SUVH8_ARATH
ID SUVH8_ARATH Reviewed; 755 AA.
AC Q9C5P0; Q9TP24;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH8;
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 8;
DE Short=H3-K9-HMTase 8;
DE AltName: Full=Protein SET DOMAIN GROUP 21;
DE AltName: Full=Suppressor of variegation 3-9 homolog protein 8;
DE Short=Su(var)3-9 homolog protein 8;
GN Name=SUVH8; Synonyms=SDG21, SET21; OrderedLocusNames=At2g24740;
GN ORFNames=F27A10.5;
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 [GENOMIC DNA], 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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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: Cys residues in the pre-SET domain normally bind 3 zinc ions
CC that are arranged in a triangular cluster, but here these Cys residues
CC are only partially conserved, suggesting that the pre-Set domain may
CC not bind a zinc cluster.
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=AAD26896.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF344451; AAK28973.1; -; Genomic_DNA.
DR EMBL; AC007266; AAD26896.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC07623.1; -; Genomic_DNA.
DR PIR; C84640; C84640.
DR RefSeq; NP_180049.2; NM_128034.2.
DR AlphaFoldDB; Q9C5P0; -.
DR SMR; Q9C5P0; -.
DR STRING; 3702.AT2G24740.1; -.
DR iPTMnet; Q9C5P0; -.
DR PaxDb; Q9C5P0; -.
DR PRIDE; Q9C5P0; -.
DR EnsemblPlants; AT2G24740.1; AT2G24740.1; AT2G24740.
DR GeneID; 817010; -.
DR Gramene; AT2G24740.1; AT2G24740.1; AT2G24740.
DR KEGG; ath:AT2G24740; -.
DR Araport; AT2G24740; -.
DR TAIR; locus:2047266; AT2G24740.
DR eggNOG; KOG1082; Eukaryota.
DR HOGENOM; CLU_004556_2_1_1; -.
DR InParanoid; Q9C5P0; -.
DR OMA; MTRRIGP; -.
DR OrthoDB; 197626at2759; -.
DR PhylomeDB; Q9C5P0; -.
DR PRO; PR:Q9C5P0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9C5P0; baseline and differential.
DR Genevisible; Q9C5P0; AT.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:TAIR.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034968; P:histone lysine methylation; IEA:InterPro.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0008361; P:regulation of cell size; IMP:TAIR.
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; PS51575; SAM_MT43_SUVAR39_2; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS51015; YDG; 1.
PE 3: Inferred from homology;
KW Centromere; Chromatin regulator; Chromosome; DNA-binding; Metal-binding;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Zinc.
FT CHAIN 1..755
FT /note="Histone-lysine N-methyltransferase, H3 lysine-9
FT specific SUVH8"
FT /id="PRO_0000186079"
FT DOMAIN 310..448
FT /note="YDG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00358"
FT DOMAIN 528..578
FT /note="Pre-SET"
FT DOMAIN 581..723
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 739..755
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT DNA_BIND 174..186
FT /note="A.T hook"
FT REGION 62..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 591..593
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 624
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 626
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 676
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 679..680
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 682
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 743
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 745
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 750
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 755 AA; 84528 MW; 4B5BF379B8BF0C27 CRC64;
MVSTPPTLLM LFDDGDAGPS TGLVHREKSD AVNEEAHATS VPPHAPPQTL WLLDNFNIED
SYDRDAGPST GPVHRERSDA VNEEAHATSI PPHAPPQTLW LLDNFNIEDS YDRDAGPSTS
PIDREASHEV NEDAHATSAP PHVMVSPLQN RRPFDQFNNQ PYDASAGPST GPGKRGRGRP
KGSKNGSRKP KKPKAYDNNS TDASAGPSSG LGKRRCGRPK GLKNRSRKPK KPKADDPNSK
MVISCPDFDS RITEAERESG NQEIVDSILM RFDAVRRRLC QLNYRKDKIL TASTNCMNLG
VRTNMTRRIG PIPGVQVGDI FYYWCEMCLV GLHRNTAGGI DSLLAKESGV DGPAATSVVT
SGKYDNETED LETLIYSGHG GKPCDQVLQR GNRALEASVR RRNEVRVIRG ELYNNEKVYI
YDGLYLVSDC WQVTGKSGFK EYRFKLLRKP GQPPGYAIWK LVENLRNHEL IDPRQGFILG
DLSFGEEGLR VPLVNEVDEE DKTIPDDFDY IRSQCYSGMT NDVNVDSQSL VQSYIHQNCT
CILKNCGQLP YHDNILVCRK PLIYECGGSC PTRMVETGLK LHLEVFKTSN CGWGLRSWDP
IRAGTFICEF TGVSKTKEEV EEDDDYLFDT SRIYHSFRWN YEPELLCEDA CEQVSEDANL
PTQVLISAKE KGNVGRFMNH NCWPNVFWQP IEYDDNNGHI YVRIGLFAMK HIPPMTELTY
DYGISCVEKT GEDEVIYKGK KICLCGSVKC RGSFG
