GenomeNet

Database: UniProt
Entry: A8WTV9
LinkDB: A8WTV9
Original site: A8WTV9 
ID   SUV42_CAEBR             Reviewed;         326 AA.
AC   A8WTV9;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   16-JAN-2019, entry version 59.
DE   RecName: Full=Histone-lysine N-methyltransferase Suv4-20 {ECO:0000250|UniProtKB:Q09265};
DE            EC=2.1.1.43 {ECO:0000255|PROSITE-ProRule:PRU00903};
DE   AltName: Full=SET domain-containing protein 4 {ECO:0000250|UniProtKB:Q09265};
GN   Name=set-4 {ECO:0000312|EMBL:CAP23921.1}; ORFNames=CBG02629;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP23921.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP23921.1};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A.,
RA   D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E.,
RA   Griffiths-Jones S., Harris T.W., Hillier L.W., Kamath R.,
RA   Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P.,
RA   Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M.,
RA   Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M.,
RA   Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for
RT   comparative genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Histone methyltransferase that specifically di- and
CC       trimethylates 'Lys-20' of histone H4 (H4K20me2/me3). H4 'Lys-20'
CC       trimethylation represents a specific tag for epigenetic
CC       transcriptional repression. Contributes to dosage compensation of
CC       X chromosome-relative to autosome-linked gene expression, possibly
CC       by converting H4K20me1 to H4K20m2/me3 on autosomes. Involved in
CC       the regulation of growth and body fat metabolism downstream of the
CC       TOR complex 2 pathway. {ECO:0000250|UniProtKB:Q09265}.
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 {ECO:0000250|UniProtKB:Q09265}.
CC       Chromosome {ECO:0000250|UniProtKB:Q09265}.
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; HE601438; CAP23921.1; -; Genomic_DNA.
DR   RefSeq; XP_002630905.1; XM_002630859.1.
DR   ProteinModelPortal; A8WTV9; -.
DR   SMR; A8WTV9; -.
DR   STRING; 6238.CBG02629; -.
DR   GeneID; 8572421; -.
DR   KEGG; cbr:CBG02629; -.
DR   CTD; 8572421; -.
DR   WormBase; CBG02629; CBP47083; WBGene00025648; Cbr-set-4.
DR   eggNOG; KOG2589; Eukaryota.
DR   eggNOG; ENOG410XPH8; LUCA.
DR   HOGENOM; HOG000007250; -.
DR   InParanoid; A8WTV9; -.
DR   KO; K11429; -.
DR   OMA; KMNISPA; -.
DR   OrthoDB; 889290at2759; -.
DR   Proteomes; UP000008549; Chromosome II.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Chromatin regulator; Chromosome; Complete proteome; Methyltransferase;
KW   Nucleus; Reference proteome; Repressor; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN         1    326       Histone-lysine N-methyltransferase Suv4-
FT                                20.
FT                                /FTId=PRO_0000396641.
FT   DOMAIN      163    273       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
SQ   SEQUENCE   326 AA;  37513 MW;  B42DA8EDC7809F23 CRC64;
     MSHAPGEGRP VSSLFPARCN EEVASQNATT MATLNEIELS EIEELSLNFK ETPRQDHSMT
     PVELCYFDDF ATTLVVDAVL NFSTHKMCKK RRYLYGDEQR VARELMERFR KDQDWTPAIY
     GFLNMRSVRS FIEKLAFNKQ LEFRDHIIRF LNVFHHDSGY TIQECTRYSL EGNQGAKLVA
     TRAWYRGDKI QRLSGVVCLL STQDEDTILQ PEGSDFSVMY SNRKRCSTLW LGPGAYINHD
     CRPTCEFVSH GSTAHIRVLR DMVAGDEITC FYGSEFFGPK NMDCECLTCE KTKRGKFSTS
     DEEENDEPSA LSEKRIKYGL RSRSRV
//
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