ID A0A1S8BE46_9PEZI Unreviewed; 1547 AA.
AC A0A1S8BE46;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=BK809_0004396 {ECO:0000313|EMBL:OMP85725.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:OMP85725.1, ECO:0000313|Proteomes:UP000190776};
RN [1] {ECO:0000313|EMBL:OMP85725.1, ECO:0000313|Proteomes:UP000190776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F98.1 {ECO:0000313|EMBL:OMP85725.1,
RC ECO:0000313|Proteomes:UP000190776};
RA Robert-Siegwald G., Vallet J., Abou-Mansour E., Xu J., Rey P., Bertsch C.,
RA Rego C., Larignon P., Fontaine F., Lebrun M.-H.;
RT "Draft genome sequence of Diplodia seriata F98.1, a fungal species involved
RT in grapevine trunk diseases.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; 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:ARBA00000040};
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:OMP85725.1}.
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DR EMBL; MSZU01000084; OMP85725.1; -; Genomic_DNA.
DR STRING; 420778.A0A1S8BE46; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000190776; Unassembled WGS sequence.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15571; ePHD; 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; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF7; LYSINE-SPECIFIC DEMETHYLASE 4B-RELATED; 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 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:UP000190776};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 73..114
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 349..512
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 599..722
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1502..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..552
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1404
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1547 AA; 170371 MW; 9462AE370FF1DC77 CRC64;
MEDLPMTDAQ NAPADTGAKQ ASDQKAALTP PTSEDMDRGK RDGSSSELSE LELDDEEDIG
DIEPDHYWDG GKIPVFKPTM DQFRSFKKFI DKIDKYGMKS GIVKVVPPPE WRDSLPNLDE
AVKKIKVKNP ITQDFSGSRG QYTQQNVEKQ RSYNLPEWKA LTNQWEHKPP AKRGERRGDV
APPPRTRATR NREASVATPP AEPGVKRTRG RPRKNPPKEV KKEVDEDSSV VETVEHMDTQ
PTVPPTPSSP PDEATAVNKK VATLQKAAGD GSPKPRGRQP KSISSRRKHN RGETTDDVDE
QAFDDFDYHL EGVEEFTPER CAELEQNYWK TINFGQPMYG ADMPGSLFDE NTTSWNVAKL
ENLLDVLGTK VPGVNTAYLY LGMWKATFAW HLEDVDLYSI NYIHFGAPKQ WYSISQEDAR
KFENAMKSVW PNDAKNCSQF LRHKTYLISP QRLESEFGIK VNKLVHYEGE FVLTYPYGYH
SGYNIGYNCA ESVNFATEAW LEYGRIAKKC DCESDSVWVD VAEIERKLRG EPTPEYIEET
DEEDDEDDTE ETGHDLPSPP SSVKGKPKAS SRKRKRETGD KATEGKVKRV KLRLRVPKEE
PCILCPNDVT FDVLLPTDNG QKAHRLCALY TPETYIIEEN GVERVCNVAN IDKARLELKC
NYCRSKRGAC FQCAAKKCIR AFHATCAAAA GVQIDEGPVP TFDEDGTEYY CDGFDLRCRF
HRPRRPKFTD VDSLENNKLI PDFAKSLEPK QVVQAQYLSG EIFAGTVVEN KPEELSVIID
VLPTSFERVE VEWKYLLVLD PAQSLRPKPS TNAIPLPEHL NQASSTLNAK NQKDGPPEMD
TPFCDANTEF KWAEFHTATA AEIKNPFQAK VGITMPQQLW HYLGKTSTEA KAQYTDDLRR
QQHNPKSNFL DTVKPPPRPV QAYQSRAIGP AYSSGVNINA LNGAMAAQRQ SMQPHYGQKP
YEYKPRSGPA YTAQQAAYPP YPYNGQPAGR SGPFPYSPVP PYPYSPVSYQ DARKSSAGSA
NSPPTQTPHH PPNYVPPYHQ TTSHSPYASV YGDPRAGQPV HYPNYHRPSF SNPYHHPLRP
VAASPPAAGS AISATSMSPS AHSSSPAIRS DSISSTSSKS PDLEYLQFLQ RFPYLLNSYL
RRPKVYESPY PGTSGFSEAY NPRRIMAEKQ AQRQAVAYPQ PQGGYPGANG YGGSQQPHGY
QQPYAPGHPP AQNTRPGLTF QSAQDFRADV NRTQASQMSN MPKFEMLIKQ LSQANETAAR
RFAARTQAHQ AQQHQQQDAH APLPPSHQAQ VQYHHAPPPS SSTALAAAAA AVAAASHHHH
HHQSGQHERQ VAPPPLPIAT TTTTPLGGYT GPSNTRGYRP GYGYDSGAFG PDTQTKVPSP
FNQPVTPHAR PPRPPRPAPA LAPASAAPAA PVVATPVTPT QQSSSTTAAA GNGAASAGEG
RRTPQRPAVS PLSDAGDDRM VAGETTTTMM MTPLPPPATS TSTTSAATAA AAAAAAAAVE
AATLAQAQTE QQQQQQQQQQ QQQTAAIPPP AAADASDGGG RETWRYT
//
