ID A0A218Z918_9HELO Unreviewed; 1553 AA.
AC A0A218Z918;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 02-APR-2025, entry version 23.
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=B2J93_9542 {ECO:0000313|EMBL:OWP03696.1};
OS Diplocarpon coronariae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Diplocarpon.
OX NCBI_TaxID=2795749 {ECO:0000313|EMBL:OWP03696.1, ECO:0000313|Proteomes:UP000242519};
RN [1] {ECO:0000313|EMBL:OWP03696.1, ECO:0000313|Proteomes:UP000242519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:OWP03696.1,
RC ECO:0000313|Proteomes:UP000242519};
RA Cheng Q.;
RT "Draft genome sequence of Marssonina coronaria NL1: causal agent of apple
RT blotch.";
RL Submitted (APR-2017) 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:OWP03696.1}.
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DR EMBL; MZNU01000173; OWP03696.1; -; Genomic_DNA.
DR STRING; 503106.A0A218Z918; -.
DR InParanoid; A0A218Z918; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000242519; 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:UP000242519};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 59..100
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 321..484
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 575..697
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1470..1537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..186
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..200
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..524
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..553
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..910
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1137
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1308
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1409
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1514
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1553 AA; 172685 MW; 75D62CF64BEF58B8 CRC64;
MSTDTAAVPA AQPAPAGLNS PPDSMSAIKD SGSDSELSDL EPEVYALDVE PAYISDGNVP
VFQPTMDEFA DFTRYMTAIN KYGMRSGIVK VIPPPEWVAA QPRLDEAIKT VRVKEPIKQD
IMGTGGTYRQ ANIVHQRSYN LPQWRQLCEQ SEHQPPAKRG ERRANQDKQV RTAPKPKASG
KATTIGAKKK GAGRPQKSKS RSGITEQDET STPDRLPTPV SPKMKAEEDN QSIKMEEDDY
DTPTKLKGGR QPKAISVSSR RKNNKRETGI VDEAAFKDFK YELEGEDFSK ERCDELERNY
WKTLTYAPPL YGADMPGTLF DERTTTWNLG KLENILDVLG SKIPGVNTAY LYLGMWKATF
AWHLEDVDLY SINYVHFGAP KQWYSISQGD ARRFEAAMKT IWPTDAKACD QFLRHKTFLI
SPSQLASNFN IKVNKIVAHP GEFVITFPYG YHSGYNLGYN CAEAVNFGME SWLEYGRVAK
KCECSEAQDS VWIDVHEIDR KLRGEETEYE ETDDEEEEEE EEEESKIIEL LTPPESSGGG
SKPKIPKRKR KRPTNNNEDK SNAKRIRVRI KGPSKEPCIL CPNDIPSEPL LFTEDGQRAH
RKCALYIPET SIESGEKETI VDIKYINKAR LELKCNYCRS KKGACFQCSQ KKCTRAYHAT
CAAAAGVLVE QGEIPVFGED GTEYKEWGIE FSCRFHRTKR DKKFDGDALG EDKRLLKAGL
ELKAGDVCQM QYYRGDIFAG AVVENRTSEE MVLVDILPRG DRVEVEYKWL LIPDPADYHL
QKPSAKAIPM PKSFKDKESL NTTKRQVDDL PRADDPFVEG CTWAEFKCEN INRNPAQVKV
DFSKENQTWF YLGKNSTDAK AQFTEDPAKP RHNPKGHFLD TIPKPTPAVP RKSYAASFPS
KPNPNVSSNS HTPIRPSQSS ARPSENLNRP DKPYIYKPRN SSEMYSVDQE AYRDQQNFLQ
RSTPAPYAFG TDPRYRTAEA LRPANQHSTE DSSNVNGPQS RTGTVGTGAR PAPAMNATRP
GSGGGPPPPH SAYRLAAPSM PKPMNPFGSR PQSSSTKPNP FAKYSYLQRE HNRSPLEYKS
PYRPGGGFMN GYQGSLQAHL QQTMFRPGGS TMNMSSMPSL GGSSRSSNTG SQSASSNIVK
VPANNSHRAA GPANPPGPAA VRAPAYSPKP IQTQPVATPA TAVPNSQGKP GSSHLHPAIR
REYNTMYNHQ YLSQQPSPSS VLQPPAMYHR HATPLQAPYQ SLSTPQSQAR QYPQQPSQPQ
LKNLHQASQR SQPHCSTTST ASQATYRETV PQSTTGPPNS QPQYQSSQKA RNPPAHLPAA
QQYQPSPPKR GTSVQSSTPQ NQYQSSPMAR NSSVNSPAAQ QQQFEPVQAA AASLMNSPAS
QKQLQSSETE RNSAPRSPNS QQQNQTPQTV TSASDRPHVP PQHYQPSPTV AKSHIEPYAS
HQHYQPSLNT MAQNSPPQYQ SLSAIHNLQP PSAHKATSEA QYQHASRASM QESKPVYPHQ
QYFQQQQVQP QEYHPTPKPP DQNAPVRDPP DVPADSTTLV ERMMMALKRA PAA
//
