ID A0A0C7MW36_9SACH Unreviewed; 514 AA.
AC A0A0C7MW36;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=LALA0_S10e04456g {ECO:0000313|EMBL:CEP64188.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP64188.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP64188.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP64188.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) 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}.
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DR EMBL; LN736369; CEP64188.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7MW36; -.
DR STRING; 1245769.A0A0C7MW36; -.
DR HOGENOM; CLU_024336_0_1_1; -.
DR OrthoDB; 51543at2759; -.
DR Proteomes; UP000054304; Unassembled WGS sequence.
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:UP000054304};
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_5005111855"
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; 56519 MW; BD30D162243F309B CRC64;
MRSSTLIAAT LSCAQAFVLP QTFLDAFQLP STSDINVESF WPHKPYFLKH QVDPQSFPDD
IELAELNSTA WDLYQIAQTS NKSYGNPTRV IGSAGHWNTI RYILRQFDDL RDYYEISTQS
FKALSGKVLS YNLNYTSGGK VPTSQAFSLS PPVKPFIGKL VEIPNLGCSD ADFEALDVSK
GSIALIERGE CPFGKKSDLA GKHGFKAAVI YDNNPKSTEG VSGSLEKPTK HTVSTIGVSF
AVGQELILGI TLDPDYSLYF GMDSYVKEIK TKNVIADTKH GDPENIVALG AHSDSVAAGP
GLNDDGSGTI SLLTVAKHLS NYKINNKVRF AFWSAEEEGL VGSNYYVDQL SEEENLKIRL
FMDYDMMASP NYQYQIYNAS NSVNPRGSEE LRDLYIDYYT KYGHNYTLIP FDGRSDYVGF
IENGIPGGGI AAGAEGVNTD NGEVLDACYH ALCDDVSNLN WDAFLTNTQL IAYSVAHFAD
SLEDFPERNA NETKSFASTE NMPKYAYKGG ALIL
//
