GenomeNet

Database: UniProt
Entry: O64827
LinkDB: O64827
Original site: O64827 
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   16-JAN-2019, entry version 115.
DE   RecName: Full=Histone-lysine N-methyltransferase SUVR5;
DE            EC=2.1.1.43;
DE   AltName: Full=C2H2 zinc finger-SET histone methyltransferase;
DE            Short=Protein C2H2 SET;
DE   AltName: Full=Protein SET DOMAIN GROUP 6;
DE   AltName: Full=Suppressor of variegation 3-9-related protein 5;
DE            Short=Su(var)3-9-related protein 5;
GN   Name=SUVR5; Synonyms=CZS, SDG6, SET6;
GN   OrderedLocusNames=At2g23740/At2g23730/At2g23750;
GN   ORFNames=F27L4.8/F27L4.9/F27L4.7;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Seki M., 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,
RP   INTERACTION WITH LDL1/SWP1, AND DISRUPTION PHENOTYPE.
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
RT   encoding SET domain proteins that can be assigned to four
RT   evolutionarily conserved 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.,
RA   Groth M., Vashisht A.A., Wohlschlegel J., Jacobsen S.E.;
RT   "The SET-domain protein SUVR5 mediates H3K9me2 deposition and
RT   silencing at stimulus response genes in a DNA methylation-independent
RT   manner.";
RL   PLoS Genet. 8:E1002995-E1002995(2012).
CC   -!- FUNCTION: Histone methyltransferase that functions together with
CC       its binding partner LDL1/SWP1 as one of the regulators of flower
CC       timing in Arabidopsis (PubMed:17224141). Mediates H3K9me2
CC       deposition and regulates gene expression in a DNA methylation-
CC       independent manner. Binds DNA through its zinc fingers and
CC       represses the expression of a subset of stimulus response genes.
CC       May represent a novel mechanism for plants to regulate their
CC       chromatin and transcriptional state, which may allow for the
CC       adaptability and modulation necessary to rapidly respond to
CC       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(+) +
CC         N(6)-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; EC=2.1.1.43;
CC   -!- SUBUNIT: Component of a regulatory complex with LDL1/SWP1.
CC       Interacts with LDL1/SWP1. {ECO:0000269|PubMed:17224141}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}. Note=Associates with euchromatic regions.
CC       {ECO:0000250}.
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
CC       are arranged in a triangular cluster; some of these Cys residues
CC       contribute to the binding of two zinc ions within the cluster.
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Displays reduced dimethylation of lysine 9
CC       and lysine 27 of histone H3 and hyperacetylation of histone H4
CC       within the FLC locus and shows a moderate delayed flowering
CC       (PubMed:17224141). Delayed flowering (PubMed:23071452).
CC       {ECO:0000269|PubMed:17224141, ECO:0000269|PubMed:23071452}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       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};
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   UniGene; At.45723; -.
DR   UniGene; At.52882; -.
DR   ProteinModelPortal; O64827; -.
DR   STRING; 3702.AT2G23740.2; -.
DR   iPTMnet; O64827; -.
DR   PaxDb; O64827; -.
DR   PRIDE; O64827; -.
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   eggNOG; COG2940; LUCA.
DR   InParanoid; O64827; -.
DR   OMA; SCNSNFL; -.
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:0006342; P:chromatin silencing; IMP:TAIR.
DR   GO; GO:0034968; P:histone lysine methylation; IDA:UniProtKB.
DR   GO; GO:1900109; P:regulation of histone H3-K9 dimethylation; IMP:TAIR.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
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;
KW   Complete proteome; DNA-binding; Metal-binding; Methyltransferase;
KW   Nucleus; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1382       Histone-lysine N-methyltransferase SUVR5.
FT                                /FTId=PRO_0000233369.
FT   DOMAIN     1145   1221       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN     1224   1356       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1366   1382       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   ZN_FING     735    758       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     769    792       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     838    861       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION     1234   1236       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION     1313   1314       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   COMPBIAS    722    726       Poly-Asp.
FT   METAL      1147   1147       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1147   1147       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1149   1149       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1154   1154       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1154   1154       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1159   1159       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1182   1182       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1203   1203       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1203   1203       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1207   1207       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1209   1209       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1213   1213       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1316   1316       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1370   1370       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1372   1372       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL      1377   1377       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   BINDING    1277   1277       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING    1355   1355       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   CONFLICT    881    881       Y -> H (in Ref. 1; AAZ83311).
FT                                {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
//
DBGET integrated database retrieval system