A6SSG4 (A6SSG4_BOTFB) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Proteasome subunit alpha type RuleBase RU000551
EC=3.4.25.1 RuleBase RU000551

Gene names

ORF Names:

BC1G_15795 EMBL EDN22972.1

Organism

Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) [Complete proteome]

Taxonomic identifier

332648 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Leotiomycetes › Helotiales › Sclerotiniaceae › Botryotinia

Protein attributes

Sequence length	279 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity By similarity. RuleBase RU000551
Catalytic activity	Cleavage of peptide bonds with very broad specificity. RuleBase RU000551
Subunit structure	The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits By similarity. RuleBase RU000551
Subcellular location	Cytoplasm. Nucleus By similarity RuleBase RU000551.
Sequence similarities	Belongs to the peptidase T1A family. RuleBase RU000551

Ontologies

Keywords
Cellular component	Cytoplasm RuleBase RU000551 Nucleus SAAS SAAS000426 RuleBase RU000551 Proteasome RuleBase RU000551 EMBL EDN22972.1
Molecular function	Hydrolase Protease Threonine protease RuleBase RU000551
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex, alpha-subunit complex Inferred from electronic annotation. Source: InterPro
Molecular function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A6SSG4 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: F30F0209A3CB6DBF	FASTA	279	30,075
	10 20 30 40 50 60 MADRYSFSLT TFSPSGKLVQ IEYALNAVNQ GVTSLGIKAT NGIVLATEKK SSSTLIDPPS 70 80 90 100 110 120 LSKVSLITPN IGMVYSGMGP DYRVLVDKAR KVSHTGYKRI YNEYPPTRIL VQDVARVMQE 130 140 150 160 170 180 ATQSGGVRPY GVSLLIAGWD DGIEPESEDV AGAEVHPDEK KPSGKTGGIL KGGPMLYQVD 190 200 210 220 230 240 PSGSYFPWKA TAIGKNATSA KTFLEKRYTE GLELEDAVHI ALLTLKETIE GEMNGDTVEI 250 260 270 GIVGPPADHL MGIEGVEGAQ GPRFRKLSPQ EIEDYLTNL

References

[1]

"Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea." Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E. , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M. PLoS Genet. 7:E1002230-E1002230(2011) [PubMed: 21876677] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B05.10.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH477035 Genomic DNA. Translation: EDN22972.1.
RefSeq	XP_001545761.1. XM_001545711.1.
3D structure databases
ProteinModelPortal	A6SSG4.
SMR	A6SSG4. Positions 1-279.
ModBase	Search...
Protein-protein interaction databases
STRING	A6SSG4.
2D gel databases
World-2DPAGE	0005:A6SSG4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5426222.
KEGG	bfu:BC1G_15795.
Phylogenomic databases
OMA	ADRYSFS.
OrthoDB	EOG4QC4FD.
Family and domain databases
InterPro	IPR000426. Proteasome_asu_N. IPR023332. Proteasome_suA-type. IPR001353. Proteasome_sua/b. [Graphical view]
KO	K02726.
Pfam	PF00227. Proteasome. 2 hits. PF10584. Proteasome_A_N. 1 hit. [Graphical view]
SMART	SM00948. Proteasome_A_N. 1 hit. [Graphical view]
PROSITE	PS00388. PROTEASOME_A_1. 1 hit. PS51475. PROTEASOME_A_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A6SSG4_BOTFB

Accession

Primary (citable) accession number: A6SSG4

Entry history

Integrated into UniProtKB/TrEMBL:	August 21, 2007
Last sequence update:	August 21, 2007
Last modified:	January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)