SUVH1_TOBAC
ID SUVH1_TOBAC Reviewed; 704 AA.
AC Q93YF5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH1;
DE EC=2.1.1.- {ECO:0000305|PubMed:15546353};
DE EC=2.1.1.368 {ECO:0000305|PubMed:15546353, ECO:0000305|PubMed:15574848};
DE EC=2.1.1.369 {ECO:0000305|PubMed:15546353};
DE AltName: Full=Histone H3-K9 methyltransferase 1;
DE Short=H3-K9-HMTase 1;
DE AltName: Full=NtSet1;
DE AltName: Full=Suppressor of variegation 3-9 homolog protein 1;
DE Short=Su(var)3-9 homolog protein 1;
GN Name=SUVH1; Synonyms=SET1;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11737775; DOI=10.1046/j.1365-313x.2001.01135.x;
RA Shen W.-H.;
RT "NtSET1, a member of a newly identified subgroup of plant SET-domain-
RT containing proteins, is chromatin-associated and its ectopic overexpression
RT inhibits tobacco plant growth.";
RL Plant J. 28:371-383(2001).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LHP1.
RX PubMed=15546353; DOI=10.1111/j.1365-313x.2004.02240.x;
RA Yu Y., Dong A., Shen W.-H.;
RT "Molecular characterization of the tobacco SET domain protein NtSET1
RT unravels its role in histone methylation, chromatin binding, and
RT segregation.";
RL Plant J. 40:699-711(2004).
RN [3]
RP FUNCTION.
RX PubMed=15574848; DOI=10.1093/pcp/pch184;
RA Shen W.-H., Meyer D.;
RT "Ectopic expression of the NtSET1 histone methyltransferase inhibits cell
RT expansion, and affects cell division and differentiation in tobacco
RT plants.";
RL Plant Cell Physiol. 45:1715-1719(2004).
CC -!- FUNCTION: Histone methyltransferase. Methylates in vitro both 'Lys-9'
CC and 'Lys-27' of histone H3. Required for in vivo dimethylation of 'Lys-
CC 9'. H3 'Lys-9' methylation represents a specific tag for epigenetic
CC control for plant development and transcriptional repression.
CC {ECO:0000269|PubMed:15546353, ECO:0000269|PubMed:15574848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(27)-[histone H3] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(27)-[histone H3] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60300, Rhea:RHEA-COMP:15539, Rhea:RHEA-
CC COMP:15544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00908, ECO:0000305|PubMed:15546353};
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:15546353, ECO:0000305|PubMed:15574848};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(27)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(27)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60296, Rhea:RHEA-COMP:15544, Rhea:RHEA-COMP:15548,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.369;
CC Evidence={ECO:0000305|PubMed:15546353};
CC -!- SUBUNIT: Interacts with LHP1. {ECO:0000269|PubMed:15546353}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000305}.
CC Note=Associated with chromatin.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers.
CC {ECO:0000269|PubMed:11737775}.
CC -!- DOMAIN: The SET domain is required for methyltransferase activity and
CC ectopic effect on plant growth.
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; AJ294474; CAC67503.1; -; mRNA.
DR RefSeq; NP_001311665.1; NM_001324736.1.
DR AlphaFoldDB; Q93YF5; -.
DR SMR; Q93YF5; -.
DR STRING; 4097.Q93YF5; -.
DR GeneID; 107761901; -.
DR KEGG; nta:107761901; -.
DR PhylomeDB; Q93YF5; -.
DR BRENDA; 2.1.1.368; 3645.
DR BRENDA; 2.1.1.371; 3645.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005694; C:chromosome; 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; IBA:GO_Central.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034968; P:histone lysine methylation; IEA:InterPro.
DR GO; GO:0016571; P:histone methylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc.
FT CHAIN 1..704
FT /note="Histone-lysine N-methyltransferase, H3 lysine-9
FT specific SUVH1"
FT /id="PRO_0000281048"
FT DOMAIN 265..412
FT /note="YDG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00358"
FT DOMAIN 487..548
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 551..681
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 688..704
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 489
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 495
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="1"
FT /evidence="ECO:0000250"
FT BINDING 504
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 534
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 561..563
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 593
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 595
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 635
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 638..639
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 641
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 692
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 694
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 699
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
SQ SEQUENCE 704 AA; 77401 MW; 65F4A47A43E8316F CRC64;
MEQGLRSDGN NPPSIDKTRV LDVKPLRCLA PVFPSPNGMS SVSTPQPSPF VCVPPTGPFP
PGVAPFYPFV APNDSGRPGE SSQQTPSGVP NQGGPFGFAQ PISPVPLNSF RTPTTANGNS
GRSRRAVDDD DYSNSQDQND QFASGFSVHV NNVEDSGTGK KRGRPKKPRR AQQAEGLTPV
EVDVEPLLTQ LLTSFKLVDL DQVKKADGDK ELAGRVLLVF DLFRRRMTQI DESRDGPGSG
RRPDLKASNM LMTKGVRTNQ TKRIGNAPGI EVGDIFFFRM ELCLVGLHAP TMAGIDYMSV
KLTMDEEPLA VSIVSSGGYD DDGGDGDVLI YTGQGGVQRK DGQVFDQKLE RGNLALEKSV
HRANEVRVIR GVKDVAYPTG KIYIYDGLYK IQESWAEKNK VGCNVFKYKL LRVPGQPEAF
KVWKSIQQWK DGVASRVGVI LPDLTSGAES QPVCLVNDVD DEKGPAYFTY IPSLKYSKPF
VMPRPSPSCH CVGGCQPGDS NCACIQSNGG FLPYSSLGVL LSYKTLIHEC GSACSCPPNC
RNRMSQGGPK ARLEVFKTKN RGWGLRSWDP IRGGGFICEY AGEVIDAGNY SDDNYIFDAT
RIYAPLEAER DYNDESRKVP FPLVISAKNG GNISRFMNHS CSPNVYWQLV VRQSNNEATY
HIAFFAIRHI PPMQELTFDY GMDKADHRRK KCLCGSLNCR GYFY
