ID A0A0A2L0J6_PENIT Unreviewed; 1395 AA.
AC A0A0A2L0J6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 02-APR-2025, entry version 32.
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=PITC_056840 {ECO:0000313|EMBL:KGO72698.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO72698.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO72698.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO72698.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO72698.1}.
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DR EMBL; JQGA01000867; KGO72698.1; -; Genomic_DNA.
DR STRING; 40296.A0A0A2L0J6; -.
DR HOGENOM; CLU_001442_1_3_1; -.
DR OMA; EQMWYYL; -.
DR OrthoDB; 9547406at2759; -.
DR PhylomeDB; A0A0A2L0J6; -.
DR Proteomes; UP000030104; 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 FunFam; 2.60.120.650:FF:000047; 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:UP000030104};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 89..130
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 352..515
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 595..720
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..28
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..292
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1395 AA; 155991 MW; E2FFEC5D2EA91B77 CRC64;
MMATSLDQSQ RESLAGEPII ETISITPPQS ANGKKEAPEG VPSELSDLEL DHQSAPASDT
TKIKQEEFEE KVEEIEEIEP DHYYGGGKVP VFKPTMDQFR DFQSFINKIN KYGMQAGIVK
VIPPKEWSES LPPLDEAVKK IRVKNPIMQE FHGSHGTYTQ ANIERQRSYN LPQWKGLCEE
SSHQPPARRG ERRRNQERVN RAAPTPRPPS ARPEGQKRRP GRPPKRANQV KVKEEPPADD
AEKSRLEGPP TPVSPETNPV QPKTEDLSEG ESLPTTKPKG RQPRSVTSRR KNNRGDAMDQ
VDEEAYTGFD YRIHDHEEYN AERCEELETN YWKSLMYNNP MYGADMPGSL FEDSTETWNV
AKLPNLLDVL GQKVPGVNTA YLYMGMWKAT FAWHLEDVDL YSINYIHFGA PKQWYSISQE
DAPRFEQAMR SIWSSDAKNC DQFLRHKTYL VSPSLLKSQY GITVNRLVHY EGEFVITFPY
GYHSGYNIGY NCAESVNFAT EQWLDYARIA KKCNCEADSV WIDVDEIERK LRGESTPEYY
GEFESEFDGF EGASDLLTPP RSVPGKTSTR GRKRKNPNDG PSTKRPRLHP EGPRKLPCLL
CPNNLDYEDL LPTEDGKGHA HRRCAAFIEE TTILRDASGA EVVCDIDKIP KARLGLKCLF
CREVRGACFQ CNFGKCTRAY HATCALLAGV QVEHGAIAVI ADDGTQYSIP SVDLKCKFHR
QKRPNGVLGE SSDVDRRVIE SARRLVQGNL IQFQADKEIN GAIVLENRPS ERSLLLKVLP
RGDVIEMPYR WMLVVRKSNF TPLALGIQPL PAHLARKPEQ RKELESAVPA AGSAFGDSRS
PYQWAEFETV DGTRNQFAPL RTVNLQGEQM WYYLGMQSTE SRAQYTHNPS VSIHNPRANF
LDSVKSLGMG VSARASKISP HHFHYAATAP APLYQRNLTQ SQNQQNIYSS NVNTPHLQSR
PPSSALQHLA PPPPFIPVAG AAAGAPAMPS AFRTLPQSAR HAPYPSVVKS HAQQQHHLPS
TNTFANVREL IARRRLAQIT DHANVFAGYT IVSPELVVET LLGPMGSIPP ANGLEKLELA
MAQQRVQPRA ADGTLLPPQT LNMRSEEVTR LLQMLRFSLV SHRERLDVIQ KKELEGIKQE
TVDRGSVAAA KMPGKYAYLD QQRSLAPNVY QSPYNMPSGL SEYAKATYGL VPAADDPPKP
SLSNDYFNNL PQEHQEKILK ACGSFVQRAI ERSASHSRQS SSSNLRLSAA LAKQTENPTI
DITPVEDPPL LSGLDMPLHA DSPCSSFGRS HLRFQSPNEF PIHGPDPHPD HHDLFGDQQL
NTRFWQNGPW VGGDGNTPND ENRPFFGPHI FGPHERLKHD YASSDISLGK GPGSLHSVDM
AGFGPDLNDD LGLSP
//
