ID A0A1G4M769_LACFM Unreviewed; 578 AA.
AC A0A1G4M769;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=LAFE_0B00232g1_1 {ECO:0000313|EMBL:SCV99684.1};
GN ORFNames=LAFE_0B00232G {ECO:0000313|EMBL:SCV99684.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCV99684.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; LT598489; SCV99684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4M769; -.
DR STRING; 4955.A0A1G4M769; -.
DR OMA; MSTHEKV; -.
DR OrthoDB; 3672990at2759; -.
DR Proteomes; UP000190831; Chromosome b.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05674; M20_yscS; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR017141; Pept_M20_carboxypep.
DR InterPro; IPR047177; Pept_M20A.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE_HYDROLASE PM20D1; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037217; Carboxypeptidase_S; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037217-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000190831};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR037217-2}.
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 280..435
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 162
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-1"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-1"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 541
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
SQ SEQUENCE 578 AA; 65477 MW; D1E2514ADAEB95FB CRC64;
MPYGLKSTPV SSRRATFLRH RGSIISVILF LFFGVAISAS HLTKNYMINS KTNLCGKTNA
IIPKFNKSVD VIFEDPQFKE LSIKKLSGAL QIPTEIFDNN PSPEDDLEYY QEFFKLHEYL
SESFPLIYQH LKVQKVNHIN LVYTWEGKNR LLKPMLFTAH QDVVPVERKT VSKWKFPPFS
GHYDEDSDTI WGRGAIDCKT MMIAELEAVE QLLKDGFIPE RTIIIAFGFD EETAGLQGAR
KLGTFFEEQY GQNGIYSIVD EGAMVQEIDK NIFIAAPIVQ EKGYVDVEFT VNGVGGHSSI
PPKHTTIGIA SDIVLTLENN PFSFDMGLDS AFYGYLCCVA EHDSNFPLEY RKAILEAPYD
DKQRKKMVKF TSQVPSMREL MRTSQAVDVF NGGMKANALP EVTKFLVNHR IDLKSSVDET
FARDVKIAKT IAEKYGYGLY ANDREEIAPT ELGYIKVEAL KGLNPSPSSP TRGSPVWDIF
TGTIQNVYEN GLFKKSPQNE LYITKNTISA NSDTKYYWNL TENIYRFFGN VEPPQMWGVV
HSVDEHIPVS AHLTTVAFIY QYIVNVNENA VTDSFQRD
//
