ID M4A3F4_XIPMA Unreviewed; 2105 AA.
AC M4A3F4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(27) demethylase {ECO:0000256|ARBA:ARBA00034525};
DE EC=1.14.11.68 {ECO:0000256|ARBA:ARBA00034525};
GN Name=KDM6B {ECO:0000313|Ensembl:ENSXMAP00000008998.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000008998.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000008998.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000008998.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224,
CC Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, 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=1.14.11.68; Evidence={ECO:0000256|ARBA:ARBA00034421};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000256|ARBA:ARBA00034483}.
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DR STRING; 8083.ENSXMAP00000034817; -.
DR Ensembl; ENSXMAT00000009012.2; ENSXMAP00000008998.1; ENSXMAG00000008979.2.
DR Ensembl; ENSXMAT00000027974.1; ENSXMAP00000034817.1; ENSXMAG00000008979.2.
DR eggNOG; KOG1124; Eukaryota.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000160414; -.
DR HOGENOM; CLU_001909_0_0_1; -.
DR OMA; ARCSPGM; -.
DR OrthoDB; 20251at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032452; F:histone demethylase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1370; -; 1.
DR Gene3D; 2.10.110.20; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR046941; KDM6_GATAL_sf.
DR InterPro; IPR048562; KDM6A_B-like_C-hel.
DR InterPro; IPR048560; KDM6A_B-like_GATAL.
DR PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR14017:SF5; LYSINE-SPECIFIC DEMETHYLASE 6B; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF21322; KDM6_C-hel; 1.
DR Pfam; PF21326; KDM6_GATAL; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852}.
FT DOMAIN 1803..1966
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1704..1723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1743..1787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..455
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..921
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..951
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1443
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1763..1779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2105 AA; 235512 MW; F9D73A9C35A9D3DA CRC64;
MHHSVEQLSG RGTRDSFPLD GLNRGPWHPV SGRAWQTTAR CSPAMNQPQL LHHLPPAALG
GLNHHSKYLS NGPMRGEEKL DLPPAMFPGM HREQQRPPPQ HLHPPPPPPH RVWEQQYDSH
HAPHPHPVLS LPNDHTMRLF NGYPGSGAHL LNPHLPPNRP NPLLKDPQGP PLLGEEMRAQ
VHQRGYPGKM PGGQLKRPGP PLGEHSVIQH TPPVSHHIPP HPVVEDTPSP SKRRKSLDQV
SHSGLQHFSG QSPSSSQQQT PTHHHALKPA FWNPIHKDNG VPWKPHTSDR KHPHEYQESN
KQGMCSYTSK TSPNSSSPSN LSPHPPNSSP GGYHQGCAPH LQKDVLQPQA VNHHSPHSSY
PNPSSKLDLG PSCQAVEPRG LNKQRSLLGG GHTPPTPTRG DKDHRVRAQS SPANASATSN
KNNSSSSSVP YCHYQPHPGL RHPGAPPPPP PASSTSVPQQ QQSGPSEAWR YQSRPSSHSL
ESRVYVPPGL LPQPQQSHNQ VVDSRLSGSH QHQRHISPTV PPTNSTRTPV ITSNPPMSLS
SCTNSRYTSS SDRVTVANVS SRSMSPPGGC SVNNRTNQNS WRGMTDPKTQ NSTSPKSQMD
ALLQPGCQRG RAQQQDQPKP QHQESTRSPP TNGKMSYYAQ ANPQQSPRQF SSSSLFSLGN
QRVEDSVITR RDSNPFPNSP STYCPASLPS VNTLSRGSRP NHQPHSTSTQ MFSTPQASTS
VPQSMGDVLD KLDAELEGHM QAEERRRRDR EEQERKKEEE KQKRELEMRR KLEEERQKKQ
QQEEERKRRE MEKILMERKR RELAKLEEER KKLEWEKREQ ERKRKEWERQ EEERKRREAE
RLERKKREIE RAKEEKRKLE EEKRMEQKKE ESLCSAKGKE QTAIENLERL LSGNTPTVPP
PPPLSVPTPP SAAPPSISQA SPPYPWLSRG GVPPAPTAQA PSNPTERLRP PPLTPQTEYA
REKQRLREMG SNGGGGATFN PSTLNTSGMN QPIHPSKPPA MQAAPNQSKD SGRERDLPTL
AIREPPKLYQ AFSRDNLPLP PLPSSSAIAR GINKKLTESS WENNGTESDS AQFEEEPSEM
STMLPDGLAN IMAMLDESIK KEEELYSSEK NGCAALIHNF IPGADPMKSY LCAPDLIPAT
KHQPNQEDLG SNPSPPVLSR QGSLASPCSR TSSLEEEEVY HKAAPSVPLS TKPTVDMEIG
VGNTNYRHSD LAKLYGLPEQ IRSEADEESE EDSEAPSCSP PPQRPHLHQT GVNSTFKSLA
TLLESQKYAY RGGPFGRPPP SALVGVKYSS SLSLGPDICR QQQGSSPTSD STSPPFSPAV
PSQKSFPHSL LEDKKIKTED SDVWTDEGEM EERVNSMEER KTIKPIKVIK TEQELTTISE
SSLKELGKSC EVMLCRHSLD RSDRQVKSED RDKPEKVKEH KDKKRKHGHS HSSRKYKDKK
ERKKHREKRD DASSSSSSSS SSHKRHRDGK SHKEKKHRRV LGDLNLHRRE SEKDRAHCES
DKKKRKDGFG SSSERAAWTS SSGEVSSEPK NGTDAGSLLG STDLMKLKAL SDGPPKELKI
RLIKVESGDR ETFIASEVEE KRIPLAEISI KNTASEIIRS CKSARIKGKF KESYLLQAFS
VKPIISTDEP IPREKLNPPT PSIYLESKRD AFSPVLLQFC TDPKNPVTVI RGLAGSLRLN
LGLFSTKSLV EASADQAVEV RTQVQQPADE NWNASGTGQT WPCESSRSYT TIAKYAQYQA
SSFQESLQEE KGSDEEDEDD EKKPLVGADA NKDGSKESNN GEQKPVGKII KFGTNIDLSD
PKRWKAQLQE LQKLPAFMRV ASSGNMLSHV GHTILGMNTV QLYMKVPGSR TPGHQENNNF
CSVNINIGPG DCEWFSVHED YWEAINDFCE KHGVDYLTGS WWPVLEDLYS ANIPVYRFIQ
RPGDLVWINA GTVHWVQAVG WCNNIAWNVG PLNGYQYQLA LERFEWNEVK KVKSIVPMIH
VSWNVARTVK ITDPDTYKMI KHCLLQSMKH IQILRDQLIS EGKKISYQSR VKDEPAYYCN
ECDVEVFNLL FVTCENSSRK TYVVHCEDCA RQRSPNLNNV VVLEQYRIEE LMNAYDSFVL
ASSSR
//
