ID   MCPB_ARTOC              Reviewed;         539 AA.
AC   C5FYJ7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 46.
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; ORFNames=MCYG_07414;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; DS995707; EEQ34595.1; -; Genomic_DNA.
DR   RefSeq; XP_002843631.1; XM_002843585.1.
DR   AlphaFoldDB; C5FYJ7; -.
DR   SMR; C5FYJ7; -.
DR   EnsemblFungi; EEQ34595; EEQ34595; MCYG_07414.
DR   GeneID; 9230807; -.
DR   eggNOG; ENOG502SIAH; Eukaryota.
DR   HOGENOM; CLU_026103_1_0_1; -.
DR   OMA; SNGADYQ; -.
DR   OrthoDB; 617352at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
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; Reference proteome;
KW   Secreted; Signal; Virulence.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..539
FT                   /note="Carboxypeptidase 2"
FT                   /id="PRO_0000384109"
FT   REGION          49..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        460
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   539 AA;  59781 MW;  B6902AC21A154A79 CRC64;
     MVAYSILTLI SLGLGSHCAS ALQYGYNQVP VHKDSDVVAG AFPPINGTHL QSPAFTTPGT
     VPRDFSDGKA GPTRDEIMDN FLRRLARSNG WMAYHEADFM SEEGRKFPYL YLSGTNSSLE
     NPGSGKKLRV WLQGGVHGNE PAGDQSMLAL LGEMAQNQQW TAKVLEKMDI LVLPRYNPDG
     VFYFQRYLAT NFDPNRDHVK LARQQTRDIK QLFTKFNPHI ATDMHEFSAG RAFGPKKDVI
     YAADALFSAA KNLNIDEGIR QLSEKLFAKR MGKDIEAAGL RWDPYITQGD STNSKLLLLE
     AGTDAKIGRN AMGLTQCVAF LCETRGIGIA DQHFERRTLS GLVMAKSIIQ TAVDNFDEVY
     NTIERGIDRF THSKGSIVLT DKSPISARTF GMLNSTDGKL IDYPIDFAST TPATPVLTRS
     RPRAYLIPQS WTDVVKRLEV LGLKAEKLPY SYTGRVEALN VTSVAFDKEY YEGVVTATVE
     TKLVEQNMRL PAGTYLLSTT QKNAALAFVA LEPEYMDSFA SFGIIPVSKG DQYPIFRLK