SUVR5_ARATH
ID SUVR5_ARATH Reviewed; 1382 AA.
AC O64827; A0MA41; A0MA42; B9DGK7; C0Z2K8; O64828; O64829;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Histone-lysine N-methyltransferase SUVR5 {ECO:0000303|PubMed:23071452};
DE EC=2.1.1.- {ECO:0000269|PubMed:17224141};
DE AltName: Full=C2H2 zinc finger-SET histone methyltransferase {ECO:0000303|PubMed:17224141};
DE Short=Protein C2H2 SET {ECO:0000303|PubMed:17224141};
DE AltName: Full=Protein SET DOMAIN GROUP 6;
DE AltName: Full=Suppressor of variegation 3-9-related protein 5 {ECO:0000303|PubMed:23071452};
DE Short=Su(var)3-9-related protein 5 {ECO:0000303|PubMed:23071452};
GN Name=SUVR5 {ECO:0000303|PubMed:23071452};
GN Synonyms=CZS {ECO:0000303|PubMed:17224141}, SDG6, SET6;
GN OrderedLocusNames=At2g23740 {ECO:0000312|Araport:AT2G23740};
GN ORFNames=F27L4.7 {ECO:0000312|EMBL:AAC17088.1},
GN F27L4.8 {ECO:0000312|EMBL:AAC17089.1},
GN F27L4.9 {ECO:0000312|EMBL:AAC17099.1};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 269-1382, FUNCTION, CATALYTIC
RP ACTIVITY, INTERACTION WITH LDL1/SWP1, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=17224141; DOI=10.1016/j.ydbio.2006.11.012;
RA Krichevsky A., Gutgarts H., Kozlovsky S.V., Tzfira T., Sutton A.,
RA Sternglanz R., Mandel G., Citovsky V.;
RT "C2H2 zinc finger-SET histone methyltransferase is a plant-specific
RT chromatin modifier.";
RL Dev. Biol. 303:259-269(2007).
RN [5]
RP 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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23071452; DOI=10.1371/journal.pgen.1002995;
RA Caro E., Stroud H., Greenberg M.V., Bernatavichute Y.V., Feng S., Groth M.,
RA Vashisht A.A., Wohlschlegel J., Jacobsen S.E.;
RT "The SET-domain protein SUVR5 mediates H3K9me2 deposition and silencing at
RT stimulus response genes in a DNA methylation-independent manner.";
RL PLoS Genet. 8:E1002995-E1002995(2012).
CC -!- FUNCTION: Histone methyltransferase that functions together with its
CC binding partner LDL1/SWP1 as one of the regulators of flower timing in
CC Arabidopsis (PubMed:17224141). Mediates H3K9me2 deposition and
CC regulates gene expression in a DNA methylation-independent manner.
CC Binds DNA through its zinc fingers and represses the expression of a
CC subset of stimulus response genes. May represent a novel mechanism for
CC plants to regulate their chromatin and transcriptional state, which may
CC allow for the adaptability and modulation necessary to rapidly respond
CC to environment or developmental cues (PubMed:23071452).
CC {ECO:0000269|PubMed:17224141, ECO:0000269|PubMed:23071452}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000269|PubMed:17224141};
CC -!- SUBUNIT: Component of a regulatory complex with LDL1/SWP1
CC (PubMed:17224141). Interacts with LDL1/SWP1 (PubMed:17224141).
CC {ECO:0000269|PubMed:17224141}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17224141}. Chromosome
CC {ECO:0000250|UniProtKB:Q5DW34}. Note=Associates with euchromatic
CC regions. {ECO:0000250|UniProtKB:Q5DW34}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O64827-1; Sequence=Displayed;
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.
CC {ECO:0000250|UniProtKB:O43463}.
CC -!- DISRUPTION PHENOTYPE: Displays reduced dimethylation of lysine 9 and
CC lysine 27 of histone H3 and hyperacetylation of histone H4 within the
CC FLC locus and shows a moderate delayed flowering (PubMed:17224141).
CC Delayed flowering (PubMed:23071452). {ECO:0000269|PubMed:17224141,
CC ECO:0000269|PubMed:23071452}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17088.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to three different genes At2g23730, At2g23740 and At2g23750.; Evidence={ECO:0000305};
CC Sequence=AAC17089.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to three different genes At2g23730, At2g23740 and At2g23750.; Evidence={ECO:0000305};
CC Sequence=AAC17099.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to three different genes At2g23730, At2g23740 and At2g23750.; Evidence={ECO:0000305};
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DR EMBL; AC004482; AAC17088.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC004482; AAC17089.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC004482; AAC17099.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07484.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62021.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62024.1; -; Genomic_DNA.
DR EMBL; AK317189; BAH19874.1; -; mRNA.
DR EMBL; AK318822; BAH56937.1; -; mRNA.
DR EMBL; DQ104397; AAZ83310.1; -; Genomic_DNA.
DR EMBL; DQ104398; AAZ83311.1; -; mRNA.
DR PIR; T02416; T02416.
DR PIR; T02417; T02417.
DR RefSeq; NP_001189585.1; NM_001202656.2. [O64827-1]
DR RefSeq; NP_001324204.1; NM_001335864.1. [O64827-1]
DR RefSeq; NP_001324207.1; NM_001335861.1. [O64827-1]
DR AlphaFoldDB; O64827; -.
DR STRING; 3702.AT2G23740.2; -.
DR iPTMnet; O64827; -.
DR PaxDb; O64827; -.
