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Database: UniProt
Entry: A0A8H6QTX1_9EURO
LinkDB: A0A8H6QTX1_9EURO
Original site: A0A8H6QTX1_9EURO 
ID   A0A8H6QTX1_9EURO        Unreviewed;      1421 AA.
AC   A0A8H6QTX1;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 16.
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=CNMCM7691_007483 {ECO:0000313|EMBL:KAF7178669.1};
OS   Aspergillus felis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=1287682 {ECO:0000313|EMBL:KAF7178669.1, ECO:0000313|Proteomes:UP000641853};
RN   [1] {ECO:0000313|EMBL:KAF7178669.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CNM-CM7691 {ECO:0000313|EMBL:KAF7178669.1};
RA   Dos Santos R.A.C., Rivero-Menendez O., Steenwyk J.L., Mead M.E.,
RA   Goldman G.H., Alastruey-Izquierdo A., Rokas A.;
RT   "Draft genome sequences of strains closely related to Aspergillus parafelis
RT   and Aspergillus hiratsukae.";
RL   Submitted (JUN-2020) 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:KAF7178669.1}.
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DR   EMBL; JACBAG010001876; KAF7178669.1; -; Genomic_DNA.
DR   Proteomes; UP000641853; 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   FunFam; 2.60.120.650:FF:000047; 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:UP000641853};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          81..122
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          345..508
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          588..713
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          171..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          950..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1009..1050
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..286
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1012..1050
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1421 AA;  157870 MW;  1FC2000413E5D117 CRC64;
     MMAAALDQPP FASLAGSRPN DAASITPPHS ANGKKEVPDG VPSELSDLEL DPSASTVKIE
     DSVEGEEDVI EPDHYYGGGK IPVFKPTMEQ FRDFQSFISK VDHYGMRSGI VKVIPPKEWL
     DAQPPLDEPI KKIRVKNPIM QEFHGSHGTY TQANIERQRT YNLPQWKALC EESSHQPPAR
     RGERRRNQER ATRTPAAPKP QTTGSSSQKR GPGRPPKRAN QVKVKEEPPA DDALEKTKPE
     GPPTPVSPES NPVETKSEDL SDGESLPEPK PKGRQPKSVT ARRKHNKGDN IDSVDEEAFK
     NFDYRIHDQE EYTQERCEEL ETAYWKSLMF NNPLYGADMP GSLFDDSTTS WNVAKLPNLL
     DVIGQKVPGV NTAYLYLGMW KATFAWHLED VDLYSINYIH FGAPKQWYSI SQEDAPRFEQ
     VMKSIWPSDA KSCDQFLRHK TYLVSPSLLK SQYGITVNKL VHYEGEFVIT YPYGYHSGFN
     LGYNCAESVN FATEKWLDYG RVAKKCNCEA DSVWIDVDEI ERKLRGEATP EYYDDFDSDM
     DVMEGASDLL TPPRSVPEKT STRGRKRKHP GETTKAKRMR VNVEIPRKAP CMLCPNDLDY
     EDLLPTEDGK SHAHRRCALY TEETSILRDE SGKEVVCDID YIPKARMGLK CLFCREVRGA
     CFQCNFGKCT RSYHATCALL AGVQVEHGSI AVIADDGNQY SIPSVDLKCK YHRQKRPNWM
     TNDAADYDRK VNATAQRLVA GDLVQFQADK EINGAVVLQN RPEERTLLVK ILPRGWLLIV
     RKSNFAPLAP GTKPLPAHLA RKPDARKELE SAVPVAGNPF GDGRSPYQWA EFETVDVTKH
     VSAPPPLHVD LNKGEQIWYY MGQSSTECRA QYTHNPSLSV HNPRSNFLDS VKSLGGVVTR
     LPSYPHHFPQ YASASASAVV APPRQHHHLL SPAAAATAAA ASAAAAAAAN RPSLLQRPPL
     APPPAAAPRS SSSTVASAAA ASAMPSAYRT LPTQSARHAP YPQVLKAHNL HQQQQQQQHP
     FYHSPQPLQS QQQQQNNNNT NAATTTNGLP ANTFANVREL IARRRLAQIT DHANVFAGYT
     IVSPELVVET LLGPMGSVPP PNGLEKLELA MAQQRVQPRA PDGTLLPLQP LNMRSEEVTR
     LLQMLRFSLV SHRERLDVLQ KRESENIKQE ATAKGSAASA KLAGKYAYLD QQRAQAPTVY
     QSPYDMPSGF TEYAKKTYEL IPCAPELPKH SLANDYFASL STEDQEKILK TCGSYVQRAI
     ERSAPHSRQN SASNLRLTSA LAQQTENPTI DITTVEDLPL SGLDLPLHAD SPSSSFSRSH
     LRFQSPNDFT SHGPEAHHDH HDLFGDQQAN TRFWQHGPWA AGDGNTPNEE NRPFFGPHER
     LKHDYASSDI SLGRGPGSLH SVDMAGFGLD GTDDICAELS P
//
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