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Q9T0G7

- SUVH9_ARATH

UniProt

Q9T0G7 - SUVH9_ARATH

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Protein
Histone-lysine N-methyltransferase family member SUVH9
Gene
SUVH9, SDG22, SET22, At4g13460, T6G15.10
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Histone methyltransferase family member that plays a role in gene silencing. According to 1 Publication, the protein does not bind S-adenosyl-L-methionine and lacks methyltransferase activity. Instead, it may function downstream of DRM2 in RNA-directed DNA methylation, binding to methylated DNA and recruiting DNA-directed RNA polymerase V to chromatin (1 Publication).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi434 – 4341Zinc 1
Metal bindingi434 – 4341Zinc 2
Metal bindingi436 – 4361Zinc 1
Metal bindingi440 – 4401Zinc 1
Metal bindingi440 – 4401Zinc 3
Metal bindingi444 – 4441Zinc 1
Metal bindingi446 – 4461Zinc 2
Metal bindingi472 – 4721Zinc 2
Metal bindingi472 – 4721Zinc 3
Metal bindingi476 – 4761Zinc 2
Metal bindingi478 – 4781Zinc 3
Metal bindingi482 – 4821Zinc 3

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. histone-lysine N-methyltransferase activity Source: InterPro
  3. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. DNA mediated transformation Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT4G13460-MONOMER.
ARA:GQT-2273-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase family member SUVH9
Alternative name(s):
Histone H3-K9 methyltransferase 9
Short name:
H3-K9-HMTase 9
Protein SET DOMAIN GROUP 22
Suppressor of variegation 3-9 homolog protein 9
Short name:
Su(var)3-9 homolog protein 9
Gene namesi
Name:SUVH9
Synonyms:SDG22, SET22
Ordered Locus Names:At4g13460
ORF Names:T6G15.10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G13460.

Subcellular locationi

Nucleus Inferred. Chromosomecentromere By similarity
Note: Associates with centromeric constitutive heterochromatin Inferred.1 Publication

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 650650Histone-lysine N-methyltransferase family member SUVH9
PRO_0000186080Add
BLAST

Proteomic databases

PaxDbiQ9T0G7.
PRIDEiQ9T0G7.

Expressioni

Gene expression databases

GenevestigatoriQ9T0G7.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi140 – 16728
Helixi178 – 19215
Beta strandi215 – 2173
Helixi219 – 2246
Beta strandi234 – 2385
Beta strandi242 – 2465
Beta strandi249 – 2568
Beta strandi268 – 2725
Helixi291 – 30111
Beta strandi306 – 3127
Beta strandi322 – 33817
Beta strandi344 – 3529
Helixi360 – 37213
Helixi374 – 3763
Beta strandi382 – 3854
Beta strandi391 – 3944
Beta strandi396 – 3994
Helixi407 – 4104
Beta strandi411 – 4133
Helixi445 – 4495
Turni450 – 4523
Helixi487 – 4893
Beta strandi495 – 4995
Beta strandi501 – 51111
Beta strandi518 – 5214
Beta strandi525 – 5273
Helixi529 – 5379
Helixi545 – 5473
Helixi551 – 5533
Turni554 – 5574
Turni560 – 5623
Beta strandi580 – 5823
Beta strandi584 – 5874
Helixi589 – 5924
Beta strandi600 – 60910
Beta strandi617 – 6248
Beta strandi633 – 6353

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NJ5X-ray2.40A134-650[»]
ProteinModelPortaliQ9T0G7.
SMRiQ9T0G7. Positions 138-637.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini205 – 352148YDG
Add
BLAST
Domaini432 – 49059Pre-SET
Add
BLAST
Domaini493 – 637145SET
Add
BLAST

Domaini

Although both SET and pre-SET domains are present, the absence of the post-SET domain may explain the lack of methyltransferase activity. Besides, the Cys residues in the SET domain that normally bind a zinc ion are not conserved.
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.

Sequence similaritiesi

Contains 1 pre-SET domain.
Contains 1 SET domain.
Contains 1 YDG domain.

Phylogenomic databases

eggNOGiCOG3440.
HOGENOMiHOG000238382.
InParanoidiQ9T0G7.
KOiK11420.
OMAiSWFDVGK.
PhylomeDBiQ9T0G7.

Family and domain databases

Gene3Di2.30.280.10. 1 hit.
InterProiIPR025794. Hist-Lys_N-MeTrfase_plant.
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]
SMARTiSM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
SM00466. SRA. 1 hit.
[Graphical view]
SUPFAMiSSF88697. SSF88697. 1 hit.
PROSITEiPS50867. 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.

