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Q55FN5 (HDA11_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

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

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. HD type 1 subfamily.

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

Sequences

Sequence LengthMass (Da)Tools
Q55FN5 [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

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AAFI02000003 Genomic DNA. Translation: EAL73465.1.
RefSeqXP_647498.1. XM_642406.1.

3D structure databases

HSSPHSSP built from PDB template 1W22 based on UniProtKB Q9BY41.
ProteinModelPortalQ55FN5.
ModBaseSearch...

Protein-protein interaction databases

STRING44689.DDBDRAFT_0189724.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0234190; DDB0234190; DDB_G0268024.
GeneID8616305.
KEGGddi:DDB_G0268024.

Organism-specific databases

dictyBaseDDB_G0268024. hdaA.

Phylogenomic databases

eggNOGCOG0123.
KOK06067.
OMAWFGGPLL.
ProtClustDBCLSZ2431548.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetSearch...

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: May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Dictyostelium discoideum

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

SIMILARITY comments

Index of protein domains and families

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