ID   SCPC_ARTBC              Reviewed;         629 AA.
AC   D4AQ54;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 44.
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_06361 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_06361;
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; ABSU01000005; EFE34598.1; -; Genomic_DNA.
DR   RefSeq; XP_003015238.1; XM_003015192.1.
DR   AlphaFoldDB; D4AQ54; -.
DR   SMR; D4AQ54; -.
DR   MEROPS; S10.016; -.
DR   EnsemblFungi; EFE34598; EFE34598; ARB_06361.
DR   GeneID; 9520962; -.
DR   KEGG; abe:ARB_06361; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_3_1; -.
DR   OMA; NFPPNSM; -.
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   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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..629
FT                   /note="Carboxypeptidase Y homolog ARB_06361"
FT                   /id="PRO_5003053399"
FT   ACT_SITE        235
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
FT   ACT_SITE        453
FT                   /evidence="ECO:0000250|UniProtKB:P08819"
FT   BINDING         456
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        405
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        463
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        554
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        326..355
FT                   /evidence="ECO:0000250|UniProtKB:P00729"
SQ   SEQUENCE   629 AA;  69708 MW;  A82AD3E78D24EF51 CRC64;
     MLITWLLDVL LLAPPVAAGY PPKPKNLITI ESKALPGATI TYKEVPKGVC GNVRSYSGYI
     NFPPNSMREA PQDFPVHIYF WYFESQVKPE TDPLAIYING GPGAGSMVGV FVESGPCRMS
     EDAQSTVLNE HSWNKEANLL YIDQPVQTGF SYDVLTNATF DFKTNILSPE GPDHDPSKDG
     TLLAGTFGSG DPSKTANTTL NAARHMWNIV QVWSQDFSPY ADNRENDKIS LWSESYGGRY
     APGFMAYFLQ QNNRIKAGLL TGSVLHLDTV GIINGCVDLI SQQKSNIDFP YNKNTYGIQA
     IDDAGYDKAM HAYGKRGGCL DQILECHALA KRYDPNAYGH VDEVNYVCER ANSYCNTEVD
     GIYVDGAKRG LFDIAQCHLD PFPSNSFLGY LAKTEVQEAL GVPANHTDPS YTVEHVFNVT
     GDYVRSDRGG HLLDIANLLD ARVKVAMVYG DRDFICNWVG AENVSLSVDY KDAKNFRRAG
     YADVYTDDSG VPKAQVRQHG LFSFTRVYQA GHMMLAYQPQ VGYEIFRRAM FNMDIATGTV
     TDDIEFYSTQ GEVNSTHAEP PLPTVPPTCN FWGMAMSCAK NQIEAIQKGE ASIVNNIIVS
     PTQARGECPT PQPTRKSWFY NNEQQSFII