(data stored in SCRATCH zone)

SWISSPROT: LAP1_ASPFU

ID   LAP1_ASPFU              Reviewed;         388 AA.
AC   Q4W9P4;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   11-DEC-2019, entry version 63.
DE   RecName: Full=Leucine aminopeptidase 1;
DE            EC=3.4.11.-;
DE   AltName: Full=Leucyl aminopeptidase 1;
DE            Short=LAP1;
DE   Flags: Precursor;
GN   Name=lap1; ORFNames=AFUA_4G04210;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Extracellular aminopeptidase that allows assimilation of
CC       proteinaceous substrates and which contributes to pathogenicity.
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL84569.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AAHF01000016; EAL84569.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_746607.1; XM_741514.1.
DR   SMR; Q4W9P4; -.
DR   STRING; 746128.CADAFUBP00009601; -.
DR   GeneID; 3504012; -.
DR   KEGG; afm:AFUA_4G04210; -.
DR   EuPathDB; FungiDB:Afu4g04210; -.
DR   HOGENOM; HOG000217592; -.
DR   InParanoid; Q4W9P4; -.
DR   KO; K05994; -.
DR   OrthoDB; 1257666at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   InterPro; IPR007484; Peptidase_M28.
DR   Pfam; PF04389; Peptidase_M28; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4W9P4.
DR   SWISS-2DPAGE; Q4W9P4.
KW   Aminopeptidase; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW   Protease; Reference proteome; Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..88
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000412425"
FT   CHAIN           89..388
FT                   /note="Leucine aminopeptidase 1"
FT                   /id="PRO_0000412426"
FT   METAL           188
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250"
FT   METAL           207
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250"
FT   METAL           207
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000250"
FT   METAL           246
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000250"
FT   METAL           273
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250"
FT   METAL           355
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        232
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        322..326
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  43128 MW;  CDFB7AD884C6852D CRC64;
     MKVLTAIALS AIAFTGAVAA VITQEAFLNN PRIHHDQEKY LIELAPYRTR WVTEEEKWAL
     KLDGVNFIDI TEEHNTGFYP TLHSASYVKY PPKMQYAEEV AALNKNLSKE NMKANLERFT
     SFHTRYYKSQ TGIRSATWLF DQVQRVVSES GAAEYGATVE RFSHPWGQFS IIARIPGRTN
     KTVVLGAHQD SINLFLPSIL AAPGADDDGS GTVTILEALR GLLQSDAIAK GNASNTVEFH
     WYSAEEGGML GSQAIFSNYK RNRREIKAML QQDMTGYVQG ALNAGVEEAI GIMVDYVDQG
     LTQFLKDVVT AYCSVGYLET KCGYACSDHT SASKYGYPAA MATEAEMENT NKKIHTTDDK
     IKYLSFDHML EHAKLSLGFA FELAFAPF
//

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