ID   A0A1V2L3V9_CYBFA        Unreviewed;       484 AA.
AC   A0A1V2L3V9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE            EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN   ORFNames=BON22_3786 {ECO:0000313|EMBL:ONH66494.1};
OS   Cyberlindnera fabianii (Yeast) (Hansenula fabianii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=36022 {ECO:0000313|EMBL:ONH66494.1, ECO:0000313|Proteomes:UP000189513};
RN   [1] {ECO:0000313|Proteomes:UP000189513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=65 {ECO:0000313|Proteomes:UP000189513};
RX   PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA   van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT   "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT   and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT   Zimbabwe.";
RL   Genome Announc. 5:E00064-E00064(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ONH66494.1}.
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DR   EMBL; MPUK01000007; ONH66494.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V2L3V9; -.
DR   STRING; 36022.A0A1V2L3V9; -.
DR   VEuPathDB; FungiDB:BON22_3786; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 1156at2759; -.
DR   Proteomes; UP000189513; 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:UP000189513};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   484 AA;  52629 MW;  95BEDF62B6CB1495 CRC64;
     MQHAHDFVAF LNASPTPYHA VDNLKKRLVA HGFTELSERV SWAGKVSRGQ KYFVTRNNSS
     LIAFSVGAKW APGNSVAIVG AHTDSPCLKI KPISKKTNEG FIQVGVELYG GGIWHSWFDS
     DLSLAGRVMV KDGDKYVSKL VNIHKALLKI PTLAIHLDRD VNTKFEFNKE SQLLPIAGLT
     NASPAKSSGG CCGSEDSKLT NEEFQSLTSV IQRHNEELVD LIASEAGVES QSIEDFELLL
     YDHKESCIGG LHDEFIFSAR LDNLTSCFTG TEGLIHSSTE ESLANESGVR LISCFDHEEI
     GSSSAQGADS NFLPNILDRL TGLTAIPEED SKTAVHASRI LESSSKSFFL SSDVAHGIHP
     NYVNKYDSNH KPKLGEGPVI KINANQRYMT NSPGIVLLKE CAKRANVPLQ LFVVANGSPC
     GSTIGPILAS KTGIRTLDLG NPILSMHSIR ETGSSHDVEK AIKLFKSFYD NFSTIEPTII
     VDGE
//