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YO12_CAEEL
ID   YO12_CAEEL              Reviewed;         593 AA.
AC   P34668;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   24-OCT-2003, sequence version 2.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Putative ATP-dependent RNA helicase ZK686.2;
DE            EC=3.6.4.13;
GN   ORFNames=ZK686.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Probable ATP-binding RNA helicase.
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
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DR   EMBL; FO080431; CCD63647.1; -; Genomic_DNA.
DR   PIR; D88511; D88511.
DR   PIR; S44912; S44912.
DR   RefSeq; NP_498690.2; NM_066289.5.
DR   AlphaFoldDB; P34668; -.
DR   SMR; P34668; -.
DR   STRING; 6239.ZK686.2; -.
DR   iPTMnet; P34668; -.
DR   EPD; P34668; -.
DR   PaxDb; P34668; -.
DR   PeptideAtlas; P34668; -.
DR   EnsemblMetazoa; ZK686.2.1; ZK686.2.1; WBGene00022792.
DR   GeneID; 176088; -.
DR   KEGG; cel:CELE_ZK686.2; -.
DR   UCSC; ZK686.2; c. elegans.
DR   CTD; 176088; -.
DR   WormBase; ZK686.2; CE34464; WBGene00022792; -.
DR   eggNOG; KOG0350; Eukaryota.
DR   GeneTree; ENSGT00550000075141; -.
DR   HOGENOM; CLU_003041_15_3_1; -.
DR   InParanoid; P34668; -.
DR   OMA; KFHPLAV; -.
DR   OrthoDB; 973872at2759; -.
DR   PhylomeDB; P34668; -.
DR   PRO; PR:P34668; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00022792; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0043186; C:P granule; IEA:UniProt.
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   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   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.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..593
FT                   /note="Putative ATP-dependent RNA helicase ZK686.2"
FT                   /id="PRO_0000055095"
FT   DOMAIN          150..341
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          386..533
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          552..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           377..380
FT                   /note="DEAD box"
FT   COMPBIAS        42..65
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..593
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         163..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   593 AA;  66545 MW;  B13AB2CB7032E748 CRC64;
     MKRKNQKEDS DTENDDEIEP ANGDGIEQEM NRVTNGNEDD ESVGNDVAEP METEDVEDSG
     EVEIEETAQN GEREIFKVLG KQEMKNLEAL KVTSSWVQNA TTFSATIDSS TSQKLSQIEL
     PEHLTVPSAI STWFPVQYAV LPSLFFEIRS PPPLRPRDVA IAAPTGSGKT ICYVLPVLAA
     VGSKPSKILQ AVILVPVQTL VAQIVDEFKR WNDESGVAKV VSLSGANDFE KEARQLASDP
     PNVIVATPAR LVQHLTSKIP PPIDLSKLRF LIVDEADRMG KLMREEWLDL VEFLCGGMER
     VACLKDIIRQ RRAPQKIVLS ATLSKDVEEL HLWNLFKPRL FSATAVSVKD ITSGIPQVDH
     VSGRLALPSS ISHRLVVTDP KFHPLAVYQQ ITRNKFNRTL IFVNEVSSSN RLAHVLKELC
     KDQFEVDYFT AQLFGKRRYK MLEKFNKNEN RVLICSDVLA RGTDLNKVDC VINYNLPADD
     KLFVHRAGRT GRAGQDGYVI SVGDKESKRL FVKMLKVTNL WGDTVEEQME EYIFEKDMDR
     YSKALESLKA TVSSQAKTGG SRQIAKRSGF EAKRKSRPNA RGEKPWLKKK TTE
 
 
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