ID A0A165FBV5_9BASI Unreviewed; 1139 AA.
AC A0A165FBV5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CALCODRAFT_470968 {ECO:0000313|EMBL:KZT56522.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT56522.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT56522.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT56522.1,
RC ECO:0000313|Proteomes:UP000076842};
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; KV423976; KZT56522.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165FBV5; -.
DR STRING; 1353952.A0A165FBV5; -.
DR InParanoid; A0A165FBV5; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000076842; 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; PF13832; zf-HC5HC2H_2; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 53..94
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 292..458
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 537..664
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 813..840
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 141..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 126381 MW; 3FB6939E7671C905 CRC64;
MPLPSRTSSA ESAIPPQPDH FYPSPFNRPD WRDPADPESC IWPEEDPAAS RGIPVFKPTW
DDFEDFEAYV TAIAPWGKRS GIVKVIPPKE WTDSLPSVVP QLADVRLRNP IAQEMIGGSG
LFRQSNIEKR RTYSVQEWAK MCDKEESRTP SPSTTLKKER SEKKELSKKR KRRRVEETDA
EDDDAREEKE VERGVAILSD HQYDAPPTPE SLPDPAPRIA TDGSNAVDKD VRIDENFFAS
FDPKTSWLPP DTKPEDYTPE VCARLDRNFW RSIGNLGSPA WYGADMKGSL FTDETTSWNV
SKLPNPLSRL LDQTNRKLPG VNTPYLYFGM WRAAFAWHVE DMDLYSINYI HFGAPKLWWA
IPSEKYGAFE RTMKGYFPAD AKSCSQFLRH KSFLVSPTVL ANSSCRPNVL VQHQGEFVIT
FPHGYHAGIN LGFNCAESVN FALQGWEDAV RKADWCKCEK DSVKLDVDAL HEEAKEIQAK
EARSAPPKES KSSKKRKIEE TALEEEPKVV KRAKRRHSVP NPKQVATDAS PSATTPTRAC
ILCPGADEDT LLRVHDVPAA IRKLSTVHAW AHERCAAIIP ETWVDTLDGE KCVFGVDVIE
KARWDLKCAA CTKTTLKNYG AKIQCTRGKC PRAFHVSCAM EKSEVQFKEV EEVEKEVVFA
DMGAGCGDQP QEQTPGEQGI PIDMEMPAAQ HLNAHTAEVP IHDQEEASQR TMKVIKTIKK
PIIELLCPVH NPDMRILAKQ RKDEARKRSV LALKEGDRIR IRLSSGVFEV TLLGIDEAAE
KVEVMWDDQS KREIKWGSIH WGAVSEEVLA ASKAKQEAKE EALETKLRQY QEALRLAKKH
RPILPAPSIA GYTPVQPSGA LNGAVPAASN APSSAPNYLT SVFTIPPSAS NLAPTGPCTS
SVNTLSPPCD HSASRPEEQI ARRADETAAP SYIVGHPSSG TYPTGYWATV SHPGYWQHPS
FISQGWYDYH GRWHEGPVPT YAHHESDGNS NSTVSTSPNH GIALYDYRGF LVDRYPTDVG
CSAPPPGPNP ALADHDAMQP GPGPSADSTA SQTTPTSPSS NNAALPRSTS PEAHQAPRLL
QVPPSVVLNN PDLVPLLNSL MQNETMRNTL QRLKETFSTQ LTPPIGIPTV DYNHTDIVS
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