ID A0A3P9MX72_POERE Unreviewed; 1382 AA.
AC A0A3P9MX72;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
GN Name=KDM5B {ECO:0000313|Ensembl:ENSPREP00000001921.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000001921.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000001921.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000001921.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000256|ARBA:ARBA00000604};
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 JARID1 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00006801}.
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DR Ensembl; ENSPRET00000001966.1; ENSPREP00000001921.1; ENSPREG00000001348.1.
DR GeneTree; ENSGT00940000157076; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000001348; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0034647; F:histone H3K4me/H3K4me2/H3K4me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16874; ARID_KDM5B; 1.
DR CDD; cd15603; PHD1_KDM5B; 1.
DR CDD; cd15687; PHD3_KDM5B; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR048615; KDM5_C-hel.
DR InterPro; IPR047981; KDM5B_ARID.
DR InterPro; IPR047978; KDM5B_PHD1.
DR InterPro; IPR047979; KDM5B_PHD3.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF3; LYSINE-SPECIFIC DEMETHYLASE 5B; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF21323; KDM5_C-hel; 1.
DR Pfam; PF00628; PHD; 3.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 15..56
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 80..170
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 231..281
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 375..541
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1093..1147
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1322..1376
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1023..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1382 AA; 156478 MW; 2512A98FF659B28C CRC64;
MSLLRPDEFK PPPECPVFEP SWEEFRDPYA FINKIRPIAE RTGICKVRPP PDWQPPFACD
VDKLHFVPRI QRLNELEAQT RVKLNFLDQI AKFWDLQGCT LKIPHVERKI LDLYKLNKLV
ADEGGFDIVC QDRRWTKIAV QMGFSPGKAV GSHLRGHYER ILYPYNLFQS GANLLVSCTF
TSCSVLVQTT CVKTEPGETG DSKPNLRRRM GSIVVKQEPV DVSAFVSQVD LVVCLVCGSG
GDEDRLLLCD GCDDSYHTFC LIPPLNDVPK GDWRCPKCLA QECSKPHEAF GFEQAHRDYS
LRAFGQMADA FKSDYFNMPV HMVPMELVEK EFWRLVGAIE EDVTVEYGAD IASKEFGSGF
PIPNGKFKVS PADEKYLKCG WNLNNLAMMN PSVLTHVTAD ICGMTLPWLY VGMCFSSFCW
HIEDHWSYSI NYLHWGEPKT WYGAPGFAAE QLEKVMKKLA PELFESQPDL LHQLVTIMNP
NTLMAHGVPI YRTNQCAGEF VITFPRAYHS GFNQGFNFAE AVNFCTVDWM PLGRQCVDHY
RLLHRYNVFS HDEMVCNMAT KAETLNVVLA SAVHKDMALM IKEEQELRDK VKKMGVVNCK
EAKYDHLQDD ERQCANCRTT CYLSAITCPC SQGVLVCLYH INSLCSCHVS NYTLNYRYTM
DDLFPMMNAV KQRAELYDEW ASRVTQTLEA KLEKKKGLPV FRSLLTESET RLFPDNDLLR
RLRLVTQDAE KCASVAQQLL NGKKQTRYRC GSGKSRSQLT VEELSSFVRQ LYNLCCSLPQ
APQLKELLNR IEDFQQHSEK VLVEESPSVV EIQSLLDVSF DFDVDLPELP QLRERLEQAR
WLEAVQLASA QPNMLTLEAM RRLIDQGVGL APHPSVEKAM ARLQEQLTLS EHWEEKASSL
LKARPPHSIE TLSAAAEKAS VIPAHLPNCL LLKDTIRKAR EWLQEAEERQ ASGCVLVADS
LSDMLLRGQA IQVQLEPLDR LESLMADVQK WKESAATTFL LKDSTLTLLE VLCPRFEAGA
AGSPKRKAKK GKESLKNNKK KPTRLNSLSD VEKALSETQD STSAMATLEE LRVREMETFF
SLRAANESKL LPTADCMDLK VCSCQKAPMG AMLQCELCRD AFHSVCVRDP AESRETQPWL
CPHCQRSEKP PLSKVLSLLA SLHDVGVRLP EGDALNYLVE RTLNWQQRTQ QILQTCDLPE
LEERPETPPT LTHWVSGCDN THNNTQGPCS LSLNCELEEL MVEGLLLQVS LPQVQSLYCI
LLDRANSQQS NRAASPAEEE PSEHSKHMQQ KVNKKKLQRR PASTSSSPRS DFSQSDDSDE
EMAVCPAESC LLPEGDEVDW VQCDGRCNQW FHQVCVGVTA ETAEKEDYVC VXCSLNDRQT
RK
//
