ID M2QFI3_CERS8 Unreviewed; 1228 AA.
AC M2QFI3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=CERSUDRAFT_156544 {ECO:0000313|EMBL:EMD35808.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD35808.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD35808.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD35808.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB445799; EMD35808.1; -; Genomic_DNA.
DR AlphaFoldDB; M2QFI3; -.
DR STRING; 914234.M2QFI3; -.
DR HOGENOM; CLU_001442_1_0_1; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000016930; 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; PF13771; zf-HC5HC2H; 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:UP000016930};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 60..101
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 360..526
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 636..781
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1228 AA; 132980 MW; 527B3327071F8FC6 CRC64;
MSTSASSPPS LTPSRSPSPE LPLQPDHFYG SENQQLPPSP RSDGKTWLDP ADDPLAQRGI
PVFKPTMEEF QDFEAYMSRV ECWGMRSGIV KVIPPKEWTD KLPSPLDQLG GVKLKSPIEQ
HMLGRGGLFR QENVEKRRIM SMREWAELCA QEDLRAPGVD DIGLHARATN GTAKARTRRT
RRKRESETAE PDQAGEGVQV KEEEEEPSAS HDHDRGSRSL ASPPSSIAAP TPAPAPDSEA
EIEGELVDGE HKPGASEAVA VADSSAETRP EEEVSEEKPK TKGRRTQTRQ AREANLAERA
AKDKVFLENF DPHSDWLPPN TTPFDYTPEF CRELERRYWR NCGLGRPAWY GADMAGSLFT
QETKSWNVAS LYSALTRLLP SSSQGLPGVN TPYLYFGMWR ATFAWHVEDM DLFSINYIHF
GAPKYWYAIP QARASALEQT MRGYFPKDVS QCSQFLRHKS FLASPTLLSQ SSCRPNTVVQ
HQGEFVITFP RGYHAGFNLG LNCAESVNFA LESWIELGRK AKACGCVNFS VRIDVDQLLR
DRAAERLELQ TGQPTQLDDP STAAAENREK SKSPRKRKAE GPESSAPKPK KLKLKVEKPA
SAVSAGASSS SSSSKPAKTL TKVTLKLGPR PKEPDTFPCC LCVSPSEESL LRVQDPPMWR
VDTQPRASGA AWMAHEQCAT VVPETWVDEV EVGEPGPDGT RRKERVVFGV DGIVKDRWNL
KCAACTKNRH KAHGAPIQCT KGKCPKAFHV SCARDGAASG IIYNVVREVE KEVVLLDPQA
SATLPTPPKE MGEIPAAGEQ PMDVDGTAQP PAQSSDSTPD PAGPRVLKLI RKHEVQVLCP
QHNPAIAEAK RTMKQDKIRQ QLLALPANER IKLRVSAGVF EVTLVQVLEE SKSVEVIWDR
GLKREFKWGS VVFGNTEGLT VGQKPSEAAV ETNQFGMVAA SSQSRLSFPP LNSTPATYEV
RPQLGAPAAV TPTLTPAPTA TPVPGPSSVQ EPQSHTPTPA PTGTTPYYAY QAPGRTATYQ
YAPGAWTYQY SSQTFRQQYS APSPTSLPSS PSTILAATTS SPNPMASIPN SSTPAPSSLA
PTYALSQYAP YQPTVYPGYS PYGTYRFPTQ QQGGASGAKE LQWQRPYTGP KSAPGTGYGQ
QMGPVQATPQ TTPYGAYAYA WPHAPLRPPA AGAATAGAYM APATGATSTP ASAAPPPAAA
AVPAPESTVN VPASFAASSA TVSPTPAA
//
