ID   SCPD_ARTBC              Reviewed;         497 AA.
AC   D4B0Q6;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 2.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Carboxypeptidase Y homolog ARB_02032 {ECO:0000305};
DE            EC=3.4.16.5 {ECO:0000250|UniProtKB:P00729};
DE   AltName: Full=Serine carboxypeptidase ARB_02032 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_02032;
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: Involved in degradation of small peptides.
CC       {ECO:0000250|UniProtKB:P00729}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid with broad specificity.;
CC         EC=3.4.16.5; Evidence={ECO:0000250|UniProtKB:P00729};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE31163.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000024; EFE31163.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003011803.1; XM_003011757.1.
DR   AlphaFoldDB; D4B0Q6; -.
DR   SMR; D4B0Q6; -.
DR   STRING; 663331.D4B0Q6; -.
DR   MEROPS; S10.014; -.
DR   EnsemblFungi; EFE31163; EFE31163; ARB_02032.
DR   GeneID; 9523576; -.
DR   KEGG; abe:ARB_02032; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_12_3_1; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR033124; Ser_caboxypep_his_AS.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..497
FT                   /note="Carboxypeptidase Y homolog ARB_02032"
FT                   /id="PRO_0000435280"
FT   ACT_SITE        204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        403
FT                   /evidence="ECO:0000250|UniProtKB:P08819"
FT   ACT_SITE        469
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        393
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   497 AA;  54755 MW;  AAC5E0C3EBFEDC4B CRC64;
     MRFTQIVAAA LCLGATEAAV APIDRARKVL GNQHAFDKRD ASGDTAKAPK HLTSKNKKFY
     VDPNSIPGVP FDIGESYAGN LANTPAGNSS LFFWYFPSEN PEAKNEITIW LNGGPGCSSM
     IGLLQENGPF LWQPGTDGPV KNPYAWSKLT NMVWVDQPAG TGFSPGPPTV KDEIDVANQF
     SDFWKNFMDT FDLHHSDVYL AGESYAGQYI PYIASGMLDR KDSEYFNVQG ITIIDPSIGA
     TEVIIDAPSV PALHRFNNII DLNETFVNDI TKKWESCGYK KFMDDALKFP PAGPMTVPGK
     SAGCDVWDEI IAAVKEVNPC FNIYHLRDNC PSPSNVMNGP KNFFNNKQIQ EAIHAHPTDY
     RLCGESQIFG PHRNDRSVPS SYGPLASVIE RTNNTIIAHG DLDFLLFTEG SLASIQNMTW
     GGLQGFQKEP SDKFYVPYKD GSEVGGAGFV GKTHRERGLT WVTVDLAGHE IPQYAPTAAY
     RMLEYMLGRV QSLTETH