ID   A0A1G4MKP3_LACFM        Unreviewed;       514 AA.
AC   A0A1G4MKP3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=LAFE_0H13432G {ECO:0000313|EMBL:SCW04434.1};
OS   Lachancea fermentati (Zygosaccharomyces fermentati).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=4955 {ECO:0000313|EMBL:SCW04434.1, ECO:0000313|Proteomes:UP000190831};
RN   [1] {ECO:0000313|EMBL:SCW04434.1, ECO:0000313|Proteomes:UP000190831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 6772 {ECO:0000313|EMBL:SCW04434.1};
RA   Devillers H.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M28 family.
CC       {ECO:0000256|RuleBase:RU361240}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT598491; SCW04434.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4MKP3; -.
DR   STRING; 4955.A0A1G4MKP3; -.
DR   OMA; PNYEYEV; -.
DR   OrthoDB; 51543at2759; -.
DR   Proteomes; UP000190831; Chromosome h.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02130; PA_ScAPY_like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF17; AMINOPEPTIDASE Y; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|RuleBase:RU361240};
KW   Metal-binding {ECO:0000256|RuleBase:RU361240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190831};
KW   Signal {ECO:0000256|RuleBase:RU361240};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT   CHAIN           17..514
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5009028982"
FT   DOMAIN          158..246
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          273..473
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   514 AA;  56867 MW;  A0678DBE3CA190FA CRC64;
     MKLSLLVGAG AMCANAFVLP QNFLNVFTVD ELPGEQALFP KPHLPYFLKH LVDPEKFPED
     ITIEELNATA WDLLDVAETS NNTFGHPTRV IGSPGHWNTI RYILKQFDDM RDYYDISVES
     FKALTGEVKS YNLTYPDGKQ VSSAQPFSLS PPVETFLGKL VEIPNLGCSD ADFKALEIGE
     DSIALIERGE CPFGLKSELA GKHGFKAVVI YDNDPHSKKG VSGTLEKPKK HTVSTIGVSY
     ADGQKLVASI ERDHDFALVF SMDSYVKRIK TKNIIADTKH GDPDNIVALG AHSDSVANGP
     GINDDGSGTA SLLTVAKHLS NYKIKNKVRF AFWSAEEEGL LGSNRYVKEL SPEENYKIRL
     FMDYDMMASP NYQYQIYDAN NVDNPRGSEE LKDLYINYYV NNNLNYTLIP FDGRSDYVAF
     IKNGIPAGGI ATGAEGVNKE NGEAFDKCYH DLCDDVSNLA FDAFLTNTKL IAYSVATYAK
     SLEGFPERDV NETVALKNTD APYEYKYKGG SLIA
//