ID   JHD1_CANGA              Reviewed;         403 AA.
AC   Q6FPL6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   04-NOV-2008, entry version 27.
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=CAGL0J02860g;
OS   Candida glabrata (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5478;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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.
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DR   EMBL; CR380956; CAG60777.1; -; Genomic_DNA.
DR   RefSeq; XP_447828.1; -.
DR   GeneID; 2889738; -.
DR   KEGG; cgr:CAGL0J02860g; -.
DR   HOGENOM; Q6FPL6; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR003347; TF_JmjC_AAH.
DR   SMART; SM00558; JmjC; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Complete proteome; Dioxygenase; Iron;
KW   Metal-binding; Nucleus; Oxidoreductase; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    403       JmjC domain-containing histone
FT                                demethylation protein 1.
FT                                /FTId=PRO_0000226794.
FT   DOMAIN      141    328       JmjC.
FT   METAL       224    224       Iron; catalytic (By similarity).
FT   METAL       226    226       Iron; catalytic (By similarity).
FT   METAL       296    296       Iron; catalytic (By similarity).
FT   BINDING     221    221       Substrate (By similarity).
FT   BINDING     241    241       Substrate (By similarity).
SQ   SEQUENCE   403 AA;  47030 MW;  F327A0D7EB1217BD CRC64;
     MAVKIEQALG EKRSLNDNDE VPRKKRYNFR KKVELDYSAL NEGEDKKSKF FHPHIALFEK
     EFEKCLSNVT EDMSMTCSEY CKRFDDIDFP LKISDPENSG MVVSTNNKTT RDLTVDDITQ
     AVGDDYFVNV MDVQSQENER WSLREWCNYF NKPAEEKDRI RNVISLEVSH VEDLQYDRPD
     IVDDKDLVDI VWNNVENLDT ENDPRPKVTK YCLMSVKNAF TDYHLDFAGT SVYYNLAFGK
     KKFILYPPTP ENIENYIEWS TSTYQNMLFL GEKLTGGVAM ELNGGDLFMI PSGYIHVVYT
     PEDSLIFGGN YLTFRDISQQ LKIVDVEKQT GVTKRYTFPM FDEVMGRTCE WLCQNQKKGK
     QMQVKKETVN DLISYMKSGK TKYKPTNFIN KKQMLQELSN LYL
//