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