Q4PCU8 (Q4PCU8_USTMA) 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:

UM02065.1 EMBL EAK83185.1

Organism

Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) [Reference proteome] EMBL EAK83185.1

Taxonomic identifier

237631 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago › Ustilago maydis

Protein attributes

Sequence length	569 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
Caution	The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. EMBL EAK83185.1

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)
	Q4PCU8 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 18845DA862E52669	FASTA	569	63,301
	10 20 30 40 50 60 MSSTFLASNS IVNTYNGTSA SGAPPSADEP LFAPISSSSN PNSSRVCYFF DSDIGNYHYG 70 80 90 100 110 120 PGHPMKPTRI RMCHSLVMNY GLYKRMEIFR AKPATKREMS QFHTDEYVEF LNRVTPDNVD 130 140 150 160 170 180 SFVREQAKFN VGDDCPVFDG LFEYCSISAG GSMEGAARLS RDKCDIAINW AGGLHHAKKG 190 200 210 220 230 240 EASGFCYIND IVLGILELLR YHPRVLYIDI DVHHGDGVEE AFYTTDRVMT CSFHKYGEFF 250 260 270 280 290 300 PGTGELRDIG IGKGKMYSCN FPLRDGITDE SYKSVFEPVI SQIMQHYQPS AVVLQCGSDS 310 320 330 340 350 360 LAGDKLGCFN LSMRGHANCV EYVKSFGLPL LLLGGGGYTM RNVSRAWAFE TGLAAGQELN 370 380 390 400 410 420 AQIPVNEYYE YFGPDYRLDV RPNNMQDLNT REYLEKIKIQ VFENLRQTAH APSVQGHVEP 430 440 450 460 470 480 RSIVESMHLQ HVNGDMEERI DLGDKNGMQI LDDKYPDERL VDTREFQDHS TRADELDRDA 490 500 510 520 530 540 RANPTRIDDA VHARAARPAL ADSRNPTADP SEHAIDEQIQ ADAMAKLLAP KPTLQAEHPL 550 560 SSSAQPAHTP NSHQPSHSPT PPAPNPPHP

References

[1]

"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis." Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W. Nature 444:97-101(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 521 / FGSC 9021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACP01000075 Genomic DNA. Translation: EAK83185.1.
RefSeq	XP_758212.1. XM_753119.1.
3D structure databases
ProteinModelPortal	Q4PCU8.
ModBase	Search...
Protein-protein interaction databases
STRING	5270.UM02065.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	UM02065T0; UM02065P0; UM02065.
GeneID	3630120.
KEGG	uma:UM02065.1.
Phylogenomic databases
eggNOG	COG0123.
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

Q4PCU8_USTMA

Accession

Primary (citable) accession number: Q4PCU8

Entry history

Integrated into UniProtKB/TrEMBL:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	April 3, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)