ID   JHD1_CANAL              Reviewed;         478 AA.
AC   Q5A847;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-NOV-2008, entry version 28.
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; ORFNames=CaO19.3281, CaO19.10791;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(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.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
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DR   EMBL; AACQ01000049; EAK98956.1; -; Genomic_DNA.
DR   EMBL; AACQ01000048; EAK99023.1; -; Genomic_DNA.
DR   RefSeq; XP_717905.1; -.
DR   RefSeq; XP_717971.1; -.
DR   GeneID; 3640438; -.
DR   GeneID; 3640450; -.
DR   KEGG; cal:CaO19.10791; -.
DR   KEGG; cal:CaO19.3281; -.
DR   CGD; CAL0003411; orf19.3281.
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:0005515; F:protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR013129; TF_JmjC.
DR   InterPro; IPR003347; TF_JmjC_AAH.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00249; PHD; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW   Oxidoreductase; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    478       JmjC domain-containing histone
FT                                demethylation protein 1.
FT                                /FTId=PRO_0000226793.
FT   DOMAIN      217    383       JmjC.
FT   ZN_FING       5     68       PHD-type.
FT   METAL       269    269       Iron; catalytic (By similarity).
FT   METAL       271    271       Iron; catalytic (By similarity).
FT   METAL       351    351       Iron; catalytic (By similarity).
FT   BINDING     266    266       Substrate (By similarity).
FT   BINDING     286    286       Substrate (By similarity).
SQ   SEQUENCE   478 AA;  55460 MW;  5DA6D1654795CF5D CRC64;
     MPINSESCPL CKVHSNTIKK EDEDEEDNKT SWIQCSKCKV WYHVHCLDLP TDEIDQIVIY
     HCPECVPKYG ESTYKRKSKR ARVSIDYQSL NEGDTFAIDK SSHFHLHNFL NFKGETNINV
     IDKLTKTYAL NTQMEKPILI PQADLSKNGM QLPIEKNEIT IDYITDCCGE DTPLEVMDVI
     SQQGISPPWK LKQWREYFKT NEEKRDRIRN VISLEISDVA KLGVDFTRPK CVRDMDVVDR
     VWIEEDEQKR SKVTKYCLMS VKNSFTDFHI DFGGTSVYYT VLSGAKTFLF FPPTDNNLEL
     YKSWCLEPSQ NFIWYPEYTI TKNKKKIKPT GGFKVDLQPG DLFIIPSGWI HAVHTPQDSI
     VIGGNYLTIR DMVMQLKINE IERETKVPTK FRFPMFNKVL WLTAWYYYNH QNEFQSDIGE
     DEDGNAILTR LIGHLQGHLE LSKTNATAKR SIPKTIGKPM VFINKLLAWK EDLYGTAV
//