ID A0A8H4TYU6_9HYPO Unreviewed; 1526 AA.
AC A0A8H4TYU6;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 13.
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=FSARC_5692 {ECO:0000313|EMBL:KAF4966643.1};
OS Fusarium sarcochroum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium lateritium species complex.
OX NCBI_TaxID=1208366 {ECO:0000313|EMBL:KAF4966643.1, ECO:0000313|Proteomes:UP000622797};
RN [1] {ECO:0000313|EMBL:KAF4966643.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 20472 {ECO:0000313|EMBL:KAF4966643.1};
RX PubMed=33059601;
RA Kim H.S., Lohmar J.M., Busman M., Brown D.W., Naumann T.A., Divon H.H.,
RA Lysoe E., Uhlig S., Proctor R.H.;
RT "Correction to: Identification and distribution of gene clusters required
RT for synthesis of sphingolipid metabolism inhibitors in diverse species of
RT the filamentous fungus Fusarium.";
RL BMC Genomics 21:712-710(2020).
RN [2] {ECO:0000313|EMBL:KAF4966643.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 20472 {ECO:0000313|EMBL:KAF4966643.1};
RA Kim H.-S., Proctor R.H., Brown D.W.;
RL Submitted (MAY-2020) 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:KAF4966643.1}.
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DR EMBL; JABEXW010000279; KAF4966643.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000622797; 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:UP000622797};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 114..155
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 391..554
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 641..764
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1485..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..72
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..259
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..595
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..962
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1401
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1526 AA; 168255 MW; 61C837F39F5FE594 CRC64;
MSESTSTSID AGIAVATAPN SHDTVAATAP NDSKPKDAAT AQSDPAFLHS PPDSNNLAKS
DGSDSELSDL EGEPILSDAP QPLPSSDNGP SDDSKNDAND DIGEVLPDHW SGAVPIFKPT
MHQFRDFKRF MEAVDSYGMK SGIIKIIPPQ EWKDSLPRLD DLVKQVKVRE PIKQDIMGSN
GTYRQVNILH GRSYNLPQWR QLCDQSEHQP PARRGERRAN AEKPKPRTRA AAVAKPTDVS
TPKKRGRGRP AKRGGRGGRR VKEEPAEDGE DRPMTPVSPK PDATETEDKP VESVEKDPGV
EDDEDYEPTV SRMGGSRQAK AKTQTVSARR KYSRREGSAM IDEAAFKDWD YKMDVSEYTP
ERCEELERAY WKTLTYAQPL YGADLMGTLF DESTEEWNLN KLPNLLDVLG TKVPGVNTAY
LYLGMWKATF AWHLEDVDLY SINYLHFGAP KQWYSISQAD ARRFEAAMKN VWPTDAKACD
QFLRHKGFLI SPQHLKSHYN ITVNKCVSYP GEFVVTYPYG YHSGYNLGYN CAEAVNFALD
SWLDIGKIAK KCECAQAQDS VWVNVYEIER KLRGEETEYE ETEDEDEGDE DDDEQSGLPT
PPSGSGVKFK GTGHKRKRGP GEKGGRAKVK KIKLRLKTKA EPPCCLCPND SQTAELLPTD
DGRKAHRLCA HYLPETYIEA IDGQETIVNV SEIHKDRLDL KCLYCRSKRG ASFQCSQKKC
ARAYHPTCAA AAGVFVEEEE VPVFGEDGKE YKEQAFEFSC RFHRTKRDKK MDGDALEADS
RIRTAASKLQ PGETCQLQYY KGDIFAGVVV ENRANEQTLL LDILPNGDRL EVEWKWLLVA
DPADYRLPKA SANALPMPAS QKAKEKLKAK RLHDGKPKKD DPFVEGCTWA EFQLHPVTNK
EQVKIDFSKP DQIWHYLAKG STDARAQFTE DPAKRRHNPK GNFLSTVPKP VKPAKPPKPA
PTHAPRYPYQ STTPYAAPYN AAPGAAPGAA RLEKPYVYKP RKPAENNFPP QGTFTTQKFT
PAAPSPTPAQ QRPMYYHYSH PQPPVQQSAP AYSAQRFEVR PSSAYAPAGS APRVHSPMNT
AAHHQHNQHS QWPKTTAAPV HVSPPAPAAA THPYHSAYQT PAPVTQQQAH PVQSRPQVKG
SWQVHSSIYQ KYPFFQVNHN RDSSKYRTPY AAWGGFTNGY EGNLRAHIMA NKDAFLKGPL
KDRVLSSNQN YGAHNSPYNR PSAAPPQAPP VSQMSPGAQN PFRQAPISQP VPTASPGAAP
PAFGHLPRPA IKAQYLPPTQ TQTQAPPPPL PQQQQMAQPP NQNSKPKPGT IFKAYKIPPK
ESPVPLPANF LAAMTSTPNA SAASQQPENK GSPADAKSTR DMQVAQQSPS REPIADKQPL
GTKISKTPVP IPRLPGFPQV PAPREQQSAP SQTRQSQSTG RLSSQTGGLA STPGGTQLQA
VAAAQDGKPQ HLGPITANSN PGYEPQTAPA QQASMIANKH HPTAPAVKIT PHEPQGFPDV
PGSGSMEFME RLLANLRTIA QRDDTA
//
