C5FHR9 (AMPP1_ARTOC) 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:	MCYG_01718

Organism

Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis) [Complete proteome]

Taxonomic identifier

554155 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Onygenales › Arthrodermataceae › Arthroderma › Arthroderma otae

Protein attributes

Sequence length	624 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 – 624	624	Probable Xaa-Pro aminopeptidase P		PRO_0000411777
Sites
	Metal binding	421	1	Manganese 2 By similarity
	Metal binding	432	1	Manganese 1 By similarity
	Metal binding	432	1	Manganese 2 By similarity
	Metal binding	530	1	Manganese 1 By similarity
	Metal binding	544	1	Manganese 1 By similarity
	Metal binding	544	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	C5FHR9 [UniParc]. Last modified July 28, 2009. Version 1. Checksum: 5169AF9E340FDAB4	FASTA	624	69,198
	10 20 30 40 50 60 MTLFRSHLRF LFKPRFLYFQ SPTGQSSRPF STSQILRTAL DMPPPPVDTT QRLAKLRELM 70 80 90 100 110 120 KQNKVDVYIV PSEDSHQSEY IAPCDGRRAF ISGFTGSAGC AIVSMSKAAL STDGRYFSQA 130 140 150 160 170 180 AKQLDANWKL LKRGVEGVPT WEEWTAEQAE NGKVVGVDPS LITAADARKL SQTLKATGGS 190 200 210 220 230 240 LVGIDQNLID IVWGDERPAR PVTTITVQPV ELAGKPFEEK VEALRKELAT KKRSAMVISA 250 260 270 280 290 300 EIYVDDSRLS PEARKQLEGK VVLKPYDAIF QASKVLAESK ASASDGAASG KFLLSNKASW 310 320 330 340 350 360 SLSLALGGEQ NVDEVRSPIT DAKAIKNDVE LEGFRKCHIR DGAALIEYFA WLENALIKEG 370 380 390 400 410 420 AKLDEVDGAD KLYEIRKKYD LFVGNSFDTI SSTGANGAII HYKPEKSTCS VIDPKAMYLC 430 440 450 460 470 480 DSGGQYKDGT TDTTRTLHFG EPTEFQKKAY ALVLKGHISI DNAIFPKGTT GYAIDSFARQ 490 500 510 520 530 540 HLWREGLDYL HGTGHGVGSF LNVHEGPMGI GSRAQYAEVP LSAKNVLSNE PGYYEDGNFG 550 560 570 580 590 600 IRLENLVICK EVETTHKFGD KPFLGFEYIT MVPFCQKLLD ASLLTEAERK WVNDYHAKVW 610 620 EKTSPFFEKD ELTLNWLKRE TQPI

References

[1]

"Comparative genome analysis of Trichophyton rubrum and related dermatophytes reveals candidate genes involved in infection." Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W., Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E., Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I., Rossi A., Saif S. , Samalova M., Saunders C.W., Shea T., Summerbell R.C., Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C. MBio 3:E259-E259(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4605 / CBS 113480.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS995702 Genomic DNA. Translation: EEQ28899.1.
RefSeq	XP_002848784.1. XM_002848738.1.
3D structure databases
ProteinModelPortal	C5FHR9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	9227763.
Phylogenomic databases
OrthoDB	EOG45F0XX.
Family and domain databases
Gene3D	3.90.230.10. 1 hit.
InterPro	IPR000587. Creatinase. IPR000994. Pept_M24_structural-domain. IPR001131. Peptidase_M24B_aminopep-P_CS. [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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPP1_ARTOC

Accession

Primary (citable) accession number: C5FHR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	July 28, 2009
Last modified:	March 6, 2013
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program