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MCPB_TRIVH
ID   MCPB_TRIVH              Reviewed;         518 AA.
AC   D4D4Z1;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 37.
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=TRV_02159;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
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:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE43078.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ACYE01000116; EFE43078.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003023696.1; XM_003023650.1.
DR   AlphaFoldDB; D4D4Z1; -.
DR   SMR; D4D4Z1; -.
DR   EnsemblFungi; EFE43078; EFE43078; TRV_02159.
DR   GeneID; 9582248; -.
DR   KEGG; tve:TRV_02159; -.
DR   HOGENOM; CLU_026103_1_0_1; -.
DR   Proteomes; UP000008383; 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; Secreted; Signal;
KW   Virulence.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..518
FT                   /note="Probable carboxypeptidase 2"
FT                   /id="PRO_0000397763"
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   518 AA;  57640 MW;  B1BDE11346AF79EB CRC64;
     MVAYHLLTLI SLGLGSHCAS ALQYGYNQLS THKDSAVVAG AFPAINGTHL QSPAFTSPGT
     VPRGFSDGTS GPTRDETMEG FMRRLARSNS WMAYHEADFK SEEGRKFPYM YLSASNSSVE
     NPSSRKLRVW LQGGVHGNEP AGDQSMLALL GDLAANQKWA AKLLEKMDIL VLPRYNPDGV
     FYFQRYLATN FDPNRDHIKL ARQQTRDIKE LFARFSPHIA TDMHEFTAGR TFGPKRDIIY
     AADALFSAAK NLNIDEGIRQ LSEELFAKRM GKDIEAAGLR WDPYITLGES SSSKLLLLEA
     GTDAKIGRNA MGLSQCVVFL CETRGIGIAG QHFERRTLSG LVMAKSILQT AVDNFDEVYN
     TIERGIRRFT NSRNDIVLSD KSPVMERTFG MLNITDASLF DYPIDFATTT PAEAVLTRSR
     PRAYLIPPSW PDIVKRLEVF GVKADKLPYS YVGPVEALNV TSVTFDKEYY EGVVTTTVET
     KLVERNIRLP AGSYLVKTNQ KNAALAFVSL EVRTLYPF
 
 
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