Q6BMV1 (Q6BMV1_DEBHA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

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

Gene names

Ordered Locus Names:

DEHA2F02420g

Organism

Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome] EMBL CAG88776.1

Taxonomic identifier

284592 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces › Debaryomyces hansenii › Debaryomyces hansenii var. hansenii

Protein attributes

Sequence length	497 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
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)
	Q6BMV1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 315304CA25F508ED	FASTA	497	55,881
	10 20 30 40 50 60 MYVQLPFDDL KVDPTQKKRV AYFYDADVGN YAYGAGHPMK PHRIRMAHSL IMNYGLYKKM 70 80 90 100 110 120 EIYRAKPATK QEMCQFHTDE YIDFLSRVSP DNLDMFAKEQ IKFNVGDDCP VFDGLFEYCG 130 140 150 160 170 180 ISGGGSMEGA ARLNRGKCDI AINYAGGLHH AKKSEASGFC YLNDIVLGII ELLRYHPRVL 190 200 210 220 230 240 YIDIDVHHGD GVEEAFYTTD RVMTCSFHKY GEFFPGTGEL RDIGVGKGKY HAINVPLRDG 250 260 270 280 290 300 IDDATYKSIF EPVISKVMEW YQPSAIVLQC GGDSLSGDRL GCFNLSMSGH ANCINFVKSF 310 320 330 340 350 360 NVPMMVVGGG GYTMRNVART WSFEAGLLNN VVLPSELPYN EYYEYYGPDY KLDVRPSNMY 370 380 390 400 410 420 NANSPEFLNK ILTNILTNLE NTKHAPSVQM NYVPNDAEDL GDIDEDTQEA IDTKGGSQQA 430 440 450 460 470 480 RDEITQPDNE FYEDDDKDAG SRDIQNFSKS ASASESKPAE LETTAQPETL EEPEDEKMLT 490 DEELKEINEL NSNENNA

References

[1]

"Genome evolution in yeasts." Genolevures Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382138 Genomic DNA. Translation: CAG88776.1.
RefSeq	XP_460469.1. XM_460469.1.
3D structure databases
ProteinModelPortal	Q6BMV1.
ModBase	Search...
Protein-protein interaction databases
STRING	4959.Q6BMV1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2903047.
KEGG	dha:DEHA2F02420g.
Phylogenomic databases
HOGENOM	HOG000225180.
KO	K06067.
OMA	IPEDAPH.
OrthoDB	EOG4RV60J.
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

Q6BMV1_DEBHA

Accession

Primary (citable) accession number: Q6BMV1

Entry history

Integrated into UniProtKB/TrEMBL:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)