ID   A0A3B0JWT3_DROGU        Unreviewed;       424 AA.
AC   A0A3B0JWT3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Blast:Carboxypeptidase B {ECO:0000313|EMBL:SPP77181.1};
GN   ORFNames=DGUA_6G007824 {ECO:0000313|EMBL:SPP77181.1};
OS   Drosophila guanche (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP77181.1, ECO:0000313|Proteomes:UP000268350};
RN   [1] {ECO:0000313|Proteomes:UP000268350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   EMBL; OUUW01000002; SPP77181.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0JWT3; -.
DR   STRING; 7266.A0A3B0JWT3; -.
DR   OMA; SDDYAFY; -.
DR   OrthoDB; 3540647at2759; -.
DR   Proteomes; UP000268350; Unassembled WGS sequence.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03860; M14_CP_A-B_like; 1.
DR   Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036990; M14A-like_propep.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   Pfam; PF02244; Propep_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:SPP77181.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..424
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017290682"
FT   DOMAIN          174..196
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
SQ   SEQUENCE   424 AA;  47689 MW;  B9DCED7A28AF3710 CRC64;
     MTKFLGLLVL LLVAALVAAD QDYEGYRIYE VTPENALQAQ LLHQLSLQGF DFLSESRLLG
     RPSRLIVSPA QLAQFEELLQ GQQLAHSLLN DNLGASIAEE FALRQLQRRL SPITGKGRLS
     TERYYTHEEI INYIDDLAER YPRRVFVRTV GWSYEKRVLK TITISNGDGR AGKKVIFMDG
     GFHAREWISP AAVLYVIDQL VEQFEQNADL LQDYDWVILP LVNADGYEHS QSGTLARMWR
     KTRQPYTYAG QTCYGADPNR NFGFHWNEEG ASSNPCADTY AGPTPFSEPE TIVVRDLMHT
     LADRGVMYLT IHSYGNYILY PWGWTSDLPD TWEDLDAVAR TGAEAIENAT GTVYTYGSST
     NVLYIAAGAS DDYGFYVGFN VSITMELTGA GSIGFNPPVT RIDEFVTETW IGIRAMAEKL
     IEIY
//