ID   SUV92_MOUSE             Reviewed;         477 AA.
AC   Q9EQQ0; Q8BNK2; Q9CUK3; Q9JLP7;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-NOV-2023, entry version 176.
DE   RecName: Full=Histone-lysine N-methyltransferase SUV39H2;
DE            EC=2.1.1.355;
DE   AltName: Full=Histone H3-K9 methyltransferase 2;
DE            Short=H3-K9-HMTase 2;
DE   AltName: Full=Suppressor of variegation 3-9 homolog 2;
DE            Short=Su(var)3-9 homolog 2;
GN   Name=Suv39h2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND CHARACTERIZATION.
RC   STRAIN=C57BL/6J;
RX   PubMed=11094092; DOI=10.1128/mcb.20.24.9423-9433.2000;
RA   O'Carroll D., Scherthan H., Peters A.H.F.M., Opravil S., Haynes A.R.,
RA   Laible G., Rea S., Schmid M., Lebersorger A., Jerratsch M., Sattler L.,
RA   Mattei M.-G., Denny P., Brown S.D.M., Schweizer D., Jenuwein T.;
RT   "Isolation and characterization of Suv39h2, a second histone H3
RT   methyltransferase gene that displays testis-specific expression.";
RL   Mol. Cell. Biol. 20:9423-9433(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11701123; DOI=10.1016/s0092-8674(01)00542-6;
RA   Peters A.H.F.M., O'Carroll D., Scherthan H., Mechtler K., Sauer S.,
RA   Schofer C., Weipoltshammer K., Pagani M., Lachner M., Kohlmaier A.,
RA   Opravil S., Doyle M., Sibilia M., Jenuwein T.;
RT   "Loss of the Suv39h histone methyltransferases impairs mammalian
RT   heterochromatin and genome stability.";
RL   Cell 107:323-337(2001).
RN   [5]
RP   FUNCTION.
RX   PubMed=14690609; DOI=10.1016/s1097-2765(03)00477-5;
RA   Peters A.H.F.M., Kubicek S., Mechtler K., O'Sullivan R.J., Derijck A.A.,
RA   Perez-Burgos L., Kohlmaier A., Opravil S., Tachibana M., Shinkai Y.,
RA   Martens J.H.A., Jenuwein T.;
RT   "Partitioning and plasticity of repressive histone methylation states in
RT   mammalian chromatin.";
RL   Mol. Cell 12:1577-1589(2003).
RN   [6]
RP   FUNCTION.
RX   PubMed=14690610; DOI=10.1016/s1097-2765(03)00479-9;
RA   Rice J.C., Briggs S.D., Ueberheide B., Barber C.M., Shabanowitz J.,
RA   Hunt D.F., Shinkai Y., Allis C.D.;
RT   "Histone methyltransferases direct different degrees of methylation to
RT   define distinct chromatin domains.";
RL   Mol. Cell 12:1591-1598(2003).
RN   [7]
RP   FUNCTION.
RX   PubMed=14702045; DOI=10.1038/ng1278;
RA   Garcia-Cao M., O'Sullivan R., Peters A.H.F.M., Jenuwein T., Blasco M.A.;
RT   "Epigenetic regulation of telomere length in mammalian cells by the Suv39h1
RT   and Suv39h2 histone methyltransferases.";
RL   Nat. Genet. 36:94-99(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   FUNCTION IN CIRCADIAN RHYTHMS, AND IDENTIFICATION IN A LARGE PER COMPLEX.
RX   PubMed=24413057; DOI=10.1038/nsmb.2746;
RA   Duong H.A., Weitz C.J.;
RT   "Temporal orchestration of repressive chromatin modifiers by circadian
RT   clock Period complexes.";
RL   Nat. Struct. Mol. Biol. 21:126-132(2014).
RN   [10]
RP   UBIQUITINATION.
RX   PubMed=30111536; DOI=10.15252/embj.201898981;
RA   Zhang Y.L., Zhao L.W., Zhang J., Le R., Ji S.Y., Chen C., Gao Y., Li D.,
RA   Gao S., Fan H.Y.;
RT   "DCAF13 promotes pluripotency by negatively regulating SUV39H1 stability
RT   during early embryonic development.";
RL   EMBO J. 37:0-0(2018).
