ID   ECM14_PENRW             Reviewed;         522 AA.
AC   B6H233;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ecm14; ORFNames=Pc13g03770;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: Inactive carboxypeptidase that may play a role in cell wall
CC       organization and biogenesis. {ECO:0000250|UniProtKB:P38836}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00730};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250|UniProtKB:P38836}. Secreted
CC       {ECO:0000250|UniProtKB:P38836}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved Glu residue in position 467 essential for
CC       carbopeptidase activity. The mature form lacks catalytic activity
CC       towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}.
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DR   EMBL; AM920428; CAP91446.1; -; Genomic_DNA.
DR   RefSeq; XP_002558814.1; XM_002558768.1.
DR   AlphaFoldDB; B6H233; -.
DR   SMR; B6H233; -.
DR   STRING; 1108849.XP_002558814.1; -.
DR   EnsemblFungi; CAP91446; CAP91446; PCH_Pc13g03770.
DR   GeneID; 8313477; -.
DR   KEGG; pcs:Pc13g03770; -.
DR   VEuPathDB; FungiDB:PCH_Pc13g03770; -.
DR   eggNOG; KOG2650; Eukaryota.
DR   HOGENOM; CLU_019326_1_0_1; -.
DR   OMA; SACEGNV; -.
DR   OrthoDB; 524270at2759; -.
DR   BioCyc; PCHR:PC13G03770-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c13.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
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   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW   Metal-binding; Reference proteome; Secreted; Signal; Vacuole; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..159
FT                   /evidence="ECO:0000250|UniProtKB:P38836"
FT                   /id="PRO_0000453249"
FT   CHAIN           160..522
FT                   /note="Inactive metallocarboxypeptidase ecm14"
FT                   /id="PRO_5000408934"
FT   BINDING         251..254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         251
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         254
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         326..327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         383
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         384..385
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   CARBOHYD        367
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        320..343
FT                   /evidence="ECO:0000250|UniProtKB:P15085"
SQ   SEQUENCE   522 AA;  58450 MW;  28FEDEC149AC189B CRC64;
     MRLFSPILVA STLIPLISAV PAGSSITPPP PLQPSYFTHS SPRPWARLRD WIIGSIWDID
     HKHRSSKHSS PPSNIHDRYG SDVVLRFHLR QPDEAEALAS ASQVLFLDIW AITSEFVDIR
     LADDMIPSLL DLLPLTLRTS YTPLMDNLAD EIYASYPSRH RSDSDFKSGL ASAELKTISN
     CDLFFQEYQP LSVITQWMRL MASMFSSHVR MTSVGVSYEG RDIPALRLGT SHNTETTSGP
     RKTILIVGGS HAREWISTST VTYVAYSLIT HYGYSPAVTR LLHEYDWVLI PTINPDGYVY
     SWESDRLWRK NRQPTGLPLC PGVDLDRAWD YEWDGESTRS NPCSENYAGA EPFEALESQR
     LAQWAQNQTA HGGAEIVGFL DLHSYSQQIL YPYSYSCSSV PPTLESLEEL ALGLAKAIRQ
     TSHESYDVTS ACEGILTQGA AAGITSGGSA LDWFYHKLHT RFSYQIKLRD RGSYGFLLPS
     EHIVPTGKEI FRALLTFGKF VWGEEASDIS LEDMTGDQIP LN