A7ENP9 (AMPP2_SCLS1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable Xaa-Pro aminopeptidase SS1G_06948
EC=3.4.11.9

Alternative name(s):
Aminoacylproline aminopeptidase
Prolidase

Gene names

ORF Names:

SS1G_06948

Organism

Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum) [Reference proteome]

Taxonomic identifier

665079 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Leotiomycetes › Helotiales › Sclerotiniaceae › Sclerotinia › Sclerotinia sclerotiorum

Protein attributes

Sequence length	556 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 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 – 556	556	Probable Xaa-Pro aminopeptidase SS1G_06948		PRO_0000411851
Sites
	Metal binding	305	1	Manganese 2 By similarity
	Metal binding	316	1	Manganese 1 By similarity
	Metal binding	316	1	Manganese 2 By similarity
	Metal binding	460	1	Manganese 1 By similarity
	Metal binding	501	1	Manganese 1 By similarity
	Metal binding	501	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7ENP9 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: 2B65FDCBC3613FCC	FASTA	556	62,970
	10 20 30 40 50 60 MDFRSLIASS VAQDKDREFE VRPSSRGSWS CKEVDEFDAL SIEYEPKPIE KYPAKLHARQ 70 80 90 100 110 120 VKKYLGLQEG LIYLPGLPSF NYEDSDMQPA FRQRRYFYYL TGVNFPDCIV TYSIHRDQLW 130 140 150 160 170 180 LWIPPPNSGR SVIYNGSRPT AKEIMAKYDL DHVETLPHLD SYLTWYAHTE PGKIHVLHDY 190 200 210 220 230 240 QTPNNVELQI TRKNGSQSIM SESPFDSTKL EEAMNTARAI KSPYELKMIR KASAITAQGH 250 260 270 280 290 300 INVLRGLRYL SNEAEIEAIF TATCIARQAK TQAYGVIAGS GENASTLHYM ANNEPLKGRQ 310 320 330 340 350 360 LLCLDAGCEW DCYASDVTRT VPISGEYTEE AQAIYDLVAK MQDECIEMLK PGANYRDVHM 370 380 390 400 410 420 HAHKVALRGL MELGLVEGGT FNELYMAGVS VAFFPHGLGH YVGLEVHDVG PGGMIITNRL 430 440 450 460 470 480 FDFNRKPADW TDAYFQILSD SGINSGGGAI LSKDMVVTVE PGIYFSRYAL EEVYLKSPKY 490 500 510 520 530 540 AKYINKELLQ KYYPVGGVRI EDDLLITEDG YENLTTAPKG EAALKIINEG REQEEKRVVC 550 EKAAESKRKQ KKTWFW

References

[1]

"Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea." Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E. , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M. PLoS Genet. 7:E1002230-E1002230(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 18683 / 1980 / Ss-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH476629 Genomic DNA. Translation: EDO04465.1.
RefSeq	XP_001591502.1. XM_001591452.1.
3D structure databases
ProteinModelPortal	A7ENP9.
ModBase	Search...
Protein family/group databases
MEROPS	M24.A09.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	EDO04465; EDO04465; SS1G_06948.
GeneID	5488121.
KEGG	ssl:SS1G_06948.
Phylogenomic databases
eggNOG	COG0006.
KO	K14213.
OrthoDB	EOG4897VR.
Family and domain databases
Gene3D	3.90.230.10. 2 hits.
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_SCLS1

Accession

Primary (citable) accession number: A7ENP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	September 11, 2007
Last modified:	March 6, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program