E5ABQ8 (AMPP1_LEPMJ) 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:	Lema_P022290

Organism

Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam) [Complete proteome]

Taxonomic identifier

985895 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › dothideomyceta › Dothideomycetes › Pleosporomycetidae › Pleosporales › Pleosporineae › Leptosphaeriaceae › Leptosphaeria › Leptosphaeria maculans complex › Leptosphaeria maculans › Leptosphaeria maculans 'brassicae' group

Protein attributes

Sequence length	605 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
Technical term	Complete proteome
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 – 605	605	Probable Xaa-Pro aminopeptidase P		PRO_0000411793
Sites
	Metal binding	402	1	Manganese 2 By similarity
	Metal binding	413	1	Manganese 1 By similarity
	Metal binding	413	1	Manganese 2 By similarity
	Metal binding	511	1	Manganese 1 By similarity
	Metal binding	525	1	Manganese 1 By similarity
	Metal binding	525	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	E5ABQ8 [UniParc]. Last modified February 8, 2011. Version 1. Checksum: 9FF7A79350FAB05F	FASTA	605	67,951
	10 20 30 40 50 60 MAKVDTTERL AELRKLMKER NVDIYMVPSE DSHQSEYIAP CDARRGSAGY AVITHDKAAL 70 80 90 100 110 120 ATDGRYFNQA EKQLDGNWEL LKQGIQDVPT IQDWTADQVE GGKVVAVDPS VVTAADARKL 130 140 150 160 170 180 ADKIKKKGGE YKAVDDNLVD KIWSDRPSRP HEKVIVQPIE FSGKSFEDKI EDLRKELEKK 190 200 210 220 230 240 KSLGFVVSML DEIAWLFNLR GSDIPYNPVF FSYAVVTPTT VTLYVDDHKL PEEVKKHLGD 250 260 270 280 290 300 KVTIRPYNAI FEELTTLSKE AFTKDKADAT SKFLTSSRAS WALNKALGGE DRVEETRSPV 310 320 330 340 350 360 GDAKAVKNEV ELEGMRQCHL RDGAALSEYF AWLEDQLINK KAELDEVDGA DKLEAIRKKH 370 380 390 400 410 420 DKFMGLSFDT ISSTGANAAV IHYKPEKGEC AVIDAKAIYL CDSGAQYRDG TTDTTRTVHF 430 440 450 460 470 480 TEPTEMEKKA YTLVLKGNMA LERVKFPKGT TGFALDSLAR QFLWAEGLDY RHGTGHGVGS 490 500 510 520 530 540 FLNVHEGPIG IGTRVQYSEV SLAVGNVVSD EPGYYEDGKF GIRIENMIMV KEVETSHKFG 550 560 570 580 590 600 DKPYLGFEHV TMTPHCRNLV DMSLLGEDEK QFINDYHKEV YEKTSGYFED DALTLKWLKR ETAPY

References

[1]

"Effector diversification within compartments of the Leptosphaeria maculans genome affected by Repeat-Induced Point mutations." Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P., Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S., Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L., Fudal I., Goodwin S.B., Gout L. , Glaser N., Linglin J., Kema G.H.J., Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J., Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G., Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H., Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J. Nat. Commun. 2:202-202(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8.

Cross-references

Sequence databases
EMBL GenBank DDBJ	FP929138 Genomic DNA. Translation: CBY01099.1.
RefSeq	XP_003844578.1. XM_003844530.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CBY01099; CBY01099; LEMA_P022290.1.
GeneID	13291739.
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_LEPMJ

Accession

Primary (citable) accession number: E5ABQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	February 8, 2011
Last modified:	March 6, 2013
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program