JHD1_USTMA
ID JHD1_USTMA Reviewed; 669 AA.
AC Q4P5U1; A0A0D1CKW7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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; ORFNames=UMAG_04522;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., 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., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003152; KIS67423.1; -; Genomic_DNA.
DR RefSeq; XP_011390848.1; XM_011392546.1.
DR AlphaFoldDB; Q4P5U1; -.
DR SMR; Q4P5U1; -.
DR STRING; 5270.UM04522P0; -.
DR PRIDE; Q4P5U1; -.
DR EnsemblFungi; KIS67423; KIS67423; UMAG_04522.
DR GeneID; 23564680; -.
DR KEGG; uma:UMAG_04522; -.
DR VEuPathDB; FungiDB:UMAG_04522; -.
DR eggNOG; KOG1633; Eukaryota.
DR HOGENOM; CLU_413428_0_0_1; -.
DR InParanoid; Q4P5U1; -.
DR OMA; DWVTRDW; -.
DR OrthoDB; 1384737at2759; -.
DR Proteomes; UP000000561; Chromosome 13.
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 InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR Pfam; PF17811; JHD; 1.
DR SMART; SM00558; JmjC; 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..669
FT /note="JmjC domain-containing histone demethylation protein
FT 1"
FT /id="PRO_0000226799"
FT DOMAIN 332..494
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 65..126
FT /note="PHD-type"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 390
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 392
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
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
