ID A0A9P7Z0M3_9HELO Unreviewed; 1552 AA.
AC A0A9P7Z0M3;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
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=BJ878DRAFT_132474 {ECO:0000313|EMBL:KAG9243157.1};
OS Calycina marina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Pezizellaceae; Calycina.
OX NCBI_TaxID=1763456 {ECO:0000313|EMBL:KAG9243157.1, ECO:0000313|Proteomes:UP000887226};
RN [1] {ECO:0000313|EMBL:KAG9243157.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TRa3180A {ECO:0000313|EMBL:KAG9243157.1};
RX PubMed=34372938;
RA Hagestad O.C., Hou L., Andersen J.H., Hansen E.H., Altermark B., Li C.,
RA Kuhnert E., Cox R.J., Crous P.W., Spatafora J.W., Lail K., Amirebrahimi M.,
RA Lipzen A., Pangilinan J., Andreopoulos W., Hayes R.D., Ng V.,
RA Grigoriev I.V., Jackson S.A., Sutton T.D.S., Dobson A.D.W., Rama T.;
RT "Genomic characterization of three marine fungi, including Emericellopsis
RT atlantica sp. nov. with signatures of a generalist lifestyle and marine
RT biomass degradation.";
RL IMA Fungus 12:21-21(2021).
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:KAG9243157.1}.
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DR EMBL; MU254001; KAG9243157.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000887226; 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:UP000887226};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 65..106
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 330..493
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 583..705
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1514..1535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..211
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..534
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1116
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1234
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1331
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1372
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1401..1412
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1552 AA; 175779 MW; F8F6F93C92558497 CRC64;
MSIVAPAVQP HEMESHLHSP PESSKESPLL KNDASASDSE LSDIEDPEGN AGVIEPESWA
DDGRVPVFRP TMEQFKSFPR YMQGVNPYGM KSGIVKVIPP PEWKAALPRL DEAIKTIRVK
EPIKQDIMGT SGTYRQANIL HQRSYNLPQW RNLCEQSEHQ PPAKRGERRM NQDKPTVPRN
ATRKAKAEAS TTKSTPATGG KRKPGRSARG KANKDASATP DRLPTPVSPS MKHEDDLESV
KAEQDDDEEA PVRGRMGGRQ SQAISVSSRR KYNRREATAK VDEIAFKDFK YELCEDFSAE
RCEELERAYW KTLTYAPPLY GADMPGSLFT DATTTWNLGK LENILDVLGT KIPGVNTAYL
YLGMWKATFA WHLEDVDLYS INYLHFGAPK QWYSISQGDA RRFEAAMKTI WPTDAKACDQ
FLRHKTFLIS PSHLLQNFNI KVNKIVCHPG EFVITFPYGY HSGYNLGYNC AEAVNFGMES
WLEYGRVAKK CDCSQAQDSV WIDVREIERK MRGEETEFEE TDDEDEDEED EDETGCLNIS
TPPRGNGEIK LQAPMKKRKR PVTEKGQPVA LKRVRLRLKA PAREPCILCP NDIPGEPLLT
TEDGEKVHRM CALYIPETSI DSGEKEIVRD VKHIAKARMD LKCNYCRSKK GACFQCSQKK
CIRAYHATCA AAAGVFVEQG EVPVFGEDGT EYKEQGIEFS CRFHRTKRDK NLQANDLSEL
GKVRKTGLAL NTGDTCQMQY YRADIFAGIV VENCRSEETL LVNILPRGER IEVEYKWLLV
PSPSDYKMVK PSANAIPMPK SYKAKESLNT SKRKADDDTP LAGDVFLEGC IWTEFKNDSA
PRNPYQVKVD FAKENQIWYY LGKNSTEARA QFTEDPRKMR HNPRGLFLET IPRTTNTIPR
QSYAASYPTH ISQNAVNTSK GSIRLPPQKQ IYRKDNRLFA YKPSIPDNNT VYRVDPQAYL
SQQNFLHAAT PSVPQPASVK KTPTLAFGTD PRYSTAPPIL PGATVDTYAR YSGNQKTPPN
PAHGLHYQQS KVQLPRLQSS HLNALSSTQL SPQFEQTKPQ SVPQQPRVQY EQPKAQPPQQ
QYRQNLAQQT QYQPQQQPQA RLQPPQQPRA VLAPPASYRP AYTPPVSQPP RQNPFQARKP
AYRSDPFSKY AYLQREHNRS ALDYKTPYRP GGGFMNGYEG NLKRHLEQKM FKNSQGPVSD
VVPPAPSHVS DHQRMYSGGQ PSPTSYSPSS QPPYDQAAPN PQQSVFQPQQ IIKPGSQNGW
DKREPTKHSP AVGQEYTNGT YRPGCQEPRP TSSHYSASFP NMTQGPMRYG SPQVQNQYQQ
PQRTQKYQNQ QPSSVAHMSS QKYQRHQRSP VTQQQRYQTH QQSPVLQSSQ QVYRSHQNPP
VLQAPPQGYD SHQASPPLHS PQYFQPYQNQ QQYPPPPRPV VSPAPTRPNT GTTVKVILPP
GQAHMQYHQH QIPQQGGYRD PKPVYSHQQH FQKNLPAGPS QAQFQPPPSR PVQTQHYHSA
PMYSELYAMA QSQEYTAPYR QQSPRDYPDV PPDSTSLVEK MMADLRKIRS RV
//
