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Database: UniProt
Entry: W9IYT5_FUSOX
LinkDB: W9IYT5_FUSOX
Original site: W9IYT5_FUSOX 
ID   W9IYT5_FUSOX            Unreviewed;       529 AA.
AC   W9IYT5;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE            EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN   ORFNames=FOYG_02587 {ECO:0000313|EMBL:EWY97829.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY97829.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY97829.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal aspartate or glutamate from a
CC         peptide, with a preference for aspartate.; EC=3.4.11.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001335};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; JH717840; EWY97829.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9IYT5; -.
DR   HOGENOM; CLU_019532_2_0_1; -.
DR   OrthoDB; 1156at2759; -.
DR   Proteomes; UP000030753; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05658; M18_DAP; 1.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030753};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
FT   REGION          222..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  58103 MW;  28B5B71AB6120858 CRC64;
     MLALFRVSSR RTSPFRTSID TTPRLFPASF STSSSIMAPP QEALDFVEFV NESPTPYHAV
     QSASARFEKA GFKLIRERDS WASTLRPGGK YYLTRNASTI VAFTIGRKWR PGNPVAIIGA
     HTDSPCLRLK PVSKKTNVGY LQIGVETYGG GIWTSWFDRD LSIAGRVLVK EGDNFVSKLI
     KVDKPLIRIP TLAIHLHRQT NFDPNKETEL FPIAGLVAAE LNKGTKDEKP EEKKDDNEED
     EEFRPLKVMT ERHHPQVLDV ISAEAGVEVS AIIDFELILY DTQKSCIGGL NDEFIFSPRL
     DNLGMTYCSV EGLIESVKDE SSLEEDSTIR LTVCFDHEEI GSTSAQGANS NLLPSVIRRL
     SVLPGKDTAS EGSYEAVHHD NEEATAYEQT LSRSFLVSAD MAHSVHPNYA GKYESSHQPA
     MNGGTVIKIN ANQRYATNSP GIVLLQECAR TAGVPLQLFV VRNDSPCGST IGPGLAAALG
     MRTLDLGNPQ LSMHSIRETG GTADVAYGIK LFKGFFENYG SLEPKILID
//
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