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Database: UniProt
Entry: J4KL42_BEAB2
LinkDB: J4KL42_BEAB2
Original site: J4KL42_BEAB2 
ID   J4KL42_BEAB2            Unreviewed;      1275 AA.
AC   J4KL42;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
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=BBA_09517 {ECO:0000313|EMBL:EJP61549.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP61549.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP61549.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP61549.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(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; JH725205; EJP61549.1; -; Genomic_DNA.
DR   RefSeq; XP_008602836.1; XM_008604614.1.
DR   AlphaFoldDB; J4KL42; -.
DR   STRING; 655819.J4KL42; -.
DR   GeneID; 19892529; -.
DR   HOGENOM; CLU_001442_4_2_1; -.
DR   InParanoid; J4KL42; -.
DR   OrthoDB; 48111at2759; -.
DR   Proteomes; UP000002762; 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   Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          99..140
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          379..542
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          626..749
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          1..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          834..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          920..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1079..1114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1146..1179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..582
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        849..866
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1079..1102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1146..1173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1275 AA;  142820 MW;  E4CB2FEDF7FE42BD CRC64;
     MDSDSVNVAT GPASAPVVDD AQQHLESSDP SQLNFLHSPP DSNNAVKSDA SDSELSELEE
     EPALDAPPHG LSASAEPPAA EDDKDDIGDV SPDHWSGTVP VFKPTMDQFK DFKKFMNKVD
     SYGMTSGIIK IIPPQEWKDA QPNLDELVKQ IRVREPIKQD IMGFNGTYRQ VNILHGRSYN
     LPQWRQLCDQ SEHQPPARRG ERRANTDRPK PPRPKPSAPK QPKTSMPKKR GRGRPAKNKP
     KHDEAAAEPD NRPMTPVSPK PATDEPNEEK PEIVNSVETD APDPEAEQES APAPSRMGGR
     MGGTKLAKEK TQSVSARRKN GRREGSVTID EEAFKNFDYK MDISDYTAER CEELERAYWK
     TLTYAPPLYG ADMMGTLFED SADTWNLNKL PNLLDVLGTK IPGVNTAYLY LGMWKATFAW
     HLEDVDLYSI NYLHFGAPKQ WYSISQADAP RFEKAMKSIW PADAKSCSQF LRHKGYLISP
     QHLLSHYGIR VNKCLSYPGE FVVTYPYGYH SGYNLGYNCA EAVNFALDSW LPMGKIAKRC
     ECSQAQDSVW IDVYEIERKL RGEPTPEYYE ETEDDEDEDD KDMSGLPSPP SNGVKFKDGR
     KRKHGGDKGQ RLKIKKVRLR LKSRADPPCC LCPNDFVGMD VLPTNDGRKA HRMCAMFIPE
     TYIDTVEGQD VVCNVNNIHR DRLDLKCLFC RSKRGACFQC SQKKCARAYH ATCAAAAGVF
     IEEQDIPVYG QDGVEYKEQA FEFSCRFHRT RRDKKLDSLA LEGDERIHRA AEAVKSTEIC
     QFQYAKGDIF AGMVIDNRHD EETFLISIVP SGERIEIEWK WLLIPDPSDY HLPKASPNAL
     PLPASEKARN RLNAKRQDDD KPRKDDEFAE GYTWAEFNLF DDVVNKDQAK VDFAKPDQLW
     HYLGKTSTEA KAQYTEDVTK QRHNPGGNFL ETIPKPPKPV TAPKYKQYRQ GVPSGYMHQQ
     YNGGYIPPLS VGNTVMSRPY THQQYGHVQA SVPAYHQPAQ MGWNNTQSEG PRYSVHPSVY
     QTYQYFQVHY NREPARYRTP YATYGGFING YETNYRTTLM ANGSQADMMR RLSFAGSLPS
     AGIPQNSKHR TATHNAKISP AATPPSKTDK AKATPLQKVY QIPSKQSPVP LPPGFLAAMA
     TSTPASAPVK ASQPAPPSTM SAAQATRATS SETLPAKPIE PAKISTTPVP LPSFALTPQQ
     HASALKNMHT AQYNGDVDIN SSAADSTVAI LRQSNQAQLE QQEFVDVPGR ESMEFVDNMM
     RNLRRASQQG MSPNP
//
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