ID   MCPB_ARTBC              Reviewed;         526 AA.
AC   D4B1S6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Probable carboxypeptidase 2;
DE            EC=3.4.17.-;
DE   AltName: Full=Carboxypeptidase M14B;
DE   AltName: Full=Carboxypeptidase MCPB;
DE   Flags: Precursor;
GN   Name=MCPB; ORFNames=ARB_02407;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- FUNCTION: Extracellular metalloprotease that contributes to
CC       pathogenicity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   EMBL; ABSU01000027; EFE30708.1; -; Genomic_DNA.
DR   RefSeq; XP_003011348.1; XM_003011302.1.
DR   AlphaFoldDB; D4B1S6; -.
DR   SMR; D4B1S6; -.
DR   EnsemblFungi; EFE30708; EFE30708; ARB_02407.
DR   GeneID; 9524249; -.
DR   KEGG; abe:ARB_02407; -.
DR   eggNOG; ENOG502RDMV; Eukaryota.
DR   HOGENOM; CLU_026103_1_0_1; -.
DR   OMA; SNGADYQ; -.
DR   Proteomes; UP000008866; 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   1: Evidence at protein level;
KW   Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Signal; Virulence.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..526
FT                   /note="Probable carboxypeptidase 2"
FT                   /id="PRO_0000397762"
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        116
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   526 AA;  58561 MW;  601707DDD7794495 CRC64;
     MVAYRLLALI SLGLGSHCAS ALQYGYNQLS THKDSAVVAG AFPAINGTHL QSPAFTSPGT
     VPRGFSDGTS GPTRDETMEG FMRRLARSNS WMAYHEADFK SEEGRKFPYM YLSASNSSVE
     NPSSHKLRVW LQGGVHGNEP AGDQSMLALL GDLAANQKWA AKLLEKMDIL VLPRYNPDGV
     FYFQRYLATN FDPNRDHVKL ARQQTRDIKE LFTRFSPHIA TDMHEFTAGR TFGPKKDIIY
     AADALFSAAK NLNIDEGIRQ LSEKLFAKRM GKDIEAAGLR WDPYITQGES SSSKLLLLEA
     GTDAKIGRNA MGLSQCVVFL CETRGIGIAD QHFERRTLSG LVMAKSILQT AVDNFDEVYN
     TIERGIRRFT NSRNDIVLTD KSPIMERTFG MLNITDASLF DYPIDFATTT PAEAVLTRSR
     PRAYLIPPSW PDIVKRLEVF GVKADKLPYS YVGPVEALNV TSVTFDKEYY EGVVTTTVQT
     KLVERNIRLP AGSYLVKTNQ KNAALAFVAL EVRTKDLLPV LIMDVY