KMT5A_DROPS
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 03-AUG-2022, entry version 81.
DE RecName: Full=Histone-lysine N-methyltransferase PR-Set7 {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=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; 7237.FBpp0284106; -.
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 methyltransferase activity (H4-K20 specific); ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016571; P:histone methylation; ISS:UniProtKB.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR016858; Hist_H4-K20_MeTrfase.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 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 PR-Set7"
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
