ID A0AAE0D585_COLKA Unreviewed; 1634 AA.
AC A0AAE0D585;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
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=CKAH01_05861 {ECO:0000313|EMBL:KAK2756340.1};
OS Colletotrichum kahawae (Coffee berry disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=34407 {ECO:0000313|EMBL:KAK2756340.1, ECO:0000313|Proteomes:UP001281614};
RN [1] {ECO:0000313|EMBL:KAK2756340.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CIFC_Que2 {ECO:0000313|EMBL:KAK2756340.1};
RA Baroncelli R.;
RT "Colletotrichum kahawae CIFC_Que2 genome sequencing and assembly.";
RL Submitted (FEB-2023) 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:KAK2756340.1}.
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DR EMBL; VYYT01000211; KAK2756340.1; -; Genomic_DNA.
DR Proteomes; UP001281614; 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; IPR001965; Znf_PHD.
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 SMART; SM00249; PHD; 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 Reference proteome {ECO:0000313|Proteomes:UP001281614};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 96..137
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 375..538
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 625..748
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..67
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..238
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..581
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1209
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1327
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1442
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1532
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1595
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1634 AA; 181154 MW; B14D3F18EC6F33EF CRC64;
MSTDAVSAPV PEPAPVPAQS TADGDKEEPT IECATKPAFL HSPPDSNNAP KSDGSDSELS
DLDDDAVEAP PKQDEAQPEV EDDIGEVLPD HWSGTVPVFK PTMHQFKDFK LFMTKVDKYG
MKSGIIKIIP PSEWKENLPK LDDLVKQIRV REPIKQDIMG SNGTYRQVNI VHGRSYNLPQ
WRQLCDQSEH QPPARRGERR ANVEKPKPRS APRPRPATRS TPSGSKKRGR GRPARGKAKI
QEEEEANEEG NRPMTPVSPK ADAEVEIKKE EVVDSVEDPG MDVDEDEPRP VGRMGRMGGI
KPSKPKTQSV SARRKYSRRE GSAMIDEEAF KDFNYQMDVS DYTPERCEEL ERIYWKTLTY
APPLYGADLM GTLFDESTEM WNLNKLPNLL DVLGTKVPGV NTAYLYLGMW KATFAWHLED
VDLYSINYLH FGAPKQWYSI SQADARRFEA AMKNIWPTDA KACDQFLRHK GFLISPSHLK
QHYNITVNKC VSYPGEFVVT YPYGYHSGYN LGYNCAEAVN FALESWLPMG KIAKRCECAQ
AQDSVWVDVY DIERKLRGEE TEYEETDEDE DDEDEDEDED ASGLLSPPNG NTVVIKTSRK
RKRAGDKGGK IKVKKIRLKV KTRAEPICCL CPSDIPGAEI LPTDDGRKAH RMCALYLPET
YIDTVDDKEI IANVANINKE RLDLKCLYCR SKKGACFQCS QKKCARAYHA TCAAAAGVFV
EEAEVPVFGE DGTEYKEQAF EFSCRFHRTK RDRKFDGDSL EEDERIRKAA AALKKGEICQ
LQYYKVDIFA GVVVENRADE QMLLLDIIPN GYGSPVRFER KRLTCDSDRL EVEWKWLLLP
DPSDYHLPKA SAKAIPMPSS QKAKDKLNAK RPADEVPRKD APFVEGYTWA EFHPYNECAN
PNQVKIDLSK DNQVWHYLGK TSTEAKAQYS EDPAKEQHNP KSNYLGTIPK PPKPVSATAA
QRRPSSIPPQ PIPMASPSVA IQSGLKTEKP YVYKPRKPVE PSYAGPGAFT TQKFTPKASP
SPSPMGQQLY FGSDPRYQMQ QGHYAQQRFT PNIHQPYNPA SPGQYAVSSN MQRQSPYGTP
VQQPGGSAKP TQQMWATPSQ SPIPQPPPAG YSQAPTPQNH RRYSAAPSPS VAMKYAFFQV
HHNRASKTYR TPYAPWGGFT NGYEGNLRAH LMRTSPEAFF KNNRQGSVPS ASPAPSSAGR
PPAPAHSSPY YNTFTTAAPQ GSIGVYGQKT TASSYSSPGP RPTHDPARTQ YTSMSPSPVP
NGSQPSPHGY NNAWNSQQQP PSTPLHPAIR PQYGAWMNQP QQPQPHNQAT PPDHHQQAQQ
QQQTPRQPAD PQPPAGHAQS AEKKAEAASK PAAPKVQYKI PEKQTPVPLP AKYLAAMGKM
APTPTKACPQ SNGTPSQDKS TPSSAPANST RTPQVAGTQN SSAQASSPSR PSTSSKKASP
PVSQTPVPLP QTAVPAPPQR MPFTNQFSAS RPSQPPYQPQ TQAHTGQPNP RPLQPVGQPH
TEHHSLNPAE ILAQIATQPR MNPPTPTTPH QPMPSAAPQQ TPVPHYYAGQ QMPQAHNGMM
PQQQHFQHYA PASQSQYPPP QPQYAHQYPP QYTAPSYPPQ SAPAGDVPLP EVPADSTALV
ERMMQNLRRA ASNG
//
