Reviewed, UniProtKB/Swiss-Prot Q55FN5 (HDA11_DICDI)

Names and origin

Protein names

Recommended name:
    Type-1 histone deacetylase 1
    EC=3.5.1.98

Gene names

ORF Names:

DDB_G0268024

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	495 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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.
Sequence similarities	Belongs to the histone deacetylase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chromatin regulator Hydrolase Repressor
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histone 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 component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone deacetylase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 495	495	Type-1 histone deacetylase 1		PRO_0000331369
Regions
	Compositional bias	294 – 297	4	Poly-Gly
	Compositional bias	457 – 480	24	Poly-Asn
Sites
	Active site	136	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55FN5-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: B325100AB480CD63	FASTA	495	56,633
	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

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. , 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.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000003 Genomic DNA. Translation: EAL73465.1.
RefSeq	XP_647498.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q55FN5.
Genome annotation databases
GeneID	3398507.
KEGG	ddi:DDB_0234190.
Organism-specific databases
dictyBase	DDB_G0268024.
Phylogenomic databases
OMA	TGDRLGC.
Family and domain databases
InterPro	IPR000286. His_deacetylse. IPR003084. His_deacetylse_1. [Graphical view]
Gene3D	G3DSA:3.40.800.20. His_deacetylse. 1 hit.
PANTHER	PTHR10625. His_deacetylse. 1 hit. PTHR10625:SF28. His_deacetylse_1. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PIRSF	PIRSF037913. His_deacetylse_1. 1 hit.
PRINTS	PR01270. HDASUPER. PR01271. HISDACETLASE.
ProtoNet	Search...

Entry information

Entry name

HDA11_DICDI

Accession

Primary (citable) accession number: Q55FN5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	May 24, 2005
Last modified:	November 3, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)