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Reviewed, UniProtKB/Swiss-Prot Q55FN5 (HDA11_DICDI)

Last modified February 9, 2010. Version 34. 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Type-1 histone deacetylase 1
      Short name=DdHdaA
    EC=3.5.1.98
Gene names
Name: hdaA
ORF Names: DDB_G0268024
OrganismDictyostelium discoideum (Slime mold) [Complete proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

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Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes By similarity.

Catalytic activity

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity.

Developmental stage

Expressed throughout growth and development. Ref.2

Sequence similarities

Belongs to the histone deacetylase family. Type 1 subfamily.

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Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   LigandMetal-binding
   Molecular functionChromatin regulator
Hydrolase
Repressor
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processhistone deacetylation

Inferred from electronic annotation. Source: InterPro

regulation of transcription

Inferred from electronic annotation. Source: UniProtKB-KW

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhistone deacetylase activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495Type-1 histone deacetylase 1
PRO_0000331369

Regions

Compositional bias294 – 2974Poly-Gly
Compositional bias457 – 48024Poly-Asn

Sites

Active site1361Proton acceptor By similarity
Metal binding1711Divalent metal cation By similarity
Metal binding1731Divalent metal cation By similarity
Metal binding2591Divalent metal cation By similarity
Binding site941Substrate By similarity
Binding site1441Substrate; via carbonyl oxygen By similarity
Binding site2981Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q55FN5-1 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: B325100AB480CD63

FASTA49556,633
        10         20         30         40         50         60 
MSTRKVSYFY DNEVGNHYYG PNHPMKPHRM RMTHDLVLNY GIYKKMQIFR PRKASELELT 

        70         80         90        100        110        120 
NFHSDDYINF LKLVTPDNMH DYSKQLVKFN VREDCPVFDG MYNFCQISSG GSIGCAVKVN 

       130        140        150        160        170        180 
SKESDVAINW AGGLHHAKKS EASGFCYTND IVLSILELLK HHERVLYIDI DIHHGDGVEE 

       190        200        210        220        230        240 
AFYTTDRVMT VSFHKYGDYF PGTGDVKDIG ADKGKYYSLN FPLKDGIDDE SYQSIFRPII 

       250        260        270        280        290        300 
RSVMDFYRPG AVVIQCGADS LTGDRLGCFN LTLRGHAQCI EFLKSFNVPL VVLGGGGYTI 

       310        320        330        340        350        360 
KNVARCWTYE TSILVDSELK DELPYNDYLE YYGPEYRLHI TPNNMENQNT KDYLEKLKIQ 

       370        380        390        400        410        420 
LLENLRNLNH APAAAHHDIP PDSFNYSDDE DDEDPDVRIS EADRDKKVHH QGELSDSDEE 

       430        440        450        460        470        480 
DGRRNYSNGL EATSTSRRNQ VSISAYDKER PSYNSRNNNN NNNNNNNNNN NNNNNSNNNN 

       490 
SHHHNEDADV DMDSG

« Hide

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References

« Hide 'large scale' references
[1]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed: 15875012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[2]"Histone deacetylases regulate multicellular development in the social amoeba Dictyostelium discoideum."
Sawarkar R., Visweswariah S.S., Nellen W., Nanjundiah V.
J. Mol. Biol. 391:833-848(2009) [PubMed: 19576222] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AAFI02000003 Genomic DNA. Translation: EAL73465.1.
RefSeqXP_647498.1.

3D structure databases

HSSPHSSP built from PDB template 1W22 based on UniProtKB Q9BY41.
SMRQ55FN5. Positions 7-368.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ55FN5.

Genome annotation databases

GeneID8616305.
KEGGddi:DDB_0234190.

Organism-specific databases

dictyBaseDDB_G0268024. hdaA.

Phylogenomic databases

eggNOGKOG1342.
HOGENOMHBG396919.
OMAIFKPVIS.
PhylomeDBQ55FN5.

Family and domain databases

InterProIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
[Graphical view]
Gene3DG3DSA:3.40.800.20. His_deacetylse. 1 hit.
PANTHERPTHR10625. His_deacetylse. 1 hit.
PTHR10625:SF28. His_deacetylse_1. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetSearch...

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Entry information

Entry nameHDA11_DICDI
AccessionPrimary (citable) accession number: Q55FN5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: May 24, 2005
Last modified: February 9, 2010
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase

SIMILARITY comments

Index of protein domains and families

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