ID A0A8H4HEV1_9EURO Unreviewed; 1437 AA.
AC A0A8H4HEV1;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 14.
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=CNMCM6805_002947 {ECO:0000313|EMBL:KAF4242434.1};
OS Aspergillus fumigatiaffinis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=340414 {ECO:0000313|EMBL:KAF4242434.1, ECO:0000313|Proteomes:UP000653565};
RN [1] {ECO:0000313|EMBL:KAF4242434.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM6805 {ECO:0000313|EMBL:KAF4242434.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [2] {ECO:0000313|EMBL:KAF4242434.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM6805 {ECO:0000313|EMBL:KAF4242434.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-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:KAF4242434.1}.
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DR EMBL; JAAAPX010000017; KAF4242434.1; -; Genomic_DNA.
DR Proteomes; UP000653565; 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:UP000653565};
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..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Polar residues"
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 969..980
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1058
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1437 AA; 159612 MW; 3CBF114A0B59705B CRC64;
MMAAALDQPP FASLTGSRPN DASSITPPHS ANGKKEVPDG VPSELSDLEL DSGASAVKIE
DSVEGEDDVI EPDHYYGCGK IPVFKPTMEQ FRDFQSFIGK VDQYGMRSGI VKVIPPKEWL
DAQPPLDEAV KKIRVKNPIM QEFHGSHGTY TQANIERQRT YNLPQWKALC EESSHQPPAR
RGERRRNQER VTRTPAAPKP QTTGSSSQKR GPGRPPKRAN QVKVKEEPPA DDVLEKTKPE
GPPTPVSPES NPVETKSEEL SDGESLPEPK PKGRQPKSVT ARRKHNKGDN IDLVDEEAFK
NFDYRIHDQQ EYTQERCEEL ETAYWKSLMF NNPLYGADMP GSLFDNSTTS WNVAKLPNLL
DVIGQKVPGV NTAYLYLGMW KATFAWHLED VDLYSINYIH FGAPKQWYSI SQEDAPRFEQ
VMKSIWPSDA KSCDQFLRHK TYLVSPSLLK SQYGITVNKL VHYEGEFVIT YPYGYHSGFN
LGYNCAESVN FATEKWLDYG RVAKKCNCEA DSVWIDVDEI ERKLRGEATP EYYDDFDSDM
DVIEGASDLL TPPRSVPEKT STRGRKRKHP GETTKAKRMR VNVEIPRKAP CVLCPNDLDY
EDLLPTEDGK SHAHRRCALY TEETSILRDE SGKEVVCDID YIPKARMGLK CLFCREVRGA
CFQCNFGKCT RSYHATCALL AGVQVEHGSI AVIADDGNQY SVPSVDLKCK YHRQKRPTWM
TNDAADYDRK VNATARRLVA GDLVQFQADK EINGAVVLQN RPEERTLLVK ILPRGWLLIV
RKSNFAPLAP GTKPLPAHLA RKPDARKELE SAVPVAGNPF GDGRSPYHWA EFETVDVTKH
VSAPPPLHVD LNKGEQIWYY MGQTSTECRA QYTHNPSVSV HNPRSNFLDS VKSLGGVVTR
LPSYPHHFPQ YASASASAVV APPPRQHNHH LLSPAVAATA AAASAAAAAA ANRPSLLQRP
PLAPPPAAAP RSSSSSTVAS AAAASAMPSA YRTLPTQSAR HAPYPQVIKA HNNHQQQQQH
PFYHSPQPLQ SQQQQQNNNN NNNNNNNNNN NNNNNTTNSA TANGLPANTF ANVRELIARR
RLAQITDHAN VFAGYTIVSP ELVVETLLGP MGSVPPPNGL EKLELAMAQQ RVQPRAPDGT
LLPLQPLNMR SEEVTRLLQM LRFSLVSHRE RLDVLQKRES ENIKQEATAK GSAASAKLAG
KYAYLDQQRA QAPTVYQSPY DMPSGFTEYA KKTYELIPCA PELPKPSLAN DYFASLSTED
QEKILKTCGS FVQRAIERSA PHSRQNSASN LRLTSALAQQ TENPTIDITT VEDLPLSGLD
LPLHADSPCS SFSRSHLRFQ SPNDFTSHGP ETHHDHHDLF GDQQANTRFW QHGPWAAGDG
NTPNEENRPF FGPHERLKHD YASSDISLGR GPGSLHSVDM AGFGLDGTDD ICAELSP
//
