A4I0X6 (A4I0X6_LEIIN) 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:

LINJ_24_1410 EMBL CAM68400.1

Organism

Leishmania infantum [Reference proteome]

Taxonomic identifier

5671 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmaniinae › Leishmania › Leishmania › Leishmania donovani species complex

Protein attributes

Sequence length	536 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
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)
	A4I0X6 [UniParc]. Last modified May 1, 2007. Version 1. Checksum: 28DEB24A4A029B71	FASTA	536	58,127
	10 20 30 40 50 60 MSTPEQLPAL SAAGSPSSGG ASSHHSPHEA SLSFPASVIP GDASAESPRA WSMPRSSTAS 70 80 90 100 110 120 EESAATSQLQ QKPDAPESRL GGRKVVYFVD HSVTSIAYAE GHLMRPSRVR ALHALVHSLG 130 140 150 160 170 180 LDNAECMTVC HARPATAEEM GAFHRSAYLE CLRQAPVICG NPLDEMSLAF QKEFDVPFAS 190 200 210 220 230 240 QNGDCPLFPE VWALVSSQAG ASLACAEALV RGDATVAMNW AGGMHHAAAA HASGFCFVND 250 260 270 280 290 300 IVLCIRRLLR HYQRVLYVDL DVHHGDGVEG AFYGNHRVMT LSLHQFGNGF FPGTGDYPTR 310 320 330 340 350 360 ETADSFAINV PLPTRTGDAA YLLSFRTALS SVVQCFDPEA MVVQCGADTI AGDLIGRLCV 370 380 390 400 410 420 TTLAHTQCVA DVLSLERPTV LLGGGGYHVF HTARCWAIHT ATALGRTAAQ LPLYIPRTDP 430 440 450 460 470 480 YYMDYRRECT PKRPTLHVFL DPDVDDPLPL GDSLAFWRQL CRSIQWQMRA ARLVRQGFFR 490 500 510 520 530 TLQLCRQRRA ALLRQFATQE AGRESGIGVS GPKRPRSANA TDRDAKEGVE DRVVSA

References

[1]

"Comparative genomic analysis of three Leishmania species that cause diverse human disease." Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A., Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A., Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T., Hance Z. , Jagels K., Moule S., Ormond D., Rutter S., Sqaures R., Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S., Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P., Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K., Mottram J.C., Smith D.F., Berriman M. Nat. Genet. 39:839-847(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JPCM5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	FR796456 Genomic DNA. Translation: CAM68400.1.
RefSeq	XP_001465967.1. XM_001465930.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	5671.LinJ24.1050.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5069396.
KEGG	lif:LINJ_24_1410.
Phylogenomic databases
eggNOG	COG0123.
KO	K06067.
OMA	CHARPAT.
ProtClustDB	CLSZ2456459.
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

A4I0X6_LEIIN

Accession

Primary (citable) accession number: A4I0X6

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2007
Last sequence update:	May 1, 2007
Last modified:	April 3, 2013
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)