A6RK67 (AMPP1_BOTFB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable Xaa-Pro aminopeptidase P
Short name=AMPP
Short name=Aminopeptidase P
EC=3.4.11.9

Alternative name(s):
Aminoacylproline aminopeptidase
Prolidase

Gene names

Name:	ampp
ORF Names:	BC1G_00838

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	601 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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 601	601	Probable Xaa-Pro aminopeptidase P		PRO_0000411785
Sites
	Metal binding	398	1	Manganese 2 By similarity
	Metal binding	409	1	Manganese 1 By similarity
	Metal binding	409	1	Manganese 2 By similarity
	Metal binding	507	1	Manganese 1 By similarity
	Metal binding	521	1	Manganese 1 By similarity
	Metal binding	521	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6RK67 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 5801A6788426641C	FASTA	601	66,963
	10 20 30 40 50 60 MESINTTERL AGLRELMKKN KVDIYIVPSE DSHSSEYIAA CDARREFISG FSGSAGCAVV 70 80 90 100 110 120 TLEKAALATD DNWLLLKQGL QDVPTWQEWA AEQSENGKVV GVDPTIMSAS DARKLTEKIK 130 140 150 160 170 180 KRGGNDLVAV EENLVDLVWG DSRPSRPKEP VKVLARKFAG KDVKTKLEDL RKELLKKKSS 190 200 210 220 230 240 GLIVSMLDEI AWLFNLRGND IPYNPVFFSY ASVTSSSATL YVDSSKLSDE CTAHLNENGV 250 260 270 280 290 300 SVRDYSKIFG DAEVLSQSLD AEDTKVKKFL VSSRASWALK RALGGDAKVD EVRSPIGDAK 310 320 330 340 350 360 SVKNETELEG MRACHVRDGA ALIEYFAWLE HQLVVEKVKM DEVTAADRLE QLRSKQKNFV 370 380 390 400 410 420 GLSFDTISST GPNAAVIHYK PEPGNCSIID PNAVYLCDSG AQYFDGTTDT TRTLHFGEPT 430 440 450 460 470 480 EMEKKAYTLV LKGNIALDVA IFPKGTSGFA LDVLARQFLW EEGLDYRHGT GHGVGSFLNV 490 500 510 520 530 540 HEGPIGIGTR IQYSEVPLAP GNVISNEPGY YEDGSFGIRI ENIIMVKEIE TKHQFGEKPY 550 560 570 580 590 600 LGFEHVTMVP YCRKLIDETL LTRKEKHWLN EYHADIYSKT KDFFKGDELT MSWLEREIEP L

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	CH476843 Genomic DNA. Translation: EDN23365.1.
RefSeq	XP_001560810.1. XM_001560760.1.
3D structure databases
ProteinModelPortal	A6RK67.
ModBase	Search...
Protein-protein interaction databases
STRING	332648.A6RK67.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5441454.
KEGG	bfu:BC1G_00838.
Phylogenomic databases
eggNOG	COG0006.
KO	K01262.
OMA	SRYWEQA.
OrthoDB	EOG45F0XX.
Family and domain databases
Gene3D	3.90.230.10. 1 hit.
InterPro	IPR000587. Creatinase. IPR000994. Pept_M24_structural-domain. IPR001131. Peptidase_M24B_aminopep-P_CS. [Graphical view]
Pfam	PF01321. Creatinase_N. 1 hit. PF00557. Peptidase_M24. 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

AMPP1_BOTFB

Accession

Primary (citable) accession number: A6RK67

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	August 21, 2007
Last modified:	April 3, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program