ID   ECM14_ASPFC             Reviewed;         586 AA.
AC   B0XRS8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-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=AFUB_024700;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(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 490 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; DS499595; EDP54414.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XRS8; -.
DR   SMR; B0XRS8; -.
DR   EnsemblFungi; EDP54414; EDP54414; AFUB_024700.
DR   VEuPathDB; FungiDB:AFUB_024700; -.
DR   HOGENOM; CLU_019326_1_0_1; -.
DR   PhylomeDB; B0XRS8; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
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   Gene3D; 3.30.70.340; -; 1.
DR   InterPro; IPR036990; M14A-like_propep.
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; Secreted; Signal; Vacuole; Zinc.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..170
FT                   /evidence="ECO:0000250|UniProtKB:P38836"
FT                   /id="PRO_0000453235"
FT   CHAIN           171..586
FT                   /note="Inactive metallocarboxypeptidase ecm14"
FT                   /id="PRO_0000411176"
FT   REGION          540..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         262..265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         337..338
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         394
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         395..396
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        331..354
FT                   /evidence="ECO:0000250|UniProtKB:P15085"
SQ   SEQUENCE   586 AA;  66069 MW;  75EBD76A10552D58 CRC64;
     MRLLLSVLLL LVASLGLVSA VPAGSSITPP PPIEPIQWLS SRSTDSRRPW IRVRDWVIES
     IWGISKDASH HRSVKASPRS RSPSRSLTRY GSDVVLRFHL RNAEEAEALA EATDVLFLDV
     WTSTSEFVDI RLAQEVIPSL LGLLPDSLRT AYTPLIDNLA EMIYATYPTR RPAGFEDQPG
     FIPSMRQSTQ FGDLFFRDYQ PLSVIVPWMR LMASMFSSHV QMINVGVSHE GREIPALRLG
     RTRGQTADPY PRKTIVVVGG SHAREWISTS TVIYVAYSLI TRYGKSQQVT RLLEDFDWVF
     VPTLNPDGYV YTWESDRLWR KNRQPTSLHF CPGIDLDRAW EFQWDGERTR SNPCSENYAG
     TEPFEGTEAH QLAQWALNET QTNNAKIVGF LDLHSYSQQI LYPFSFSCSS VPPTLESLEE
     LGIGLAKVIR LTTHEIYDVT AACEGTITAD DQARNSPPQR PIFPTGGSSG GSALDWFYHQ
     LHTDYAYQIK LRDRGSYGFL LPSEYIVPTG KEIFNVVLTF GKFLIGDLAQ NTDLDWDAEL
     QRTEPDEAPA SQGDGPAPAT QQVLQADVDD EETEWVENAR SEFRRR