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Database: UniProt
Entry: Q0CXE5_ASPTN
LinkDB: Q0CXE5_ASPTN
Original site: Q0CXE5_ASPTN 
ID   Q0CXE5_ASPTN            Unreviewed;       498 AA.
AC   Q0CXE5;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE            EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN   ORFNames=ATEG_01639 {ECO:0000313|EMBL:EAU38396.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU38396.1, ECO:0000313|Proteomes:UP000007963};
RN   [1] {ECO:0000313|Proteomes:UP000007963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) 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; CH476595; EAU38396.1; -; Genomic_DNA.
DR   RefSeq; XP_001209004.1; XM_001209004.1.
DR   AlphaFoldDB; Q0CXE5; -.
DR   STRING; 341663.Q0CXE5; -.
DR   MEROPS; M18.A01; -.
DR   EnsemblFungi; EAU38396; EAU38396; ATEG_01639.
DR   GeneID; 4315825; -.
DR   VEuPathDB; FungiDB:ATEG_01639; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   HOGENOM; CLU_019532_2_0_1; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 1156at2759; -.
DR   Proteomes; UP000007963; 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:UP000007963};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
FT   REGION          195..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   498 AA;  54042 MW;  1B120CAABA71EE1D CRC64;
     MTSKLAQNLK QPALDFLSFV NASPTPFHAV QSAKELLVKA GFQEIKEKDS WASTCRPGGK
     YYLTRNSSTI VAFAVGKKWK PGNPISMVGA HTDSPVLRVK PVSNKRGEGY MQVGVETYGG
     GIWHTWFDRD LGAAGRAMVR MADGSIVQKL IKIDRPILRI PTLAIHLDRQ ETFSFNKETQ
     LFPIAGLVAA ELNRTGGDSN GAEKDTQKAA ESSTEFSPLK SITERHHPYF VELIAAEAGV
     KPIDILDFEM ILFDTQKSCL GGLQEEFIFS PRLDNLNSSF CATVGLIDSV ADASALDDEP
     SIRLIALFDH EEIGSRTAQG ADSNMLPAVI RRLSVLPSAA AGNEDVSTAF EETLSTSFLL
     SADMAHAIHP NYSGKYESDH RPEINKGPVI KINANARYAT NSPGIVLLQE VARKAAEGGR
     EGVPLQLFVV RNDSSCGSTI GPMLSAALGA RTLDLGNPQL SMHSIRETGG TYDVGHSIRL
     FTSFFQHYSS LSKTILVD
//
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