SUV42_CAEBR
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 03-AUG-2022, entry version 72.
DE RecName: Full=Histone-lysine N-methyltransferase Suv4-20 {ECO:0000250|UniProtKB:Q09265};
DE EC=2.1.1.362 {ECO:0000250|UniProtKB:Q09265, 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., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT 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 transcriptional
CC repression. Contributes to dosage compensation of X chromosome-relative
CC to autosome-linked gene expression, possibly by converting H4K20me1 to
CC H4K20m2/me3 on autosomes. Involved in the regulation of growth and body
CC fat metabolism downstream of the TOR complex 2 pathway.
CC {ECO:0000250|UniProtKB:Q09265}.
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:Q09265, ECO:0000255|PROSITE-
CC ProRule:PRU00903};
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:Q09265,
CC 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 methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar4-20
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00903}.
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DR EMBL; HE601438; CAP23921.1; -; Genomic_DNA.
DR RefSeq; XP_002630905.1; XM_002630859.1.
DR AlphaFoldDB; A8WTV9; -.
DR SMR; A8WTV9; -.
DR STRING; 6238.CBG02629; -.
DR GeneID; 8572421; -.
DR KEGG; cbr:CBG_02629; -.
DR CTD; 8572421; -.
DR WormBase; CBG02629; CBP47083; WBGene00025648; Cbr-set-4.
DR eggNOG; KOG2589; Eukaryota.
DR HOGENOM; CLU_040002_1_1_1; -.
DR InParanoid; A8WTV9; -.
DR OMA; RDHIVRF; -.
DR OrthoDB; 889290at2759; -.
DR Proteomes; UP000008549; Chromosome II.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034772; P:histone H4-K20 dimethylation; IEA:InterPro.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IBA:GO_Central.
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 3: Inferred from homology;
KW Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..326
FT /note="Histone-lysine N-methyltransferase Suv4-20"
FT /id="PRO_0000396641"
FT DOMAIN 163..273
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 294..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
