ID   CBPYB_ARTBC             Reviewed;         508 AA.
AC   D4ANB6;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Carboxypeptidase Y homolog ARB_05721 {ECO:0000305};
DE            EC=3.4.16.5 {ECO:0000250|UniProtKB:P00729};
DE   Flags: Precursor;
GN   ORFNames=ARB_05721;
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).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(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:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; ABSU01000003; EFE35677.1; -; Genomic_DNA.
DR   RefSeq; XP_003016322.1; XM_003016276.1.
DR   AlphaFoldDB; D4ANB6; -.
DR   SMR; D4ANB6; -.
DR   ESTHER; trit1-f2s2t8; Carboxypeptidase_S10.
DR   EnsemblFungi; EFE35677; EFE35677; ARB_05721.
DR   GeneID; 9521805; -.
DR   KEGG; abe:ARB_05721; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   OMA; TFGYWET; -.
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; 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; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   1: Evidence at protein level;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..508
FT                   /note="Carboxypeptidase Y homolog ARB_05721"
FT                   /id="PRO_0000434922"
FT   ACT_SITE        204
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
FT   ACT_SITE        410
FT                   /evidence="ECO:0000250|UniProtKB:P08819"
FT   ACT_SITE        484
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
FT   BINDING         413
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
FT   BINDING         485
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        451
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        282..305
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
FT   DISULFID        289..298
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
FT   DISULFID        332..338
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
SQ   SEQUENCE   508 AA;  57171 MW;  F2553A309E893E12 CRC64;
     MELYLNMLSF WYILLATSFF GPSQAVYQAP LSVDESQKVT IEEGFQIFTS KHSPQHSIRI
     KKQDGSICDA HSAQYTGWLD IGPKHLFFWY FESQNDPEND PLTLWMTGGP GYSSMLGMLE
     EVGPCLVNEY GNGTKYNPWG WSKKSSMLFV DQPVGVGFSY GDEGHDIPND SYLAAVDMHR
     FLQLFISEVF PNKLNSPFHI SGESYGGHYI PYLGAQIVRQ NKLYPNEPQV QLKSCLIGNG
     CMSHMHTTFG YWETLCTTNP GVEKPIFNET RCDIMAKNMP RCMKVAEVCR RNPDPAICLS
     AQSVCDEGIT GLYNKESDVK GGRNRFDITT PCQADDICYV QGLHLQNYLN TKLVWDALSP
     PKEVKEYKFA SKNVEHAFGL TSDSMVPSTE EVEFLLSNQI HIMSYQGNLD LACNTAGNLK
     WMHDIPWKGQ AELSSKALVP WKSVLASTGK NETVGRMKEV KIRVTDSATF ATRYAFVTVD
     NAGHMVPQDR PDVAFDLMNR WISGETFV