ID   MCPB_TRIEQ              Reviewed;         538 AA.
AC   B8XGR2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Carboxypeptidase 2;
DE            EC=3.4.17.-;
DE   AltName: Full=Carboxypeptidase M14B;
DE   AltName: Full=Carboxypeptidase MCPB;
DE   Flags: Precursor;
GN   Name=MCPB; Synonyms=CARB2;
OS   Trichophyton equinum (Horse ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=63418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Preuett B.L., Abdel-Rahman S.M.;
RT   "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT   and Trichophyton equinum.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular metalloprotease that contributes to
CC       pathogenicity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   EMBL; FJ348244; ACL37334.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8XGR2; -.
DR   GO; GO:0005576; C:extracellular region; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Secreted; Signal;
KW   Virulence.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..538
FT                   /note="Carboxypeptidase 2"
FT                   /id="PRO_0000384110"
FT   REGION          53..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        393
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   538 AA;  59975 MW;  FDE1355489B8E873 CRC64;
     MVAYRFLTLI SLGLGSHCAS ALQYGYNQVS THKDSAVVAG AFPAINGTHL QSPAFTSPGT
     VPRGFSDGTS GPTRDETMEG FMRRLARSNS WMTYHKANFK SEEGRKFPYM YLSASKSSIE
     KPSSHKLRVW LQGGVHGNEP AGDQSMLALL GDLAANQKWA AKLLEKMDIL VLPRYNPDGV
     FYFQRYLATN FDPNRDHIKL ARQQTRDIKE LFARFSPHIA TDMHEFTAGR AFGPKKDIIY
     AADALFSSAK NLNIDEGIRQ LSEKLFAKRM GKDIEAAGLR WDPYITQGES SSSKLLLREA
     GTDAKIGRNA MGLSQCVVFL CETRGIGIAD QHFERRTLSG LVMVKSILQT AVDNFDEVYN
     TIERGIRRFT NSRNDIVLTD RSPIMERTFG MLNTTDATLF DYPIDFATTT PAQAVLTRSR
     PRAYLIPPSW PDIVKRLEVF GVKADKLPYS YVGPVEALNV TSVTFDKEYY EGVVTTTVET
     KLVERNIRLP AGSYLVKTNQ KNAALAFVAL EPENIDSFAS FGVIPVSTGD QYPIFRLK