ID   A0A178ECR4_9PLEO        Unreviewed;       455 AA.
AC   A0A178ECR4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Metal-dependent amidase/aminoacylase/carboxypeptidase {ECO:0000313|EMBL:OAL53778.1};
GN   ORFNames=IQ07DRAFT_677214 {ECO:0000313|EMBL:OAL53778.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL53778.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL53778.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL53778.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KV441639; OAL53778.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178ECR4; -.
DR   STRING; 765867.A0A178ECR4; -.
DR   InParanoid; A0A178ECR4; -.
DR   OrthoDB; 3684955at2759; -.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:OAL53778.1};
KW   Hydrolase {ECO:0000313|EMBL:OAL53778.1};
KW   Protease {ECO:0000313|EMBL:OAL53778.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..455
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008085257"
SQ   SEQUENCE   455 AA;  49247 MW;  C0A5D8DCA360E938 CRC64;
     MPAQCAPPIL LFTSLLLLNI FAMNVLNGWS LQRPLGPANL SSQTLDPSAL VPIIKQYRPD
     LARYADFYRN VHQNPEVSGL EAETAALVAS QLRDLGFEVT ADIGGHGVVG IFRNGPGKTV
     LIRAELDALP IQEQTDVPYK STKRMVDRYG NERPIMHACG HDMNMATLLG ATKLLKAAKS
     QWSGTLISLF QPYEERTGGA QAMVDDSLYE IIPIPDVMLG QHVVPLPAGQ IAVKSGPILV
     AADSVNVRVT GGPCEGSANP QWCVDPIPLA MNIVTQLQEH VRMHIGSDDD ATVACWGFHA
     GIPGNDYVTY ADFLLDVKTI RGDVRSKVLD LIEEKIRSDC AAANTPREPS FNYSVRAPLT
     SNNDETTAQV QAAFHVYFGS DSTSMKLTRA CEDFATLGAP HNVPYTYWNF GGSKKADGEI
     PSNHSPFFAP QIEPTLLAGT DAMALAVLSF VAKES
//