ID I3KCV8_ORENI Unreviewed; 865 AA.
AC I3KCV8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 62.
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 Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000018953.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000018953.2}
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; I3KCV8; -.
DR Ensembl; ENSONIT00000018970.2; ENSONIP00000018953.2; ENSONIG00000015056.2.
DR GeneTree; ENSGT00940000156431; -.
DR InParanoid; I3KCV8; -.
DR OMA; NDHAQTK; -.
DR Proteomes; UP000005207; Linkage group LG1.
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:UP000005207};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 173..288
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..826
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 97687 MW; 6DA98EEFC5909475 CRC64;
MKWLGESKNM VLNGRRHGNK LTGEQTVSQS QTRSQHPQRA SLRHNKSHTR NRRCSRRFNA
ASLEAERRYV PSSGMTAKEL CENDDLTTSL ILDPYLGFQT HKMNTRFRPI KGRQEELKEI
IERFKKHDNL EKAFKALTSG DWARNIFLHK TKAQEKLFKQ HVFVYLRMFA TDSGFEILPC
NRYSSEQNGA KIVATKEWKR NDKIEYLVGC IAELSESEEN LLLRHGENDF SVMYSTRKNC
AQLWLGPAAF INHDCRPNCK FVSTGRDTAC VKVLRDIEPG EEISCYYGDG FFGENNEFCE
CYTCERRGTG AFKSKAGLPV EVPVINSKYG LRETDKRLNR LKKLGEGNRT SDSHSVGSHT
DVDSQEMPKT HQSARKRTSS SSSSSGLKYK NRTQTRQTLS RALTTSCSKQ GRVNRVPKRL
RSQSKPSLSK VQLRSRKRVA EPKALAKRET CQLGLTDSKM SLCKGVTVKK EKDGQELVQQ
TLGQQGYLTR HTAKENGHLP AVQSSEGSQC SMYRTRRSTR TLVKARETAS GVKLEPSAMD
GLSPVPGGVV IKTEPADMEE YLHHGVELEH PSLDAGYARR RSSTRQKRPA RLRTERTIKC
EDTYGESFTQ VVGSHAADFS DCGNMLLSFA DQHRDYNCVT HGSKSFHRDK GKGSCRSQDK
GKKKRRITRY DAQLILENNT GIPKLTLRRR RDSSSSKTTD PNDPVGSSHL SASTVNSPSS
SKISIKFSKD HDKDKGSSYI AKLNNGFAPV VHSNSTKLKI QLKREDDARR LSQTKVDQIS
FNGDMSQGLE TRNGGHLTQK VLADPSSDDE DKEGEDDDDY FDNEFEDDFI PLPPAKRLRL
IVGKDSIDID ISSRRREDQS LRLNA
//
