C0SCV1 (AMPP1_PARBP) 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:	PABG_05506

Organism

Paracoccidioides brasiliensis (strain Pb03) [Complete proteome]

Taxonomic identifier

482561 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Onygenales › mitosporic Onygenales › Paracoccidioides › Paracoccidioides brasiliensis

Protein attributes

Sequence length	608 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 – 608	608	Probable Xaa-Pro aminopeptidase P		PRO_0000411802
Sites
	Metal binding	393	1	Manganese 2 By similarity
	Metal binding	404	1	Manganese 1 By similarity
	Metal binding	404	1	Manganese 2 By similarity
	Metal binding	514	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)
	C0SCV1 [UniParc]. Last modified May 5, 2009. Version 1. Checksum: 286F0C4AF489CB43	FASTA	608	67,767
	10 20 30 40 50 60 METVDTSQRL ARLRELMKER NVDVYQFISG FSGSAGCAIV SMTKAALSTD GRYFNQASKQ 70 80 90 100 110 120 LDNNWLLLKR GIESMPTWQE WTAEQLEGGK VVGVDPSLIT ASDARSLSET IKKSGGSLLG 130 140 150 160 170 180 VQENLVDLVW GKDRPCRPSE KVTVHPVEFA GKSFEEKITD LRKELEKKKS AGFVVSMLDE 190 200 210 220 230 240 VAWLFNLRGN DIPYNPVFFS YAIITPSTAD LYIDEEKLSA DVKKHLGDKV SLKPYTSIFE 250 260 270 280 290 300 DAKALGQSAQ AEVNGGASDP PRKFFISTKA SWSLSLALGG ANKVEEVRSP ISDAKAIKND 310 320 330 340 350 360 TELEGMRACH IRDGAALTKY FAWLENELVN KKTVLNEVEA SDKLEEIRSK QKNFVGLSFD 370 380 390 400 410 420 TISSSGPNAA VVHYKAERKN CSIIDPEAVY LCDSGAQYLD GTTDTTRTLH FGEPTEKERK 430 440 450 460 470 480 AYTLVLKGMI AIDTAIFPKG TTGFSLDTLA RQFLWKEGLD YLHGTGHGVG SYLVSQELTD 490 500 510 520 530 540 YKNVHEGPIG IGTRVQYSET PLSVGNVISD DSLEPGYYED GKFGIRIENI IMAREVKTTF 550 560 570 580 590 600 SFGERPWLGF EHVTMTPLCR KLIDPSLLND AEKKWINEYH SEVWEKTSGY FAEDELTRNW LKRETQPI

References

[1]

"Annotation of Paracoccidioides brasiliensis Pb03." McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Ma L.-J., Henn M.R., Jaffe D.B., Young S.K., Gnerre S., Berlin A., Heiman D., Hepburn T., Sykes S., Yandava C., Alvarado L., Kodira C.D., Guigo R., Borodovsky M. , Goldman B., Klein B., Mendoza L., Nino-Vega G., San-Blas G., Sil A., Soares C.M., Taylor J., Lander E.S., Nusbaum C., Galagan J.E., Birren B.W. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Pb03.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS544811 Genomic DNA. Translation: EEH23295.1.
3D structure databases
ProteinModelPortal	C0SCV1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.90.230.10. 1 hit.
InterPro	IPR000587. Creatinase. IPR000994. Pept_M24_structural-domain. [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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPP1_PARBP

Accession

Primary (citable) accession number: C0SCV1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	May 5, 2009
Last modified:	March 6, 2013
This is version 20 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program