ID H3CCQ4_TETNG Unreviewed; 838 AA.
AC H3CCQ4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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};
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:ENSTNIP00000006027.1, 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:ENSTNIP00000006027.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine;
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:ARBA00023995};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60345;
CC Evidence={ECO:0000256|ARBA:ARBA00023995};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4]
CC + S-adenosyl-L-homocysteine; 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:ARBA00001543};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61993;
CC Evidence={ECO:0000256|ARBA:ARBA00001543};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60348, Rhea:RHEA-COMP:15555, Rhea:RHEA-
CC COMP:15556, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; EC=2.1.1.362;
CC Evidence={ECO:0000256|ARBA:ARBA00000167};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60349;
CC Evidence={ECO:0000256|ARBA:ARBA00000167};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; H3CCQ4; -.
DR STRING; 99883.ENSTNIP00000006027; -.
DR Ensembl; ENSTNIT00000006175.1; ENSTNIP00000006027.1; ENSTNIG00000003440.1.
DR GeneTree; ENSGT00940000156431; -.
DR HOGENOM; CLU_328991_0_0_1; -.
DR InParanoid; H3CCQ4; -.
DR OMA; NDHAQTK; -.
DR TreeFam; TF106433; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR CDD; cd19184; SET_KMT5B; 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:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE KMT5B-RELATED; 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 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Myogenesis {ECO:0000256|ARBA:ARBA00022541};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 171..286
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 93576 MW; F25CC5F264376048 CRC64;
MKWLGESKNM VLNGRRHGAK LTSETPGSQN QTRSQNPQRA SLRHSKNRNR RCSRRFNAAN
PEAERRYVPS SGMTAKELCE NDDLTTSLIL DPYLGFQTHK MNTRFRPIKG RQEELKELIE
GFKKHDNLEK TFRALTSADW SRNLFLHKTK AQEKLFKQHV FVYLRMFATD SGFEILPCNR
YSSEQNGAKI VATKAWKRND KIEYLVGCIA ELSESEENML LRHGENDFSV MYSTRKNCAQ
LWLGPAAFIN HDCRPNCKFV STGRDTACVK VLRDIEPGEE ISCYYGDGFF GENNEFCECY
TCERRGTGAF KSKAGLQVEV PVINSKYGLR ETDKRLNRLK KMEEGSKSSD GNSVGSQTTV
DSQEIKRTSS SSSSSSGLKF KNRTQSRQTW SRPVTTSCSK QGRVNNNRVP KRLKSQPKPS
LSKVQLRSRR AGAEPKALAK AETCQLGLRC KGVTVKKEKG GQELLEQTLA QQGCLTRHAA
KESCALAHVR GSDASQCSAY RTRRSTRTHV KAQDSSAGLT LEASALDGLS PVPGGVVIKT
EPADMEEYLH PPIGLQQPAL EGSYAQRGSC PRRKRLARLR TKRTIKTEDS YGEAFVPVSS
GHAASFSDCS SVLVNFADRH RDYNGVANGG KAKGGCRSQD RGKKKRRITR YDAQLILENN
TGIPKLTLRR RRDSSSSKTG DPMATSNLSA SAVNPASSSK ISIKFSKERD KEKGGSYIAK
LNNGFAPAVH ANATKLKIHL KREDDARRLS QAKAEQVAFN GDVAQTLDAR NGAHWTQNVL
AEPSSDEDEE DDYFDNEFED DFIPLPPAKR LRLIVGKDSI DIDISSRRRE DQSLRLNA
//
