ID   ECM14_ASPFU             Reviewed;         586 AA.
AC   Q4X1U0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ecm14; ORFNames=AFUA_2G08790;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000001; EAL93175.1; -; Genomic_DNA.
DR   RefSeq; XP_755213.1; XM_750120.1.
DR   AlphaFoldDB; Q4X1U0; -.
DR   SMR; Q4X1U0; -.
DR   STRING; 746128.CADAFUBP00002413; -.
DR   EnsemblFungi; EAL93175; EAL93175; AFUA_2G08790.
DR   GeneID; 3513255; -.
DR   KEGG; afm:AFUA_2G08790; -.
DR   VEuPathDB; FungiDB:Afu2g08790; -.
DR   eggNOG; KOG2650; Eukaryota.
DR   HOGENOM; CLU_019326_1_0_1; -.
DR   InParanoid; Q4X1U0; -.
DR   OMA; SACEGNV; -.
DR   OrthoDB; 524270at2759; -.
DR   Proteomes; UP000002530; Chromosome 2.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome; 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_0000453237"
FT   CHAIN           171..586
FT                   /note="Inactive metallocarboxypeptidase ecm14"
FT                   /id="PRO_0000411178"
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