ID A0AA39UY32_9LECA Unreviewed; 1460 AA.
AC A0AA39UY32;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
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=JMJ35_009402 {ECO:0000313|EMBL:KAK0508318.1};
OS Cladonia borealis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae; Cladoniaceae;
OC Cladonia.
OX NCBI_TaxID=184061 {ECO:0000313|EMBL:KAK0508318.1, ECO:0000313|Proteomes:UP001166286};
RN [1] {ECO:0000313|EMBL:KAK0508318.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ANT050790 {ECO:0000313|EMBL:KAK0508318.1};
RA Park H.;
RT "Complete genome of Cladonia borealis.";
RL Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 2-
CC oxoglutarate + 2 O2 = N(6)-methyl-L-lysyl(9)-[histone H3] + 2
CC formaldehyde + 2 succinate + 2 CO2; 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:ARBA00049349};
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK0508318.1}.
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DR EMBL; JAFEKC020000021; KAK0508318.1; -; Genomic_DNA.
DR Proteomes; UP001166286; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0051864; F:histone H3K36 demethylase activity; IEA:TreeGrafter.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter.
DR CDD; cd15571; ePHD; 1.
DR FunFam; 2.60.120.650:FF:000024; Putative jumonji family transcription factor; 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; IPR055500; DUF7072.
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:SF7; [HISTONE H3]-TRIMETHYL-L-LYSINE(9) DEMETHYLASE; 1.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF23258; DUF7072; 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:UP001166286};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 82..123
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 350..513
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 598..721
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1403..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..219
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..553
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..575
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1241
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1270
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1435
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1460 AA; 164822 MW; 7D7AC65A9CA55A98 CRC64;
MAAAVMSPPR EVGEVKVEIE QQDEKPALTP PTSEKTDKKD DDSGSELSDL EPEEREPSVA
PKSEPIEEEE IFPDHYYEGG KVPVFKPTVD QFRSFPQFIK KIDKYGMKSG IVKIIPPKEW
RDALPALDEQ VKTIKVKNPI TQEFHGTHGT YTQANIEKQR SYNLPQWKEL SEESSHQPPA
KRGERRRNQE KSTRAPSTRT RNTTGTSAGS KKKAGRPRVR AIPTTVLNHE EGTEEGTGES
RAQTPLTPIS PPPEPTKVKK EPLSVDEAPK PKGRQPKSDQ SKSVSSRRQH NRRDQVDVID
EEAFKGFDYR AYNQDEWTTE RVQELETAYW KSLNFSNPMY GADMPGSLFD DSTKEWNVAK
LENLLDVLGQ KVPGVNTAYL YLGMWKASFA WHLEDVDLYS INYIHFGAPK QWYSISQEDA
RRFEAAMRTI WPNDAKNCDQ FLRHKTYLIS PSVLQSQFNI RVNRLVHHEG EFVITFPYGY
HSGYNLGYNC AESVNFATES WLDYGKVARK CNCETDSVWV DVREIERKLR GEPTPEYYEE
TDDDEDEEDD DEPTNLPTPP GSDKGKPKRT HKRKRDTTDK DNKPKIKKLR IRIKAPAHEP
CILCPNDSKY EELLPTDNGK EAHWRCAKYT PETYISEENG SKIICNIAGI PKDRLELKCN
YCRNKKGSVF QCSQKKCTRA YHATCAAQAG VLVDIGPVPY FDDDGTEYID EDIDFRCRIH
RGRRGKHVDA AALEEVPLIR KTATKLTVGE VVQMQYLFGD IFAGFVLENR KTEQTLLIEV
LPKGEKLEVD YKWLVVFDPL NSQRPMISEN AKPWPAELAR KNRTSGKDPT INEGPKPNEL
FCDSTSFRWE EFETRKEFRN PEQVKVDISK PKKLWFYLGR DSTEARAHFT SDLAMPKNDP
SGNFLETVRI ATVAATAASV QRKSFPAPHP LNQNAINAVR ANYPPQQPKA QTTCYTSSSP
TKERPYHGKY AIAERDQIYT NSQAYQRRLQ HEVPTNLYQP QYQYPGDAYQ NYRAPQAPMG
SMVPTASMIS GRPATQQAST GAPDYTMRTH NIGSFPNTSS YAPPRPPLYE PPRSAYDNQS
QTVPTPTQPA PYSRPQAPVA NMTGSAPKAS SPTSQTCFSR PSSAQRRPSG SSVVTTPVAE
TKQVSHLAVS KEYTYLHDAE MARPKVYQSP YAPEGGFTAA YLPLPAVAPK MRSRALSTSE
EFLMKRTPSQ QERVNKSLSE DRARAQEEAQ ALVQQQVQQQ AKGHDPHGHN HSRSNSLNQQ
FHHPQPQHLP MSAIQQPQPP YRLQSPPHYH NPHASANSYQ QYNHYSPTYA TNALHHHQGG
PAYQYQQIQN YQQPHLHPPY RKNTPPQQQS YFRPTPTQVT PGEIQYQSPH DFQMQVQREA
QHSSHGHSFE HFLKGVHSAA GVHATQADGG GGSSWSGNYG ASSGGSGDGG DGNGQGSPLK
YEMNGGGGEM LPQMREGSRF
//
