ID   SUVH1_ARATH             Reviewed;         670 AA.
AC   Q9FF80;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH1;
DE            EC=2.1.1.368 {ECO:0000305|PubMed:15775980};
DE   AltName: Full=Histone H3-K9 methyltransferase 1;
DE            Short=H3-K9-HMTase 1;
DE   AltName: Full=Protein SET DOMAIN GROUP 32;
DE   AltName: Full=Suppressor of variegation 3-9 homolog protein 1;
DE            Short=Su(var)3-9 homolog protein 1;
GN   Name=SUVH1; Synonyms=SDG32, SET32; OrderedLocusNames=At5g04940;
GN   ORFNames=MUG13.20;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, NOMENCLATURE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11691919; DOI=10.1093/nar/29.21.4319;
RA   Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
RA   Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
RT   "The Arabidopsis thaliana genome contains at least 29 active genes encoding
RT   SET domain proteins that can be assigned to four evolutionarily conserved
RT   classes.";
RL   Nucleic Acids Res. 29:4319-4333(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15775980; DOI=10.1038/sj.emboj.7600604;
RA   Naumann K., Fischer A., Hofmann I., Krauss V., Phalke S., Irmler K.,
RA   Hause G., Aurich A.-C., Dorn R., Jenuwein T., Reuter G.;
RT   "Pivotal role of AtSUVH2 in heterochromatic histone methylation and gene
RT   silencing in Arabidopsis.";
RL   EMBO J. 24:1418-1429(2005).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=16384625; DOI=10.1016/j.jplph.2005.10.015;
RA   Fischer A., Hofmann I., Naumann K., Reuter G.;
RT   "Heterochromatin proteins and the control of heterochromatic gene silencing
RT   in Arabidopsis.";
RL   J. Plant Physiol. 163:358-368(2006).
CC   -!- FUNCTION: Histone methyltransferase. Methylates 'Lys-9' of histone H3.
CC       H3 'Lys-9' methylation represents a specific tag for epigenetic
CC       transcriptional repression. {ECO:0000269|PubMed:15775980}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(9)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + 2 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:64444, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC         COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61976; EC=2.1.1.368;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00908,
CC         ECO:0000305|PubMed:15775980};
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Note=Associates
CC       with centromeric constitutive heterochromatin.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves stems and flowers.
CC       {ECO:0000269|PubMed:11691919}.
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.
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   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00908}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF344444; AAK28966.1; -; mRNA.
DR   EMBL; AB005245; BAB11516.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90806.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90807.1; -; Genomic_DNA.
DR   RefSeq; NP_196113.1; NM_120576.1.
DR   RefSeq; NP_850767.1; NM_180436.2.
DR   AlphaFoldDB; Q9FF80; -.
DR   SMR; Q9FF80; -.
DR   BioGRID; 15655; 3.
DR   STRING; 3702.Q9FF80; -.
DR   PaxDb; 3702-AT5G04940-1; -.
DR   ProteomicsDB; 226518; -.
DR   EnsemblPlants; AT5G04940.1; AT5G04940.1; AT5G04940.
DR   EnsemblPlants; AT5G04940.2; AT5G04940.2; AT5G04940.
DR   GeneID; 830376; -.
DR   Gramene; AT5G04940.1; AT5G04940.1; AT5G04940.
DR   Gramene; AT5G04940.2; AT5G04940.2; AT5G04940.
DR   KEGG; ath:AT5G04940; -.
DR   Araport; AT5G04940; -.
DR   TAIR; AT5G04940; SUVH1.
DR   eggNOG; KOG1082; Eukaryota.
DR   HOGENOM; CLU_004556_2_1_1; -.
DR   InParanoid; Q9FF80; -.
DR   OMA; EDACEEM; -.
DR   OrthoDB; 5481936at2759; -.
DR   PhylomeDB; Q9FF80; -.
DR   BRENDA; 2.1.1.368; 399.
DR   PRO; PR:Q9FF80; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FF80; baseline and differential.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0031490; F:chromatin DNA binding; IDA:TAIR.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:TAIR.
DR   GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:TAIR.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0040029; P:epigenetic regulation of gene expression; TAS:TAIR.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd10545; SET_AtSUVH-like; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 2.30.280.10; SRA-YDG; 1.
DR   InterPro; IPR025794; H3-K9-MeTrfase_plant.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR036987; SRA-YDG_sf.
DR   InterPro; IPR003105; SRA_YDG.
DR   PANTHER; PTHR45660; HISTONE-LYSINE N-METHYLTRANSFERASE SETMAR; 1.
DR   PANTHER; PTHR45660:SF73; HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9 SPECIFIC SUVH1; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF02182; SAD_SRA; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00466; SRA; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS51575; SAM_MT43_SUVAR39_2; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS51015; YDG; 1.
DR   Genevisible; Q9FF80; AT.
PE   2: Evidence at transcript level;
KW   Centromere; Chromatin regulator; Chromosome; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; Zinc.
FT   CHAIN           1..670
FT                   /note="Histone-lysine N-methyltransferase, H3 lysine-9
FT                   specific SUVH1"
FT                   /id="PRO_0000186072"
FT   DOMAIN          211..357
FT                   /note="YDG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00358"
FT   DOMAIN          432..492
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT   DOMAIN          495..639
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          654..670
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   REGION          53..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..90
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         436
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         440
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         440
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         447
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         449
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         475
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         475
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         479
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         481
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         484
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         505..507
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         541
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         543
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         593
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         596..597
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         599
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         658
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         660
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         665
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   670 AA;  74471 MW;  C92CE89FF5C630F1 CRC64;
     MERNGGHYTD KTRVLDIKPL RTLRPVFPSG NQAPPFVCAP PFGPFPPGFS SFYPFSSSQA
     NQHTPDLNQA QYPPQHQQPQ NPPPVYQQQP PQHASEPSLV TPLRSFRSPD VSNGNAELEG
     STVKRRIPKK RPISRPENMN FESGINVADR ENGNRELVLS VLMRFDALRR RFAQLEDAKE
     AVSGIIKRPD LKSGSTCMGR GVRTNTKKRP GIVPGVEIGD VFFFRFEMCL VGLHSPSMAG
     IDYLVVKGET EEEPIATSIV SSGYYDNDEG NPDVLIYTGQ GGNADKDKQS SDQKLERGNL
     ALEKSLRRDS AVRVIRGLKE ASHNAKIYIY DGLYEIKESW VEKGKSGHNT FKYKLVRAPG
     QPPAFASWTA IQKWKTGVPS RQGLILPDMT SGVESIPVSL VNEVDTDNGP AYFTYSTTVK
     YSESFKLMQP SFGCDCANLC KPGNLDCHCI RKNGGDFPYT GNGILVSRKP MIYECSPSCP
     CSTCKNKVTQ MGVKVRLEVF KTANRGWGLR SWDAIRAGSF ICIYVGEAKD KSKVQQTMAN
     DDYTFDTTNV YNPFKWNYEP GLADEDACEE MSEESEIPLP LIISAKNVGN VARFMNHSCS
     PNVFWQPVSY ENNSQLFVHV AFFAISHIPP MTELTYDYGV SRPSGTQNGN PLYGKRKCFC
     GSAYCRGSFG
//