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Database: UniProt
Entry: P0CO41
LinkDB: P0CO41
Original site: P0CO41 
ID   JHD1_CRYNB              Reviewed;         879 AA.
AC   P0CO41; Q55NZ6; Q5KEG2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   19-FEB-2014, entry version 15.
DE   RecName: Full=JmjC domain-containing histone demethylation protein 1;
DE            EC=1.14.11.27;
DE   AltName: Full=[Histone-H3]-lysine-36 demethylase 1;
GN   Name=JHD1; OrderedLocusNames=CNBG4160;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Tremellales; Tremellaceae; Filobasidiella;
OC   Filobasidiella/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.,
RA   D'Souza C.A., Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J.,
RA   Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I.,
RA   Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E.,
RA   Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L.,
RA   Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A.,
RA   Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R.,
RA   Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W.,
RA   Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen
RT   Cryptococcus neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-
CC       36' of histone H3, thereby playing a central role in histone code
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein N(6),N(6)-dimethyl-L-lysine + 2-
CC       oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate +
CC       formaldehyde + CO(2).
CC   -!- CATALYTIC ACTIVITY: Protein N(6)-methyl-L-lysine + 2-oxoglutarate
CC       + O(2) = protein L-lysine + succinate + formaldehyde + CO(2).
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- DOMAIN: The JmjC domain mediates the demethylation activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC   -!- SIMILARITY: Contains 1 JmjC domain.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
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DR   EMBL; AAEY01000039; EAL19469.1; -; Genomic_DNA.
DR   RefSeq; XP_774116.1; XM_769023.1.
DR   GeneID; 4937452; -.
DR   KEGG; cnb:CNBG4160; -.
DR   KO; K10276; -.
DR   OrthoDB; EOG73NGDR; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0070544; P:histone H3-K36 demethylation; IEA:GOC.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF02373; JmjC; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Complete proteome; Dioxygenase; Iron;
KW   Metal-binding; Nucleus; Oxidoreductase; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    879       JmjC domain-containing histone
FT                                demethylation protein 1.
FT                                /FTId=PRO_0000410125.
FT   DOMAIN      416    598       JmjC.
FT   ZN_FING      23    116       PHD-type.
FT   METAL       475    475       Iron; catalytic (By similarity).
FT   METAL       477    477       Iron; catalytic (By similarity).
FT   METAL       566    566       Iron; catalytic (By similarity).
FT   BINDING     472    472       Substrate (By similarity).
FT   BINDING     492    492       Substrate (By similarity).
SQ   SEQUENCE   879 AA;  98215 MW;  20A94315BF25D2BF CRC64;
     MSEQVGQREA VDSPQATGVK TPPEPCPLCR ETGPPQPPSI TEEGKTNEDI DFIWVACNKC
     DEWYHSACLF LGDEKWRGTI PKEIISTVET NFGDEGAWTN WVEWIGKWYC APCLARSTSP
     SNPRPPRHPL VATMKRASIQ PKDIDQAGKP LKRSASTSAP LLKSNIKRPR TSTKGQETAS
     PEIDMKSERE QQAESTAGTP ASDAPQGRPK RKTAQIDYRN LNNSIATPTH QWLELIADPE
     KYGRTILDAN YPALPGKLLT RAWLESQPLP GQPSSISPDL LPTRFWGPDR EPLIVRPENG
     GFSSLGGHLP SKDLTVQDVA NLVGPDRMVD VIDVSSQHSS QWTLQKWAEY IQSSSGNTSV
     RNPKVYNVIS LEISGTELAK KVKPPKIVRE IDWVDNFWRF SAGAGGKDVK EKGRGNDSRE
     SSEIRKEGSH LTEGDNAGGE IEEDLEGLKE KTNTPYPKVQ LYCLMGMKGA WTDWHVDFAA
     SSVYYTIHSG AKVKLSCFVS FFSPGSYHSQ VFFFVKPTEQ NLKAYAEWSG SYEKQQDTWL
     GDMVDEVRKV ELHAGDTMII PTGYIHAVYT PMDSIVFGGN FLHSYNVDTQ LRLRQIEIDT
     KVPQRFRFPM FDRLCWYVAD KYCSDLRHLR AYRPRATTTP KPPHFRVLQC LSYLANFLVS
     QTGILEDPEA EDKARKLVHD RIPGDIVKDP EGLAKELKWR VERELGALGL LGEEASGVEA
     EEFKSNGTAN GSVKIKGKEV SRKRDRLSKV FDKKAISRTW DFHPPAWSEN RQSPQIETTT
     VQLPRPSTSS SDAISGSGPG ASPGASANGG ANENEQAELT TMLVKQTRKR MRELDDGTVI
     EESQETTFVE KKTVWGPKLD KEKISQPQGK VEEDMDIDH
//
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