ID   SUVH7_ARATH             Reviewed;         693 AA.
AC   Q9C5P1; Q9LMU9;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH7;
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q8GZB6};
DE            EC=2.1.1.367 {ECO:0000250|UniProtKB:Q8GZB6};
DE   AltName: Full=Histone H3-K9 methyltransferase 7;
DE            Short=H3-K9-HMTase 7;
DE   AltName: Full=Protein SET DOMAIN GROUP 17;
DE   AltName: Full=Suppressor of variegation 3-9 homolog protein 7;
DE            Short=Su(var)3-9 homolog protein 7;
GN   Name=SUVH7; Synonyms=SDG17, SET17; OrderedLocusNames=At1g17770;
GN   ORFNames=F2H15.1;
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], AND NOMENCLATURE.
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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   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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine
CC         = H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60284, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC         COMP:15542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC         Evidence={ECO:0000250|UniProtKB:Q8GZB6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.367;
CC         Evidence={ECO:0000250|UniProtKB:Q8GZB6};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358}.
CC       Chromosome, centromere {ECO:0000250}. Note=Associates with centromeric
CC       constitutive heterochromatin. {ECO:0000250}.
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAF97258.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF344450; AAK28972.1; -; mRNA.
DR   EMBL; AC034106; AAF97258.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE29634.1; -; Genomic_DNA.
DR   PIR; G86312; G86312.
DR   RefSeq; NP_564036.1; NM_101640.1.
DR   AlphaFoldDB; Q9C5P1; -.
DR   SMR; Q9C5P1; -.
DR   BioGRID; 23594; 1.
DR   STRING; 3702.Q9C5P1; -.
DR   PaxDb; 3702-AT1G17770-1; -.
DR   EnsemblPlants; AT1G17770.1; AT1G17770.1; AT1G17770.
DR   GeneID; 838355; -.
DR   Gramene; AT1G17770.1; AT1G17770.1; AT1G17770.
DR   KEGG; ath:AT1G17770; -.
DR   Araport; AT1G17770; -.
DR   TAIR; AT1G17770; SUVH7.
DR   eggNOG; KOG1082; Eukaryota.
DR   HOGENOM; CLU_004556_2_1_1; -.
DR   InParanoid; Q9C5P1; -.
DR   OMA; PLRTIWP; -.
DR   OrthoDB; 685580at2759; -.
DR   PhylomeDB; Q9C5P1; -.
DR   PRO; PR:Q9C5P1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C5P1; baseline and differential.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0140947; F:histone H3K9me2 methyltransferase activity; IEA:RHEA.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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:SF18; HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9 SPECIFIC SUVH7-RELATED; 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; Q9C5P1; AT.
PE   2: Evidence at transcript level;
KW   Centromere; Chromatin regulator; Chromosome; DNA-binding; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; Zinc.
FT   CHAIN           1..693
FT                   /note="Histone-lysine N-methyltransferase, H3 lysine-9
FT                   specific SUVH7"
FT                   /id="PRO_0000186078"
FT   DOMAIN          227..373
FT                   /note="YDG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00358"
FT   DOMAIN          454..516
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT   DOMAIN          519..660
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          677..693
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   DNA_BIND        129..141
FT                   /note="A.T hook"
FT   REGION          64..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         458
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         458
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         461
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         466
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         466
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         471
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         473
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         498
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         498
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         502
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         504
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         508
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         529..531
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         562
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         564
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         614
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         617..618
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         620
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         681
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         683
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         688
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   693 AA;  77632 MW;  E03E22BC2863E2D7 CRC64;
     MDKSIPIKAI PVACVRPDLV DDVTKNTSTI PTMVSPVLTN MPSATSPLLM VPPLRTIWPS
     NKEWYDGDAG PSSTGPIKRE ASDNTNDTAH NTFAPPPEMV IPLITIRPSD DSSNYSCDAG
     AGPSTGPVKR GRGRPKGSKN STPTEPKKPK VYDPNSLKVT SRGNFDSEIT EAETETGNQE
     IVDSVMMRFD AVRRRLCQIN HPEDILTTAS GNCTKMGVKT NTRRRIGAVP GIHVGDIFYY
     WGEMCLVGLH KSNYGGIDFF TAAESAVEGH AAMCVVTAGQ YDGETEGLDT LIYSGQGGTD
     VYGNARDQEM KGGNLALEAS VSKGNDVRVV RGVIHPHENN QKIYIYDGMY LVSKFWTVTG
     KSGFKEFRFK LVRKPNQPPA YAIWKTVENL RNHDLIDSRQ GFILEDLSFG AELLRVPLVN
     EVDEDDKTIP EDFDYIPSQC HSGMMTHEFH FDRQSLGCQN CRHQPCMHQN CTCVQRNGDL
     LPYHNNILVC RKPLIYECGG SCPCPDHCPT RLVQTGLKLH LEVFKTRNCG WGLRSWDPIR
     AGTFICEFAG LRKTKEEVEE DDDYLFDTSK IYQRFRWNYE PELLLEDSWE QVSEFINLPT
     QVLISAKEKG NVGRFMNHSC SPNVFWQPIE YENRGDVYLL IGLFAMKHIP PMTELTYDYG
     VSCVERSEED EVLLYKGKKT CLCGSVKCRG SFT
//