KMT5C_XENLA
ID KMT5C_XENLA Reviewed; 761 AA.
AC A0JMZ4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Histone-lysine N-methyltransferase KMT5C {ECO:0000305};
DE AltName: Full=Lysine-specific methyltransferase 5C {ECO:0000250|UniProtKB:Q86Y97};
DE AltName: Full=Suppressor of variegation 4-20 homolog 2;
DE Short=Su(var)4-20 homolog 2;
DE Short=Suv4-20h2;
DE AltName: Full=[histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B {ECO:0000250|UniProtKB:Q86Y97};
DE EC=2.1.1.362 {ECO:0000250|UniProtKB:Q86Y97};
DE AltName: Full=[histone H4]-lysine20 N-methyltransferase KMT5B {ECO:0000250|UniProtKB:Q86Y97};
DE EC=2.1.1.361 {ECO:0000250|UniProtKB:Q86Y97};
GN Name=kmt5c {ECO:0000250|UniProtKB:Q86Y97}; Synonyms=suv420h2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone methyltransferase that specifically methylates
CC monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2)
CC of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2)
CC and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription
CC and maintenance of genome integrity. In vitro also methylates
CC unmodified 'Lys-20' (H4K20me0) of histone H4 and nucleosomes (By
CC similarity). H4 'Lys-20' trimethylation represents a specific tag for
CC epigenetic transcriptional repression. Mainly functions in pericentric
CC heterochromatin regions, thereby playing a central role in the
CC establishment of constitutive heterochromatin in these regions. KMT5C
CC is targeted to histone H3 via its interaction with RB1 family proteins
CC (RB1, RBL1 and RBL2) (By similarity). Facilitates TP53BP1 foci
CC formation upon DNA damage and proficient non-homologous end-joining
CC (NHEJ)-directed DNA repair by catalyzing the di- and trimethylation of
CC 'Lys-20' of histone H4 (By similarity). May play a role in class switch
CC reconbination by catalyzing the di- and trimethylation of 'Lys-20' of
CC histone H4 (By similarity). {ECO:0000250|UniProtKB:Q6Q783,
CC ECO:0000250|UniProtKB:Q86Y97}.
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:0000250|UniProtKB:Q86Y97};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60349;
CC Evidence={ECO:0000250|UniProtKB:Q86Y97};
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:0000250|UniProtKB:Q86Y97};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61993;
CC Evidence={ECO:0000250|UniProtKB:Q86Y97};
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:0000250|UniProtKB:Q86Y97};
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}.
CC Note=Associated with pericentric heterochromatin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar4-20
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00903}.
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DR EMBL; BC126060; AAI26061.1; -; mRNA.
DR RefSeq; NP_001090519.1; NM_001097050.1.
DR AlphaFoldDB; A0JMZ4; -.
DR SMR; A0JMZ4; -.
DR DNASU; 779432; -.
DR GeneID; 779432; -.
DR KEGG; xla:779432; -.
DR CTD; 779432; -.
DR Xenbase; XB-GENE-6252183; kmt5c.L.
DR OrthoDB; 236983at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 779432; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0034772; P:histone H4-K20 dimethylation; IEA:InterPro.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0045830; P:positive regulation of isotype switching; ISS:UniProtKB.
DR Gene3D; 1.10.10.1700; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR041938; Hist-Lys_N-MTase_N.
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; PTHR12977; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR PROSITE; PS50280; SET; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Chromosome; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Zinc.
FT CHAIN 1..761
FT /note="Histone-lysine N-methyltransferase KMT5C"
FT /id="PRO_0000281796"
FT DOMAIN 109..218
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 445..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86Y97"
FT BINDING 114..117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86Y97"
FT BINDING 121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86Y97"
FT BINDING 160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86Y97"
FT BINDING 182..183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86Y97"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q86Y97"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q86Y97"
FT BINDING 230
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86Y97"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q86Y97"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q86Y97"
SQ SEQUENCE 761 AA; 85058 MW; 077E1547D9ED5149 CRC64;
MGSNRLTARE LCENDDLATS LVLDPYLGFR THKMNVSAMP TIRRQHHLRE ALQTFCKKKD
LEAAYQSLTA GGWARHYFHS RTRQQESLLK THIFRYLRMF LPESGFMILS CSRYSLEMNG
AKVVSTKSWS KNEKIELLVG CIAELSKADE TLLRFGDNDF SVMYSTRKKC AQLWLGPAAF
INHDCRPNCK FVPTEGNTAC VKVLREIKTG EEITCFYGDS FFGEKNEMCE CCTCERKGDG
AFKQQNTEQT VSTSLEKYQL RETDGRLKRL SESACKPSPQ VTTKKKGSKL RLSLRLKRIP
ASRRKGAFYR RVKTFASSRY FYKSHLMKHI PLKPVKIALP RGTVLRDVRI ILHNCKKCNQ
ASRPKSQHER QCCKLGKEPL VSLRREDLSP ERLKFRLSCP GGSCPPIIQT ANVGCNAKDC
SQTEAGKSNL EQITTAELCE HLSFSPVPSH NEDDNSFYEP EIPGSLLGPE SPSSEPLSNN
LNLECNSPEP IVINTVYPHY NGGVTSDSHP HALKQFGITH YIQVDLRKDV TLEPGRSQPD
KSSLEAEKKQ IPNNKHSQHP VISDDHLVAN LNAETQSNAV SPPTNTPICE ALNGSLEHKV
FSLRSRPVSF RPRKTSDNKI TLFKRRRSSV KQGVRCVKLN GHVKLTGQLV PSKLHPPPGA
GANHLTDAMH SDPKLLLKPY VELGLNNNLK RQSLTGLPPS TVLTGDAFNI LHSPPASKQS
TEGATKNVAF NPFTPSKRLR LVVSHGSIAL DMASTSSEET S
