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JHD1_YARLI
ID   JHD1_YARLI              Reviewed;         510 AA.
AC   Q6C423;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=JmjC domain-containing histone demethylation protein 1;
DE            EC=1.14.11.27 {ECO:0000250|UniProtKB:P40034};
DE   AltName: Full=[Histone-H3]-lysine-36 demethylase 1;
GN   Name=JHD1; OrderedLocusNames=YALI0E30393g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-36'
CC       of histone H3, thereby playing a central role in histone code.
CC       {ECO:0000250|UniProtKB:P40034}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
CC         + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2
CC         succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC         COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:61976; EC=1.14.11.27;
CC         Evidence={ECO:0000250|UniProtKB:P40034};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The JmjC domain mediates the demethylation activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC       {ECO:0000305}.
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DR   EMBL; CR382131; CAG80193.1; -; Genomic_DNA.
DR   RefSeq; XP_504589.1; XM_504589.1.
DR   AlphaFoldDB; Q6C423; -.
DR   SMR; Q6C423; -.
DR   STRING; 4952.CAG80193; -.
DR   EnsemblFungi; CAG80193; CAG80193; YALI0_E30393g.
DR   GeneID; 2912961; -.
DR   KEGG; yli:YALI0E30393g; -.
DR   VEuPathDB; FungiDB:YALI0_E30393g; -.
DR   HOGENOM; CLU_003540_6_2_1; -.
DR   InParanoid; Q6C423; -.
DR   OMA; FLMFPPT; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR   GO; GO:0140680; F:histone H3-di/monomethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR041070; JHD.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   Pfam; PF17811; JHD; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW   Oxidoreductase; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..510
FT                   /note="JmjC domain-containing histone demethylation protein
FT                   1"
FT                   /id="PRO_0000226800"
FT   DOMAIN          216..365
FT                   /note="JmjC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   ZN_FING         2..53
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          475..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         260
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ   SEQUENCE   510 AA;  57824 MW;  AF2ACF8B12D39990 CRC64;
     MPNRCDFCTS SSTKDKQQWT QCDGCDRWVH DVCVSITDPV SYAKYHCPTC TKTKGPSLYK
     RQSKRKKIDI DYAAMHSGNV DMSLRTRHVH SSRFTDVAAS AQNKEPFKRV SGTELTLDWA
     QSSDGLNEPV IVPKEYKDTL GMYIPEDLTV RQVAEAVGME SPVEVINVVS QNGSPGWNMG
     KWTEYYEDIE GRDTILNVIS LEISASALGK TIVRPTLVRE LDLVDRVWPT NTDAARESKP
     RVSLYALMSV EDSFTDFHID FAGSSVFYHV LKGRKSFMFI RPTARNLAAY SQWCLSADQN
     VVFLPDVLSP DSDIYTVHLS PGDTMYIPSG WIHAVHSPQD SLVVGGNFIT PLNMKTQIDI
     AGIEVRTKVP MKFRYPLFAG VMWYYVLQLL ANPERLNTMS TKERDGLNSV AEYLSGFIKT
     MSPTMKDVQY RRFVANFPME IRPFPGKTLL DYCAMLDFYP KGVQETVDID IRKKKGESKE
     KHKIESQLPE EKILQGSKLE SKEEVQTENF
 
 
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