SUVH1_ARATH
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 03-AUG-2022, entry version 142.
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}.
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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.AT5G04940.1; -.
DR PaxDb; Q9FF80; -.
DR PRIDE; Q9FF80; -.
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; locus:2175289; AT5G04940.
DR eggNOG; KOG1082; Eukaryota.
DR HOGENOM; CLU_004556_2_1_1; -.
DR InParanoid; Q9FF80; -.
DR OMA; YNPFKWN; -.
DR OrthoDB; 274915at2759; -.
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 Genevisible; Q9FF80; AT.
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:0003690; F:double-stranded DNA binding; IBA:GO_Central.
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:0034968; P:histone lysine methylation; IEA:InterPro.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; TAS:TAIR.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 2.30.280.10; -; 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 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; SSF82199; SSF82199; 1.
DR SUPFAM; SSF88697; SSF88697; 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.
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