Q9T0G7-1 [UniParc]FASTAAdd to Basket

« Hide

MGSSHIPLDP SLNPSPSLIP KLEPVTESTQ NLAFQLPNTN PQALISSAVS    50
DFNEATDFSS DYNTVAESAR SAFAQRLQRH DDVAVLDSLT GAIVPVEENP 100
EPEPNPYSTS DSSPSVATQR PRPQPRSSEL VRITDVGPES ERQFREHVRK 150
TRMIYDSLRM FLMMEEAKRN GVGGRRARAD GKAGKAGSMM RDCMLWMNRD 200
KRIVGSIPGV QVGDIFFFRF ELCVMGLHGH PQSGIDFLTG SLSSNGEPIA 250
TSVIVSGGYE DDDDQGDVIM YTGQGGQDRL GRQAEHQRLE GGNLAMERSM 300
YYGIEVRVIR GLKYENEVSS RVYVYDGLFR IVDSWFDVGK SGFGVFKYRL 350
ERIEGQAEMG SSVLKFARTL KTNPLSVRPR GYINFDISNG KENVPVYLFN 400
DIDSDQEPLY YEYLAQTSFP PGLFVQQSGN ASGCDCVNGC GSGCLCEAKN 450
SGEIAYDYNG TLIRQKPLIH ECGSACQCPP SCRNRVTQKG LRNRLEVFRS 500
LETGWGVRSL DVLHAGAFIC EYAGVALTRE QANILTMNGD TLVYPARFSS 550
ARWEDWGDLS QVLADFERPS YPDIPPVDFA MDVSKMRNVA CYISHSTDPN 600
VIVQFVLHDH NSLMFPRVML FAAENIPPMT ELSLDYGVVD DWNAKLAICN 650
Length:650
Mass (Da):72,174
Last modified:May 1, 2000 - v1
Checksum:iB2F291C5FA18A6E9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF344452 mRNA. Translation: AAK28974.1.
AL049656 Genomic DNA. Translation: CAB41104.1.
AL161536 Genomic DNA. Translation: CAB78388.1.
CP002687 Genomic DNA. Translation: AEE83282.1.
CP002687 Genomic DNA. Translation: AEE83283.1.
PIRiT06648.
RefSeqiNP_001031625.1. NM_001036548.1.
NP_193082.1. NM_117420.2.
UniGeneiAt.3118.

Genome annotation databases

EnsemblPlantsiAT4G13460.1; AT4G13460.1; AT4G13460.
AT4G13460.2; AT4G13460.2; AT4G13460.
GeneIDi826978.
KEGGiath:AT4G13460.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF344452 mRNA. Translation: AAK28974.1 .
AL049656 Genomic DNA. Translation: CAB41104.1 .
AL161536 Genomic DNA. Translation: CAB78388.1 .
CP002687 Genomic DNA. Translation: AEE83282.1 .
CP002687 Genomic DNA. Translation: AEE83283.1 .
PIRi T06648.
RefSeqi NP_001031625.1. NM_001036548.1.
NP_193082.1. NM_117420.2.
UniGenei At.3118.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4NJ5 X-ray 2.40 A 134-650 [» ]
ProteinModelPortali Q9T0G7.
SMRi Q9T0G7. Positions 138-637.
ModBasei Search...

Proteomic databases

PaxDbi Q9T0G7.
PRIDEi Q9T0G7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G13460.1 ; AT4G13460.1 ; AT4G13460 .
AT4G13460.2 ; AT4G13460.2 ; AT4G13460 .
GeneIDi 826978.
KEGGi ath:AT4G13460.

Organism-specific databases

TAIRi AT4G13460.

Phylogenomic databases

eggNOGi COG3440.
HOGENOMi HOG000238382.
InParanoidi Q9T0G7.
KOi K11420.
OMAi SWFDVGK.
PhylomeDBi Q9T0G7.

Enzyme and pathway databases

BioCyci ARA:AT4G13460-MONOMER.
ARA:GQT-2273-MONOMER.

Gene expression databases

Genevestigatori Q9T0G7.

Family and domain databases

Gene3Di 2.30.280.10. 1 hit.
InterProi IPR025794. Hist-Lys_N-MeTrfase_plant.
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 SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
SM00466. SRA. 1 hit.
[Graphical view ]
SUPFAMi SSF88697. SSF88697. 1 hit.
PROSITEi 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

« Hide 'large scale' publications
  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], NOMENCLATURE.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [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. "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.
  5. "SRA-domain proteins required for DRM2-mediated de novo DNA methylation."
    Johnson L.M., Law J.A., Khattar A., Henderson I.R., Jacobsen S.E.
    PLoS Genet. 4:E1000280-E1000280(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, LACK OF METHYLTRANSFERASE ACTIVITY, LACK OF S-ADENOSYL-L-METHIONINE BINDING.
  6. "SRA- and SET-domain-containing proteins link RNA polymerase V occupancy to DNA methylation."
    Johnson L.M., Du J., Hale C.J., Bischof S., Feng S., Chodavarapu R.K., Zhong X., Marson G., Pellegrini M., Segal D.J., Patel D.J., Jacobsen S.E.
    Nature 507:124-128(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 134-650 IN COMPLEX WITH ZINC IONS, SUBCELLULAR LOCATION, FUNCTION.

Entry informationi

Entry nameiSUVH9_ARATH
AccessioniPrimary (citable) accession number: Q9T0G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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