B2AW39 (AMPP2_PODAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable Xaa-Pro aminopeptidase Pa_7_5850
EC=3.4.11.9

Alternative name(s):
Aminoacylproline aminopeptidase
Prolidase

Gene names

ORF Names:

Pa_7_5850

Organism

Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) [Complete proteome]

Taxonomic identifier

515849 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Sordariales › Lasiosphaeriaceae › Podospora › Podospora anserina

Protein attributes

Sequence length	558 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 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 – 558	558	Probable Xaa-Pro aminopeptidase Pa_7_5850		PRO_0000411848
Sites
	Metal binding	304	1	Manganese 2 By similarity
	Metal binding	315	1	Manganese 1 By similarity
	Metal binding	315	1	Manganese 2 By similarity
	Metal binding	495	1	Manganese 1 By similarity
	Metal binding	528	1	Manganese 1 By similarity
	Metal binding	528	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	B2AW39 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: 7F13EEBF001F66C8	FASTA	558	61,298
	10 20 30 40 50 60 MLADIAKHSA IEVKLPKAHK KNSSSGSSSP TSPATRGNNK RSASWTDYGT PPNAAWLHEK 70 80 90 100 110 120 IKFPAKTHVT KVASKLPPTA NGIIYLPGAE DKYYEDSDQG PAFRQRRHFY YLTGANFPGC 130 140 150 160 170 180 AVTYDLHKDH LILWIPYTDP RTILWYGRTP TLEEVRASTD VDEVRYVAGV NRYICASLTP 190 200 210 220 230 240 GASIYVLHPD QAPQLESPKG VVQIDTHSLR PAIETARVVK TDYEIAQIRR ANAVSSAAHR 250 260 270 280 290 300 AALSRLSRLG NERELEAIFA GYCIAQGAHT QAYPIIAGAG PAASTLHYDN NNAPLKPHQF 310 320 330 340 350 360 VVLDAGCEWN CYASDITRTY PIPGSFSAEA KAIYHAVLRM QRECVERIKP GVVYSSLHLH 370 380 390 400 410 420 ACKVAIEELL RLGILHNGTK EEILARGTIA GFFPHGLGHH VGLEVHDVSG RERLLLDSKS 430 440 450 460 470 480 SLGPAGGVKS ARCRLSPSKR ELVLPETLAV MFRDEMKEGG GGDGQGKGVV QMQKAKRSAG 490 500 510 520 530 540 GGRQRLEEGM VVTVEPGMAY FLDVPYHAHF INKKALEQYW DLGGVRIEDD ILVTKTGYEN 550 LTDVPREIEE VLKVMNPS

References

[1]

"The genome sequence of the model ascomycete fungus Podospora anserina." Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M., Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V., Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M., Contamine V., Arnaise S. , Bourdais A., Berteaux-Lecellier V., Gautheret D., de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B., El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H., Debuchy R., Wincker P., Weissenbach J., Silar P. Genome Biol. 9:R77.1-R77.22(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S / ATCC MYA-4624 / DSM 980 / FGSC 10383.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU633900 Genomic DNA. Translation: CAP68613.1.
RefSeq	XP_001907940.1. XM_001907905.1.
3D structure databases
ProteinModelPortal	B2AW39.
ModBase	Search...
Protein family/group databases
MEROPS	M24.A09.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6192525.
KEGG	pan:PODANSg4975.
Phylogenomic databases
KO	K14213.
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_PODAN

Accession

Primary (citable) accession number: B2AW39

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	May 20, 2008
Last modified:	March 6, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program