ID   A0A1L0DDQ2_9ASCO        Unreviewed;       471 AA.
AC   A0A1L0DDQ2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000256|ARBA:ARBA00026187};
DE   AltName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000256|ARBA:ARBA00026213};
GN   ORFNames=SAMEA4029010_CIC11G00000001276 {ECO:0000313|EMBL:SGZ54700.1};
OS   [Candida] intermedia.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ54700.1, ECO:0000313|Proteomes:UP000182334};
RN   [1] {ECO:0000313|EMBL:SGZ54700.1, ECO:0000313|Proteomes:UP000182334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ54700.1,
RC   ECO:0000313|Proteomes:UP000182334};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inactive carboxypeptidase that may play a role in cell wall
CC       organization and biogenesis. {ECO:0000256|ARBA:ARBA00025210}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   EMBL; LT635759; SGZ54700.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L0DDQ2; -.
DR   STRING; 45354.A0A1L0DDQ2; -.
DR   OrthoDB; 3540647at2759; -.
DR   Proteomes; UP000182334; Chromosome iv.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd03860; M14_CP_A-B_like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF147; INACTIVE METALLOCARBOXYPEPTIDASE ECM14; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000182334};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          351..361
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
SQ   SEQUENCE   471 AA;  54062 MW;  525A1F90356C581D CRC64;
     MKVYKLALFT ALAAAIQIPI SLNVFRDPER PHFSTLEESL WPIDLNPYIN QVVVRISSSG
     DVIKYLRSHG LNIWAKNPSE RTVDVQGHES DIKNMLAHFE ISDANYIIHD LAQTVLESYP
     EKLKQGSFQT FAESSFDEVT AAAEDSIHAA AEVFFKLYRP LLSIDAWLKL LEETYPDVVT
     TEVIGKTYEE RDFKVLHVLI PDSDIPHDEK RTIVITGGVH AREWISVSST LYTIYEMLNV
     YENSPERWKE LAKLDFLFIP VLNPDGYEYS WNSDRLWRKN RQQVEGGDGA RCMGIDIDHS
     FDYHWTQSSD GVCGEEYSGQ APFEAYELKI WDEYLNSTNV NHNIWGYIDL HSYSQEILYP
     YAYSCNETPR DEENLIELAY GITKAIRLTS GKSYSVLPAC VDRDLDLIPD LGSGSALDFM
     YHHRAYWAYQ VKLRDSGAHG FLLPDKYIQP VGEEIAAGIR FFSRFILSED R
//