ID   SCPF_ARTBC              Reviewed;         486 AA.
AC   D4ASE6;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 2.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Carboxypeptidase Y homolog ARB_07161 {ECO:0000305};
DE            EC=3.4.16.5 {ECO:0000250|UniProtKB:P00729};
DE   AltName: Full=Serine carboxypeptidase ARB_07161 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_07161;
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=EFE34210.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000007; EFE34210.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003014599.1; XM_003014553.1.
DR   AlphaFoldDB; D4ASE6; -.
DR   SMR; D4ASE6; -.
DR   STRING; 663331.D4ASE6; -.
DR   MEROPS; S10.001; -.
DR   EnsemblFungi; EFE34210; EFE34210; ARB_07161.
DR   GeneID; 9520651; -.
DR   KEGG; abe:ARB_07161; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_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; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 2.
DR   Pfam; PF00450; Peptidase_S10; 2.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..486
FT                   /note="Carboxypeptidase Y homolog ARB_07161"
FT                   /id="PRO_0000435281"
FT   ACT_SITE        241
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        403
FT                   /evidence="ECO:0000250|UniProtKB:P08819"
FT   ACT_SITE        462
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
FT   BINDING         406
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        430
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        281..305
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
FT   DISULFID        288..298
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
FT   DISULFID        327..334
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
SQ   SEQUENCE   486 AA;  54906 MW;  09BA0A1C705CC376 CRC64;
     MKGLLSLLLV GAANALAASY EPRSLTEDML QGKEKEVWDA IKGEIPGAQL DDYFNPPTAH
     QREPDEKWDG KLEGKSVNTL WVEEGKDKPS GIEEYGMRFK TVDPSSLGVD NVTQYSGYLD
     NKKNGQHLFF WFFESRRDPQ YDPVILWLNG GPGCSSMTSL FMELGPARVG QDLKLTRNPN
     SWNNRASIIF LDQPVNVGFS YGKSGAFNTP SASKDVFAFL TLFFKKFPQY ALQDFHIAGE
     SYAGHYIPFA SYPPMACGKG GYSAVLDQPT CKAMEAAVPQ CQKEIKRCYD KPTDVATCVK
     GAKFCKDALV RPYSRTGQSI YDIRGRCEDP KDLCYPILGW IAKYLNQRHV QKAIGAEVSH
     FKGCSNHISS QFFAHGDYNQ PFHRKIPGIL KDVNVLVYAG DADYICNWLG VKEWTEALQW
     PGRHIFRRKN LSVVYHSVNK WPLGRVKYHN GLAFLQVFKA GHRVPYDQPE NALDFFNRWL
     AGEWTP