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
//