ID   G4TH26_SERID            Unreviewed;       476 AA.
AC   G4TH26;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE            EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN   ORFNames=PIIN_04538 {ECO:0000313|EMBL:CCA70601.1};
OS   Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS   (Piriformospora indica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Sebacinales; Serendipitaceae; Serendipita.
OX   NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA70601.1, ECO:0000313|Proteomes:UP000007148};
RN   [1] {ECO:0000313|EMBL:CCA70601.1, ECO:0000313|Proteomes:UP000007148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA70601.1,
RC   ECO:0000313|Proteomes:UP000007148};
RX   PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA   Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA   Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA   Kogel K.H.;
RT   "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT   the Mutualistic Root Symbiont Piriformospora indica.";
RL   PLoS Pathog. 7:e1002290-e1002290(2011).
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:CCA70601.1}.
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DR   EMBL; CAFZ01000088; CCA70601.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4TH26; -.
DR   STRING; 1109443.G4TH26; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   HOGENOM; CLU_019532_2_0_1; -.
DR   InParanoid; G4TH26; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 1156at2759; -.
DR   Proteomes; UP000007148; 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:UP000007148};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   476 AA;  52182 MW;  17B505F1720B4207 CRC64;
     MLGAMQPTGA VRKAALGLVS FINASPTPYH ATMEATTRLE KAGFDRLREE SEWDIKPGGK
     YYFSRNQSAV VAFTVPKRWA PGGGISMVAT HIDTCNLRVR PVSKKIANGY LQVAVETYGG
     GIWHTWFDRD LSLAGRVIVS DGDNGPFTSR MIKIDRPILR VPSLAIHLDR GVNEQFKFNQ
     ETEFVPILGQ QISSELNAPI HKEGESKGQG LDVSENHHPA LLHLLAEELS IKPEQINDFE
     LHLYDVQPSC LGGLSEEFVF SPRLDNQMTS YCALEALIES TSEASTEACE SQHESNVNLI
     ALFNHEEVGS VSTTGAEGSL IPTVISRLSP SSEALARTTA KSFLISSDMG HGIHPNYRNK
     YQENHRPQLN GGVVIKTNAK QRYTTDAIGS FLIKRLVAKR GGKVQEFEVR NDMACGSTVG
     PALSKMGVRT VDVGLAQLSM HSIRETGGSH DVRAGIDLFL SFFEGFNDID KELSLL
//