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 03-APR-2013, entry version 12.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); IEA:EC.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
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-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; 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; 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 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 1 879 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
//
