ID A0A9P5CY75_9EURO Unreviewed; 1318 AA.
AC A0A9P5CY75;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
GN ORFNames=GY632_2102 {ECO:0000313|EMBL:KAF3897757.1};
OS Trichophyton interdigitale.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=101480 {ECO:0000313|EMBL:KAF3897757.1, ECO:0000313|Proteomes:UP000749309};
RN [1] {ECO:0000313|EMBL:KAF3897757.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCMS-IGIB-CI14 {ECO:0000313|EMBL:KAF3897757.1};
RA Kumar P.;
RT "Whole Genome Sequence of Trichophyton interdigitale from India.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 2-
CC oxoglutarate + 2 O2 = N(6)-methyl-L-lysyl(9)-[histone H3] + 2
CC formaldehyde + 2 succinate + 2 CO2; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.66; Evidence={ECO:0000256|ARBA:ARBA00049349};
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF3897757.1}.
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DR EMBL; JAAQVJ010000047; KAF3897757.1; -; Genomic_DNA.
DR Proteomes; UP000749309; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0051864; F:histone H3K36 demethylase activity; IEA:TreeGrafter.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter.
DR CDD; cd15571; ePHD; 1.
DR FunFam; 2.60.120.650:FF:000024; Putative jumonji family transcription factor; 1.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR055500; DUF7072.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694:SF7; [HISTONE H3]-TRIMETHYL-L-LYSINE(9) DEMETHYLASE; 1.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF23258; DUF7072; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 66..107
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 323..486
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 563..670
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1318 AA; 146896 MW; 8C3209406DB70384 CRC64;
MSEQHSVPGG NTAASMTPPA SADGEKMHLH GINSCSASPR PSIEDDGTSP ILEDIQPDHY
YEGGRVPVFK PTMDQFRDFR AFIRCIDKYG MKSGIVKVVP PKEWTDSLPA LDEAVKTIRI
KNPIVQEFTG SHGTFTQANI EKQRSYNLPQ WKALSEEISH QPPARRGERR WTQGKTRGTA
KSHGNKGESQ KRKTTSSKRK ASEELPERQD DGQGSKPESP PTPVSPVSKP VKAKSEELSD
GEPLPAPKPK GRQPKSVSAR RKNNRDEQDD YIDEEAFIDF DYRLSSNEEF TAERCEELET
AYWKSLMYNN PMYGADMPGS LFDDAVTSWN VANLPNLLDV LGQKVPGVNT AYVYLGMWKA
TFAWHLEDVD LYSINYIHFG APKQWYSISQ EDLPRFEAAM RSIWPTDSKN CSQFLRHKTY
LISPTVLKSQ YGITANKLVH YEGEFVITFP YGYHSGFNLG YNCAESVNFA TESWLDYARI
AKKCHCETDT VWIDVEEIER KLRGETTPEY YDETRSEQYE GASDLLTPPR SVPEKSTRPR
KRKVDGIEPK SKRAKLHLDS PKKPPCVLCP NSMDYEELLP TEGGQAQAHR RCALFIEETS
ILKDDLGREI VCDIDKIPKA RMGLKCLFCR EVKGACFQCV QVEFGETSVV ADDGQEYSVP
AIDLKCKYHR QKRFGSLPSQ TLDMDSKVLE TAIKLKPGDL MQFQADKEIN GAVVLENRPL
ERSLMLKVLP RGDVIELPYR WTLIVKKTNF PPLPPNILPL PAHLSRKPDS RNDSNSSMPS
HGMIFGDTSS SYRWEDFICE QPPFNPDSCT VDLTKPETLW YYIGKTSTDC RAQYTHNVDI
SIHNPRSNFL ESVRTARAPT VPAKALCRPV YNTNAVVSGS PSVTRPLLGS TPTTTMPPAV
QSTRAVSPAK SQASSPQTND GLPVWSPSDA AMKSTMARRL IASITEHANA TAGYTIVNPD
FVVQTLLGDD TSPIPKNGLE KLRTSMSESQ VPVRSLDGTV TYQPLNMEAD DVDHLIRMLR
FAVSSLTSVV NVPEKPKAPE QQQVVAPEPV KVLQPQSQEP AAQSVSGKWA YLELQRRQAP
PVYCSPYAPG FGFSDYAKGE YGLVGTPQLS RKEPLAADYF AKLSPEDQEK IVQACGPVPP
ASENFSTLDG SIIATHGPAN QNLLFSSTET AAPNISAAMV PDSHLHPLSA FDMTLRADSP
ASSFNRVPLH YQSPQEYGSH LDNESSLLPR HLHDHHDLFG DQQANTRFWQ RSVPWNDVDT
PSHDEEHRPF FGPHLRPPGH EYASSDMEFG KGPGSLHSMD MAGFGFDGPD DLLPDPSP
//
