ID A0A165VVZ0_9AGAM Unreviewed; 1083 AA.
AC A0A165VVZ0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=NEOLEDRAFT_1174576 {ECO:0000313|EMBL:KZT30281.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT30281.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT30281.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT30281.1,
RC ECO:0000313|Proteomes:UP000076761};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; 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:ARBA00000040};
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
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DR EMBL; KV425552; KZT30281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165VVZ0; -.
DR STRING; 1314782.A0A165VVZ0; -.
DR InParanoid; A0A165VVZ0; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000076761; Unassembled WGS sequence.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15571; ePHD; 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; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF7; LYSINE-SPECIFIC DEMETHYLASE 4B-RELATED; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF13771; zf-HC5HC2H; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 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:UP000076761};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 62..103
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 349..515
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 609..751
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 118473 MW; A6ADFD10A20E83E3 CRC64;
MSSASGTPSL TPSPSRSPTP APPPVQPDHF YGSDDVHLPP SPNSDGRTWL EPEDDEYATR
GIPVFKPTME EFADFEGYMN KIECWGMRSG IVKVIPPKEW RDALPPVTDQ LTQVKLKSPI
EQIMLGRGGL FRQQNMEKRR VMSVREWLEL CNKDDYRAPG VDEVGLYHGQ NASGKTRARR
GRGRKAASEK AETAEPEAEE ALIKEDPDEG VNAIDSPAKS LASPPHSAAG AEFLIIPEDG
AEVQANESSE AKEIVEELAE DGPEEKSKPK SRRGGQSRTA KEANLAERAK QDEAFFELFD
PHSDWLPPNT TPFDYTPALC QKLERHYWRN CGLGKPAWYG ADMAGSLFTD ETKCWNVAKL
PSLLARLLPP SSKGLLGVNT PYLYFGMWRA TFAWHVEDMD LFSINYIHFG APKFWYAIPQ
SRAVSLENTM RGYFPKDTSQ CPQFLRHKSF LASPTLLSQS SCRPNTLVQH AGEFVITYPR
GYHAGFNLGF NCAESVNFAL DSWLELGRKA KACECVSDSV RIDVDQLLLD RATEQAVVAK
ASKRKDKAKA SRKRKSEGGE ESHKAKKARP SKSASSKGLA NAHASGSGPS PSKVTVVLKL
PPKPKEPSTF PCCLCVSTST NDLLRVQDPP VTRPPEVLLE NDKWMAHESC AKVVPETWVD
EVDIDNANGS KGKERVVFGV DGIVKDRWNL KCSACSKSRL KAHGAPIQCT KGKCPKAFHV
SCARDGAVAG IIYEQVREVE KEVVLIDPIA KTSQEMNTAH HITSQQPNAA SMDIDGQVLQ
SNGAVIPSPA ADSAPHVLKV IKKIEVSCLC PQHNPAVLEA KKASKMNKIR KDLLALPNMA
RIKVRVSAGV FEVSLVRVIE ESNSVEVLWD RGLKREFKWG SVVFGNTDGV VGQKPSEAAP
ESEKGPNSSS THVLQFSKPS GPPPLLGSTQ QAPRGTPAPQ MQHYQHAYPA QQSGYNYWAY
QYGRMAQSNY YQPSSYPGYP YSGYAHTTYG AQPYGAMPYQ SYAATPPMPG APPVPSQAPA
PYYSQPVPPL QWKQPYVGPS ESGVSSPHSN QIQSNTGSRP PSAVPSGFAA SIPQVVPSAS
GQS
//
