ID   KMT5A_DROPS             Reviewed;         691 AA.
AC   Q297V5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=Histone-lysine N-methyltransferase Set8 {ECO:0000250|UniProtKB:Q9VFK6};
DE            EC=2.1.1.361 {ECO:0000250|UniProtKB:Q9VFK6};
DE   AltName: Full=PR/SET domain-containing protein 07;
GN   Name=Set8 {ECO:0000250|UniProtKB:Q9VFK6};
GN   Synonyms=PR-Set7 {ECO:0000250|UniProtKB:Q9VFK6}; ORFNames=GA17259;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Histone methyltransferase that specifically monomethylates
CC       'Lys-20' of histone H4. H4 'Lys-20' monomethylation is enriched during
CC       mitosis and represents a specific tag for epigenetic transcriptional
CC       repression. Mainly functions in euchromatin regions, thereby playing a
CC       central role in the silencing of euchromatic genes. Required for cell
CC       proliferation, possibly by contributing to the maintenance of proper
CC       higher-order structure of DNA and chromosome condensation during
CC       mitosis. {ECO:0000250|UniProtKB:Q9VFK6}.
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:Q9VFK6, ECO:0000255|PROSITE-
CC         ProRule:PRU00904};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC       Note=Specifically localizes to mitotic chromosomes. Associates to
CC       chromatin-dense and transcriptionally silent euchromatic regions (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. Histone-lysine methyltransferase family. PR/SET subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00904}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL28100.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CM000070; EAL28100.2; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q297V5; -.
DR   SMR; Q297V5; -.
DR   STRING; 46245.Q297V5; -.
DR   eggNOG; KOG1085; Eukaryota.
DR   InParanoid; Q297V5; -.
DR   Proteomes; UP000001819; Genome assembly.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005700; C:polytene chromosome; ISS:UniProtKB.
DR   GO; GO:0042799; F:histone H4K20 methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0140944; F:histone H4K20 monomethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0016571; P:histone methylation; ISS:UniProtKB.
DR   CDD; cd10528; SET_SETD8; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR016858; KMT5A-like.
DR   InterPro; IPR047266; KMT5A-like_SET.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   PANTHER; PTHR46167; N-LYSINE METHYLTRANSFERASE KMT5A; 1.
DR   PANTHER; PTHR46167:SF1; N-LYSINE METHYLTRANSFERASE KMT5A; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51571; SAM_MT43_PR_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Chromatin regulator; Chromosome;
KW   Methyltransferase; Mitosis; Nucleus; Reference proteome; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN           1..691
FT                   /note="Histone-lysine N-methyltransferase Set8"
FT                   /id="PRO_0000317003"
FT   DOMAIN          555..676
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..447
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         565..567
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00904"
FT   BINDING         610
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190,
FT                   ECO:0000255|PROSITE-ProRule:PRU00904"
FT   BINDING         637..638
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00904"
SQ   SEQUENCE   691 AA;  74929 MW;  6F565E222ABE4444 CRC64;
     MIMVRRRARP AKETGGGSAA AAVASDGALS MDTAAAVAVA GGNHLLDDQY FASPKRKDCR
     LMKASENLKI SSDVVALEEE ANNKGVKPTK ALTDRTIGVP LATRSQTRTI ENFFKADAAA
     KCGITLNTHH PEPIKEQKTI STTELPLSDE LGDEELERVV GDLLYDGHST ASSDSPSYQN
     ENEHEEVMQD TFALRETSPV PVLMADFQTH RSGLRDSHSS SHSSSSSGGA SATTDNIFLQ
     EPVLTLDIDR TPTKASSIKI NKSFELASAV FSSPPSVLNA CRFNQIVTLN GGGQCEPQPV
     VVAQPQPQPQ LQLPPHHNGF ELDQHDSSSC DSGVACNLTI SAESPAAGGG AGAAARRRKP
     ATPHRILCPS PIKTLPRGDG GGLIVPGARK TSGIMMKGDL LSPRKSPRKL PTTTAAVAAC
     KSRRRLNQPK PQAPYQPQQP QPPPGTQPTN EDVVAAEELE NLNKIPIANS NKSNNHVKAM
     LKPAPAKPRA ALTKGSKTKT GSKIQPGPLP LAATNGNREM TDFFPVRRSV RKTKTAVKEE
     WLRNLEQAVL EERSEGLQVR NFMGKGRGVV AVRHFKRNEF VVEYVGDLIS ISDATDRERR
     YALDENAGCY MYYFKHKNQQ YCIDATVDTG KLGRLINHSR AGNLMTKVVV IKQRPHLVLL
     AKDDIAPGEE LTYDYGDRSK ESLLHHPWLA F
//