ID G1N2Z7_MELGA Unreviewed; 1102 AA.
AC G1N2Z7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 24-JAN-2024, entry version 71.
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 Name=KDM4B {ECO:0000313|Ensembl:ENSMGAP00000006048.3};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000006048.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000006048.3, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000006048.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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 -!- 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 JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
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DR AlphaFoldDB; G1N2Z7; -.
DR Ensembl; ENSMGAT00000006794.3; ENSMGAP00000006048.3; ENSMGAG00000005999.3.
DR GeneTree; ENSGT00940000159248; -.
DR HOGENOM; CLU_001442_0_1_1; -.
DR InParanoid; G1N2Z7; -.
DR TreeFam; TF106449; -.
DR Proteomes; UP000001645; Chromosome 30.
DR Bgee; ENSMGAG00000005999; Expressed in thymus and 17 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR GO; GO:0051864; F:histone H3K36 demethylase activity; IEA:Ensembl.
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 GO; GO:0007420; P:brain development; IEA:Ensembl.
DR CDD; cd15714; ePHD_JMJD2B; 1.
DR CDD; cd15576; PHD_JMJD2B; 1.
DR CDD; cd20464; Tudor_JMJD2B_rpt1; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.10.330.70; -; 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; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047483; Tudor_KDM4B_rpt1.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694:SF7; [HISTONE H3]-TRIMETHYL-L-LYSINE(9) DEMETHYLASE; 1.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF18104; Tudor_2; 2.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
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:UP000001645};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 15..57
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 143..309
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 797..910
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 374..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..465
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 125132 MW; 464AC92CA3F80AB8 CRC64;
MGSENPSPQN PGCKIMTFRP TLEEFRDFGK YVAYIESQGA HRAGLAKVIP PKEWKPRKTY
DDIDDMVIPA PIQQVVTGQS GLFTQYNIQK KPMTVGEYRR LANSEKYCTP RHQDFEDLER
KYWKNLTFVS PIYGADISGS LYDTDVEEWN IGNLNTLLDM VEHECGIIIE GVNTPYLYFG
MWKTTFAWHT EDMDLYSINY LHFGEPKSWY AIPPEHGKRL ERLAKGFFPG SSQGCDAFLR
HKMTLISPSI LKKYGIPFDR ITQEAGEFMI TFPYGYHAGF NHGFNCAEST NFATLRWIDY
GKMATQCTCR KDMVKISMDV FVRVLQPERY DLWKQGKDIA VLDHMKPTAL TSPELDAWNE
TKADLKAKLL RRIGDEEEDN KHRSHRKRSQ PRRHKTEDQK SLGDVMAIET ALEDVKVKEE
LKRGPDLEEE DRSKVVEGEG DSKVKARPPK VKGERKKKHL FHQHQHHLQT SQPLQQQQQQ
QLPLPPAVQQ QQAEEEAAAA PAASTADKSL LTTPLNIVQP SEAPVEEDDF KPRPIIPMLY
VVPRTKKVVF DKEHMSCQQA FEQFATQKSP GWREQTVSLE IPVKEEESAE AENTEIATET
AAFSKMKMEI KKSRRHPLGK PPTRSPLSVV KQETSSDEET FPFSGEEDMS DPEALKSLLS
LQWKNKAPNF PAERKFNAAA ALSEPYCAVC TLFYPYNQSL QMDKEAVPVS AGETTSFVHL
SKCGQKTKPL IPEMCFTSSG ENIEPLPSNS YIGEDGTSSL ISCAKCCLQV HASCYGIRPD
LVNESWSCSR CSANAWAAEC CLCNLRGGAL QMTTDGRWVH IICAIAVPEA RFLNVIERHP
VDIAAIPEQR WKLKCVYCRK RMKKVSGACI QCSYEHCSTS FHVTCAHAAG VPMEPDDWPY
VVSITCFKHK AANQNIQFRR EVTLGQTVIT KNRNGLYYRC KVIGMTTQTF YEVNFDDGSY
SDNVYPESII SRDCIQLGPP PEGEMVQLQW TDGIIYKAKF IAAQINHIYQ VEFEDGSQLM
VKRGDIYTLE EELPKRVKSR LSLSTGAPQE DVFSGDEMRA AKRPRLGNAR NPEEYGQNPD
YLAFMESLLQ TQYQPGTQSN MF
//