Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9C5P4

- SUVH3_ARATH

UniProt

Q9C5P4 - SUVH3_ARATH

Protein

Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH3

Gene

SUVH3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (09 May 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression.

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi432 – 4321Zinc 1By similarity
    Metal bindingi432 – 4321Zinc 2By similarity
    Metal bindingi434 – 4341Zinc 1By similarity
    Metal bindingi438 – 4381Zinc 1By similarity
    Metal bindingi438 – 4381Zinc 3By similarity
    Metal bindingi445 – 4451Zinc 1By similarity
    Metal bindingi447 – 4471Zinc 2By similarity
    Metal bindingi473 – 4731Zinc 2By similarity
    Metal bindingi473 – 4731Zinc 3By similarity
    Metal bindingi477 – 4771Zinc 2By similarity
    Metal bindingi479 – 4791Zinc 3By similarity
    Metal bindingi483 – 4831Zinc 3By similarity
    Binding sitei540 – 5401S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei542 – 5421S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei592 – 5921S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi598 – 5981Zinc 4By similarity
    Metal bindingi657 – 6571Zinc 4By similarity
    Metal bindingi659 – 6591Zinc 4By similarity
    Metal bindingi664 – 6641Zinc 4By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi108 – 12013A.T hookAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
    3. histone methyltransferase activity Source: TAIR
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. regulation of gene expression, epigenetic Source: TAIR

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Transferase

    Keywords - Ligandi

    DNA-binding, Metal-binding, S-adenosyl-L-methionine, Zinc

    Enzyme and pathway databases

    BioCyciARA:AT1G73100-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH3 (EC:2.1.1.43)
    Alternative name(s):
    Histone H3-K9 methyltransferase 3
    Short name:
    H3-K9-HMTase 3
    Protein SET DOMAIN GROUP 19
    Suppressor of variegation 3-9 homolog protein 3
    Short name:
    Su(var)3-9 homolog protein 3
    Gene namesi
    Name:SUVH3
    Synonyms:SDG19, SET19
    Ordered Locus Names:At1g73100
    ORF Names:F3N23.30
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G73100.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation. Chromosomecentromere 1 Publication
    Note: Associates with centromeric constitutive heterochromatin.

    GO - Cellular componenti

    1. chromosome Source: TAIR
    2. chromosome, centromeric region Source: UniProtKB-SubCell
    3. nucleus Source: TAIR

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 669669Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH3PRO_0000186074Add
    BLAST

    Proteomic databases

    PaxDbiQ9C5P4.
    PRIDEiQ9C5P4.

    Expressioni

    Tissue specificityi

    Expressed in leaves stems and flowers.1 Publication

    Gene expression databases

    GenevestigatoriQ9C5P4.

    Interactioni

    Protein-protein interaction databases

    BioGridi28860. 3 interactions.
    IntActiQ9C5P4. 2 interactions.
    MINTiMINT-8068307.
    STRINGi3702.AT1G73100.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9C5P4.
    SMRiQ9C5P4. Positions 155-666.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini208 – 355148YDGPROSITE-ProRule annotationAdd
    BLAST
    Domaini430 – 49162Pre-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini494 – 638145SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini653 – 66917Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni504 – 5063S-adenosyl-L-methionine bindingBy similarity
    Regioni595 – 5962S-adenosyl-L-methionine bindingBy similarity

    Domaini

    Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity.
    In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.By similarity

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.PROSITE-ProRule annotation
    Contains 1 A.T hook DNA-binding domain.Curated
    Contains 1 post-SET domain.PROSITE-ProRule annotation
    Contains 1 pre-SET domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation
    Contains 1 YDG domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3440.
    HOGENOMiHOG000238382.
    InParanoidiQ9C5P4.
    KOiK11420.
    OMAiIHIAFFA.
    PhylomeDBiQ9C5P4.

