ID   A0A1V6RLP7_9EURO        Unreviewed;       525 AA.
AC   A0A1V6RLP7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000256|ARBA:ARBA00026187};
DE   AltName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000256|ARBA:ARBA00026213};
GN   ORFNames=PENVUL_c038G04448 {ECO:0000313|EMBL:OQE02771.1};
OS   Penicillium vulpinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE02771.1, ECO:0000313|Proteomes:UP000191518};
RN   [1] {ECO:0000313|Proteomes:UP000191518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000256|ARBA:ARBA00004116}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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:OQE02771.1}.
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DR   EMBL; MDYP01000038; OQE02771.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6RLP7; -.
DR   STRING; 29845.A0A1V6RLP7; -.
DR   OrthoDB; 3540647at2759; -.
DR   Proteomes; UP000191518; Unassembled WGS sequence.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191518};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..525
FT                   /note="Inactive metallocarboxypeptidase ECM14"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012144584"
FT   DOMAIN          242..264
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
SQ   SEQUENCE   525 AA;  58537 MW;  88FFA86F209D4D14 CRC64;
     MRLYSPILVA STLLPLISAV PAGSSITPPP PLRPVQLTHS TPRPWTRLRD WVIGSIWDTD
     YKRCSSKHSS PPSNIYDRYG SDVVLRFHLR EPDDAQALAA ASQVLFLDIW AITSKFVDIR
     LADDMIPSLL DLLPSTLRTS YTPLMDNLAD QIYASYPSRQ RTDSDFGPGS VSGGLKAISN
     GDLFFQEYQP LPVITQWMRL MASMFSSHVR MISVGVTYEG REIPALRIGT TPDAEPTSGP
     RKTIVIVGGT HAREWISTST VTYVAYSLIT HYGYSPAVTR LLEEYDWVLI PTLNPDGYVY
     SWESDRLWRK NRQPTGLPLC PGVDLDRAWD YEWDGESTRS NPCSENYAGA EPFEALESQR
     LAQWAQNETA HGRAEIVGFV DLHSYSQQIL YPYSYTCSSV PPTLESLEEL ALGLAKAIRQ
     TSHESYDVTS ACEGILTNGA ASGITAGGSA LDWFYHKLHA KFSYQIKLRD RGSYGFLLPS
     EHIVPTGKEI FHALLTFGKF VWGEEALDLS FEDVMGDQIP LSDSL
//