Q54VQ7 (HDA22_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Type-2 histone deacetylase 2
Short name=DdHdaC
EC=3.5.1.98

Gene names

Name:	hdaC
ORF Names:	DDB_G0280195

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	1704 AA.
Sequence status	Complete.
Protein existence	Evidence 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 after cells enter the multicellular phase upon starvation. Ref.2
Sequence similarities	Belongs to the histone deacetylase family. HD type 2 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	Metal-binding
Molecular function	Chromatin regulator Hydrolase Repressor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H3 deacetylation Inferred from electronic annotation. Source: GOC histone H4 deacetylation Inferred from electronic annotation. Source: GOC regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro NAD-dependent histone deacetylase activity (H3-K14 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K18 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K9 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H4-K16 specific) Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1704	1704	Type-2 histone deacetylase 2		PRO_0000331372
Regions
	Compositional bias	25 – 30	6	Poly-Asn
	Compositional bias	45 – 55	11	Poly-Asn
	Compositional bias	58 – 68	11	Poly-Asn
	Compositional bias	225 – 237	13	Poly-Asn
	Compositional bias	246 – 286	41	Poly-Asn
	Compositional bias	360 – 367	8	Poly-Glu
	Compositional bias	543 – 549	7	Poly-Gln
	Compositional bias	561 – 579	19	Poly-Asn
	Compositional bias	673 – 680	8	Poly-Gln
	Compositional bias	1037 – 1040	4	Poly-Thr
	Compositional bias	1489 – 1506	18	Poly-Gln
	Compositional bias	1513 – 1534	22	Thr-rich
	Compositional bias	1540 – 1548	9	Poly-Asn
	Compositional bias	1551 – 1568	18	Poly-Asn
	Compositional bias	1585 – 1616	32	Poly-Asn
Sites
	Metal binding	1256	1	Divalent metal cation By similarity
	Metal binding	1258	1	Divalent metal cation By similarity
	Metal binding	1350	1	Divalent metal cation By similarity
	Binding site	1165	1	Substrate By similarity
	Binding site	1227	1	Substrate; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54VQ7 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 84E83B42FB36896E	FASTA	1,704	190,816
	10 20 30 40 50 60 MSTNNIIEGD EDTKTTITNE SNTDNNNNNN DDNKNNTENT TSPTNNNNTN DNDNNSDNNN 70 80 90 100 110 120 NKNNNNNNSQ VTEEQQVTLE DSGSEDDINF EEHELSDSAE EDEDEMEDDD EDADGRQNQN 130 140 150 160 170 180 PNSAGGKRRG RPSKVQQSTN THLSQTTPES PTIFTPDGKV PKRISTSTNN TPNTQSALKT 190 200 210 220 230 240 NKRPRLTSDE EKDLMLSEES DGGVGEDDDS IMSTNDKPQD ENQSNQNQNN NNNNNNNTTT 250 260 270 280 290 300 TTTTTNNSNN NNQNLNQNNN NNNNNNNINN NNNNNNSNND NNNNNNRPAR GRPKTNGSRS 310 320 330 340 350 360 EERKRIQLQQ YIQATQGSST TTSDPNNQNN QINQINQNNQ NNQNNQNNQN NSLGEEEFGE 370 380 390 400 410 420 EFEEEEEDMG QPKKKTKYKT SKKSVPNHLD IRPCWFVGCV KADRSLKILR PCLIPTCKTH 430 440 450 460 470 480 AIKSEVRISE ALRRGDFVND ESSGVKDKVC GICGDKKDLH HCGNNGCAFG FCNDCVEIAA 490 500 510 520 530 540 MKHNNHPNGN KWICWVCQFV RTKAKEKERT RWVKEQLNPG LTSISRKFRR GPELDMAQAQ 