ID A0A1V6SVH4_9EURO Unreviewed; 1398 AA.
AC A0A1V6SVH4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 02-APR-2025, entry version 24.
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=PENFLA_c022G05475 {ECO:0000313|EMBL:OQE18027.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE18027.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE18027.1}.
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DR EMBL; MLQL01000022; OQE18027.1; -; Genomic_DNA.
DR STRING; 254877.A0A1V6SVH4; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000191342; 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:UP000191342};
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..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..298
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 931..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1020
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 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 576..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..948
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1398 AA; 156013 MW; 5993D568452C3EB2 CRC64;
MMATALDQSQ RDSLGGEPVV ESVSITPPHS ANGKKEAPEG VPSELSDLEL DHQSAPAPDT
IKIKQEEVEE KAEEVEEIEP DHYYGGGKIP VFKPTMDQFR DFQGFINKID KYGMQAGIVK
VVPPKEWSES LPPLDEAVKK IRVKNPIMQE FHGSHGTYTQ ANIERQRSYN LPQWKGLCEE
SSHQPPARRG ERRRNQERVN RAAPTPRPPS ARPEGQKRRP GRPPKRANQV KVKEEPPADD
AEKTRLEGPP TPVSPETNPV QPKTEDLSEG ESLPTTKPKG RQAKSVTSRR KNNRGDAMDQ
VDEEAYTGFD YRIHDHEEYT AERCEELETN YWKSLMYNNP MYGADMPGSL FEDSTETWNV
AKLPNLLDVL GQKVPGVNTA YLYMGMWKAT FAWHLEDVDL YSINYIHFGA PKQWYSISQE
DAPRFEQAMR SIWSSDAKNC DQFLRHKTYL VSPSLLKSQY GITVNRLVHY EGEFVITFPY
GYHSGYNIGY NCAESVNFAT EQWLDYARIA KKCNCEADSV WIDVDEIERK LRGESTPEYY
GGFESELDGF EGASDLLTPP RSVPEKTSTR GRKRKNPDDG PNTKRPKLHP EGPRKLPCLL
CPNNLDYEDL LPTEDGKGHA HRRCAAFIEE TTILRDASGT EVVCDIDKIP KARLGLKCLF
CREVRGACFQ CNFGKCTRAY HATCALLAGV QVEHGAIAVI ADDRTQYSVP SVDLKCKFHR
QKRPNGVLGE SSDVDRRVIE SARRLVQGNL IQFQADKEIN GAIVLENRPS ERSLLLKVLP
RGDVIEMPYR WMLVVRKSNF TPLALGIQPL PAHLARKPEQ RKELESAVPA AGSAFGDSRS
PYQWAEFETV DGTRNQFAPL STVNLQGEQM WYYLGMQSTE SRAQYTHNPS VSIHNPRANF
LDSVKSLGMG VSARASKISP HHFHYAATAP APPYQRNLNQ PNQQNQQNIY SHPNVNTPHL
QSRPPSSALH LAPPPPSVPV AGAAAGAPAM PSAFRTLPNQ SARHAPYPSV VKSHAQQQHH
LPSTNTFANV RELIARRRLA QITDHANVFA GYTIVSPELV VETLLGPMGS IPPANGLEKL
ELAMAQQRVQ PRAADGTLLP PQTLNMRSEE VTRLLQMLRF SLVSHRERLD VIQKKESEGI
KQETVDRGSV AAAKMPGKYA YLDQQRSLAP NVYQSPYNMP SGLSEYAKTT YGLVPAADDP
PKPSLANDYF NSLSQEHQEK ILKTCGSFVQ RAIERSASHS RQSSSSNLRL SAALAKQTEN
PTIDITPVED PPLLSGLDMP LHADSPCSSF GRSHLRFQSP NEFPIHGPDP HPDHHDLFGD
QQANTRFWQN GPWVGGDGNT PNDENRPFFG PHLFGPHDRL KHDYASSDIS LGKGPGSLHS
VDMAGFGPDM NDDLGLSP
//
