ID   F2RRL8_TRIT1            Unreviewed;      1168 AA.
AC   F2RRL8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=TESG_01457 {ECO:0000313|EMBL:EGD93927.1};
OS   Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=647933 {ECO:0000313|Proteomes:UP000009172};
RN   [1] {ECO:0000313|Proteomes:UP000009172}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112818 {ECO:0000313|Proteomes:UP000009172};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; GG698481; EGD93927.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2RRL8; -.
DR   HOGENOM; CLU_001442_1_3_1; -.
DR   OrthoDB; 48111at2759; -.
DR   Proteomes; UP000009172; 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; IPR001965; Znf_PHD.
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   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   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1..35
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          251..414
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          491..616
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          85..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1168 AA;  131396 MW;  C2E4CFAB13D78F0E CRC64;
     MDQFRDFRAF IRCIDKYGMK SGIVKVVPPK EWTDSLPALD EAVKTIRIKN PIVQEFTGSH
     GTFTQANIEK QRSYNLPQWK ALSEEISHQP PARRGERRWT QGKTRGTAKS HGNKGESQKR
     KTTSSKRKAS EELPERQDDG QGSKPESPPT PVSPVSKPVK AKSEELSDGE PLPAPKPKGR
     QPKSVSARRK NNRDEQDDYI DEEAFIDFDY RLSSNEEFTA ERCEELETAY WKSLMYNNPM
     YGADMPGSLF DDAVTSWNVA NLPNLLDVLG QKVPGVNTAY VYLGMWKATF AWHLEDVDLY
     SINYIHFGAP KQWYSISQED LPRFEAAMRS IWPTDSKNCS QFLRHKTYLI SPTVLKSQYG
     ITANKLVHYE GEFVITFPYG YHSGFNLGYN CAESVNFATE SWLDYARIAK KCHCETDTVW
     IDVEEIERKL RGETTPEYYD ETRSEQYEGS SDLLTPPRSV PEKSTRPRKR KVDGIEPKSK
     RAKLHLDSPK KPPCVLCPNS MDYEELLPTE GGQAQAHRRC ALFIEETSIL KDDLGREIVC
     DIDKIPKARM GLKCLFCREV KGACFQCMYG KCARSYHPTC ALLAGVQVEF GKTSVVADDG
     QEYSVPAIDL KCKYHRQKRF GSLPSQTLDM DSKVLETAIK LKPGDLMQFQ ADKEINGAVV
     LENRPLERSL MLKVLPRGDV IELPYRWTLI VKKTNFPPLP PNILPLPAHL SRKPDSRNDS
     NSSMPSHGMI FGDTSSSYRW EDFICEQPPF NPDSCTVDLT KPETLWYYIG KTSTDCRAQY
     THNVDISIHN PRSNFLESVR TARAPPIPAK ALYRPTLLGD DTSPIPKNGL EKLRTSMSES
     QVPVRSLDGT VTYQPLNMEA DDVDHLIRML RFAVSSLTSV VNVPEKPKAP EQQQVVAPEP
     VKVLQPQSQE PAAQSVSGKW AYLELQRRQA PPVYCSPYAP GFGFSDYAKG EYGLVGTPQL
     SRKEPLAADY FAKLSPEDQE KIVQACGPVP PASENFSTLD GSIIATHGPA NQNLLFSSTE
     TAAPNISAAM VPDSHLHPLS AFDMTLRADS PASSFNRVPL HYQSPQEYGS HLDNESSLLP
     RHLHDHHDLF GDQQANTRFW QRSVPWNDVD TPSHDEEHRP FFGPHLRPPG HEYASSDMEF
     GKGPGSLHSM DMAGFGFDGP DDLPDPSP
//