550 560 570 580 590 600 FLQQQQQQQT SPNEKRSSQF NSNNSNNNNN NNSNNNNNNS GFDPSGSPNN QQNQKRLRKK 610 620 630 640 650 660 INASSDIYET RKYTKKRNDE DSAPPSPTSI IGNSVMVGSS GAAGGGIIKN TTVVVEQQGY 670 680 690 700 710 720 SATPPSPNTL MVQQQQQLQQ THQQARLSQQ QAQLQQLKAL QQQHQHQQQN NGNFNNLIES 730 740 750 760 770 780 VLSPNREPLN PIDNFVDQTF TAVKFFSTLS QNPPDEIKER IDNFVDLMMR IKTVRWASDY 790 800 810 820 830 840 GLVWRMIEEL SNLIKRNLLS SQSVVEMYSE LKSLEEGALE NMTTNARNVP LERAITMVFE 850 860 870 880 890 900 NHETAGLIGK ECCSTRNALI YSIEVALRAI ADYQHDLEDN LMEESLRSNK VSTEIEQIEH 910 920 930 940 950 960 QIKANLDEIH KFKYQEVELL DSLSKVRGAI AAHESIRDTL QKKSSELKVD MLLIKNGISD 970 980 990 1000 1010 1020 KEKETKSQQA TLENEIYALK LLITMVESIY WIHDYFYESR VGECEKLINN KLSQLQNKLE 1030 1040 1050 1060 1070 1080 TQIPHPPNAL DNAIPNTTTT VMGEDGQPVI VPTTVDIKNK FKTIAIYHKI CMQHKVPNFH 1090 1100 1110 1120 1130 1140 LEKPDRIQVA VSCINEFASN PLVDIFDNPP EVDMRYVMAV HDANYIKKLE TSLPPENSEF 1150 1160 1170 1180 1190 1200 ETHLESDKSG AMVTVASHKD FEGDDDNIYD TFVSHRSIKA ALRASGSVCA AVDSVSRSGY 1210 1220 1230 1240 1250 1260 TRAFCAIRPP GHHAGRYGRT SDAPSQGYCL INNVAIGAKY ASLTAGYSRI AVVDFDVHHG 1270 1280 1290 1300 1310 1320 NGTQEILSGD DNFLFISIHV CDEKRYFYPG TGQDVGDIDE VSGQFDGNIL NIGLKRNTGS 1330 1340 1350 1360 1370 1380 AVFLQQWMNK IIPRLEAYKP QLIFLSAGFD GHKDDPTNGL KLNEEDYFVI TKMIKTVAFK 1390 1400 1410 1420 1430 1440 YCKGRIISVL EGGYGIEKTN SLQRCVNSHL KALIEDTDEE IHLANISYGH FSETQETAIP 1450 1460 1470 1480 1490 1500 KFNINNFISN PNKRGKKNNL NTINFINNNM NNINNNITNS LSNKQLERQK QLQQQQQQAQ 1510 1520 1530 1540 1550 1560 QAQQQQSPQQ SQTIENTSIT TTTTTTSTTT TLSTSDSESN NNINNNNNDY NNNNNNNSNN 1570 1580 1590 1600 1610 1620 NNNNSNNNQP TNFNSSTSSP ILSGNNNNNN NNNNNNNNNN INNNNNNNSN NNNNMNTSNP 1630 1640 1650 1660 1670 1680 TNQQSSVIIS DDMDDVQTNS NPPNPQYPLS PNSVNRGNNP SNISMSGAQR SAPLIISPKP 1690 1700 SNSPNSPSTS NNNGTPQNIN NSDN

References

	« Hide 'large scale' referencesShow '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. , 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	AAFI02000035 Genomic DNA. Translation: EAL67324.1.
RefSeq	XP_641298.1. XM_636206.1.
3D structure databases
ProteinModelPortal	Q54VQ7.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDBDRAFT_0206434.
Proteomic databases
PRIDE	Q54VQ7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0237658; DDB0237658; DDB_G0280195.
GeneID	8622431.
KEGG	ddi:DDB_G0280195.
Organism-specific databases
dictyBase	DDB_G0280195. hdaC.
Phylogenomic databases
eggNOG	COG0123.
OMA	NSEFETH.
Family and domain databases
Gene3D	3.30.40.10. 1 hit. 3.40.800.20. 1 hit.
InterPro	IPR017956. AT_hook_DNA-bd_motif. IPR000286. His_deacetylse. IPR023801. His_deacetylse_dom. IPR011011. Znf_FYVE_PHD. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
PANTHER	PTHR10625. PTHR10625. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PRINTS	PR01270. HDASUPER.
SMART	SM00384. AT_hook. 1 hit. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HDA22_DICDI

Accession

Primary (citable) accession number: Q54VQ7

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 status

Reviewed (UniProtKB/Swiss-Prot)