A2D8N0 (A2D8N0_TRIVA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Histone deacetylase PIRNR PIRNR037913
EC=3.5.1.98 PIRNR PIRNR037913

Gene names

ORF Names:

TVAG_185870 EMBL EAY23279.1

Organism

Trichomonas vaginalis [Reference proteome]

Taxonomic identifier

5722 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Parabasalia › Trichomonadida › Trichomonadidae › Trichomonas

Protein attributes

Sequence length	435 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone. PIRNR PIRNR037913
Subcellular location	Nucleus By similarity PIRNR PIRNR037913.
Sequence similarities	Belongs to the histone deacetylase family. HD Type 1 subfamily. PIRNR PIRNR037913

Ontologies

Keywords
Biological process	Transcription Transcription regulation PIRNR PIRNR037913
Cellular component	Nucleus PIRNR PIRNR037913
Molecular function	Chromatin regulator PIRNR PIRNR037913 Hydrolase PIRNR PIRNR037913 SAAS SAAS000286 EMBL EAY23279.1
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	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	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
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A2D8N0 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: C4F46DD690FAF44A	FASTA	435	49,666
	10 20 30 40 50 60 MADEKKKRIV YFYDEDVGNF FYAPNHPMKP HRIRMAHNLI LSYNLFPKLQ IYRPKKATVE 70 80 90 100 110 120 ELTRFHTPEY IQFLQMATPD NTQNQACLFD KFNVGEDSPV FEGLFEFCQS SAGGSISAAR 130 140 150 160 170 180 HLNSGHADIA INWAGGLHHA KKGEASGFCY VADCVLGILE LLERYDRVMY IDIDIHHGDG 190 200 210 220 230 240 VEEAFYTTDR VLTVSFHKFG NEFFPGTGHD KDIGLGKGRH YAVNVPLKDG MDDKSYHYIF 250 260 270 280 290 300 KPIIKHLIEW YRPQAIFLQC GADSLTGDRL GSFNLTIHGH GECVNYVKSF KLPMLVAGGG 310 320 330 340 350 360 GYTVRNVSRC WTYETAVLLD EEIEDKLPYH DYLGYYGPDY RLDLVPSNMA NLNSQESLDH 370 380 390 400 410 420 LIESITESIR HLPCAPSVQL CLKDPKKLLE DSDESDNEEF DDRLASRYVR TRLKINTLYN 430 AEDENPEEDH DVPLN

References

[1]

"Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis." Carlton J.M., Hirt R.P., Silva J.C., Delcher A.L., Schatz M., Zhao Q., Wortman J.R., Bidwell S.L., Alsmark U.C.M., Besteiro S., Sicheritz-Ponten T., Noel C.J., Dacks J.B., Foster P.G., Simillion C., Van de Peer Y., Miranda-Saavedra D., Barton G.J. , Westrop G.D., Mueller S., Dessi D., Fiori P.L., Ren Q., Paulsen I., Zhang H., Bastida-Corcuera F.D., Simoes-Barbosa A., Brown M.T., Hayes R.D., Mukherjee M., Okumura C.Y., Schneider R., Smith A.J., Vanacova S., Villalvazo M., Haas B.J., Pertea M., Feldblyum T.V., Utterback T.R., Shu C.L., Osoegawa K., de Jong P.J., Hrdy I., Horvathova L., Zubacova Z., Dolezal P., Malik S.B., Logsdon J.M. Jr., Henze K., Gupta A., Wang C.C., Dunne R.L., Upcroft J.A., Upcroft P., White O., Salzberg S.L., Tang P., Chiu C.-H., Lee Y.-S., Embley T.M., Coombs G.H., Mottram J.C., Tachezy J., Fraser-Liggett C.M., Johnson P.J. Science 315:207-212(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC PRA-98 / G3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS113179 Genomic DNA. Translation: EAY23279.1.
RefSeq	XP_001584265.1. XM_001584215.1.
3D structure databases
ProteinModelPortal	A2D8N0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5468841.
KEGG	tva:TVAG_185870.
Organism-specific databases
EuPathDB	TrichDB:TVAG_185870.
Phylogenomic databases
eggNOG	COG0123.
KO	K06067.
Family and domain databases
Gene3D	3.40.800.20. 1 hit.
InterPro	IPR000286. His_deacetylse. IPR003084. His_deacetylse_1. IPR023801. His_deacetylse_dom. [Graphical view]
PANTHER	PTHR10625. PTHR10625. 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

A2D8N0_TRIVA

Accession

Primary (citable) accession number: A2D8N0

Entry history

Integrated into UniProtKB/TrEMBL:	February 20, 2007
Last sequence update:	February 20, 2007
Last modified:	March 6, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)