JHD1_KLULA
ID JHD1_KLULA Reviewed; 478 AA.
AC Q6CIC9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=JmjC domain-containing histone demethylation protein 1;
DE EC=1.14.11.27 {ECO:0000250|UniProtKB:P40034};
DE AltName: Full=[Histone-H3]-lysine-36 demethylase 1;
GN Name=JHD1; OrderedLocusNames=KLLA0F27643g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-36'
CC of histone H3, thereby playing a central role in histone code.
CC {ECO:0000250|UniProtKB:P40034}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.27;
CC Evidence={ECO:0000250|UniProtKB:P40034};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The JmjC domain mediates the demethylation activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC {ECO:0000305}.
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DR EMBL; CR382126; CAG99018.1; -; Genomic_DNA.
DR RefSeq; XP_456310.1; XM_456310.1.
DR AlphaFoldDB; Q6CIC9; -.
DR SMR; Q6CIC9; -.
DR STRING; 28985.XP_456310.1; -.
DR EnsemblFungi; CAG99018; CAG99018; KLLA0_F27643g.
DR GeneID; 2894869; -.
DR KEGG; kla:KLLA0_F27643g; -.
DR eggNOG; KOG1633; Eukaryota.
DR HOGENOM; CLU_003540_6_2_1; -.
DR InParanoid; Q6CIC9; -.
DR OMA; MSVGNAY; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140680; F:histone H3-di/monomethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IEA:EnsemblFungi.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..478
FT /note="JmjC domain-containing histone demethylation protein
FT 1"
FT /id="PRO_0000226798"
FT DOMAIN 242..401
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 6..70
FT /note="PHD-type"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 299
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 478 AA; 54963 MW; F282BD749A1F1EF2 CRC64;
MTSGTVKCHF CKKDDSEDKG QPIWVGCEFC DGWCHLTCVP IQFVVPKLEN PSQLLAFKEK
HVESFKCTLH DESKCALLKL NGVSVGTEDI AFTKRNRLRN KRPIDYIALN EGNDKRLKHE
HPHTQAFLAC FEKWKDPKAI SSSELESDFQ IIKVPLRVSD PADSGMYVIS ANELGLVDSK
DHVKLNVEYL TKIMGDDYPL DVMDVQTQMN EKWTLSQWNE YYSHTSPSDR DRIRNVISLE
VSHVESFKDG IRRPNAVNNN DLVDIVWNFG RTETDIERPK VTKYILMSVG NAYTDFHLDF
AGTSVYYNVI SGSKKFILFP PTDYNLKKYR EWCDNDNQND IFLGDQLEAG IAMELTEGNL
FMIPCGYIHA VYTPEDSFIV GGNFLTLRDI TTQLNVVEIE HQTKVPKKFT FPQFESVMGK
TCEWLLNSDH IQSISSEDIE NLVKYLSSSN IKYKPINYQS KKELITELKN KIIKFEHT
