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DED1_PICST
ID   DED1_PICST              Reviewed;         647 AA.
AC   A3LQ01;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 3.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=ATP-dependent RNA helicase DED1;
DE            EC=3.6.4.13;
GN   Name=DED1; ORFNames=PICST_55603;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABN65127.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000496; ABN65127.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001383156.2; XM_001383119.1.
DR   AlphaFoldDB; A3LQ01; -.
DR   SMR; A3LQ01; -.
DR   STRING; 4924.XP_001383156.2; -.
DR   EnsemblFungi; ABN65127; ABN65127; PICST_55603.
DR   GeneID; 4837080; -.
DR   KEGG; pic:PICST_55603; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   HOGENOM; CLU_003041_16_3_1; -.
DR   InParanoid; A3LQ01; -.
DR   OrthoDB; 595675at2759; -.
DR   Proteomes; UP000002258; Chromosome 2.
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..647
FT                   /note="ATP-dependent RNA helicase DED1"
FT                   /id="PRO_0000285137"
FT   DOMAIN          199..388
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          399..559
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           168..196
FT                   /note="Q motif"
FT   MOTIF           332..335
FT                   /note="DEAD box"
FT   COMPBIAS        1..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         212..219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   647 AA;  68899 MW;  66B8DA2EBA0085C7 CRC64;
     MTDITQKMNE LSVQDGGSGA GNSPGAGNGP SGGNGSRRSQ YVPPHLRNRN TSSGSGFGGN
     GGGRGRGSFG GSNYNNAGNR DNTIFGGSGR SRDRGFGGRG GFRSNQSRPG VGRWVDGKHE
     PSARNERIEL ELFGTAEDTS FQSSGINFDN YDDIPVEASG DGVPDPITSF TAPPLDELLV
     ENITMSRFTK PTPVQKYSVP IVAGGRDLMA CAQTGSGKTG GFLFPVLSES YINGPAPIAE
     STGAFSSHKV HPTILVMAPT RELVSQIYDE AKKFAYRSWV KPAVVYGGAD IGQQIRNLDK
     GCDLLVATPG RLKDLLERGR VSLANIKYLV LDEADRMLDM GFEPQIRHIV QECDMPDVQD
     RQTLMFSATF PTDIQMLARD FLKDYIFLSV GRVGSTSENI TQKILYVEDE EKKSVLLDLL
     SAGDAGLTII FTETKRMADN LADFLYDQGF PATAIHGDRS QYEREKALAA FKSGAAPILV
     ATAVAARGLD IPNVAHVINY DLPSDIDDYV HRIGRTGRAG NVGIATAFFN RNNKNVVKGL
     IDLLSEANQE VPDFLAKIGR ESAFGGKTGG MRGGRGGSRG PVRDFRRGAS GGSSGGWGNS
     SGSAGGWGAA PSGGNSYNSG YSSRSNSYNS SYGSSGYGNP TSTNSWW
 
 
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