A6SL16 (AMPP2_BOTFB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable Xaa-Pro aminopeptidase BC1G_13431
EC=3.4.11.9

Alternative name(s):
Aminoacylproline aminopeptidase
Prolidase

Gene names

ORF Names:

BC1G_13431

Organism

Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)

Taxonomic identifier

332648 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Leotiomycetes › Helotiales › Sclerotiniaceae › Botryotinia › Botryotinia fuckeliana

Protein attributes

Sequence length	549 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides By similarity.
Catalytic activity	Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Cofactor	Binds 2 manganese ions per subunit By similarity.
Sequence similarities	Belongs to the peptidase M24B family.

Ontologies

Keywords
Ligand	Manganese Metal-binding
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
Gene Ontology (GO)
Biological_process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: InterPro metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 549	549	Probable Xaa-Pro aminopeptidase BC1G_13431		PRO_0000411830
Sites
	Metal binding	297	1	Manganese 2 By similarity
	Metal binding	308	1	Manganese 1 By similarity
	Metal binding	308	1	Manganese 2 By similarity
	Metal binding	452	1	Manganese 1 By similarity
	Metal binding	493	1	Manganese 1 By similarity
	Metal binding	493	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6SL16 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 03B084740D6F4D19	FASTA	549	62,098
	10 20 30 40 50 60 MSSFTAQDKD QEVRPSSSGS WACKEVDEFD ALSIEYKPKP TEKYPAKLHA RNVRKYLDVG 70 80 90 100 110 120 EGLIYLPGLP SFNYEDSDMP PAFRQRRYFY YITGVNLSDC IVTYNIHRDQ LWLWIPPPNS 130 140 150 160 170 180 GRSVIYNGAR PTIKEIMSKY DFDHVETLTH LDSYLTWYAH TEPGKIHVLH DYQAPKNIEL 190 200 210 220 230 240 QITRKNGCHS IISESPFDSS KLEEAMNTAR AIKSPYELRM IRKASAITAQ GHLNVLRGLR 250 260 270 280 290 300 HLSNEAEIEA IFTATCIAKQ AKTQAYGVIA GSGENASTLH YMANNEPLKG RQLLCLDAGC 310 320 330 340 350 360 EWDCYASDVT RTVPISGEYT EEAEAIYDIV AKMQDECIEL LKPGANYRDI HIHAHKVALK 370 380 390 400 410 420 GLMDLGLVEG GTFDELFMAG VSVAFFPHGL GHYVGLEVHD VGPGGSRITN RLYGFDKKPA 430 440 450 460 470 480 DWTDAYFQIL SNTGVTSDGG SILEKDMVVT VEPGIYFSRY ALEEVYLKSP NYAKYINKDL 490 500 510 520 530 540 LQKYYPVGGV RIEDDLLITE DGYENLTTVL KGKEALKIIN EGKEQEEEEE REANRKATES RKQKKTWFW

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B05.10.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH476959 Genomic DNA. Translation: EDN19351.1.
RefSeq	XP_001548054.1. XM_001548004.1.
3D structure databases
ProteinModelPortal	A6SL16.
ModBase	Search...
Protein family/group databases
MEROPS	M24.A09.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5428547.
KEGG	bfu:BC1G_13431.
Phylogenomic databases
eggNOG	COG0006.
KO	K14213.
OMA	GHHVGLE.
OrthoDB	EOG4897VR.
Family and domain databases
Gene3D	3.90.230.10. 2 hits.
InterPro	IPR007865. Aminopep_P_N. IPR000994. Pept_M24_structural-domain. IPR001131. Peptidase_M24B_aminopep-P_CS. [Graphical view]
Pfam	PF05195. AMP_N. 1 hit. PF00557. Peptidase_M24. 1 hit. [Graphical view]
SMART	SM01011. AMP_N. 1 hit. [Graphical view]
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
PROSITE	PS00491. PROLINE_PEPTIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPP2_BOTFB

Accession

Primary (citable) accession number: A6SL16

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	August 21, 2007
Last modified:	March 6, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program