ID A0A081CKF6_PSEA2 Unreviewed; 1429 AA.
AC A0A081CKF6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=PAN0_016d5378 {ECO:0000313|EMBL:GAK67152.1}, PSANT_06098
GN {ECO:0000313|EMBL:SPO48407.1};
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK67152.1, ECO:0000313|Proteomes:UP000053758};
RN [1] {ECO:0000313|Proteomes:UP000053758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10317 {ECO:0000313|Proteomes:UP000053758};
RA Saika A., Koike H., Hori T., Fukuoka T., Sato S., Habe H., Kitamoto D.,
RA Morita T.;
RT "Draft Genome Sequence of the Yeast Pseudozyma antarctica Type Strain
RT JCM10317, a Producer of the Glycolipid Biosurfactants, Mannosylerythritol
RT Lipids.";
RL Genome Announc. 2:e00878-e00814(2014).
RN [2] {ECO:0000313|EMBL:GAK67152.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK67152.1};
RA Morita T., Saika A., Koike H.;
RT "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT as a producer of lipase B which used in a wide range of industrial
RT applications.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SPO48407.1, ECO:0000313|Proteomes:UP000325008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34888 {ECO:0000313|Proteomes:UP000325008}, and ATCC34888
RC {ECO:0000313|EMBL:SPO48407.1};
RA Guldener U.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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; DF830083; GAK67152.1; -; Genomic_DNA.
DR EMBL; OOIQ01000018; SPO48407.1; -; Genomic_DNA.
DR RefSeq; XP_014654805.1; XM_014799319.1.
DR GeneID; 26306204; -.
DR HOGENOM; CLU_001442_7_0_1; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000053758; Unassembled WGS sequence.
DR Proteomes; UP000325008; 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:UP000053758};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 129..170
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 457..621
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 718..841
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1402..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 635..693
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1429 AA; 155645 MW; 8738AF91C3F4291F CRC64;
MSVVEPATAT ISTTPASSTQ PLPTDIDTTT TNTTAPSAPS ASASSPSDAH SPILAPNGSS
RQSTPATSAA ASDHAHAAPI KRASTPANTD PRPATPPPPS HDDKHPLADI QPAYFYPTDA
SASSSHDGIP VFEPTMQQFQ DFYAFCQAID SWGMQSGIVK VVPPKEWRDA LPDLRPPSTA
TATADSDPAD ISKVRIRNAI SQHFTPAGSG VWRQTNITRT TKIWNAKQWA ESCIQDGQKG
PEMDRMKWKV EVEGVSNGGW GPKSIGAKDS APAAILDEDG VRTRSGKARP APTTPAEPRS
NPPKRKRPDT QDPIQSQEPT SAPSSPERRS LRTAHNASAA NQSAANTPST SRDASPVKPK
KNWEADAVTP QEWRAFDYKN CWLKEALSSD QLATLNAASS PPSQPVEEAE KTSAPTLPSP
SDWTPEVCRE IESEYWRSLN FGKPPMYGAD LRGTLFDDNT QHWNVGKLDN ILTRLRLKRK
LPGVNTPYLY WGMWRATFAW HVEDMDLYSI NYIHFGAPKQ WYAIRQADRQ RFESAMAGAF
PSDSRRCPHF MRHKSYLASP SFLASHGIRP LKLVHNAGEF VITYPYGYHS GFNLGYNCAE
SVNFALDSWL DIGRKANYCH CDQSQNSVRI DVDAMLEESK EMEELERKRE LRRAKEDSVR
AIEDEELEKR RLKNEKAKER RKLKKEADDA AAAAAGPAVP ALFQGGDDFY IDPKTAHTSP
CVFCPANVSN DLVPTPAHID STNAKLKAMA ARHAHRLCAS FIPETWVGKH AKADVVCGID
GIDKARFSLK CQICPNPNLQ KLYPKIQCTR GKCPRAAHVS CALVEDHGWF VDLCPTDTAD
RLEGKKVSAK PQAQQAQGTA DDSERLVVLC RTHNPLFREA EEARKADELR ERIHSLPVPS
MVKIKTSGGM FQALMVEVCE DDDEIVIEDE GRPSRVKFQQ IILESSEPSA VKTEPEPEPT
PDAVSQGVGA AAQDGDATPS AKRRRKATAK AVANARAGSE DAVEASVAVS SDAAPKAQPV
KRARNTKAQK AASSAEGVEP QQPAESAASL APEAESGPAA KPKRKRQPAK KKAQATQAAA
DESAPAVLQA PQPPVPGTAW SSHAPQLPAP PTHQRDPRDP RATYAPQAAG PYYPGAYHEQ
QSHPSSGPMQ HVQHYPGMYG GGPPHASHAH QYVPGAAYGY PSAEYDAEAT RYSRSSVSAS
PSHLHQRAAN EHAYSGQQQY AAQQQHAAPP RHRQDEQHAQ YPYAHPQNGA AGMPQQQQAR
PLAPPGASQY GHLAAPPQGY EDRPPPLPTY ARPLAHQPQH VASSDAASAN GPAHAFPDYR
PPYHHAAPAQ THPAYHGQSQ AQAQQYQQYR SYPPQQQQQQ HPQQHPQQQA YAHADYAYHA
THPGYAARAK YAPAQGNAYA QQPQYAHAQA HANAQEQLAG AHAQPAARH
//
