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Database: UniProt
Entry: F6KJQ8_CRYGA
LinkDB: F6KJQ8_CRYGA
Original site: F6KJQ8_CRYGA 
ID   F6KJQ8_CRYGA            Unreviewed;      1856 AA.
AC   F6KJQ8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE            EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
OS   Cryptococcus gattii (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus gattii species complex.
OX   NCBI_TaxID=552467 {ECO:0000313|EMBL:AEG78610.1};
RN   [1] {ECO:0000313|EMBL:AEG78610.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21909264; DOI=10.1371/journal.ppat.1002205;
RA   Byrnes E.J.III., Li W., Ren P., Lewit Y., Voelz K., Fraser J.A.,
RA   Dietrich F.S., May R.C., Chatuverdi S., Chatuverdi V., Heitman J.;
RT   "A Diverse Population of Cryptococcus gattii Molecular Type VGIII in
RT   Southern Californian HIV/AIDS Patients.";
RL   PLoS Pathog. 7:E1002205-E1002205(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC         [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC         H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC         Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC         Evidence={ECO:0000256|ARBA:ARBA00000604};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC       {ECO:0000256|ARBA:ARBA00006801}.
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DR   EMBL; HQ396150; AEG78610.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:CGB_I0590W; -.
DR   VEuPathDB; FungiDB:CNBG_5877; -.
DR   VEuPathDB; FungiDB:I306_06593; -.
DR   VEuPathDB; FungiDB:I308_03686; -.
DR   VEuPathDB; FungiDB:I311_05393; -.
DR   VEuPathDB; FungiDB:I314_06110; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15525; PHD_UHRF1_2; 1.
DR   Gene3D; 2.30.30.1150; -; 1.
DR   Gene3D; 2.60.120.650; Cupin; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR001606; ARID_dom.
DR   InterPro; IPR036431; ARID_dom_sf.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR003349; JmjN.
DR   InterPro; IPR048615; KDM5_C-hel.
DR   InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR004198; Znf_C5HC2.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR   PANTHER; PTHR10694:SF33; LYSINE-SPECIFIC DEMETHYLASE LID; 1.
DR   Pfam; PF01388; ARID; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF02375; JmjN; 1.
DR   Pfam; PF21323; KDM5_C-hel; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF08429; PLU-1; 1.
DR   Pfam; PF02928; zf-C5HC2; 1.
DR   SMART; SM01014; ARID; 1.
DR   SMART; SM00501; BRIGHT; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00545; JmjN; 1.
DR   SMART; SM00249; PHD; 3.
DR   SUPFAM; SSF46774; ARID-like; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR   PROSITE; PS51011; ARID; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS51183; JMJN; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          177..218
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          242..331
FT                   /note="ARID"
FT                   /evidence="ECO:0000259|PROSITE:PS51011"
FT   DOMAIN          485..536
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          650..816
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          1523..1575
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          69..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          152..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1012..1046
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1026..1046
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1856 AA;  207509 MW;  CE3A7E2B9B38318F CRC64;
     MLPSNQQTTA AGPLPATPNQ LSLRRRHSSS KQDTPPNLDG PLRFNPSASE SARRGKPTFF
     SSMHFSQVLP QPIPSMAPDE RRPERQRGQR KSKVEALTKI DRSGTPIQLA AGPAATSFVP
     HTIQKSTPPP PAPHYLRNPL HRPKVVNPPF SIDSVRTKAP RHPHPRTEPR LFGLEDCPTF
     YPTPEEFKDP MAYIDSISQQ GKKYGMCKVV PPEGWHMPFR LETETFRFKA RLQRLNQLEA
     ASRAKLNFLE QLSMYHMQQG DSKIHIPLID RQPLDLWKLR REVNRSGGNL ELDRTKGWSK
     ITEVLGHKPS WTPHVRAAYM NIVLPFDNWA VRAKSASVSP LAKLNPGSSS SPSKPPPAFV
     NDTFSASPIK QGQGISRTST ASRRPAAKMR PNGMHFVSPP DKGRLPAKRA SVSGGSVLAD
     AIEVNQPGSL STAPSAAASA PMTLRINVPG FSDREGSDSE LSDEDSVLSS PSVRKAHFEP
     EYQKGEVCEI CKGEHDPGKI LLCDGCDRGF HIYCLDPPLA SVPTNEEWYC TSCLLSQGEN
     FGFEEGDEHS VASFQARDAA FSHAWWNRHN PHNSPRASVN GAQPTNNDDC ERMKPRQFGN
     VTVSEDDVER EFWRLTESSL DTVDVEYGAD IHSTSHGSAG PTPETHPLDP YSRDPWNLNN
     MPILQDSLLR YIKSDISGMT VPWIYIGMMF SAFCWHNEDH YTYSINYMYW GETKTWYGIP
     GSDAEKFEAA IKSEAPDLFE QQPGLLFQLI TMMNPGRLSD AGVKVVACDQ RPNEFVITFP
     KAYHCGFNHG INMNEAVNFA LPDWLPDGKD SVRRYREHNK APVFSHNELL ITITLFSDTI
     RTALWLKDAL IEMVEEESAR REALRAKYPK LVEDLIEEDC PEDQYQCAIC KAFCYLAQVT
     CSCTSQVSCL SHADQLCTCG KPRKILRMRY SEAQLEDIRD VVVHRAALPE QWHVRFFSLM
     ESPRPQLKSM RTLVLEGERI AHPIPDLGPL KRFVDVATSL IQQIMAITTR KSVGRRKKAS
     RGDGNRKGKR TRAERDDEED DGIDRSPTVL SDLLKQADRL AFDAPELPQL RQLMLAIEGF
     RTEASSLLIT PEDQVDRQRC KNALILGQSF GLNFPELSPL EKLVQRQEWF RQLEEEVDDA
     NMEYDDVVVF LEESLECQIP QDHALVKELS VRERKGKQWI ESVEKLLASS QITLGGISSL
     IEARQHVPVS TDILRKLESL RKSAISWQTS ARNALATHGS PVAASRLCKN VAAASKPLSN
     VVIPEIRQLQ AELKHHALWR EEASKVLGVP VARLASTIDY IRSEFENSLA PDDDAHNDRR
     VCFCRSPPAD NMVMCNVCRH SYHPRCVDVS LRHVPEEFKC AMCQRLPNDD GPSLDAFIGL
     ISPQRWNFLI NPSEFEPAQY IASAAMRYAP QALRLADPFS LSHPCRDLEL LRHTIRKIYT
     LPLVFDAYNS QTNERCVFVN WLFRRMQDVV WMKTKQITVL DRHSLTLAAG QFTSANCENG
     TPSGRARPRR RARIILAESH PHEFYCLCGM SPAGENTAAQ VECPKCGQGY HAVCVKVAEE
     LAGKSVWRCP CCTVRDGRHY QKDVEVRVQL RSHRGTDQFL DYRTIINDFA ERLVLVTRPT
     SANAITLECV DFVPAHIPDN VKTIEGGGSS LNRIKKRKST VVDGVFRNEQ AASNSVAHNL
     IAVTAKCSMD TPSTILREIP TQITSSGTNG SSVAMSTLSD IQAKSDVVSR SIYTSGESNA
     NTSVLVLAPT IQNRPTFDMH SNVSPRSCFS STPVATRAST TSVVQESSVV PSATTMCGGR
     REAAVIRKSI HDDNINSRRG SEGGNSYPDM GESIAVEETV TFGRHVVDED VIMENQ
//
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