ID   P20D1_ARTBC             Reviewed;         460 AA.
AC   D4AXX2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Probable carboxypeptidase ARB_01041;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein ARB_01041;
DE   Flags: Precursor;
GN   ORFNames=ARB_01041;
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR   EMBL; ABSU01000017; EFE32150.1; -; Genomic_DNA.
DR   RefSeq; XP_003012790.1; XM_003012744.1.
DR   AlphaFoldDB; D4AXX2; -.
DR   SMR; D4AXX2; -.
DR   STRING; 663331.D4AXX2; -.
DR   EnsemblFungi; EFE32150; EFE32150; ARB_01041.
DR   GeneID; 9522868; -.
DR   KEGG; abe:ARB_01041; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   OMA; VSGHKGM; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Protease; Reference proteome;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..460
FT                   /note="Probable carboxypeptidase ARB_01041"
FT                   /id="PRO_0000411224"
FT   ACT_SITE        207
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   460 AA;  49822 MW;  64C03DA734085BE5 CRC64;
     MQKTYIWALV SLLASSLVDA RSAVFDQTPL DIGGSDDSFD SIARIDPNNN DLLKSEMDKV
     IASSELLSLH RALVEIKSIS DNEQAVGGFL MDYLYSKNFT VEKQYVDYDD PTGKPIRSNR
     RFNIYAYPGN SASPGIILTS HIDTVPPFIP YSLSHPESAS FKRDDILISG RGTVDDKASV
     ACQVIAAMDH LEKHPDIPIG LLFVVSEEVG GRGMSTFSNS RLNSGTYHTI IFGEPTERAL
     VAGHKGMVSF TIRVHGKPAH SGYPWLGRSA VSEMLPILTE VDRLGDIPVS QGGLPSSEKY
     GRTTLNIGFM SGGVAANVVA EEAVANVAVR LAAGNPEDAK DIIFRAIRNA ATKHRKDATV
     VISNGLERPK GDIEVIFGLE AYGVVDIDAD VDGFNVTTVN YGTDVPHWKI YGDNVKRYLY
     GPGTIFVAHG KNEALTVGEL EAGLEGYKTL VAKAAERERS