E3QQU9 (LAP1_COLGM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Leucine aminopeptidase 1
EC=3.4.11.-

Alternative name(s):
Leucyl aminopeptidase 1
Short name=LAP1

Gene names

Name:	LAP1
ORF Names:	GLRG_08381

Organism

Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize anthracnose fungus) (Glomerella graminicola) [Complete proteome]

Taxonomic identifier

645133 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Hypocreomycetidae › Glomerellales › Glomerellaceae › Glomerella › Colletotrichum graminicola

Protein attributes

Sequence length	401 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Extracellular aminopeptidase that allows assimilation of proteinaceous substrates By similarity.
Catalytic activity	Release of an N-terminal amino acid from a peptide.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the peptidase M28 family. M28E subfamily.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding 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
	Signal peptide	1 – 18	18	Potential
	Propeptide	19 – 87	69	By similarity		PRO_0000412405
	Chain	88 – 401	314	Leucine aminopeptidase 1		PRO_0000412406
Sites
	Metal binding	187	1	Zinc 1 By similarity
	Metal binding	206	1	Zinc 1 By similarity
	Metal binding	206	1	Zinc 2; catalytic By similarity
	Metal binding	245	1	Zinc 2; catalytic By similarity
	Metal binding	272	1	Zinc 1 By similarity
	Metal binding	354	1	Zinc 2; catalytic By similarity
Amino acid modifications
	Glycosylation	179	1	N-linked (GlcNAc...) Potential
	Disulfide bond	321 ↔ 325		By similarity

Sequences

	Sequence		Length	Mass (Da)
	E3QQU9 [UniParc]. Last modified January 11, 2011. Version 1. Checksum: 2868A43AE5F44660	FASTA	401	44,812
	10 20 30 40 50 60 MKVAKASLLT ILAHSVSARF LAEDEINRVQ LYPAGSEPEK YLIELAPGDT RWVTEEEKWE 70 80 90 100 110 120 LRRNGNRFFD ITDHKDLGAT RLRTKTKSVF PEKCSLQDKV KPLLKDLDKS EIQKNLEKFT 130 140 150 160 170 180 SFHTRYYKSD YGRQSSEWLL AKIDSIIKDA GADKNVYAQP FPHTWQQSSI IVTIPGKSNS 190 200 210 220 230 240 TVIIGAHQDS INLWLPSILA APGADDDGSG SMTILEAFRT LLKSKDIVSG KADNTIEFHW 250 260 270 280 290 300 YSAEEGGLLG SQAIFSSYEK EGRDIKAMLQ QDMTGFVQRT LDAGQPESVG VITDFVDPGL 310 320 330 340 350 360 TGFIKKVIVE YCKVPYVETK CGYACSDHAS ASKAGYPSAF VIESAFEYSD NHIHSVDDTI 370 380 390 400 KYLSFDHMLE HAKMTLGLVY ELGFTDFTAL EKKGESVSEE L

References

[1]

"Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered by genome and transcriptome analyses." O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J., Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J., Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z., Choi J., Crouch J.A. , Duvick J.P., Farman M.A., Gan P., Heiman D., Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y., Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U., Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H., Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L., Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K., Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F., van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J., Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E., Ma L.-J., Vaillancourt L.J. Nat. Genet. 44:1060-1065(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: M1.001 / M2 / FGSC 10212.

Cross-references

Sequence databases
EMBL GenBank DDBJ	GG697368 Genomic DNA. Translation: EFQ33237.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	EFQ33237; EFQ33237; GLRG_08381.
Family and domain databases
InterPro	IPR007484. Peptidase_M28. [Graphical view]
Pfam	PF04389. Peptidase_M28. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LAP1_COLGM

Accession

Primary (citable) accession number: E3QQU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	January 11, 2011
Last modified:	April 3, 2013
This is version 9 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program