GenomeNet

Database: UniProt/TrEMBL
Entry: H9Z1X5_MACMU
LinkDB: H9Z1X5_MACMU
Original site: H9Z1X5_MACMU 
ID   H9Z1X5_MACMU            Unreviewed;       412 AA.
AC   H9Z1X5;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   RecName: Full=Histone-lysine N-methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00912};
DE            EC=2.1.1.43 {ECO:0000256|PROSITE-ProRule:PRU00912};
GN   Name=SUV39H1 {ECO:0000313|EMBL:AFH29941.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:AFH29941.1};
RN   [1] {ECO:0000313|EMBL:AFH29941.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Thymus {ECO:0000313|EMBL:AFH29941.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X.,
RA   Pandey S., Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P.,
RA   Tharp G.K., Marcais G., Roberts M., Ferguson B., Fox H.S.,
RA   Treangen T., Salzberg S.L., Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000256|PROSITE-ProRule:PRU00912,
CC       ECO:0000256|SAAS:SAAS00591578}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|SAAS:SAAS00563877}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00574581}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar3-9 subfamily. {ECO:0000256|PROSITE-
CC       ProRule:PRU00912}.
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DR   EMBL; JU473137; AFH29941.1; -; mRNA.
DR   RefSeq; NP_001248256.1; NM_001261327.1.
DR   UniGene; Mmu.32400; -.
DR   ProteinModelPortal; H9Z1X5; -.
DR   SMR; H9Z1X5; -.
DR   GeneID; 711040; -.
DR   KEGG; mcc:711040; -.
DR   CTD; 6839; -.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   KO; K11419; -.
DR   OMA; NTFVMEY; -.
DR   TreeFam; TF106452; -.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd00024; CHROMO; 1.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   InterPro; IPR011381; Histone_H3-K9_MeTrfase.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF009343; SUV39_SET; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54160; SSF54160; 1.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS51579; SAM_MT43_SUVAR39_3; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Chromosome {ECO:0000256|SAAS:SAAS00508265};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR009343-2};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00912,
KW   ECO:0000256|SAAS:SAAS00590675, ECO:0000313|EMBL:AFH29941.1};
KW   Nucleus {ECO:0000256|SAAS:SAAS00574642};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR009343-1,
KW   ECO:0000256|PROSITE-ProRule:PRU00912, ECO:0000256|SAAS:SAAS00591079};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00912,
KW   ECO:0000256|SAAS:SAAS00591533, ECO:0000313|EMBL:AFH29941.1};
KW   Zinc {ECO:0000256|PIRSR:PIRSR009343-2}.
FT   DOMAIN       43     91       Chromo. {ECO:0000259|PROSITE:PS50013}.
FT   DOMAIN      179    240       Pre-SET. {ECO:0000259|PROSITE:PS50867}.
FT   DOMAIN      243    366       SET. {ECO:0000259|PROSITE:PS50280}.
FT   DOMAIN      396    412       Post-SET. {ECO:0000259|PROSITE:PS50868}.
FT   REGION      254    256       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR009343-1}.
FT   REGION      323    324       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR009343-1}.
FT   COILED      114    141       {ECO:0000256|SAM:Coils}.
FT   METAL       181    181       Zinc 1. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       181    181       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       183    183       Zinc 1. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       186    186       Zinc 1. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       186    186       Zinc 3. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       194    194       Zinc 1. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       195    195       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       222    222       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       222    222       Zinc 3. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       226    226       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       228    228       Zinc 3. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       232    232       Zinc 3. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       326    326       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       400    400       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       402    402       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       407    407       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   BINDING     365    365       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR009343-1}.
FT   BINDING     401    401       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|PIRSR:PIRSR009343-
FT                                1}.
SQ   SEQUENCE   412 AA;  47907 MW;  AF6F959AD20C6C76 CRC64;
     MAENLKGCSV CCKSSWNQLQ DLCRLAKLSC PALGISKRNL YDFEVEYLCD YKKIREQEYY
     LVKWRGYPDS ESTWEPRQNL KCVRILKQFH KDLERELLRR HHRSKTPRHL DPSLANYLVQ
     KAKQRRALRR WEQELNAKRS HLGRITVENE VDLDGPPRAF VYINEYRVGE GITLNQVAVG
     CECQDCLWAP TGGCCPGASL HKFAYNDQGQ VRLRAGLPIY ECNSRCRCGY DCPNRVVQKG
     IRYDLCIFRT DDGRGWGVRT LEKIRKNSFV MEYVGEIITS EEAERRGQIY DRQGATYLFD
     LDYVEDVYTV DAAYYGNISH FVNHSCDPNL QVYNVFIDNL DERLPRIAFF ATRTIRAGEE
     LTFDYNMQVD PVDMESTRMD SNFGLAGLPG SPKKRVRIEC KCGTESCRKY LF
//
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