ID H3BWG1_TETNG Unreviewed; 1493 AA.
AC H3BWG1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=KDM5A {ECO:0000313|Ensembl:ENSTNIP00000000323.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000000323.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000000323.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; ENSTNIT00000001351.1; ENSTNIP00000000323.1; ENSTNIG00000006790.1.
DR GeneTree; ENSGT00940000157170; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
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; cd16873; ARID_KDM5A; 1.
DR CDD; cd15515; PHD1_KDM5A_like; 1.
DR CDD; cd15686; PHD3_KDM5A; 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); 2.
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; IPR047974; KDM5A_ARID.
DR InterPro; IPR047972; KDM5A_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:SF17; LYSINE-SPECIFIC DEMETHYLASE 5A; 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; 2.
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; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
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:UP000007303};
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 285..335
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 429..595
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1433..1487
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 185..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1493 AA; 170628 MW; C8F3D7C0AFD4CED6 CRC64;
VNMSVFAEFV PPPECPVFEP SWEDFSDPLG FINKIRPIAE KTGICKIRPP EDWQPPFACD
VRNFRFTPRI QRLNELEALT RVKLNFLDQI AKFWELQGSK IRFPHVERKV LDLYRLSKIV
SSEGGFEAVC KEKRWSKVSS RMGYPSGRGT GSLLRSHYER ILYPYELFQS GATLTGIQRL
YEEGDDPEEL DEGVGEHDEM QSKSHLLPER RSRRLKSEVS PILRENKEPK GLKIFDASPK
MMGLEIVADD GFNKKQRQLK AQAFAIKMRP RKETLEVNVM PQIDLYFCLV CGRGDEEDRL
LLCDGCDDSY HTFCLIPPLQ DVPKGDWRCP KCVAEECSKP REAFGFEQAV REYSLQSFGE
MADQFKSDYF NMPVHMVPTE LVEKEFWRLV SSIEEDVIVE YGADISSKEV GSGFPVRDGK
RRLLGDEEEY ANSGWNLNNM PVLEQSVLTH INVDISGMKV PWLYVGMCFS SFCWHIEDHW
SYSINFLHWG EPKTWYGVPA SAAEQLEAVM KKLAPELFDS QPDLLHQLVT IMNPNVLMEH
GVPVYRTNQC AGEFVVTFPR AYHSGFNQGY NFAEAVNFCT ADWLPMGRQC VAHYRRLHRY
CVFSHEELLC KMAADPESLD VELAASVFKE MGETMEEETK LRQAAQKLGV LSSEQEVFEL
LPDDERQCYK CKTTCFLSAL TCSCSPDRLV CLHHAADLCD CPHGNKCLRY RYDLEEFPAM
LYGVKTRAQS YDTWSKRVTE ALSADQKNKK DLIELKVLLE DAEDRKYPEK SLFRRLREMV
KEAETCSSVA QLLLSRKQRH SLQQSLRSEN TCNRTKLTVD ELKAFVDQLY RLPCIISQAR
QVKELLEKVE EFHERAQALS DEMPDSSKLQ ALLDLGSGLD VELPELPRLK QELQQARWLD
EVRVTLAEPH RVTLELMKRL IDSGVGLAPH HAVEKAMAEL QEILTVSERW EDKARACLQA
RPPHSLVTLE SIVLEARNIP AYLPNILALR EALQKAKDWT TKVEAIQVLS LLEQASQLES
LLARGRSIPV RLDPLAHVES QVAAARAWRE RTGRTFLKKN STYTLLQVLS PRIDIGVYGN
SKSKRKRVKE LMEKERGGFD PDVLSDLEDS KEEVRDPSSV VTAYKSKEQK EVESIHSLRA
ANLAKMAMAD RIEEVKFCLC RKTASGFMLQ CELCKDWFHG ACVPLPKTGL QKKLVLVFLC
QRSRRPRLET ILSLLVSLQK LPVRLPEGEA LQCLTERAMS WQDQARQSLA TEELSSALAK
LSVLSQQTSF HRVTSRHSSS QVSVEPRHPA SLWIMTTRRR TQMRTSGRLM VLQNAKAQLE
ELMMLGDLLE VSLDETQHIW RILQATHPPS EGDMRPPKSK DLKRVGLELG LGKSKKKKLK
LNLNKNREMK QLAKRLAKEE RGEDGLEKRK EKKILDIPSK YDWSGAEDSN DENAVCAAKN
CQRPCKDKVD WVQCDGGCDE WFHQVCVGVT CEMAENEDYI CVDCSRKAAG GSD
//
