Q5AVF0 (AMPP1_EMENI) 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:	AN11005

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	654 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.
Sequence caution	The sequence EAA61245.1 differs from that shown. Reason: Erroneous gene model prediction.

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 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 – 654	654	Probable Xaa-Pro aminopeptidase P		PRO_0000411791
Sites
	Metal binding	449	1	Manganese 2 By similarity
	Metal binding	460	1	Manganese 1 By similarity
	Metal binding	460	1	Manganese 2 By similarity
	Metal binding	558	1	Manganese 1 By similarity
	Metal binding	572	1	Manganese 1 By similarity
	Metal binding	572	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5AVF0 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 7AD6FCE3658C5174	FASTA	654	72,691
	10 20 30 40 50 60 MLFSRPPARL SWILAFQPSQ KLPRYSPRFF SISVSRFAID MEAVDTTKRL SSLRQLMREH 70 80 90 100 110 120 KVDVYIVPSE DSHQSEYIAP CDGRREFISG FSGSAGTAII SLNEAALSTD GRYFNQAAKQ 130 140 150 160 170 180 LDNNWTLLKR GVEGVPTSQE WITQQAEGGK VVGVDPALIT GAAARSLSDA LQKSGASLIG 190 200 210 220 230 240 VSQNLVDLVW GNDRPAPPRE KVRVHPEKYA GKSFQEKVSD LRKELENKKA AGFVISMLDE 250 260 270 280 290 300 IAWLLNLRGS DIPYNPVFIS YCIVTPTKVE LYIDDEKLTP EVKAHLGDDV IIKPYDSIFA 310 320 330 340 350 360 DAKALFEAKK KDPDAPSSKF LLSNRASWAL NLSLGGEDHV EEIRSPIGDA KAVKNEVELA 370 380 390 400 410 420 GMRACHIRDG AALIEYFAWL ENELVNKKST LDEVDAADKL EQLRSKQELF AGLSFDTISS 430 440 450 460 470 480 TGPNGAVIHY KPEKGSCSVI DPNAIYLCDS GGQYLDGTTD VTRTFHFGQP TELEKKAFTL 490 500 510 520 530 540 VLKGCIGLDS AVFPKGTSGF ALDVLARQHL WKEGLDFLHG TGHGIGSYLN VHEGPVGIGT 550 560 570 580 590 600 RVQYTEVPLA PGNVISDEPG FYEDGKFGIR IENVIMVREV QTTHKFGERP WLGFEHVTMC 610 620 630 640 650 PIGQNLIEPS LLSDSEIKWL NDYHAEVWEK THKYFENDEV TRKWLERETR PISK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACD01000131 Genomic DNA. Translation: EAA61245.1. Sequence problems. BN001304 Genomic DNA. Translation: CBF79990.1.
RefSeq	XP_680999.1. XM_675907.1.
3D structure databases
ProteinModelPortal	Q5AVF0.
ModBase	Search...
Protein-protein interaction databases
STRING	162425.CADANIAP00000864.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2869597.
KEGG	ani:AN7730.2.
Phylogenomic databases
eggNOG	NOG270077.
HOGENOM	HOG000255713.
KO	K01262.
OMA	SRYWEQA.
OrthoDB	EOG4H75MC.
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_EMENI

Accession

Primary (citable) accession number: Q5AVF0
Secondary accession number(s): C8VDJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	July 27, 2011
Last modified:	April 3, 2013
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program