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Database: UniProt
Entry: A0A9N9Q141_9HELO
LinkDB: A0A9N9Q141_9HELO
Original site: A0A9N9Q141_9HELO 
ID   A0A9N9Q141_9HELO        Unreviewed;      1604 AA.
AC   A0A9N9Q141;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   28-JAN-2026, entry version 10.
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=HYALB_00008790 {ECO:0000313|EMBL:CAG8982063.1};
OS   Hymenoscyphus albidus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Hymenoscyphus.
OX   NCBI_TaxID=595503 {ECO:0000313|EMBL:CAG8982063.1, ECO:0000313|Proteomes:UP000701801};
RN   [1] {ECO:0000313|EMBL:CAG8982063.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Durling M.;
RL   Submitted (JUL-2021) 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:CAG8982063.1}.
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DR   EMBL; CAJVRM010000562; CAG8982063.1; -; Genomic_DNA.
DR   OrthoDB; 9547406at2759; -.
DR   Proteomes; UP000701801; 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:UP000701801};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          70..111
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          342..505
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          595..714
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          799..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          911..960
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          982..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1055..1122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1171..1256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1272..1369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1388..1464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1514..1584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..45
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..546
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..583
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        911..925
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        937..958
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        989..1002
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1006..1017
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1073..1122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1171..1197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1198..1229
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1246..1256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1272..1289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1290..1301
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1302..1312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1321..1365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1401..1414
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1415..1439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1448..1464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1537..1571
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1604 AA;  178176 MW;  ED444ABE893D241A CRC64;
     MSAETMVAGP APGPAVEVNG LHSPPDSNTK DASDSELSDL EEEQPEQPAQ PTDEDDIGEI
     VPAYYSNDGV PVFEPTMHQF KDFTIYMNKV NPYGMRSGIV KVIPPAEWKA AQPRLDEAVR
     TIKVKEPIKQ DIMGTGGTYR QANMIHQRSY NLPQWRQLCE QSDHQPPAKR GERRANQDKP
     VTRSTPRTKP SSNGNGSAPA GKRGRGRPSK SAAARAVTVE TDDAGQSTPD RLPTPVSPSA
     KPDDNTEAVK LEPDDDIETP EKPRLGSRQA KPTTVSVSSR RKNNRREREG KIDEAAFKDF
     KYELEGNEFT PERCEELERA YWKTLTYAPP LYGADMPGTL FDDKTTSWNL GKLDNILDVM
     GSKIPGVNTA YLYLGMWKAT FAWHLEDVDL YSINYVHFGA PKQWYAIAQG DARRFEAAMK
     TIWPTDAKAC DQFLRHKTFL ISPSALLQNY NIKVNKIVAY PGEFVITFPY GYHSGYNLGY
     NCAEAVNFGL ESWLEYGRVA KKCDCDQAQD SVWINVHELE RKLRGEETEY EETDEEEEDE
     EEENENDNST LATPPLSTGG LKTKSEKKKR KRATNEKGGD SNIKRVKIRI KATTHEPCVL
     CPNDIPSEAL LPTEDGQHAH QICAQYIPET SIDEGKAMDI KYIAKGRLEL KCNYCRSKKG
     ACFQCSRKKC TRAYHATCAA AAGVLVEQGE IPVFGEDGTE YKEWGIEFSC RFHRVKREKK
     LDSDTLSDCE RLRKAGTEIK VGEVCQAQYL KGDIFAGVVV ENCKDEEVIL LDILPRGDRV
     EVEYKWLLIP DPADYHLPKP SPNALPMPKS RKDKASLNTS KRQADDIPRA EDPFVEGHTW
     AEFNHEKINL NPYQVKIDFT KETQIWFYLG KTSTEARAQY TEDPRIPRHN TKGNFLDTIP
     KPVIAAPRQS YAASYPSNAK NSTPTPIRPP AKVLPAKTDR LEKPYVYKPR EQPRHETYGV
     DAQAYRAQKD FLQRSVPQYS FGTDPRWASS TQPSKQSSSP TPFKANANST GHLPQISQVS
     VAPPQYRNTQ SSMTPNLYSS TAQYATAASY NSAQATSAVQ HRPDSQHGAA VQYSPTPKQS
     PVVQQQASKV HSTAPTQYRS TPPMATSKPN NPFGNRPQPQ RPSNVFQKYY YLQKEHNRSP
     SDYKSPYRPG GGFMNGYQGD LMEYTKATLF TGNRPGVSTS QSNATPSYNM SSSYNGTSHK
     PSPSLNSSQS PSLDSYGASP ATPYSASPSV KPPMDNSGAS VIPPKTWEKK KDSSQLHPAI
     RREFLHTILN KQTNPLPQPS PTQSRSSVLQ PPPLYERPPY PSTSYASQTY TAPHNGYAAP
     STPQNQVVPQ PTYNKPVSLS ASHPQQYSRP VAEASQNHQS PQVSYAPSFD YSGKAQGVTS
     TAAVPVAEHP RQQSSAGYHN PSTSYQTSSQ PQASFSMHQS ATAKPQATQS PSAYTTAPAS
     NPPYGHAQHT TGISTNHPQP SYSQANYAAT SSNYERNTTS QMQASPVIPP LLSNFRQSLP
     NTNSSLFQPA MKNTQAGSFH PPAPSHTTPI LPPPRQYQIQ RQSEVQKSTY QHQQSFQRPD
     TQMTSSEQHL NAQPACEPAD VPPDSCSIVE KMLRDLKKAR ADSS
//
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