ID A0AAI9ZJA8_9PEZI Unreviewed; 1665 AA.
AC A0AAI9ZJA8;
DT 24-JUL-2024, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2024, sequence version 1.
DT 28-JAN-2026, entry version 6.
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=BDP81DRAFT_452611 {ECO:0000313|EMBL:KAK1625640.1};
OS Colletotrichum phormii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=359342 {ECO:0000313|EMBL:KAK1625640.1, ECO:0000313|Proteomes:UP001243989};
RN [1] {ECO:0000313|EMBL:KAK1625640.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 102054 {ECO:0000313|EMBL:KAK1625640.1};
RG DOE Joint Genome Institute;
RA Baroncelli R., Diaz J.F., Benocci T., Peng M., Battaglia E., Haridas S.,
RA Andreopoulos W., Labutti K., Pangilinan J., Floch G.L., Makela M.R.,
RA Henrissat B., Grigoriev I.V., Crouch J.A., De Vries R.P., Sukno S.A.,
RA Thon M.R.;
RT "Comparative genomics, transcriptomics and evolutionary studies reveal
RT genomic signatures of adaptation to plant cell wall in hemibiotrophic
RT fungi.";
RL Submitted (JUN-2021) 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:KAK1625640.1}.
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DR EMBL; JAHMHQ010000019; KAK1625640.1; -; Genomic_DNA.
DR RefSeq; XP_060441635.1; XM_060592762.1.
DR GeneID; 85477624; -.
DR Proteomes; UP001243989; 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:UP001243989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 103..144
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 390..553
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 641..764
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1376..1645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..69
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..261
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..303
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..598
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1214
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1277
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1355
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1399
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1456
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1562..1571
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1572..1584
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1625
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1665 AA; 184091 MW; 54535A37D12BB9C3 CRC64;
MSTDAVSAPV SEPAPVPAQS TTGDHDEEPT LGQIECAKPA FLHSPPDSNN APKSEPSDSE
LSDLDDDAVD PSAAPTIQDE APPPPPPEDD IGEVLPDHWS GTVPVFRPTM HQFKDFKLFM
TKVDHYGMKS GIVKIIPPPE WKENLPRLDD LVKQIRVREP IKQDIMGSNG TYRQVNILHQ
RSYNLPQWRQ LCDQSEHQPP ARRGERRANV EKPKPRSAPK PRIEAKSNPA GSRKRGRGRP
RRGKAKGKNQ DDEDDAQEEQ EEEKRPMTPV SPKPAVDADV KVKKEEVVNS VEDPGMDVDE
DEPPTVGRMG RMGGARQAKP KTQTVSARRK YSKREGSAMI DEKAFEDFDY QMDVSDYTPE
RCEELERIYW KTLTYAPPLY GADLMGTLFD ESTEMWNLNK LPNLLDVLGT KVPGVNTAYL
YLGMWKATFA WHLEDVDLYS INYLHFGAPK QWYSISQADA RRFEAAMKNI WPTDAKACDQ
FLRHKGFLIS PSHLKQHYNI TVNKCVSYPG EFVVTYPYGY HSGYNLGYNC AEAVNFALDS
WLPMGKIAKR CECAQAQDSV WVDVYDIERK LRGEPTPEYE ETDEEDDEDD DEEDEDDATG
LPSPPDSNGI KSARKQKRAA RDKEGKAKTK RIRLKVKTRA EPTCCLCPSD IPGAEVLPTD
DGRKAHRMCA LYLPETYIDT VDGKEVIANV ANINKERLDL KCLYCRSKKG ACFQCSQKKC
ARAYHATCAA AAGVFVEEAE VPVFGEDGTE YKEQAFEFSC RFHRTKRDRK HTGDSLEDDV
RIREAAAALT KGDICQLQYF KGDIFAGVMV ENRADEQMFL LDIIPNGDRL EVEWKWLLLP
DPSDYHLPKA SSKAIPMPSS QKAKDQLNAK RPADEIPRKD APFVEGYTWA EFHPCNDCSN
PNQTKVDLSK DSQVWHYLGK TSTEAKAQYS DDPVKQLHNP KSNFLDTIPK PPKPVSASTS
HRRVSAIPPQ PAPLPMFAPG VAVQNGPKSE KPYVYKPRKP VETNYAGTGS FTTQKFTPKA
SAPPTPGGQQ LHFGSDPRYP IPGTQFVQEK FAPDVHQQYV PRPAPAGQGY YPPPNTMQRP
SPYSTPGPQP VLGARPAPQT WSTPSQNPRP PLPHSTSQGS TQQNHRRYSA APTPSVAMKY
AFFQVHHNRD SKTYRTPYAP WGGFTNGYEG NLRAHLMRTS PEAFFKNRQG SVQGGTPTPA
PNAGPQGPAY GGPYHNTLTN VMPQGSIGMY GVKTAAPYSS PVPQNPQNHA RTPSCSSISL
SPAPSGSQPS SHGQSQGWHA QQPQLAPLHP AIRRQYGSWA NQPQQQHPQH PQPAQQQPSQ
QPVPQQTPQQ SPASQSQPSQ AKPQSAAKPA APKVQYKIPE KQTPVPLPAK YLAAMSKMPS
AATPSKASSK STGASAQSTN LSPASGLGKG ATQATSMAAV NGSSPQTTSP LQGAPTSAGP
TTATAPPVAQ APVSVPHTPV PASNSRMPFT AQSITTAFPR QPTQPQPQVY NTPSTQPFPP
ASRPRTEHLN PAEILAQIAT TPRMNPPTPT APSHQSMPSP VPPQTTAMPG YQNHGSNWGP
TQQQQQQQQQ QQPPPQVWAP PPGQWQPQHH QQYHQHPPPQ QYQQLYQQQH PQPRPQQQHH
MQAQPPYLPP PQAPEGDMPL PEVPADSTAL VERMMQNLRR AAFQG
//
