ID   SCPE_ARTBC              Reviewed;         506 AA.
AC   D4AZG9;
DT   20-JAN-2016, 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_06361 {ECO:0000305};
DE            EC=3.4.16.5 {ECO:0000250|UniProtKB:P00729};
DE   AltName: Full=Serine carboxypeptidase ARB_01587 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_01587;
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}.
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DR   EMBL; ABSU01000021; EFE31439.1; -; Genomic_DNA.
DR   RefSeq; XP_003012079.1; XM_003012033.1.
DR   AlphaFoldDB; D4AZG9; -.
DR   SMR; D4AZG9; -.
DR   EnsemblFungi; EFE31439; EFE31439; ARB_01587.
DR   GeneID; 9519566; -.
DR   KEGG; abe:ARB_01587; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_12_2_1; -.
DR   OMA; DDNLIIW; -.
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   3: Inferred from homology;
KW   Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..506
FT                   /note="Carboxypeptidase Y homolog ARB_06361"
FT                   /id="PRO_5003054560"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000250|UniProtKB:P08819"
FT   ACT_SITE        485
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   506 AA;  56016 MW;  F6583401D94CA2ED CRC64;
     MHVAILLAII SLARAAPSTK GYTVATSLPG KSAFETRRLP DAPEILKNWA GRLDIPGTTI
     GNSLFFWLFS AEDKAYDDNL IIWLNGGPGC SSLVGAFLEN GPLRFMGNST MPERNPYSWA
     KLGHVLYIDQ PVGTGFASEK VPVTSNKEVI SNLYSWLMSF DAIFDHILRT KKVHIVGESY
     AGIYIPYIAS EIVKRKSELP VNLVSIAIGD GTIGPNTGMS SLGMVGFLEE YASKLRIPRD
     IMNAISFGDH ACGFDIIRQR AKVYPPRGPF HLPGRSGSAN NTEISNMLQK GVADESLGSC
     NIHPDTPEKI RSSIVNSTCY GHCAVFETTA DYMSSQQCFS IYNINYGCNF TNPTSTLEAY
     FSRSDVQIAL NLMHPTDPLR PFQSCNPKIL ETLMAPANRP VPPSFEILPD LLTTHKLPVH
     IYQGRLDMLI NHVGIEVTIQ NMTWNGAQGF QDSLHFEFGR QKDKAVGLWN EERGLSYHLF
     FEGGHFLPAD LPMEVLSYVK EVVLRQ