GenomeNet

Database: UniProt
Entry: Q297V5
LinkDB: Q297V5
Original site: Q297V5 
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   16-JAN-2019, entry version 72.
DE   RecName: Full=Histone-lysine N-methyltransferase PR-Set7 {ECO:0000250|UniProtKB:Q9VFK6};
DE            EC=2.1.1.43;
DE   AltName: Full=PR/SET domain-containing protein 07;
GN   Name=PR-Set7 {ECO:0000250|UniProtKB:Q9VFK6};
GN   ORFNames=GA17259 {ECO:0000312|FlyBase:FBgn0077272};
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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.,
RA   Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J.,
RA   van Batenburg M.F., Howells S.L., Scherer S.E., Sodergren E.,
RA   Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D.,
RA   Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D.,
RA   Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R.,
RA   Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L.,
RA   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:
RT   chromosomal, gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       monomethylates 'Lys-20' of histone H4. H4 'Lys-20' monomethylation
CC       is enriched during mitosis and represents a specific tag for
CC       epigenetic transcriptional repression. Mainly functions in
CC       euchromatin regions, thereby playing a central role in the
CC       silencing of euchromatic genes. Required for cell proliferation,
CC       possibly by contributing to the maintenance of proper higher-order
CC       structure of DNA and chromosome condensation during mitosis (By
CC       similarity). {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:PRU00904};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}. Note=Specifically localizes to mitotic chromosomes.
CC       Associates to chromatin-dense and transcriptionally silent
CC       euchromatic regions (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. PR/SET subfamily. {ECO:0000255|PROSITE-ProRule:PRU00904}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL28100.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; CM000070; EAL28100.2; ALT_SEQ; Genomic_DNA.
DR   SMR; Q297V5; -.
DR   STRING; 7237.FBpp0284106; -.
DR   PRIDE; Q297V5; -.
DR   FlyBase; FBgn0077272; Dpse\GA17259.
DR   InParanoid; Q297V5; -.
DR   Proteomes; UP000001819; Chromosome 2.
DR   Proteomes; UP000001819; Unassembled WGS sequence.
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:0016571; P:histone methylation; ISS:UniProtKB.
DR   InterPro; IPR016858; Hist_H4-K20_MeTrfase.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 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   Complete proteome; Methyltransferase; Mitosis; Nucleus;
KW   Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    691       Histone-lysine N-methyltransferase PR-
FT                                Set7.
FT                                /FTId=PRO_0000317003.
FT   DOMAIN      555    676       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      565    567       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   REGION      637    638       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   BINDING     610    610       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                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
//
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