CC   -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC       'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3
CC       'Lys-9' trimethylation represents a specific tag for epigenetic
CC       transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5)
CC       proteins to methylated histones. Mainly functions in heterochromatin
CC       regions, thereby playing a central role in the establishment of
CC       constitutive heterochromatin at pericentric and telomere regions. H3
CC       'Lys-9' trimethylation is also required to direct DNA methylation at
CC       pericentric repeats. SUV39H1 is targeted to histone H3 via its
CC       interaction with RB1 and is involved in many processes, such as cell
CC       cycle regulation, transcriptional repression and regulation of telomere
CC       length. May participate in regulation of higher-order chromatin
CC       organization during spermatogenesis. Recruited by the large PER complex
CC       to the E-box elements of the circadian target genes such as PER2 itself
CC       or PER1, contributes to the conversion of local chromatin to a
CC       heterochromatin-like repressive state through H3 'Lys-9'
CC       trimethylation. {ECO:0000269|PubMed:11701123,
CC       ECO:0000269|PubMed:14690609, ECO:0000269|PubMed:14690610,
CC       ECO:0000269|PubMed:14702045, ECO:0000269|PubMed:24413057}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC         N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC         COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00912};
CC   -!- SUBUNIT: Interacts with SMAD5. The large PER complex involved in the
CC       histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1
CC       and/or SUV39H2; CBX3 mediates the formation of the complex.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H5I1}.
CC       Chromosome. Chromosome, centromere. Note=Associates with centromeric
CC       constitutive heterochromatin during most stages of spermato- and
CC       spermiogenesis. Predominantly accumulates at the sex chromosomes
CC       present at the XY body.
CC   -!- TISSUE SPECIFICITY: Testis specific; predominant expression in type B
CC       spermatogonia and preleptotene spermatocytes.
CC   -!- DEVELOPMENTAL STAGE: Strong expression in early embryos with a peak at
CC       10.5 dpc. Expression is down-regulated at 17.5 dpc, and is nearly
CC       absent during postnatal development. In adult testes, prominent
CC       expression in late but not early spermatocytes.
CC   -!- DOMAIN: Although the SET domain contains the active site of enzymatic
CC       activity, both pre-SET and post-SET domains are required for
CC       methyltransferase activity. The SET domain also participates in stable
CC       binding to heterochromatin (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are
CC       arranged in a triangular cluster; some of these Cys residues contribute
CC       to the binding of two zinc ions within the cluster. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by the DCX(DCAF13) E3 ubiquitin ligase complex,
CC       leading to its degradation. {ECO:0000269|PubMed:30111536}.
CC   -!- DISRUPTION PHENOTYPE: Mice lacking Suv39h1 and Suv39h2 display severely
CC       impaired viability and chromosomal instabilities that are associated
CC       with an increased tumor risk and perturbed chromosome interactions
CC       during male meiosis. They also show a higher level of histone H3 with
CC       phosphorylated 'Ser-10' and a reduced number of cells in G1 phase and
CC       an increased portion of cells with aberrant nuclear morphologies.
CC       {ECO:0000269|PubMed:11701123}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00912}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF73152.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF149204; AAF73152.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF149205; AAG09134.1; -; mRNA.
DR   EMBL; AK015728; BAB29948.1; -; mRNA.
DR   EMBL; AK083457; BAC38921.1; -; mRNA.
DR   EMBL; AL732620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS15652.1; -.
DR   RefSeq; NP_073561.2; NM_022724.4.
DR   AlphaFoldDB; Q9EQQ0; -.
DR   SMR; Q9EQQ0; -.
DR   BioGRID; 211103; 2.
DR   DIP; DIP-32586N; -.
DR   IntAct; Q9EQQ0; 3.
DR   STRING; 10090.ENSMUSP00000027956; -.
DR   iPTMnet; Q9EQQ0; -.
DR   PhosphoSitePlus; Q9EQQ0; -.
DR   EPD; Q9EQQ0; -.
DR   MaxQB; Q9EQQ0; -.
DR   PaxDb; 10090-ENSMUSP00000027956; -.
