ID   A0A1E3HZ96_9TREE        Unreviewed;       496 AA.
AC   A0A1E3HZ96;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE            EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN   ORFNames=L202_02080 {ECO:0000313|EMBL:ODN81683.1};
OS   Cryptococcus amylolentus CBS 6039.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus.
OX   NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN81683.1, ECO:0000313|Proteomes:UP000094065};
RN   [1] {ECO:0000313|EMBL:ODN81683.1, ECO:0000313|Proteomes:UP000094065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN81683.1,
RC   ECO:0000313|Proteomes:UP000094065};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (JUN-2016) 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}.
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:ODN81683.1}.
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DR   EMBL; AWGJ01000003; ODN81683.1; -; Genomic_DNA.
DR   RefSeq; XP_018996002.1; XM_019135599.1.
DR   AlphaFoldDB; A0A1E3HZ96; -.
DR   STRING; 1295533.A0A1E3HZ96; -.
DR   GeneID; 30153389; -.
DR   OrthoDB; 1156at2759; -.
DR   Proteomes; UP000094065; 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:UP000094065};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   496 AA;  55142 MW;  503FB3B0DEECCE8B CRC64;
     MPLDIPEPPK DAVNFCNFVT HAPTPFHAVA HLTTRLFAAG FEQISERTSD TALKAGGKYF
     YTRNQSSLVA FTLPKKPTKE TAISFAAGHL DSPCLKVRPV SKKIKSGYLQ VGVELYGGGI
     WHSWFDRDLS ISGRVIIANR STSAEHKYVS KLVRIDRPIL RIPTLAIHLD RTANDNFKFN
     KETEFQPILG LVESILNEPT KTALKRTHDQ VATPPPTALS NKSQEDEMNI AMQEEKHHPK
     LLAVLADELG CDVADIQDFE LSLYDTQPSQ VGGLSNEFIF SPRIDNLMTS FSTIEALCEA
     VQSANAADET NIRAVVLFDN EEVGSVSHHG AESNILPAFV ERIAALEDYK EKGYFNLLAN
     SFVISADMGH AIHPNYESRY EANLAPKLNG GVVIKTNANQ RYTSNAQTTF LTRRVAKKAG
     VPLQEFEVRN DSSCGSTLGT FLSKHVRTVD IGLAQLSMHS IRETAGSKDV RYYIDFFRAF
     FEGFGQIDKE LRVDWK
//