DR PRIDE; O64827; -.
DR ProteomicsDB; 226531; -. [O64827-1]
DR EnsemblPlants; AT2G23740.2; AT2G23740.2; AT2G23740. [O64827-1]
DR EnsemblPlants; AT2G23740.3; AT2G23740.3; AT2G23740. [O64827-1]
DR EnsemblPlants; AT2G23740.6; AT2G23740.6; AT2G23740. [O64827-1]
DR GeneID; 816905; -.
DR Gramene; AT2G23740.2; AT2G23740.2; AT2G23740. [O64827-1]
DR Gramene; AT2G23740.3; AT2G23740.3; AT2G23740. [O64827-1]
DR Gramene; AT2G23740.6; AT2G23740.6; AT2G23740. [O64827-1]
DR KEGG; ath:AT2G23740; -.
DR Araport; AT2G23740; -.
DR TAIR; locus:2049047; AT2G23740.
DR eggNOG; KOG1082; Eukaryota.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; O64827; -.
DR OMA; VCMDSFT; -.
DR OrthoDB; 753093at2759; -.
DR PhylomeDB; O64827; -.
DR PRO; PR:O64827; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64827; baseline and differential.
DR Genevisible; O64827; AT.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0034968; P:histone lysine methylation; IDA:UniProtKB.
DR GO; GO:1900109; P:regulation of histone H3-K9 dimethylation; IMP:TAIR.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR040689; SUVR5_Znf-C2H2_3rpt.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF18868; zf-C2H2_3rep; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Chromosome; DNA-binding;
KW Metal-binding; Methyltransferase; Nucleus; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1382
FT /note="Histone-lysine N-methyltransferase SUVR5"
FT /id="PRO_0000233369"
FT DOMAIN 1145..1221
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 1224..1356
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1366..1382
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT ZN_FING 735..758
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 769..792
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 838..861
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 43..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1234..1236
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1277
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 1313..1314
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1355
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 1370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 1377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT CONFLICT 881
FT /note="Y -> H (in Ref. 1; AAZ83311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1382 AA; 155767 MW; 3FC1382898263BEC CRC64;
MEVKMDELVL DVDVEEATGS ELLVKSEPEA DLNAVKSSTD LVTVTGPIGK NGEGESSPSE
PKWLQQDEPI ALWVKWRGKW QAGIRCAKAD WPLTTLRGKP THDRKKYCVI FFPHTKNYSW
ADMQLVRSIN EFPDPIAYKS HKIGLKLVKD LTAARRYIMR KLTVGMFNIV DQFPSEVVSE
AARDIIIWKE FAMEATRSTS YHDLGIMLVK LHSMILQRYM DPIWLENSFP LWVQKCNNAV
NAESIELLNE EFDNCIKWNE VKSLSESPMQ PMLLSEWKTW KHDIAKWFSI SRRGVGEIAQ
PDSKSVFNSD VQASRKRPKL EIRRAETTNA THMESDTSPQ GLSAIDSEFF SSRGNTNSPE
TMKEENPVMN TPENGLDLWD GIVVEAGGSQ FMKTKETNGL SHPQDQHINE SVLKKPFGSG
NKSQQCIAFI ESKGRQCVRW ANEGDVYCCV HLASRFTTKS MKNEGSPAVE APMCGGVTVL
GTKCKHRSLP GFLYCKKHRP HTGMVKPDDS SSFLVKRKVS EIMSTLETNQ CQDLVPFGEP
EGPSFEKQEP HGATSFTEMF EHCSQEDNLC IGSCSENSYI SCSEFSTKHS LYCEQHLPNW
LKRARNGKSR IISKEVFVDL LRGCLSREEK LALHQACDIF YKLFKSVLSL RNSVPMEVQI
DWAKTEASRN ADAGVGEFLM KLVSNERERL TRIWGFATGA DEEDVSLSEY PNRLLAITNT
CDDDDDKEKW SFSGFACAIC LDSFVRRKLL EIHVEERHHV QFAEKCMLLQ CIPCGSHFGD
KEQLLVHVQA VHPSECKSLT VASECNLTNG EFSQKPEAGS SQIVVSQNNE NTSGVHKFVC
KFCGLKFNLL PDLGRHHQAE HMGPSLVGSR GPKKGIRFNT YRMKSGRLSR PNKFKKSLGA
VSYRIRNRAG VNMKRRMQGS KSLGTEGNTE AGVSPPLDDS RNFDGVTDAH CSVVSDILLS
KVQKAKHRPN NLDILSAARS ACCRVSVETS LEAKFGDLPD RIYLKAAKLC GEQGVQVQWH
QEGYICSNGC KPVKDPNLLH PLIPRQENDR FGIAVDAGQH SNIELEVDEC HCIMEAHHFS
KRPFGNTAVL CKDISFGKES VPICVVDDDL WNSEKPYEMP WECFTYVTNS ILHPSMDLVK
ENLQLRCSCR SSVCSPVTCD HVYLFGNDFE DARDIYGKSM RCRFPYDGKQ RIILEEGYPV
YECNKFCGCS RTCQNRVLQN GIRAKLEVFR TESKGWGLRA CEHILRGTFV CEYIGEVLDQ
QEANKRRNQY GNGDCSYILD IDANINDIGR LMEEELDYAI DATTHGNISR FINHSCSPNL
VNHQVIVESM ESPLAHIGLY ASMDIAAGEE ITRDYGRRPV PSEQENEHPC HCKATNCRGL
LS
