Q4X267 (AMPP3_ASPFU) 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:	AFUA_2G07500

Organism

Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	468 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 Reference 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 – 468	468	Probable Xaa-Pro aminopeptidase pepP		PRO_0000411865
Sites
	Metal binding	265	1	Manganese 2 By similarity
	Metal binding	276	1	Manganese 1 By similarity
	Metal binding	276	1	Manganese 2 By similarity
	Metal binding	399	1	Manganese 1 By similarity
	Metal binding	439	1	Manganese 1 By similarity
	Metal binding	439	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4X267 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 11F1A6585B4D620F	FASTA	468	51,944
	10 20 30 40 50 60 MMAAVDAILA GKYPAKAHAR RVAESLQSYR NGCPGIVYLE AQKTRLIEDN DEPAPFRQRR 70 80 90 100 110 120 PFFYLSGCPL PDSCLVYDLS EDQLTLFIPP VDPEDVIWSG LPMSTEEAQN QYDVDRVLVT 130 140 150 160 170 180 TELNSTLASI VSSHGGKAIA FTIADQVSES TQFHGFSEVN HSVLKGVIEQ SRVVKDEYEV 190 200 210 220 230 240 ALLRKANDIS AKAHIAAIKA SQTAVNEREI EGAFIATCIA NGAREQSYHP IVACGENGAT 250 260 270 280 290 300 LHYGKNDDTL IDPVTNQKKR NVLIDAGGEY RTYCADITRV IPVGGKFTAE TRQIYDIVLQ 310 320 330 340 350 360 MQTECIAMLK EGVQWEDVHA HAHRVAIRGL LKLGILRGAE DEIFEKRVSV AFFPHGLGHY 370 380 390 400 410 420 LGMDTHDTGG NPNYADKDTM FRYLRVRGRL PAGSVITVEP GVYFCRFIIE PYIKSPESNK 430 440 450 460 YIDTNVLDRY WRVGGVRIED NVLVTKDGYD NLTTAPKAVD ELERLAAS

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAHF01000001 Genomic DNA. Translation: EAL93048.1.
RefSeq	XP_755086.1. XM_749993.1.
3D structure databases
ProteinModelPortal	Q4X267.
ModBase	Search...
Protein-protein interaction databases
STRING	5085.CADAFUAP00004748.
Proteomic databases
PRIDE	Q4X267.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUAT00004748; CADAFUAP00004748; CADAFUAG00004748.
GeneID	3513766.
KEGG	afm:AFUA_2G07500.
Phylogenomic databases
HOGENOM	HOG000008763.
KO	K14213.
OMA	MFRYLRV.
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_ASPFU

Accession

Primary (citable) accession number: Q4X267

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	July 5, 2005
Last modified:	April 3, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program