ID   H0ZI28_TAEGU            Unreviewed;       850 AA.
AC   H0ZI28;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   02-SEP-2026, entry version 71.
DE   RecName: Full=[histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B {ECO:0000256|ARBA:ARBA00031786};
DE            EC=2.1.1.361 {ECO:0000256|ARBA:ARBA00012187};
DE            EC=2.1.1.362 {ECO:0000256|ARBA:ARBA00012188};
DE   AltName: Full=[histone H4]-lysine20 N-methyltransferase KMT5B {ECO:0000256|ARBA:ARBA00031835};
GN   Name=KMT5B {ECO:0000313|Ensembl:ENSTGUP00000010245.2};
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Passeroidea; Estrildidae; Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000010245.2, ECO:0000313|Proteomes:UP000007754};
RN   [1] {ECO:0000313|Ensembl:ENSTGUP00000010245.2, ECO:0000313|Proteomes:UP000007754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20360741; DOI=10.1038/nature08819;
RA   Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA   Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA   Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA   Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA   Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA   Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA   Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA   McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA   Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA   Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA   Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA   Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA   Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA   Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT   "The genome of a songbird.";
RL   Nature 464:757-762(2010).
RN   [2] {ECO:0000313|Ensembl:ENSTGUP00000010245.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = N(6)-
CC         methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine + H(+);
CC         Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361;
CC         Evidence={ECO:0000256|ARBA:ARBA00048226};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60345;
CC         Evidence={ECO:0000256|ARBA:ARBA00048226};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = N(6)-methyl-L-
CC         lysyl-[histone] + S-adenosyl-L-homocysteine + H(+);
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU00903};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC         methionine = N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] + S-
CC         adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:61992, Rhea:RHEA-
CC         COMP:15556, Rhea:RHEA-COMP:15998, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC         ChEBI:CHEBI:61976; Evidence={ECO:0000256|ARBA:ARBA00048602};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61993;
CC         Evidence={ECO:0000256|ARBA:ARBA00048602};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine
CC         = N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC         homocysteine + H(+); Xref=Rhea:RHEA:60348, Rhea:RHEA-COMP:15555,
CC         Rhea:RHEA-COMP:15556, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC         EC=2.1.1.362; Evidence={ECO:0000256|ARBA:ARBA00048710};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60349;
CC         Evidence={ECO:0000256|ARBA:ARBA00048710};
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. Histone-lysine methyltransferase family. Suvar4-20
CC       subfamily. {ECO:0000256|PROSITE-ProRule:PRU00903}.
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DR   AlphaFoldDB; H0ZI28; -.
DR   STRING; 59729.ENSTGUP00000010245; -.
DR   Ensembl; ENSTGUT00000010354.2; ENSTGUP00000010245.2; ENSTGUG00000009927.2.
DR   GeneTree; ENSGT00940000156431; -.
DR   HOGENOM; CLU_328991_0_0_1; -.
DR   InParanoid; H0ZI28; -.
DR   OMA; NDHAQTK; -.
DR   Proteomes; UP000007754; Chromosome 5.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0140944; F:histone H4K20 monomethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0140941; F:histone H4K20me methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:Ensembl.
DR   GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR   CDD; cd19184; SET_KMT5B; 1.
DR   FunFam; 1.10.10.1700:FF:000001; Histone-lysine N-methyltransferase; 1.
DR   FunFam; 2.170.270.10:FF:000006; Histone-lysine N-methyltransferase; 1.
DR   Gene3D; 1.10.10.1700; Histone-lysine N-methyltransferase; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR041938; Hist-Lys_N-MTase_N.
DR   InterPro; IPR044424; KMT5B_SET.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR039977; Suv4-20/Set9.
DR   InterPro; IPR025790; Suv4-20_animal.
DR   PANTHER; PTHR12977:SF12; HISTONE-LYSINE N-METHYLTRANSFERASE KMT5B; 1.
DR   PANTHER; PTHR12977; SUPPRESSOR OF VARIEGATION 4-20-RELATED; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR   PROSITE; PS50280; SET; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00903}; Myogenesis {ECO:0000256|ARBA:ARBA00022541};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU00903};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00903}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          168..283
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          684..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..353
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..405
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..609
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..813
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         282
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00190"
SQ   SEQUENCE   850 AA;  95565 MW;  78889F9426CD1860 CRC64;
     MKWLGESKNM VVNGRRSGSK SSNDHAQTKL QHAGKENPKT GKNGVERRSS RCSGASGFEG
     QSRYVPSSGM SAKELCENDD LATSLVLDPY LGFQTHKMNT RFRPIKGRQE ELKEVIERFK
     KDEHLEKAFK SLTSGDWARH YFLNKNKMQE RLFKEHVFIY LRMFATDSGF EILPCNRYSS
     EQNGAKIVAT KEWKRNDKIE LLVGCIAELS EMEENMLLRH GENDFSVMYS TRKNCAQLWL
     GPAAFINHDC RPNCKFVSTG RDTACVKALR DIEPGEEISC YYGDGFFGEN NEYCECYTCE
     RRGTGAFKSR VGLPAPTPVI NSKYGLRETD KRLNRLKKLG DSSKNSDSQS VSSNTDADTT
     QEKANRKSSI GVKKNSKNRT LTRQSISRIP ASSNSTSSKL THINNSRVPK RLKKPAKPLL
     SKIKLRNQCK RPEQKNASRK LEMGNLVLKE PKVVLYKNLP IKKDKELEGP VKVAVSSGCL
     TRHAAREHKL NSVKGAYEHG GIAPCTYITR RSMRTRMSLK ETSDTKLEPN TLDSYQSNLT
     GTQSDIAEQQ SRALNNNVAH GPSHKGEGRC QKSDAGTSKK KSRQGKLVKP SSKTEESDTM
     HNTPVKDEVP DLISSHSELE ERNNVVDAPV GFKDCIPGSG GCSVTTDNFK AKDSFRTAKS
     KKKRRITRYD AQLILENSSG IPKLTLRRRH DSSSKANDQE SDGMNSSKIS IKLSKDHEKD
     NNLYVAKLNN GFNSGSGNSS TKLKIQLKRE DENRGAYSED LHENGVCCSE TLSLLESRME
     VDDYGHYEEE TADESSSEED DEEEDDYDDE FDDFIPLPPA KRLRLIVGKD SIDIDISSRR
     REDQSLRLNA
//