ID A0A5N5X9W3_9EURO Unreviewed; 1395 AA.
AC A0A5N5X9W3;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 28-JAN-2026, entry version 18.
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=BDV29DRAFT_75463 {ECO:0000313|EMBL:KAB8076867.1};
OS Aspergillus leporis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=41062 {ECO:0000313|EMBL:KAB8076867.1, ECO:0000313|Proteomes:UP000326565};
RN [1] {ECO:0000313|EMBL:KAB8076867.1, ECO:0000313|Proteomes:UP000326565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 151.66 {ECO:0000313|EMBL:KAB8076867.1,
RC ECO:0000313|Proteomes:UP000326565};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics study of 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) 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; ML732175; KAB8076867.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000326565; 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:UP000326565};
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 347..510
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 589..714
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..71
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..219
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..287
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..974
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1020
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1395 AA; 156803 MW; E0A6487C8D818676 CRC64;
MMATALDQPL FESVAGPPAA DAASITPPHS ANGKKEVPDG VPSELSDLEL DPTTARAPET
ASVEEEEEEI EPDHYYGGGK VPVFRPTMDQ FRDFQSFVNK IEKYGMRSGI LKVIPPKEWS
AALPPLDEAI KKIRVKNPIM QEFHGSHGTY TQANIERQRS YNLPQWKGLC EESSHQPPAR
RGERRRNQER VTRAPPTSRT QTVRSDSQKR RPGPGRPPKR SNQVKVKEEP SEDSLERIKP
EGPPTPVSPE SNPIETKTEE LSDGESLPAP KPKGRQPKSV TSRRKHNKGD AIDYVDEETF
KDFDYRIHDH EEYTQERCEE LETAYWKSLM FNNPMYGADM PGSLFDENVT TSWNVAKLPN
LLDVLGQKVP GVNTAYLYLG MWKATFAWHL EDVDLYSINY IHFGAPKQWY SISQEDAPRF
EQAMKSIWPS DAKNCDQFLR HKTYLVSPNL LKSQYGITVN KLVHYEGEFV ITYPYGYHSG
YNLGYNCAES VNFATEKWLE YGRVAKKCHC EADSVWIDVD EIERKLRGEA TPEYYGEFES
DLDEIEGASD LLTPPRSVPE KSTRGRKRKH DSDLTKTKRV RVSVDVQRKF PCLLCPNNLD
YEDLLPTEDG KNHAHRRCAL YTEETSILRD ETGKEVVCDI DQIPKARMGL KCLFCREVRG
ACFQCNFGKC TRSYHATCAL LAGVQAEQGE VTVIADDGNH YSIPSVDLKC KYHRQKKPSW
MTSSDSPDHD RKLIETARRL VAGDLVQFQA DKEINGAVVL ENRPEERTLL VKVLPRGDVI
ELPYRWMLVV RRSNFSPLAP GTKPLPAHLA RKPEGRKELE SALPVAGNPF GDGRSPYQWA
EFETVDTTNH RFAPPPVQVN LNKGDQFWYY LGQSSTECRA QYTHNPSVSV HNPRSNFLDS
VKSLGAVMAR LPSYPHRHLT QYATAPHHLS PAAAAAATAA VAAASRPSLL QRPPLAPPRT
PSSAASAATA MPSAYRSLPT QSARHAPYPQ IAKTHHQQSH HLSQQQRSPQ QQQQQQQQHS
HYLPANTFAN VRELIARRRL AQITDHANVF AGYTIVSPEL VVETLLGPMG SVPPPSGLEK
LELAMAQQRV QPRAPDGTLL PLQPLNMRSE EVTRLLQMLR FSLVSHRDRL DVLQKKETEN
NKPESIQKGG VTAAKLPRKF AYLEQQREQA PSLYQSPYDM PSGFTEYAQK TFGLTPCEPE
LPKPSLANDY FASLSPEDQE KILKTCGSFV QRAIERSTSH SRQSSTSNLR LVSALAQQTE
NPTIDITTVE DMPLSGLDFP LHADSPSSSF SRSHLRFQSP NDFNNHGAEV HHDHHDLFGD
QQANTRFWQH GPWGAPDGNT PNEETRPFFG PHERLKHDYA SSDISLGRGP ASLHSVDMAG
FGMDATDDIC TVLSP
//
