ID A0A3Q4H1M7_NEOBR Unreviewed; 1646 AA.
AC A0A3Q4H1M7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Lysine-specific demethylase {ECO:0000256|RuleBase:RU369087};
DE EC=1.14.11.65 {ECO:0000256|RuleBase:RU369087};
GN Name=KDM3B {ECO:0000313|Ensembl:ENSNBRP00000015516.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000015516.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000015516.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of
CC histone H3, thereby playing a central role in histone code.
CC {ECO:0000256|RuleBase:RU369087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:60188, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.65;
CC Evidence={ECO:0000256|RuleBase:RU369087};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|RuleBase:RU369087};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|RuleBase:RU369087};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU369087}.
CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the
CC association with nuclear receptors. {ECO:0000256|RuleBase:RU369087}.
CC -!- DOMAIN: The JmjC domain and the C6-type zinc-finger are required for
CC the demethylation activity. {ECO:0000256|RuleBase:RU369087}.
CC -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family.
CC {ECO:0000256|RuleBase:RU369087}.
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DR Ensembl; ENSNBRT00000015939.1; ENSNBRP00000015516.1; ENSNBRG00000011731.1.
DR GeneTree; ENSGT00940000158095; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000011731; Expressed in blood and 9 other cell types or tissues.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070988; P:demethylation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1.
DR PANTHER; PTHR12549:SF8; LYSINE-SPECIFIC DEMETHYLASE 3B; 1.
DR Pfam; PF02373; JmjC; 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|RuleBase:RU369087};
KW Metal-binding {ECO:0000256|RuleBase:RU369087};
KW Nucleus {ECO:0000256|RuleBase:RU369087};
KW Reference proteome {ECO:0000313|Proteomes:UP000261580}.
FT DOMAIN 1374..1597
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 241..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1646 AA; 180195 MW; 0B8B336EF8ED7811 CRC64;
MQTMEDSLEL IGKRLLLLLD DGRSANGSES EQAAWARDWL RGTVRAVSVI GLAAPEVSVF
VEFENASQRC SWVQVYDEGV KAVLVEDSIV WARRSDVTDT SGASAPAWPA LTFRSLVDRV
GLGSLVPVEY FGNKNFEFLP DNKTVQRFEV DKDVRHPLLL EQPSLQAAIS SWRTDFELQE
IFRKGSYTIQ GRKVRVYQPE FEECWATGLV SQHDPISHIM EITLDKGEEN QMVDPRVIHV
MLTEEENGRR RKDSETMKGD SGRRRRTASE DGTFPQGRGS SPRYPGHIKE NGRAVATQGA
ADSTTTITPT PPPLKPAPSP FSTASFPSLG QMPVLVPGAP APKASSSPQL EREEGNQAAY
SKTAALVSPG PVTISWSQDS VPSVSLSASV GFSSKTSNWG SQTEGSKTAS GFRLSQAGST
APVFGDVTSQ TNGAPTTTTA SQDAPKPFGF SFGGAKTEAQ PKPDQNLFFQ CMSQKSVTSL
NLTADQTQSK DTNYFTAVSE SLSKEPPSLF KPAAPTEGLK KPEQPKVPEV QQTGNGVFNK
SSSPFQGMGG SPGGRSSGLN VGGPAVSSGA QSASKKNSNN GSSVVGLGLQ SGFNSAESHQ
NLFLQNSKES ANPFLAYGEK SSLTAFVGLT GSEPQSMGPA LDSKPNLFTM AEPPKGILSS
PFPASSAAAS TNCPMFGNAG PGGMEEVPVP FDQSQSQKFS LEDRGQSSKH DSESSSNSDL
SDLSDNEEGL EKGQIPGGPS VSAKDGAIMQ KNKVQGAAKS RPRNKPFKVG QSVLKDQSKV
RRLKQSGESF LQDGSCINVA PHLHKCRECR LERYRKYRNT GEESDDDDDP NVACRFFHFR
RLAFTRKGVL RVEGFLSPQQ SDSMAMGLWL PVPAVHEGLD LDTSKYILAN VGDQFCQLVM
SEKEAMMMVE PHQKVAWKRA VRGVREMCDV CETTLFNIHW VCRKCGFGVC LDCYRLRRNR
PREDVDETPE DEVFSWLKCA KGQPHEPQNL MPTQIIPGTA LYNIGDMVHS ARGKWGIKAN
CPCANRHTKP LVRPTAPNGI SQVQFYNFPS FLFSCLHFEK SVGSTSTSTS GTSSPCNLTQ
SSVKESRSSG EGNSSALHWL ADLATQKAKD DTKESGSLRS IMSRDSRPPF GLDSLSALSK
PSASSPKLFN SLLLGSSMAQ SKPEGSSLRD LLNSGPGKLP QGPGESGVPF PSVFTSAGSD
KLKSSLPNFL DHIIASVVET KKAEGRRTGA SEGGELGALG SRKDGVMGLS VLEPHTSHSW
LCDGRLLCLQ DPSNSNNWKI FRECWKQGQP VLVSGIHKRL KSELWRPDAF SEEFGDQDVD
LVNCRNCAII SDVKVREFWD GFEVISKRLQ DADGLPMVLK LKDWPPGEDF RDMMPTRFDD
LMDNLPLPEY TKRDGRLNLA SRLPNFFVRP DLGPKMYNAY GLISTEDRKV GTTNLHLDVS
DAVNVMVYVG IPHGEDNQEE EVLTTIEEGD VDEMTKRRVH EGKEKPGALW HIYAAKDAEK
IRELLRKVGE EQGQENPPDH DPIHDQSWYL DQVLRRRLYE EYGVQGWAIV QFLGDAVFIP
AGAPHQVHNL YSCIKVAEDF VSPEHVRHCF RLTQEFRHLS TTHTNHEDKL QVKNIIYHAV
KDAIGTLKAH ESKLTRPYSS PQTAGL
//
