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Database: UniProt/TrEMBL
Entry: A2VD66_XENLA
LinkDB: A2VD66_XENLA
Original site: A2VD66_XENLA 
ID   A2VD66_XENLA            Unreviewed;       406 AA.
AC   A2VD66;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   28-FEB-2018, entry version 81.
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=suv39h2 {ECO:0000313|Xenbase:XB-GENE-866435};
GN   Synonyms=LOC100037174 {ECO:0000313|EMBL:AAI29544.1};
GN   ORFNames=XELAEV_18017816mg {ECO:0000313|EMBL:OCT89199.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAI29544.1};
RN   [1] {ECO:0000313|EMBL:AAI29544.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen {ECO:0000313|EMBL:AAI29544.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000186698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J {ECO:0000313|Proteomes:UP000186698};
RX   PubMed=27762356; DOI=10.1038/nature19840;
RA   Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA   Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J.,
RA   Quigley I., Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B.,
RA   Simakov O., Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T.,
RA   Watanabe M., Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S.,
RA   van Kruijsbergen I., Shu S., Carlson J., Kinoshita T., Ohta Y.,
RA   Mawaribuchi S., Jenkins J., Grimwood J., Schmutz J., Mitros T.,
RA   Mozaffari S.V., Suzuki Y., Haramoto Y., Yamamoto T.S., Takagi C.,
RA   Heald R., Miller K., Haudenschild C., Kitzman J., Nakayama T.,
RA   Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V., Karimi K.,
RA   Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W., Shendure J.,
RA   DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA   Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y.,
RA   Veenstra G.J., Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT   "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL   Nature 538:336-343(2016).
RN   [3] {ECO:0000313|EMBL:OCT89199.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=J {ECO:0000313|EMBL:OCT89199.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OCT89199.1};
RA   Session A., Uno Y., Kwon T., Chapman J., Toyoda A., Takahashi S.,
RA   Fukui A., Hikosaka A., Putnam N., Stites J., Van Heeringen S.,
RA   Quigley I., Heinz S., Hellsten U., Lyons J., Suzuki A., Kondo M.,
RA   Ogino H., Ochi H., Bogdanovic O., Lister R., Georgiou G., Paranjpe S.,
RA   Van Kruijsbergen I., Mozaffari S., Shu S., Schmutz J., Jenkins J.,
RA   Grimwood J., Carlson J., Mitros T., Simakov O., Heald R., Miller K.,
RA   Haudenschild C., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA   Kinoshita T., Ohta Y., Mawaribuchi S., Suzuki Y., Haramoto Y.,
RA   Yamamoto T., Takagi C., Kitzman J., Shendure J., Nakayama T.,
RA   Izutsu Y., Robert J., Dichmann D., Flajnik M., Houston D.,
RA   Marcotte E., Wallingford J., Ito Y., Asashima M., Ueno N., Matsuda Y.,
RA   Jan Veenstra G., Fujiyama A., Harland R., Taira M., Rokhsar D.S.;
RT   "WGS assembly of Xenopus laevis.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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       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; BC129543; AAI29544.1; -; mRNA.
DR   EMBL; CM004470; OCT89199.1; -; Genomic_DNA.
DR   RefSeq; NP_001091337.1; NM_001097868.1.
DR   UniGene; Xl.70352; -.
DR   MaxQB; A2VD66; -.
DR   GeneID; 100037174; -.
DR   KEGG; xla:100037174; -.
DR   CTD; 100037174; -.
DR   Xenbase; XB-GENE-866435; suv39h2.
DR   HOVERGEN; HBG055621; -.
DR   KO; K11419; -.
DR   Proteomes; UP000186698; Chromosome 3l.
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; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
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   1: Evidence at protein level;
KW   Chromosome {ECO:0000256|SAAS:SAAS00508265};
KW   Complete proteome {ECO:0000313|Proteomes:UP000186698};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR009343-2};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00912,
KW   ECO:0000256|SAAS:SAAS00590675};
KW   Nucleus {ECO:0000256|SAAS:SAAS00574642};
KW   Proteomics identification {ECO:0000213|MaxQB:A2VD66};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
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};
KW   Zinc {ECO:0000256|PIRSR:PIRSR009343-2}.
FT   DOMAIN       43     90       Chromo. {ECO:0000259|PROSITE:PS50013}.
FT   DOMAIN      185    243       Pre-SET. {ECO:0000259|PROSITE:PS50867}.
FT   DOMAIN      246    369       SET. {ECO:0000259|PROSITE:PS50280}.
FT   DOMAIN      390    406       Post-SET. {ECO:0000259|PROSITE:PS50868}.
FT   REGION      257    259       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR009343-1}.
FT   REGION      326    327       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR009343-1}.
FT   METAL       187    187       Zinc 1. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       187    187       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       189    189       Zinc 1. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       192    192       Zinc 1. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       192    192       Zinc 3. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       197    197       Zinc 1. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       198    198       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       225    225       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       225    225       Zinc 3. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       229    229       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       231    231       Zinc 3. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       235    235       Zinc 3. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       329    329       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       394    394       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       396    396       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       401    401       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   BINDING     368    368       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR009343-1}.
FT   BINDING     395    395       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|PIRSR:PIRSR009343-
FT                                1}.
SQ   SEQUENCE   406 AA;  46133 MW;  0B2E3667722BC83A CRC64;
     MAAARGAWCV PCLASIETLQ ELCRKEMLTC TNIGITRKNL NNYEVEYLCD YRIEKGVEKF
     LVKWKGWPES CNSWEPTKNL KCPTLLKQFY SDLYKYLYAL KPNKKGVIKN NIKSLDPSLS
     DYIVKKAKQR IALRRWEEEL NRKKSHSGTL FVENAVDLEG PPIDFYYIND YKASPGVNTL
     GEAIVGCDCS DCFNGKCCPT EAGVLFAYNE HKQLKIPPGR PIFECNSRCK CGPDCPNRVV
     QKGPPYSLCI FRTDNGRGWG VKTLQKIKKN SFVMEYVGEV ITSEEAERRG QQYDSKGITY
     LFDLDYEADE FTVDAARYGN VSHFVNHSCD PNLQVFNVFI DNLDVRLPRI ALFSTRNIKA
     GEELTFDYQM KGYGDLSTDS IDMSPAKKRG RIACKCGAAT CRGYLN
//
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