DR   PeptideAtlas; Q9EQQ0; -.
DR   ProteomicsDB; 258674; -.
DR   DNASU; 64707; -.
DR   GeneID; 64707; -.
DR   KEGG; mmu:64707; -.
DR   UCSC; uc008ied.2; mouse.
DR   AGR; MGI:1890396; -.
DR   CTD; 79723; -.
DR   MGI; MGI:1890396; Suv39h2.
DR   eggNOG; KOG1082; Eukaryota.
DR   InParanoid; Q9EQQ0; -.
DR   OrthoDB; 5481936at2759; -.
DR   PhylomeDB; Q9EQQ0; -.
DR   TreeFam; TF106452; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   BioGRID-ORCS; 64707; 5 hits in 81 CRISPR screens.
DR   PRO; PR:Q9EQQ0; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9EQQ0; Protein.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0140938; F:histone H3 methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0046974; F:histone H3K9 methyltransferase activity; IGI:MGI.
DR   GO; GO:0140949; F:histone H3K9 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0140947; F:histone H3K9me2 methyltransferase activity; IGI:MGI.
DR   GO; GO:0008276; F:protein methyltransferase activity; IDA:MGI.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISO:MGI.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR   GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR   GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
DR   GO; GO:0044725; P:epigenetic programming in the zygotic pronuclei; ISO:MGI.
DR   GO; GO:0007140; P:male meiotic nuclear division; IEP:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:UniProtKB.
DR   GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   CDD; cd18639; CD_SUV39H1_like; 1.
DR   CDD; cd10532; SET_SUV39H2; 1.
DR   Gene3D; 2.40.50.40; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 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; H3-K9_MeTrfase_SUV39H1/2-like.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   PANTHER; PTHR46223; HISTONE-LYSINE N-METHYLTRANSFERASE SUV39H; 1.
DR   PANTHER; PTHR46223:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SUV39H2; 1.
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; Chromo domain-like; 1.
DR   SUPFAM; SSF82199; SET domain; 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   Biological rhythms; Cell cycle; Centromere; Chromatin regulator;
KW   Chromosome; Differentiation; Metal-binding; Methyltransferase; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW   Zinc.
FT   CHAIN           1..477
FT                   /note="Histone-lysine N-methyltransferase SUV39H2"
FT                   /id="PRO_0000186060"
FT   DOMAIN          118..176
FT                   /note="Chromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   DOMAIN          256..314
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT   DOMAIN          317..440
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          461..477
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..41
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         258
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         328..330
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         371
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         397..398
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         400
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         465
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         472
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         448
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT   MOD_RES         451
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT   MOD_RES         455
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        3
FT                   /note="T -> A (in Ref. 2; BAC38921)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        131
FT                   /note="Missing (in Ref. 1; AAF73152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        323
FT                   /note="K -> R (in Ref. 2; BAB29948/BAC38921)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        325
FT                   /note="S -> N (in Ref. 1; AAF73152)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   477 AA;  54098 MW;  4008D46CF0F07006 CRC64;
     MATARAKARG SEAGARCHRA PGPPPRPKAR RTARRRRAET LTARRSRPSA GERRAGSQRA
     WSGAPRAAVF GDECARGALF KAWCVPCLVS LDTLQELCRK EKLTCKSIGI TKRNLNNYEV
     EYLCDYKVAK GVEYYLVKWK GWPDSTNTWE PLRNLRCPQL LRQFSDDKKT YLAQERKCKA
     VNSKSLQPAI AEYIVQKAKQ RIALQRWQDY LNRRKNHKGM IFVENTVDLE GPPLDFYYIN
     EYRPAPGISI NSEATFGCSC TDCFFDKCCP AEAGVVLAYN KKQQIKIQPG TPIYECNSRC
     RCGPECPNRI VQKGTQYSLC IFKTSNGCGW GVKTLVKIKR MSFVMEYVGE VITSEEAERR
     GQFYDNKGIT YLFDLDYESD EFTVDAARYG NVSHFVNHSC DPNLQVFSVF IDNLDTRLPR
     IALFSTRTIN AGEELTFDYQ MKGSGEASSD SIDHSPAKKR VRTQCKCGAE TCRGYLN
//