ID   MCPAL_ARTBC             Reviewed;         416 AA.
AC   D4B5N0;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Metallocarboxypeptidase A-like protein ARB_03789;
DE            EC=3.4.17.-;
DE   Flags: Precursor;
GN   ORFNames=ARB_03789;
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].
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   EMBL; ABSU01000045; EFE29358.1; -; Genomic_DNA.
DR   RefSeq; XP_003015506.1; XM_003015460.1.
DR   AlphaFoldDB; D4B5N0; -.
DR   SMR; D4B5N0; -.
DR   STRING; 663331.D4B5N0; -.
DR   MEROPS; M14.014; -.
DR   EnsemblFungi; EFE29358; EFE29358; ARB_03789.
DR   GeneID; 9525352; -.
DR   KEGG; abe:ARB_03789; -.
DR   eggNOG; KOG2650; Eukaryota.
DR   HOGENOM; CLU_019326_1_1_1; -.
DR   OMA; DTIYSWM; -.
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   Gene3D; 3.30.70.340; -; 1.
DR   InterPro; IPR036990; M14A-like_propep.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   Pfam; PF02244; Propep_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Disulfide bond; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Secreted; Signal; Virulence;
KW   Zinc; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..113
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397758"
FT   CHAIN           114..416
FT                   /note="Metallocarboxypeptidase A-like protein ARB_03789"
FT                   /id="PRO_0000397759"
FT   REGION          263..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        381
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         179..182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         250..251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         306..307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        244..267
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  45819 MW;  D6E5DCFBBFC17F7B CRC64;
     MQSLLLLATL LGSALGGAIP SQSANYNGYK VMRVSGDDTS KISHIVSKLG LETWKFPKAA
     NANVDIVVPP KKVAEFEKMS HAAGLKKQVM HENLGDSIKS EMSFRPYSYG GANDTWFQSY
     HKYEDHLKFM QDFQSAHSQN SEIVTSGKSH EGRDITGVHV WGSGEKGSKP AVVFHGTVHA
     REWITTMTVE YILAQLFDDK EAGAALLEKF DFYIFPIANP DGFVFTTESD RMWRKNREQN
     EGGCYGTDLN RNWPYKWEGD GSTTDPCSET YRGPSPGSAP ETKASTSFIK GLADGAGVKM
     FVDWHSYSQL FMTPYGYSCS ARAPNDDVLQ EMASSFADAV KAVHGTSFTT GPICNTIYQA
     NGNSVDWIVD EIKGETAFAA ELRDTGMYGF VLPPEQIIPS GEETWAGVKA MFSKLK