JHD1_CRYNJ
ID JHD1_CRYNJ Reviewed; 879 AA.
AC P0CO40; Q55NZ6; Q5KEG2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
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=CNG00620;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
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., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW44468.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AE017347; AAW44468.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_571775.1; XM_571775.1.
DR AlphaFoldDB; P0CO40; -.
DR SMR; P0CO40; -.
DR STRING; 5207.AAW44468; -.
DR PaxDb; P0CO40; -.
DR eggNOG; KOG1633; Eukaryota.
DR InParanoid; P0CO40; -.
DR OrthoDB; 1384737at2759; -.
DR Proteomes; UP000002149; Chromosome 7.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
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:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 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..879
FT /note="JmjC domain-containing histone demethylation protein
FT 1"
FT /id="PRO_0000226795"
FT DOMAIN 416..598
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 23..116
FT /note="PHD-type"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 477
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 492
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 566
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 879 AA; 98240 MW; 2FF7F5CE7547B6EA 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 NAGAGGKDVK EKGRGNDSRE
GSEIRKEGSH LTEGDNAGGE IEEDLEGLKE KTNTPYPKVQ LYCLMGMKGA WTDWHVDFAA
SSVYYTIHSG AKVKLSCFVS FFSPGSYHSQ VFFFVKPTEQ NLKAYAEWSG SYEKQQDTWL
GDMVDEVRKV ELHAGDTMII PTGYIHAVYT PMDSIVFGGN FLHSYNVDTQ LRLRQIEIDT
KVPQRFRFPM FDRLCWYVAE KYCSDLRHLR AYRPRATTTP KPPHFRVLQC LSYLANFLVS
QTGILEDPEA EDKARKLVHD RIPGDIVKDP EGLAKELKWR VERELGALGL LGEEASGVEA
EEFKSNGTAN GSVKIKGKEV SRKRDRLSKV FDKKAISRTW DFHPPAWSEN RQSPQIETTT
VQLPRPSTSS SDAISGSGPG ASPGASANGG ANENEQAELT TMLVKQTRKR MRELDDGTVI
EESQETTFVE KKTIWGPKLD KEKISQPQGK VEEDMDIDH
