ID   JHD1_ASHGO              Reviewed;         486 AA.
AC   Q75AL5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-NOV-2008, entry version 39.
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=ADL088W;
OS   Ashbya gossypii (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=33169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient
RT   Saccharomyces cerevisiae genome.";
RL   Science 304:304-307(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; AE016817; AAS51832.1; -; Genomic_DNA.
DR   RefSeq; NP_984008.1; -.
DR   GeneID; 4620150; -.
DR   KEGG; ago:AGOS_ADL088W; -.
DR   NMPDR; fig|33169.1.peg.1653; -.
DR   AGD; ADL088W; -.
DR   HOGENOM; Q75AL5; -.
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; IPR003347; TF_JmjC_AAH.
DR   InterPro; IPR001965; Znf_PHD.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00249; PHD; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS01359; ZF_PHD_1; FALSE_NEG.
DR   PROSITE; PS50016; ZF_PHD_2; FALSE_NEG.
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    486       JmjC domain-containing histone
FT                                demethylation protein 1.
FT                                /FTId=PRO_0000226791.
FT   DOMAIN      245    404       JmjC.
FT   ZN_FING      28     83       PHD-type; degenerate.
FT   METAL       300    300       Iron; catalytic (By similarity).
FT   METAL       302    302       Iron; catalytic (By similarity).
FT   METAL       372    372       Iron; catalytic (By similarity).
FT   BINDING     297    297       Substrate (By similarity).
FT   BINDING     317    317       Substrate (By similarity).
SQ   SEQUENCE   486 AA;  55076 MW;  53A9F8861DCACDC7 CRC64;
     MLQQVTSTTV TGADIQLRAK LLLFSMTDDQ CVYCKGKMEH RMWVQCEACP QWVHVQCIPE
     ECLSGGEYPS RSSDIAAFEC SAHGTARARL ALKGKRRRVE AKEEPERAGT RRYRLRKRGP
     LDYIALNEGQ DVRLRHEHPH RAAFQGCFTK WSGLGRTVTS AELQQSFAEL REPVLVADPE
     HSGMQTPAMD EQVLADVLGA DYSLDVMDVQ SQQNERWTMG QWKEYMHTAR GVRDRIRNVI
     SLEVSHVPEF GQRIRRPRAV EDNDLVDLVW PVQPAPEIGA KPKVQKYVLM SAANAYTDFH
     LDFAGTSVYY SLLRGAKQFL LFPPTPANLG AYKAWCADDN QGLIFLGDRL QDGVLFSLRP
     GDLFMIPSGF IHAVYTPEDS FVVGGNYLCL RDLSTHIRIV RIEQETQVPK KFTFPKFERV
     MGLTAEWLLE GLPERLQLIT HEHAVALLDY LRDTRLKYKP AHYHTKSTML ASLEKALEGC
     EPASGP
//