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Reviewed, UniProtKB/Swiss-Prot Q8X225 (DIM5_NEUCR)

Last modified February 9, 2010. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5
    EC=2.1.1.43
Alternative name(s):
    Histone H3-K9 methyltransferase dim-5
      Short name=H3-K9-HMTase dim-5
      Short name=HKMT
Gene names
Name: dim-5
ORF Names: 29E8.110, NCU04402
OrganismNeurospora crassa [Complete proteome]
Taxonomic identifier5141 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

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Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Histone methyltransferase that specifically trimethylates histone H3 to form H3K9me3. H3K9me3 marks chromatin regions for DNA methylation. Ref.1 Ref.4

Catalytic activity

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

Cofactor

Binds 4 zinc ions per subunit.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the histone-lysine methyltransferase family. Suvar3-9 subfamily.

Contains 1 post-SET domain.

Contains 1 pre-SET domain.

Contains 1 SET domain.

Sequence caution

The sequence AAL35215.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAF06044.1 differs from that shown. Reason: Erroneous gene model prediction.

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Ontologies

Keywords
   Cellular componentNucleus
   LigandMetal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processchromatin modification

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhistone-lysine N-methyltransferase activity

Inferred from electronic annotation. Source: EC

protein binding Ref.6

Inferred from physical interaction. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

hh3P070411EBI-1268994,EBI-1270655

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 331331Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5
PRO_0000186062

Regions

Domain77 – 15983Pre-SET
Domain161 – 301141SET
Domain315 – 33117Post-SET
Region172 – 1743S-adenosyl-L-methionine binding By similarity
Region254 – 2552S-adenosyl-L-methionine binding

Sites

Metal binding791Zinc 1
Metal binding921Zinc 1 By similarity
Metal binding921Zinc 2 By similarity
Metal binding941Zinc 1
Metal binding1411Zinc 2
Metal binding1411Zinc 3 By similarity
Metal binding1451Zinc 2
Metal binding1471Zinc 3
Metal binding1511Zinc 3
Metal binding2571Zinc 4
Metal binding3191Zinc 4
Metal binding3211Zinc 4
Metal binding3261Zinc 4
Binding site2151S-adenosyl-L-methionine
Binding site2171S-adenosyl-L-methionine
Binding site2511S-adenosyl-L-methionine

Secondary structure

1 .......................................... 331
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q8X225-1 [UniParc].

Last modified December 4, 2007. Version 2.
Checksum: 2C97AB4B5E582D88

FASTA33137,572
        10         20         30         40         50         60 
MEKAFRPHFF NHGKPDANPK EKKNCHWCQI RSFATHAQLP ISIVNREDDA FLNPNFRFID 

        70         80         90        100        110        120 
HSIIGKNVPV ADQSFRVGCS CASDEECMYS TCQCLDEMAP DSDEEADPYT RKKRFAYYSQ 

       130        140        150        160        170        180 
GAKKGLLRDR VLQSQEPIYE CHQGCACSKD CPNRVVERGR TVPLQIFRTK DRGWGVKCPV 

       190        200        210        220        230        240 
NIKRGQFVDR YLGEIITSEE ADRRRAESTI ARRKDVYLFA LDKFSDPDSL DPLLAGQPLE 

       250        260        270        280        290        300 
VDGEYMSGPT RFINHSCDPN MAIFARVGDH ADKHIHDLAL FAIKDIPKGT ELTFDYVNGL 

       310        320        330 
TGLESDAHDP SKISEMTKCL CGTAKCRGYL W

« Hide

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References

« Hide 'large scale' references
[1]"A histone H3 methyltransferase controls DNA methylation in Neurospora crassa."
Tamaru H., Selker E.U.
Nature 414:277-283(2001) [PubMed: 11713521] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: ATCC 18889 / 74-OR8-1a / 40-21 / DSM 1258 / FGSC 988.
[2]"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
Nucleic Acids Res. 31:1944-1954(2003) [PubMed: 12655011] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed: 12712197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[4]"Trimethylated lysine 9 of histone H3 is a mark for DNA methylation in Neurospora crassa."
Tamaru H., Zhang X., McMillen D., Singh P.B., Nakayama J., Grewal S.I., Allis C.D., Cheng X., Selker E.U.
Nat. Genet. 34:75-79(2003) [PubMed: 12679815] [Abstract]
Cited for: FUNCTION, METHYLATION OF HISTONE H3.
[5]"Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase."
Zhang X., Tamaru H., Khan S.I., Horton J.R., Keefe L.J., Selker E.U., Cheng X.
Cell 111:117-127(2002) [PubMed: 12372305] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 30-331 IN COMPLEX WITH ZINC IONS.
[6]"Structural basis for the product specificity of histone lysine methyltransferases."
Zhang X., Yang Z., Khan S.I., Horton J.R., Tamaru H., Selker E.U., Cheng X.
Mol. Cell 12:177-185(2003) [PubMed: 12887903] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 30-331 IN COMPLEX WITH HISTONE H3; S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF419248 Genomic DNA. Translation: AAL35215.1. Sequence problems.
BX908809 Genomic DNA. Translation: CAF06044.1. Sequence problems.
AABX02000020 Genomic DNA. Translation: EAA28243.2.
RefSeqXP_957479.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML9X-ray1.98A30-331[»]
1PEGX-ray2.59A/B30-331[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ8X225. 2 interactions.
STRINGQ8X225.

Genome annotation databases

GeneID3873656.
KEGGncr:NCU04402.

Phylogenomic databases

eggNOGfuNOG10240.
OrthoDBEOG98GXKJ.

Enzyme and pathway databases

BRENDA2.1.1.43. 266.

Family and domain databases

InterProIPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamPF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTSM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEPS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDIM5_NEUCR
AccessionPrimary (citable) accession number: Q8X225
Secondary accession number(s): Q1K5Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: December 4, 2007
Last modified: February 9, 2010
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents