SGGGFPPAGG DSGASWW
 
 
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