ID A0A2B7ZUY5_9EURO Unreviewed; 1531 AA.
AC A0A2B7ZUY5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 28-JAN-2026, entry version 23.
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=GX50_00259 {ECO:0000313|EMBL:PGH36802.1};
OS [Emmonsia] crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH36802.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH36802.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH36802.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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:PGH36802.1}.
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DR EMBL; PDND01000003; PGH36802.1; -; Genomic_DNA.
DR STRING; 73230.A0A2B7ZUY5; -.
DR VEuPathDB; FungiDB:EMCG_09026; -.
DR Proteomes; UP000226031; 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:UP000226031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 115..156
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 376..539
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 621..746
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..99
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..315
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..578
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..980
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1006
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1032
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1137
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1355
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1459
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1494
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1531 AA; 169204 MW; 29CCCD40CCAD59B0 CRC64;
MAAEPSVEAI VTMPPRALDK PDDNINNNNN NTTASMTPPA SADGEKISSS SIDHNNTSSA
ASSISSSTSE LSDLDLDSNS NSNSNTTTVP ESTTTTTTIA DDEIHPDHYY GGGKIPVFKP
TMDQFRDFAA FVQKVDSYGM KSGVIKVIPP KEWTDALPSL KEPIKTIRVK NPIMQEFHGS
HGTFTQANIE KQRSYNLPQW KTLCEESSHQ PPARRGERRR NQEKVNRGAA HKSLSRSDSQ
RRKPGPKPKR VEVDKPVEDS SENHVDKSKP ESPPTPVSPE SKPVETKTEV LSDGESLPAP
KPKGRQPKSV SARRKYNRGD AADYIDEEVF KDFDYRLSGL EEFTPERCEE LETAYWKSLM
YNNPMYGADM PGSLFDDSVT SWNVAKLPNL LDVLGQKVPG VNTAYLYLGM WKATFAWHLE
DVDLYSINYI HFGAPKQWYS ISQEDMGKFE AAMKSIWPTD AKNCDQFLRH KTYLISPALL
KSQFGISVNK MVHYEGEFVI TYPYGYHSGF NLGYNCAESV NFATENWLDY ARVAKKCNCE
ADSVWIDIGE IERKLRGEST PEYYDEMGSD QDEMDMDGVS DLLTPPRSVP EKSGTRVKKR
KREGQESKAK RAKLHVGGPK KVRCVLCPNS MDYEELLATE DGKSHAHRRC ATYIEETTIL
KDDSGTEVVC DIDKVPKARL GLKCLFCREI NGACFQCMHG KCTRAYHPTC ALLAGVQVEF
GAIAVMADDG YEYSVPGVDL KCKYHRPKKY AYMQGETLDL DPKLTQAARN IRAGELVQFQ
ADKEINGAVV LENRPTERSV LVKVLPRGDV IELPYRFLLI VKKSSFPPLP AGIKPLPSHL
ARKPDAKKDL ASSLPSPGTP FGDARFVHQW GEFISAKPPL NSSSTQVDLS KPEQIWYYLG
KSSTECRAQY TENPDRSSHN PRSHFLESVK SLNAPVATTH HHQPSYARNY PSSPFARHPT
APQRPTVTSV SVSQPTQTTT AKLQPVKSPT AVTTTTTSTT TTTNITHNII KSQPVRSSQN
TSQPPTSQPT KSHLPIGKPQ LPEPHNNNHK MSVWAADITS QFTMARRLVA SITDHANLRA
GYTIVNSDFV VQTLLGQAGS VLPENGMEKL KTAMSESMVK PKSNDHNNSN TNNNGTDCAP
LQPLNMKADE VDHLLRMLRF ALMNLTPKGT AAVEKKPPEE KAPQEVLAKE PCVPRPKVEG
RYAYLDMQRR QSATVYQSPY APGFGFSDYA RREYNLIGEV FAEPKPSLAI QYFEGLSRED
KEKVIEACGL DVTVPRRKIR IQIPTVEEHL ALDAGSNHNA VGVGVGISRF GQQPSSLSSS
SSFPGASSLD AMTIDEHHHH HPPNLHNHNQ NHNQNQNHLS VFDMHMSMSM PLPAAADSPA
SASGCSTFGR PPLRYQSPHD FSLHVEHESS ILPRHLQLHD HDLFGDQQAN QRFWQRSVVP
WVDGDYGNSD AGGGGGGGSD VKSQDGRERD GHRPFFGPHE RPTGGGVGGG GGSVGHDYAS
SDLDMGRGPG SLHSMDMVGF GFDGPEDGVS P
//
