Q96WX8 (AMPP3_EMENI) 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:	AN5810

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	465 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 CAC39600.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence EAA58319.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 – 465	465	Probable Xaa-Pro aminopeptidase pepP		PRO_0000411872
Sites
	Metal binding	263	1	Manganese 2 By similarity
	Metal binding	274	1	Manganese 1 By similarity
	Metal binding	274	1	Manganese 2 By similarity
	Metal binding	397	1	Manganese 1 By similarity
	Metal binding	437	1	Manganese 1 By similarity
	Metal binding	437	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q96WX8 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 6464C44D95EF3166	FASTA	465	51,766
	10 20 30 40 50 60 MTSLDSILAD KYPAKAHARR VAEGLKALGH SGGAIYLEAQ KTRLIEDNDE PVPFRQRRPF 70 80 90 100 110 120 FYLSGCLLPD SSLVYNIDSD QLTLFIPPIN PDDVIWSGLP LSAAEALERY DVDNVLETTE 130 140 150 160 170 180 VNATLANIAA SHANNSTAFA IAEQVSEGTK FEGFSETNFN VLKGVIERTR VVKDSYEIAL 190 200 210 220 230 240 LRKANDISAK GHIAAIKASK SATNEREIEA AFIATCIANG AREQSYHPIV ACGQNGATLH 250 260 270 280 290 300 YGKNDEDLID PVTNRRKDNV LIDAGAEYRT YCADITRAFP LNGKFLPETR QIYEIVLRMQ 310 320 330 340 350 360 LECIDMLKEG VQWEDVHAHA HRVAIRGLLE LGILRGSEDE LFDKRISVAF FPHGLGHYLG 370 380 390 400 410 420 MDTHDTGGNP NYEDTDTMFR YLRVRGRLPA GSVITVEPGI YFCRFIIEPF LKNPDLQKYI 430 440 450 460 DVGTLNRYWR VGGVRIEDNV HITKDGHDNL TTAPKTIEEV ESLAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, purification and characterisation of an Aspergillus nidulans prolidase." Jalving R., Bron P., Kester H.C.M., Visser J., Schaap P.J. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: WG312.
[2]	"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.
[3]	"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	AJ296646 Genomic DNA. Translation: CAC39600.1. Different initiation. AACD01000100 Genomic DNA. Translation: EAA58319.1. Different initiation. BN001301 Genomic DNA. Translation: CBF70800.1.
RefSeq	XP_663414.1. XM_658322.1.
3D structure databases
HSSP	HSSP built from PDB template 1A16 based on UniProtKB P15034.
ProteinModelPortal	Q96WX8.
ModBase	Search...
Protein family/group databases
MEROPS	M24.A09.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2871083.
KEGG	ani:AN5810.2.
Phylogenomic databases
eggNOG	COG0006.
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_EMENI

Accession

Primary (citable) accession number: Q96WX8
Secondary accession number(s): C8V093, Q5B0X0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	July 27, 2011
Last modified:	March 6, 2013
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program