ID   A0A319A8A9_ASPLB        Unreviewed;      1120 AA.
AC   A0A319A8A9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE            EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN   ORFNames=BO96DRAFT_434963 {ECO:0000313|EMBL:PYH55565.1};
OS   Aspergillus lacticoffeatus (strain CBS 101883).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH55565.1, ECO:0000313|Proteomes:UP000247441};
RN   [1] {ECO:0000313|EMBL:PYH55565.1, ECO:0000313|Proteomes:UP000247441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH55565.1,
RC   ECO:0000313|Proteomes:UP000247441};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR   EMBL; KZ821353; PYH55565.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319A8A9; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000247441; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.410; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR11802:SF432; Y, PUTATIVE-RELATED; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000256|RuleBase:RU361156};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361156};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361156};
KW   Signal {ECO:0000256|RuleBase:RU361156}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT   CHAIN           21..1120
FT                   /note="Carboxypeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT                   /id="PRO_5036517560"
FT   DOMAIN          198..356
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
SQ   SEQUENCE   1120 AA;  121817 MW;  A7C6F676C701967D CRC64;
     MVRATQLAVA ALGLLGAAAA QLVSTGMSVT LDQIDYFVSP YPAGNVTVSA ASLTDIPSVN
     GFYPVTVVQE ETAGVSSLSS LFSTWTDVDD VFTPAFLGAV LVRGYKPDNV TATFFNSSRS
     SVLSPLESRV VPSGPYFLEQ ATGNLYPVYR LYSDYAGAFT QPLLQKPDGT FQPLSAQVAG
     LVSSTIGVPS RIYYTPSDEK PLAGARVGVK DIYSLAGVRQ SNGNRAWYNL YGENNVTGTA
     VSRLIDAGAI IVGLQKPSQF ANGETATADW VDLHSPFNPR GDGYQDPSSS SSGAGASIGS
     YEWLDLALGS DTGGSIRNPA EVQGVYGSRP SHGLVELDHV MSMSPVLDTA GVLTRDPYLW
     DRANQALYST NYTSFHGKSV RYPSKLYTID FPTTNDSAAD ALLAGFQKRL AAFLNTTTTP
     LDLSDDWSSH PPSSAPANVS LETLLNLTYP MLITKQQIPL VRDPFYADYA AKHDGRVPFV
     DPVPLSRWNW SMAYPDSALD EAIHNKTLFM DWIAENYLTP ISDPEQCSSS LIVYVGTDGS
     QRARNVYRSL PGAPSGYSKF LISNMASVPD FVIPVGEIEA YSTITQHQEK FPVAIDVLAA
     KGCDGLLVRL AQDLFEAGII NAPLAGGTLT GGPSAALFGL AYASTQAVLQ PEEPSDFRTF
     HSPYSPHHSI RIRQQNESIC AAHSAQYTGW LDIGRKHLFF WYFESQNDPA NDPLTLWMTG
     GPGGSSMIGL FEEVGPCLIN EYGNGTYYNP WGWSRNSSLL FVDQPVDVGF SYVDEGEDLP
     GDSHQAAIDM HRFLQLFVSE VFPQLQTLPV HLSGESYAGH YVPYLGSQIV QQNKLYPTEP
     QVLLHSCLVG NGYYSPRDTT YGYWETLCTT NPGVPEPVFN RTRCDIMAAN MPRCMEVSDV
     CVRNPDPAIC HAASEVCYEG VIGWYDDESG EGGRNRFDIT APCALDGICY IEAARIEQYL
     NTPAVWAALS PPKEIKEYKV TSDNVSRAFD LTSDTMTPAS EQVAFLLANQ VHFLAYQGNL
     DLACNTAGNL RWAHSLPWRG QVEFASKALR PWSWVDVVSG KGGVAGTTKE VRVKVSESTD
     KESRFALVTV DGAGHFLPQD RPDIALDMMV RWISGASFTE
//