ID A0A0G4KD02_VERLO Unreviewed; 1804 AA.
AC A0A0G4KD02;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 18-JUN-2025, entry version 29.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
DE Flags: Fragment;
GN ORFNames=BN1708_000323 {ECO:0000313|EMBL:CRJ80635.1};
OS Verticillium longisporum (Verticillium dahliae var. longisporum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRJ80635.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRJ80635.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRJ80635.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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}.
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DR EMBL; CVQH01000001; CRJ80635.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4KD02; -.
DR Proteomes; UP000044602; 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:UP000044602};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 169..210
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 451..614
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 702..825
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 73..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1695..1733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1765..1804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..149
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..298
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..309
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..363
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..659
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..680
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1043
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1085
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1232
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1305
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1610..1622
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1627..1659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CRJ80635.1"
FT NON_TER 1804
FT /evidence="ECO:0000313|EMBL:CRJ80635.1"
SQ SEQUENCE 1804 AA; 197462 MW; 402688C0C88D6BA4 CRC64;
CSCRLPSFTT RFTPQPARRA LHQQPASEIQ QLRKGKNTTE AASTFNKSHV VHRIMSTEAP
SALASAPTQV SLAPEAAQTQ TGCTNDVGNT DGHTQDRVAN VEHDAPADHI ECAKPTFLHS
PPDSNNAAKS DGSDSELSEL DDDAVDPADE PPKEDDIGEV EPDHYSGTVP VFRPTMHQFK
DFKRFMEKID HYGMQSGIVK IIPPEEWKNS LPELDDLVKQ VRVREPIKQD IMGSGGTFRQ
VNILHQRSYN VPQWRKLCEQ SEHQPPARRG ERRANADKPK PATRTRAAAS SAPKPRAAPA
KKRGGKRGAK NSGKQKKDAD DVEMEDRPMT PVSPKEDAEE GKIKTEAVVD SVETGDAEEE
EEAAPTVGRM GRMGGARPSK GATQSVSARR KYSKREGSAK IDEEAFKDFD YRMDVSDYTP
ERCEELERAY WKTLTYAPPL YGADLMGTLF DESTDTWNLN KLPNLLDVLG SKVPGVNTAY
LYLGMWKATF AWHLEDVDLY SINYLHFGAP KQWYSISQAD AKRFEAAMKN IWPTDAKACD
QFLRHKGYLI SPQQLKQNYN ITVNKCVSYP GEFVVTYPYG YHSGYNLGYN CAEAVNFALD
SWLPMGKIAK RCQCPQAQDS VWIDVYDIER KLRGEELEYE EYTDDDGDEE EDEDMEEPES
TNAPGSRAVK IKAPSRKRKR DAKDKDEKKV KKIRLRIKAR AEPPCCLCPN DIASAELIPT
NDGRKAHRMC AHYLPETYIE TIDDKEVVCN VANVAKDRLD LKCLFCRSKR GACFQCSQKK
CARAYHATCA AAAGVFVEEA EVSVWGEDGT EYKEQAFEFS CRFHRTKRDK KVDGDSLDDD
ERILNAAKAV KEGEICQLQY FKGDIFAGVV VENRKDERML LVDILPNGAR VEVEWKWLLV
ADPSDYHLPK ASARAIPMPT SQKAKQELNA KRAVDEVPRK DDTFVDGGFT WAEFHTCEPF
HNTGQVKVDL DKDTQLWYYL GKTSTEAKAQ YTESPTLQRH NPRSNYLDTL PKPAKPPKPV
SVTQRRPSQV PQRPSIPGPP RPSPLSTSSV PVPVQGPAQG PAQGPMQGPM QGPMQGPMQG
PMQGPMPMPD LSNTVKTEKP YVYKPRKPID AVWNKTQQFT TQQFAPKMSN SPSPAPNGQQ
PGYGSDPRFV GQQYAQTSQY SQHRFIPSYA PAYNPQTATY GAQGNAPPNY GQPQQQQQQQ
RTWSTPSSMN QPSSYQSGQH NSQQRSQQGQ QGTSYTDSNR PLQMHQYQPV IQQSSTPSQP
AHVSPAHVSP AQYAATQQIA TNSQKQSQQQ SQPFNPAQQQ VQVQHLQQSP ASFTAGQAQT
LVHLSRNPFF LVHFNRASHT AEGIRVPAAH KLARGPGRYH TPYNATQDSG LPTVQQPSRP
PSNPSDHTGR SNTTVPAVTT KNNPFSSPNN PALRAQSQHV QYPVSSGPAA GPSQAYASHG
AAQSHPQTSV LQHYHQQYLA LGLSQPGENA QQSHLNRPGV VDHNNASKAV QPQTQFLNAH
ASSTGFPSNQ TNRITTSAAA PLANPPSTNT HSATPRPELS STSAPVGVPP HVTGFASSTT
PAPMPSPTAV YTGTGASPGI PEKVTPVPLP AMYRAARGKT GPAPTPTPGP TKAAPQAQPQ
TPEVARASTS TLPSPTSNGA LGSTSSAQSP NAQSKTARIS ETPVPLPHQK AANSTPRTKA
SGAMFGHAST TLPTKMVVST PDSTPAQPLD ATPSRPPSQP TQVSNRAAVE TPVPLPRLPG
KVTPVPLPPQ ALQVLSAGNP VSKPSGYTGE AISETPILPP VRAPMATTQT SPEVDDMDRG
LGVH
//
