SUVH5_ARATH
ID SUVH5_ARATH Reviewed; 794 AA.
AC O82175;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH5;
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 5;
DE Short=H3-K9-HMTase 5;
DE AltName: Full=Protein SET DOMAIN GROUP 9;
DE AltName: Full=Suppressor of variegation 3-9 homolog protein 5;
DE Short=Su(var)3-9 homolog protein 5;
GN Name=SUVH5; Synonyms=SDG9, SET9; OrderedLocusNames=At2g35160;
GN ORFNames=T4C15.17;
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], NOMENCLATURE, AND TISSUE 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=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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.
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 -!- 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 -!- 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; AF344448; AAK28970.1; -; mRNA.
DR EMBL; AC004667; AAC61820.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09075.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62211.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62213.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62214.1; -; Genomic_DNA.
DR EMBL; AY062735; AAL32813.1; -; mRNA.
DR EMBL; BT003374; AAO30037.1; -; mRNA.
DR PIR; D84765; D84765.
DR RefSeq; NP_001324386.1; NM_001336549.1.
DR RefSeq; NP_001324388.1; NM_001336548.1.
DR RefSeq; NP_001324389.1; NM_001336547.1.
DR RefSeq; NP_181061.1; NM_129070.3.
DR PDB; 3Q0B; X-ray; 2.20 A; X=362-528.
DR PDB; 3Q0C; X-ray; 2.66 A; A/X=362-528.
DR PDB; 3Q0D; X-ray; 2.37 A; A/X=362-528.
DR PDB; 3Q0F; X-ray; 2.75 A; A/X=362-528.
DR PDB; 4YGI; X-ray; 2.60 A; A=362-528.
DR PDBsum; 3Q0B; -.
DR PDBsum; 3Q0C; -.
DR PDBsum; 3Q0D; -.
DR PDBsum; 3Q0F; -.
DR PDBsum; 4YGI; -.
DR AlphaFoldDB; O82175; -.
DR SMR; O82175; -.
DR BioGRID; 3429; 4.
DR DIP; DIP-62060N; -.
DR IntAct; O82175; 6.
DR STRING; 3702.AT2G35160.1; -.
DR PaxDb; O82175; -.
DR PRIDE; O82175; -.
DR ProteomicsDB; 226521; -.
DR EnsemblPlants; AT2G35160.1; AT2G35160.1; AT2G35160.
DR EnsemblPlants; AT2G35160.2; AT2G35160.2; AT2G35160.
DR EnsemblPlants; AT2G35160.3; AT2G35160.3; AT2G35160.
DR EnsemblPlants; AT2G35160.4; AT2G35160.4; AT2G35160.
DR GeneID; 818083; -.
DR Gramene; AT2G35160.1; AT2G35160.1; AT2G35160.
DR Gramene; AT2G35160.2; AT2G35160.2; AT2G35160.
DR Gramene; AT2G35160.3; AT2G35160.3; AT2G35160.
DR Gramene; AT2G35160.4; AT2G35160.4; AT2G35160.
DR KEGG; ath:AT2G35160; -.
DR Araport; AT2G35160; -.
DR TAIR; locus:2063384; AT2G35160.
DR eggNOG; KOG1082; Eukaryota.
DR HOGENOM; CLU_004556_0_0_1; -.
DR InParanoid; O82175; -.
DR OrthoDB; 75825at2759; -.
DR PhylomeDB; O82175; -.
DR EvolutionaryTrace; O82175; -.
DR PRO; PR:O82175; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82175; baseline and differential.
DR Genevisible; O82175; 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; IDA: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:0031048; P:heterochromatin assembly by small RNA; IEP:TAIR.
DR GO; GO:0034968; P:histone lysine methylation; IEA:InterPro.
DR GO; GO:0016571; P:histone methylation; IDA: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; SM00508; PostSET; 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 1: Evidence at protein level;
KW 3D-structure; Centromere; Chromatin regulator; Chromosome;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..794
FT /note="Histone-lysine N-methyltransferase, H3 lysine-9
FT specific SUVH5"
FT /id="PRO_0000186076"
FT DOMAIN 365..515
FT /note="YDG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00358"
FT DOMAIN 585..644
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 647..764
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 778..794
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 187..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:3Q0B"
FT HELIX 379..384
FT /evidence="ECO:0007829|PDB:3Q0B"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:3Q0B"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:3Q0B"
FT STRAND 405..415
FT /evidence="ECO:0007829|PDB:3Q0B"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:3Q0B"
FT HELIX 451..462
FT /evidence="ECO:0007829|PDB:3Q0B"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:3Q0B"
FT STRAND 486..501
FT /evidence="ECO:0007829|PDB:3Q0B"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:3Q0D"
FT STRAND 507..515
FT /evidence="ECO:0007829|PDB:3Q0B"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:3Q0D"
SQ SEQUENCE 794 AA; 88153 MW; 9C3BB4FA62885F17 CRC64;
MVHSESSILS SLRGGDGGGI PCSKDELAIN GSYTDPMGRR KSKRFKVAAE SEFSPDFGSI
TRQLRSRRMQ KEFTVETYET RNVSDVCVLS SQADVELIPG EIVAERDSFK SVDCNDMSVG
LTEGAESLGV NMQEPMKDRN MPENTSEQNM VEVHPPSISL PEEDMMGSVC RKSITGTKEL
HGRTISVGRD LSPNMGSKFS KNGKTAKRSI SVEEENLVLE KSDSGDHLGP SPEVLELEKS
EVWIITDKGV VMPSPVKPSE KRNGDYGEGS MRKNSERVAL DKKRLASKFR LSNGGLPSCS
SSGDSARYKV KETMRLFHET CKKIMQEEEA RPRKRDGGNF KVVCEASKIL KSKGKNLYSG
TQIIGTVPGV EVGDEFQYRM ELNLLGIHRP SQSGIDYMKD DGGELVATSI VSSGGYNDVL
DNSDVLIYTG QGGNVGKKKN NEPPKDQQLV TGNLALKNSI NKKNPVRVIR GIKNTTLQSS
VVAKNYVYDG LYLVEEYWEE TGSHGKLVFK FKLRRIPGQP ELPWKEVAKS KKSEFRDGLC
NVDITEGKET LPICAVNNLD DEKPPPFIYT AKMIYPDWCR PIPPKSCGCT NGCSKSKNCA
CIVKNGGKIP YYDGAIVEIK PLVYECGPHC KCPPSCNMRV SQHGIKIKLE IFKTESRGWG
VRSLESIPIG SFICEYAGEL LEDKQAESLT GKDEYLFDLG DEDDPFTINA AQKGNIGRFI
NHSCSPNLYA QDVLYDHEEI RIPHIMFFAL DNIPPLQELS YDYNYKIDQV YDSNGNIKKK
FCYCGSAECS GRLY
