ID A0A0N1H6Q5_9EURO Unreviewed; 1451 AA.
AC A0A0N1H6Q5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 02-APR-2025, entry version 33.
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=AB675_5445 {ECO:0000313|EMBL:KPI41813.1};
OS Cyphellophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI41813.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI41813.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI41813.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-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}.
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:KPI41813.1}.
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DR EMBL; LFJN01000008; KPI41813.1; -; Genomic_DNA.
DR RefSeq; XP_018001776.1; XM_018145656.1.
DR STRING; 1664694.A0A0N1H6Q5; -.
DR GeneID; 28737536; -.
DR VEuPathDB; FungiDB:AB675_5445; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000038010; 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:UP000038010};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 83..124
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 369..532
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 615..737
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..66
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..285
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..571
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..593
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1275
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1353
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1451 AA; 162473 MW; C4745EFEFD3BA4D8 CRC64;
MAATMATPSV EAELPAMNKH DLSSDLPTTQ VHTPPITDEA SHKESDDAAS SSSLSELGDD
IGDILDDENR MRFEEAARAG AEAEESSETM DEFRDFEKYV QGVNPYGMQS GIVLIDPPEE
WKRDRKPLDE QIKNVKIKNP ITQEFHGAQG IYTQRNMEKM RSYNIPQWRS LCESTENQPP
ARRGEKRMNA DKLLGRGSVK NKKTEGSPAP SVNGKRRGRP PKNTPVKKEP ADESNINAPL
TPTSPELQPA EKANAEEEDA EQTPEPTTGK RKPGRKPAAK PRGRQPKSAT KRETGGKASE
TTVAARRLRT AGATVDEIDE EAFRDFDYRV YDNDQWTAER CDELEDKYWK SLNFSNPMYG
ADMAGSLFDD QTKEWNVAKL PNLLDLIGAP IPGVNTAYLY LGMWRATFAW HLEDVDLYSI
NYIHFGAPKQ WYSISQKDAP KFENAMKSIW GEDAKTCDQF LRHKTYLVSP AILKSKYGVT
VNKIVHREGQ FIITFPIGYH SGYNLGYNCA ESVNFAIPDW LQYGKTARKC QCEGDSVFID
VDWFIRRMNG EPSPEYEEVE ITDDEDEDEL IDLPTPPGSD RGKIKLSSKR KRATKDVGPN
KKARKMIKIR KVSKHQPCCL CPNDFAWEEL LPTSNGQKAH RTCAMYTPET YIATVDGKEV
ISNVENISKA RLELKCYECR QKKGSCFQCS SAKCTKSYHA TCAMQAGVQV DKGEIAVWHE
GVEYRDIGFD WRCRLHRSVK RTRITSELST CNHLNNCWNK PEFVQYIKSL KAGDLVQWQI
THSDEIEAGM IMTGYDEEQE GMLVKVLPDV RVVKEIQPSW ILFIDSETSC LQKPSANARD
LPEELQGKSA QFPDSERKPS EGDTFTEDPK TEWAEFSSVA LPHNKLQKKV DLTKPKQLWL
YLGESSTESK AYYTGDPARK IHDPASQYLD TVEPARALMA PPSQPKRQSL AASFPANLQN
HTNNGFVRPR TLSGNHSAGP SQNSMLQNGT QAKNIPQAKN VNRKSSQGCD VIIGAEAKAN
EQARILQRQQ AKAQHLDQQA GLNGGIGIDQ AAVERQKQFQ MNGSQQSQTM WTGYNNTAQY
PAYQNAFNAQ RQVPQYSQQW MNPMPQMRPG SSHNQHSPHL SQPNGGQFPA YVQQSHQQFP
YNSQHQRTQS TPVSDTERIR QETARIESIR AAANRPPPPP PSAAIERQRR ISNPAYPFKS
PDQILAQKEA EKNTPPGSRP GSSYQMGSPA TTDAYRPSTS ASMSALGSRP MEFIDPTATQ
ITPPGSSAGR RSASNSLSMM PGTMGPPLQP HLHRTASAGM LERPTFNTSN ASQISNYVPR
RSVYDPLYKA QGPLQPITQP NLPPPLPQPP MAEPSPVLLA SLQPRSTSPG GYPLNDRAVP
EQLVKWKAQG GFWAKVATYY INKHVASASA YRSPFADLHN TPWRLAEQYY QSLDFEGRAK
VDDYRNNGMR N
//
