A1CSI0 (AMPP3_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Aminoacylproline aminopeptidase
Prolidase

Gene names

Name:	pepP
ORF Names:	ACLA_079510

Organism

Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]

Taxonomic identifier

344612 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus clavatus

Protein attributes

Sequence length	466 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 – 466	466	Probable Xaa-Pro aminopeptidase pepP		PRO_0000411862
Sites
	Metal binding	264	1	Manganese 2 By similarity
	Metal binding	275	1	Manganese 1 By similarity
	Metal binding	275	1	Manganese 2 By similarity
	Metal binding	398	1	Manganese 1 By similarity
	Metal binding	438	1	Manganese 1 By similarity
	Metal binding	438	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1CSI0 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 8713EE41A7DE294B	FASTA	466	51,882
	10 20 30 40 50 60 MATVDAILAA KYPAKAHARR VAERLQPHQD GRPGIIYLEA QKTRLIEDND EPVPFRQRRP 70 80 90 100 110 120 FFYLSGCLLP DSSLVYDITE DKLTLFIPPV DPEDVIWSGL PLSTDEALQQ YDVDRVSITT 130 140 150 160 170 180 EVNSTLASIA SAHGGRAVAY NIADQVSPET KFDGFSEINK SVLKGAIEQS RVVKDEYEIA 190 200 210 220 230 240 LIRKANDIST KAHVAAIKAS IIAENEREIE GAFIATCIAN GAREQAYHPI VACGENGATL 250 260 270 280 290 300 HYGRNSDALI DPVTKKKKRN VLIDAGGEYR TYCSDITRVF PLGGGFTTET RQIYEIVLQM 310 320 330 340 350 360 QVECIEMLRD GVQWEEVHAH AHHVAIRGLL ELGILRGSED EIFEKRVSVA FFPHGLGHYL 370 380 390 400 410 420 GMDTHDTGGN PNYADKDTMF RYLRVRGRLP AGSVITVEPG IYFCRFIIEP YLKSSESSKY 430 440 450 460 IDTDVLERYW SVGGVRIEDN VLVTKDGYDN LTTTPKTVEE IESLAA

References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C. PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS027060 Genomic DNA. Translation: EAW06267.1.
RefSeq	XP_001267693.1. XM_001267692.1.
3D structure databases
ProteinModelPortal	A1CSI0.
ModBase	Search...
Protein-protein interaction databases
STRING	5057.CADACLAP00007609.
Protein family/group databases
MEROPS	M24.A09.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADACLAT00007800; CADACLAP00007609; CADACLAG00007800.
GeneID	4700010.
KEGG	act:ACLA_079510.
Phylogenomic databases
HOGENOM	HOG000008763.
KO	K14213.
OrthoDB	EOG4J40RD.
Family and domain databases
Gene3D	3.90.230.10. 1 hit.
InterPro	IPR007865. Aminopep_P_N. IPR000994. Pept_M24_structural-domain. [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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPP3_ASPCL

Accession

Primary (citable) accession number: A1CSI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program