ID   PEPS_ASPPH              Reviewed;         523 AA.
AC   P52719;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Carboxypeptidase cpdS {ECO:0000303|PubMed:7772020};
DE            EC=3.4.16.- {ECO:0000269|PubMed:7772020};
DE   Flags: Precursor;
GN   Name=cpdS {ECO:0000303|PubMed:7772020};
OS   Aspergillus phoenicis (Aspergillus saitoi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND
RP   MUTAGENESIS OF SER-205; ASP-409 AND HIS-488.
RX   PubMed=7772020; DOI=10.1042/bj3080405;
RA   Chiba Y., Midorikawa T., Ichishima E.;
RT   "Cloning and expression of the carboxypeptidase gene from Aspergillus
RT   saitoi and determination of the catalytic residues by site-directed
RT   mutagenesis.";
RL   Biochem. J. 308:405-409(1995).
CC   -!- FUNCTION: Removes acidic, neutral and basic amino acids as well as
CC       proline from the C-terminal position at pH 2-5.
CC       {ECO:0000269|PubMed:7772020}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; D25288; BAA04974.1; -; mRNA.
DR   PIR; S55328; S55328.
DR   AlphaFoldDB; P52719; -.
DR   SMR; P52719; -.
DR   ESTHER; aspsa-peps; Carboxypeptidase_S10.
DR   MEROPS; S10.014; -.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
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   1: Evidence at protein level;
KW   Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..52
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000004299"
FT   CHAIN           53..523
FT                   /note="Carboxypeptidase cpdS"
FT                   /id="PRO_0000004300"
FT   ACT_SITE        205
FT                   /evidence="ECO:0000269|PubMed:7772020"
FT   ACT_SITE        409
FT                   /evidence="ECO:0000269|PubMed:7772020"
FT   ACT_SITE        488
FT                   /evidence="ECO:0000269|PubMed:7772020"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        399
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        415
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         205
FT                   /note="S->A: Impairs catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:7772020"
FT   MUTAGEN         409
FT                   /note="D->A: Impairs catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:7772020"
FT   MUTAGEN         488
FT                   /note="H->A: Impairs catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:7772020"
SQ   SEQUENCE   523 AA;  58117 MW;  9281F29689304288 CRC64;
     MRITSAIASL LLVGTATSLQ NPHRRAVPPP LTHRSVASRA VPVERRSNDF EYLTNKTARF
     LVNGTSIPEV DFDVGESYAG LLPNTPTGNS SLFFWFFPSQ NPDASDEITI WLNGGPGCSS
     LDGLLQENGP FLWQPGTYKP VPNPYSWTNL TNVVYIDQPA GTGFSPGPST VNDEEDVAAQ
     FNSWFKHFVD TFDLHGRKVY ITGESYAGMY VPYIADAMLN EEDTTYFNLK GIQINDPSIN
     SDSVMMYSPA VRHLNHYNNI FRLNSTFLSY INGKADKCGY NAFLDKAITY PPPTPFPTAP
     EITEDCQVWD EVVMAAYDIN PCFNYYHLID FCPYLWDVLG FPSLGFGPDN YFNRSDVQKI
     LHVPPTDYSV CSETVIFANG DGSDPSSWGP LPSVIERTNN TIIGHGWLDY LLFLNGSLAT
     IQNMTWNGKQ GFQSPPVEPL FVPYHYGLAE LYWGDEPDPY NLDAGAGYLG TAHTERGLTF
     SSVYLSGHEI PQYVPGALTA SWSSCLVELI VFPRRGTTPL NFS