ID JHD1_EMENI Reviewed; 1407 AA. AC Q5AW75; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 1. DT 16-JUN-2009, entry version 30. 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=AN7455; OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC 4; RX PubMed=16372000; DOI=10.1038/nature04341; RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., RA Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., RA Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., RA Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C., RA Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., RA Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., RA Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., RA Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., RA Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.; RT "Sequencing of Aspergillus nidulans and comparative analysis with A. RT fumigatus and A. oryzae."; RL Nature 438:1105-1115(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; AACD01000129; EAA62035.1; -; Genomic_DNA. DR RefSeq; XP_680724.1; -. DR GeneID; 2869726; -. DR KEGG; ani:AN7455.2; -. DR BRENDA; 1.14.11.27; 3859. 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; 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 1407 JmjC domain-containing histone FT demethylation protein 1. FT /FTId=PRO_0000226797. FT DOMAIN 577 735 JmjC. FT ZN_FING 323 382 PHD-type. FT METAL 631 631 Iron; catalytic (By similarity). FT METAL 633 633 Iron; catalytic (By similarity). FT METAL 703 703 Iron; catalytic (By similarity). FT BINDING 628 628 Substrate (By similarity). FT BINDING 648 648 Substrate (By similarity). SQ SEQUENCE 1407 AA; 156107 MW; CE85B1C78A76A2D0 CRC64; MISATSFVTA IGSRPPRYRT PSPPRRAVEP ISPCSTADYR TYRASREISA SATSDHVRST PTDKRPSPAD VPASHRSGHG RSSSTIDTLA TIALATSPTF TPLTHRPPSD KSNTTLSMFP PETEPVERPA KRPRSERDES SYTQHRSNAF SIARPPAISD SMKTDAELLL NFARPTNLYP PIPSSKRANT DDSYHNHTFH TQAQIKERNA STYWVTNHEN VIFNHSAMHN IPPSRMRSQS DGSAAISRPV IEGLRPNTSS STLPPLAFQE EADSGDRHWD MERKPVLEES QVDFCKPDET VPILSQSQPL KKELDADSNG SSQASCATCN LVRIPVDNED QDVTWISCDG CKRWFHIVCA GFKNDRETRT VDKFICKTCR PIHGQTTFVR KSSRVRTSID YAGLNQGLVK SATDSLEHHY IEPIKQNKIR FLPENFPRMR PELVTAEYFE KGNGMTEPIV IPAEFNTHAT IPPTNPEFDA LVQDAPSQEM FDELLDHLPN VDHETVIDCG QNQLDMVIPQ GLTVRTVSEL YGPEERVEVI DVKSQHGEDK RWTMQKWADY YESTGDKVVR NVISLEVSQS KLGRLIRRPK IVRDLDLQDA VWPEELKAVG NFPKVQFYCL MSVADCYTDF HIDFGGSSVY YHILKGKKTF FFIPPKDKHL KKYEEWCNSP AQDYTFLGDQ TKECYRVDLS EGDTMLIPSG WIHAVWTPEN SLVIGGNFLT RLNYGMQIKI AKIEKETKVP MKFRYPFFQK IQWYAVLKYL EEDPVPQSVL AAFSQDENYR FHRKYPIYYE FGERANTEPK GSPYHNSRFY SQAELEGLPD LAKYLLRTAL IAGSYLVEGV TADTRNAVKR SIPAMPGEPI DVIRTFGVWI AWKRGNEKAA HWTRPGVVES NAKLSLAEKR PAGRPSRRSE RNADNQRTYA ERQAVQRLSE RPAVDIQKDS APGDESVAPL ANNSPPAATS GIPVPVMNED TSQKHKTASR GSGLGPKRVA CDACRKRRIR CHHKEENNGA SGSQMTVSTS SLGHHTPTAQ DAASALNSLA AIASGAGFQN GLHSIKGMDR MDASANFATS ISATPHGVTL KVGDGSPDGL NSAKKGRSKA CDDCRKSKRR CIHDEYGRID PIKAQERSKP RATSLAKRPR VHEEAAPSSA NKRLKQESTS PVAQPVHSSH MDTETPTRAQ DSVENGVLDQ YPRKSNTQHA DGLPAEKALL PDQSSYASPP AFQADAVATK ELPATVSKPA AVLVSPPTSL ADEMDIHDQV DAGGEHVSVI YTPSSGSRQS SRQPRQVERY MPEVHFAKTA KSTTTTPQTT RRSSFGSSGR KTTPGLSSGS KKSGSRPSSS HGKKSLSPSV EKKAERHAIS SAPFGQHGRG SKSEHGTSDV DPDAESLRLI REIQEQEFGL RRRAGRA //