    Family and domain databases

    Gene3Di2.30.280.10. 1 hit.
    InterProiIPR025794. Hist-Lys_N-MeTrfase_plant.
    IPR003616. Post-SET_dom.
    IPR007728. Pre-SET_dom.
    IPR003606. Pre-SET_Zn-bd_sub.
    IPR015947. PUA-like_domain.
    IPR001214. SET_dom.
    IPR003105. SRA_YDG.
    [Graphical view]
    PfamiPF05033. Pre-SET. 1 hit.
    PF02182. SAD_SRA. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view]
    SMARTiSM00508. PostSET. 1 hit.
    SM00468. PreSET. 1 hit.
    SM00317. SET. 1 hit.
    SM00466. SRA. 1 hit.
    [Graphical view]
    SUPFAMiSSF88697. SSF88697. 1 hit.
    PROSITEiPS50868. POST_SET. 1 hit.
    PS50867. PRE_SET. 1 hit.
    PS51575. SAM_MT43_SUVAR39_2. 1 hit.
    PS50280. SET. 1 hit.
    PS51015. YDG. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9C5P4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQGVPGFNTV PNPNHYDKSI VLDIKPLRSL KPVFPNGNQG PPFVGCPPFG    50
    PSSSEYSSFF PFGAQQPTHD TPDLNQTQNT PIPSFVPPLR SYRTPTKTNG 100
    PSSSSGTKRG VGRPKGTTSV KKKEKKTVAN EPNLDVQVVK KFSSDFDSGI 150
    SAAEREDGNA YLVSSVLMRF DAVRRRLSQV EFTKSATSKA AGTLMSNGVR 200
    TNMKKRVGTV PGIEVGDIFF SRIEMCLVGL HMQTMAGIDY IISKAGSDEE 250
    SLATSIVSSG RYEGEAQDPE SLIYSGQGGN ADKNRQASDQ KLERGNLALE 300
    NSLRKGNGVR VVRGEEDAAS KTGKIYIYDG LYSISESWVE KGKSGCNTFK 350
    YKLVRQPGQP PAFGFWKSVQ KWKEGLTTRP GLILPDLTSG AESKPVSLVN 400
    DVDEDKGPAY FTYTSSLKYS ETFKLTQPVI GCSCSGSCSP GNHNCSCIRK 450
    NDGDLPYLNG VILVSRRPVI YECGPTCPCH ASCKNRVIQT GLKSRLEVFK 500
    TRNRGWGLRS WDSLRAGSFI CEYAGEVKDN GNLRGNQEED AYVFDTSRVF 550
    NSFKWNYEPE LVDEDPSTEV PEEFNLPSPL LISAKKFGNV ARFMNHSCSP 600
    NVFWQPVIRE GNGESVIHIA FFAMRHIPPM AELTYDYGIS PTSEARDESL 650
    LHGQRTCLCG SEQCRGSFG 669
    Length:669
    Mass (Da):73,439
    Last modified:May 9, 2003 - v2
    Checksum:i8878E000747FD1AB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti416 – 4161S → P in AAK28968. (PubMed:11691919)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF344446 mRNA. Translation: AAK28968.1.
    AC008017 Genomic DNA. Translation: AAD55657.1.
    CP002684 Genomic DNA. Translation: AEE35414.1.
    AY099620 mRNA. Translation: AAM20471.1.
    BT002137 mRNA. Translation: AAN72148.1.
    PIRiF96756.
    RefSeqiNP_565056.1. NM_105968.3.
    UniGeneiAt.11687.
    At.43232.

    Genome annotation databases

    EnsemblPlantsiAT1G73100.1; AT1G73100.1; AT1G73100.
    GeneIDi843641.
    KEGGiath:AT1G73100.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF344446 mRNA. Translation: AAK28968.1 .
    AC008017 Genomic DNA. Translation: AAD55657.1 .
    CP002684 Genomic DNA. Translation: AEE35414.1 .
    AY099620 mRNA. Translation: AAM20471.1 .
    BT002137 mRNA. Translation: AAN72148.1 .
    PIRi F96756.
    RefSeqi NP_565056.1. NM_105968.3.
    UniGenei At.11687.
    At.43232.

    3D structure databases

    ProteinModelPortali Q9C5P4.
    SMRi Q9C5P4. Positions 155-666.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 28860. 3 interactions.
    IntActi Q9C5P4. 2 interactions.
    MINTi MINT-8068307.
    STRINGi 3702.AT1G73100.1-P.

    Proteomic databases

    PaxDbi Q9C5P4.
    PRIDEi Q9C5P4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G73100.1 ; AT1G73100.1 ; AT1G73100 .
    GeneIDi 843641.
    KEGGi ath:AT1G73100.

    Organism-specific databases

    TAIRi AT1G73100.

    Phylogenomic databases

    eggNOGi COG3440.
    HOGENOMi HOG000238382.
    InParanoidi Q9C5P4.
    KOi K11420.
    OMAi IHIAFFA.
    PhylomeDBi Q9C5P4.

    Enzyme and pathway databases

    BioCyci ARA:AT1G73100-MONOMER.

    Gene expression databases

    Genevestigatori Q9C5P4.

    Family and domain databases

    Gene3Di 2.30.280.10. 1 hit.
    InterProi IPR025794. Hist-Lys_N-MeTrfase_plant.
    IPR003616. Post-SET_dom.
    IPR007728. Pre-SET_dom.
    IPR003606. Pre-SET_Zn-bd_sub.
    IPR015947. PUA-like_domain.
    IPR001214. SET_dom.
    IPR003105. SRA_YDG.
    [Graphical view ]
    Pfami PF05033. Pre-SET. 1 hit.
    PF02182. SAD_SRA. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view ]
    SMARTi SM00508. PostSET. 1 hit.
    SM00468. PreSET. 1 hit.
    SM00317. SET. 1 hit.
    SM00466. SRA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF88697. SSF88697. 1 hit.
    PROSITEi PS50868. POST_SET. 1 hit.
    PS50867. PRE_SET. 1 hit.
    PS51575. SAM_MT43_SUVAR39_2. 1 hit.
    PS50280. SET. 1 hit.
    PS51015. YDG. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Arabidopsis thaliana genome contains at least 29 active genes encoding SET domain proteins that can be assigned to four evolutionarily conserved classes."
      Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K., Assalkhou R., Schulz I., Reuter G., Aalen R.B.
      Nucleic Acids Res. 29:4319-4333(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, NOMENCLATURE, TISSUE SPECIFICITY.
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Heterochromatin proteins and the control of heterochromatic gene silencing in Arabidopsis."
      Fischer A., Hofmann I., Naumann K., Reuter G.
      J. Plant Physiol. 163:358-368(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY.

    Entry informationi

    Entry nameiSUVH3_ARATH
    AccessioniPrimary (citable) accession number: Q9C5P4
    Secondary accession number(s): Q9SSL7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 9, 2003
    Last sequence update: May 9, 2003
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3