ID   JHD1_USTMA              Reviewed;         669 AA.
AC   Q4P5U1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
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=UM04522;
OS   Ustilago maydis (Smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=5270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T.,
RA   Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O.,
RA   Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J.,
RA   Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.,
RA   Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W.,
RA   Guzman P., Farman M.L., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U.,
RA   Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W.,
RA   Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K.,
RA   Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen
RT   Ustilago maydis.";
RL   Nature 444:97-101(2006).
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; AACP01000161; EAK85404.1; -; Genomic_DNA.
DR   RefSeq; XP_760669.1; -.
DR   GeneID; 3632625; -.
DR   KEGG; uma:UM04522.1; -.
DR   BRENDA; 1.14.11.27; 2320.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR013129; TF_JmjC.
DR   InterPro; IPR003347; TF_JmjC_AAH.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
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; 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    669       JmjC domain-containing histone
FT                                demethylation protein 1.
FT                                /FTId=PRO_0000226799.
FT   DOMAIN      332    494       JmjC.
FT   ZN_FING      65    126       PHD-type.
FT   METAL       390    390       Iron; catalytic (By similarity).
FT   METAL       392    392       Iron; catalytic (By similarity).
FT   METAL       462    462       Iron; catalytic (By similarity).
FT   BINDING     407    407       Substrate (By similarity).
SQ   SEQUENCE   669 AA;  74838 MW;  D8C8BAB766646282 CRC64;
     MTAVAASSRV SDPLAASSSA HPRTLRSSPR KRTTSHDSSI SPSAAQSKQL PRRKKPRTEL
     VDESELDCAA CPAVGQPAPT PGKGAASDRE TWICCTHCKT WFHCICIGLE NPDDFSKWYC
     QPCITRSEQT FESGTSSSHP PFANVVRPPR RKSERAKLQI DYAAIQEGIP ADPLGRWKNL
     LNAYEFEPDQ FRRMQGHEWT FDWLLHDESA LKQPVLVPAP PDRSSQAPHV QAKAEDVAAS
     PVPRPKPARA KKQATHRLVP CHTSIPGMVV PPPEMSIFDV ADIIGHDTPV EVIDVASQSS
     SKASWTISEW AEYFNTPKEK KKKTLNVISL EVTGTPMQAY VEAPQLVRDL DWVTRDWPAE
     RRDASCSENS WPKVQRYVLM GVEGAYSDWH IDFAGSSVYY HVIWGQKTFL FAPPTARNLA
     AYKAWCSSTR QDFDWLGDHL HSLTRVDIGP GETMLIPSGW LHCVYTPKNT LVVGGNFLTD
     WNVATQWKLV EIEEATKVPR KFRFPHLKRL SWFVAKGWND RLEPLAEFET LTKEEDQVLE
     ESAQVSAQVD VGSLTEVVPP LKVLNNIELV LQSLSDDLEL IQDPYVAESG DERKVKQQKA
     AREAIPTHHV GNIQKAEAML ASLRQRVDRA KSLADAVQSE RVCLTWEATR AKKAKAANGS
     AIKSRKARR
//