B0XN37 (AMPP2_ASPFC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable Xaa-Pro aminopeptidase AFUB_014460
EC=3.4.11.9

Alternative name(s):
Aminoacylproline aminopeptidase
Prolidase

Gene names

ORF Names:

AFUB_014460

Organism

Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) [Complete proteome]

Taxonomic identifier

451804 [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	487 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 – 487	487	Probable Xaa-Pro aminopeptidase AFUB_014460		PRO_0000411824
Sites
	Metal binding	267	1	Manganese 2 By similarity
	Metal binding	278	1	Manganese 1 By similarity
	Metal binding	278	1	Manganese 2 By similarity
	Metal binding	416	1	Manganese 1 By similarity
	Metal binding	455	1	Manganese 1 By similarity
	Metal binding	455	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0XN37 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: 762B5F710F5E5D53	FASTA	487	54,519
	10 20 30 40 50 60 MRGSGRSDIV ISAVDALDIC ITLARNDCDK YPGSVAAKLG VSSGLIYLVG QPTINWGDSD 70 80 90 100 110 120 QPRPFRQRRY FYYLSGVEEA DCYLTYDIKN DLLTLYVPDF DLHRAIWMGP TLTVKEARER 130 140 150 160 170 180 YDVDQVRYHA SLKGDIQRWA DNYNKTSLLY ILHDTQKPQV LSNELRLDDE LLLPAMDAAR 190 200 210 220 230 240 GIKDEHEIRM IREANRVSAL AHRKVLENVL RMSTEAEIEG LFLDTCISHG AKNQAYEIIA 250 260 270 280 290 300 GSGENAAVLH YVKNNEPLQG RQLVCLDAGA EWNCYASDVT RTFPLAADWP TARARDIYQL 310 320 330 340 350 360 VEEMQEECIK RIQKGVRFLD LQVLAHVIAI EGLMRLGILK GGSVEEIRES GASTVFFPHG 370 380 390 400 410 420 LGHHVGLEVH DVSAKRLTAV EGDKEYYSSI LVPSMSHCPC TLSAPLLEEG MVVTVEPGIY 430 440 450 460 470 480 FSRLALANAR KLAFAKYINF DEAEKYIPIG GVRIEDDILV TSSGHENLTT APKGEEMLEI IRRGIDS

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: CEA10 / CBS 144.89 / FGSC A1163.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS499594 Genomic DNA. Translation: EDP56727.1.
3D structure databases
ProteinModelPortal	B0XN37.
ModBase	Search...
Protein family/group databases
MEROPS	M24.A09.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUBT00001451; CADAFUBP00001417; CADAFUBG00001451.
Phylogenomic databases
HOGENOM	HOG000008763.
Family and domain databases
Gene3D	3.90.230.10. 1 hit.
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_ASPFC

Accession

Primary (citable) accession number: B0XN37

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	April 8, 2008
Last modified:	March 6, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program