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Database: UniProt/SWISS-PROT
Entry: KMT5C_XENLA
LinkDB: KMT5C_XENLA
Original site: 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   16-JAN-2019, entry version 55.
DE   RecName: Full=Histone-lysine N-methyltransferase KMT5C {ECO:0000305};
DE            EC=2.1.1.43;
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;
GN   Name=kmt5c {ECO:0000250|UniProtKB:Q86Y97}; Synonyms=suv420h2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   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
CC       trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation
CC       represents a specific tag for epigenetic transcriptional
CC       repression. Mainly functions in pericentric heterochromatin
CC       regions, thereby playing a central role in the establishment of
CC       constitutive heterochromatin in these regions (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
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; EC=2.1.1.43;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00903};
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
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar4-20 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00903}.
DR   EMBL; BC126060; AAI26061.1; -; mRNA.
DR   RefSeq; NP_001090519.1; NM_001097050.1.
DR   UniGene; Xl.52028; -.
DR   ProteinModelPortal; A0JMZ4; -.
DR   SMR; A0JMZ4; -.
DR   PRIDE; A0JMZ4; -.
DR   GeneID; 779432; -.
DR   KEGG; xla:779432; -.
DR   CTD; 779432; -.
DR   Xenbase; XB-GENE-6252183; kmt5c.
DR   HOVERGEN; HBG100946; -.
DR   KO; K11429; -.
DR   OrthoDB; 236983at2759; -.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IEA:InterPro.
DR   GO; GO:0034773; P:histone H4-K20 trimethylation; IEA:InterPro.
DR   InterPro; IPR025790; Hist-Lys_N-MTase_Suvar4-20.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW   Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    761       Histone-lysine N-methyltransferase KMT5C.
FT                                /FTId=PRO_0000281796.
FT   DOMAIN      109    218       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
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
//
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