ID   A0A1I8P6M7_STOCA        Unreviewed;       507 AA.
AC   A0A1I8P6M7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00132};
GN   Name=106085896 {ECO:0000313|EnsemblMetazoa:SCAU005301-PB};
OS   Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Stomoxys.
OX   NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU005301-PB, ECO:0000313|Proteomes:UP000095300};
RN   [1] {ECO:0000313|EnsemblMetazoa:SCAU005301-PB}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU005301-PB};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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   RefSeq; XP_013105807.1; XM_013250353.1.
DR   AlphaFoldDB; A0A1I8P6M7; -.
DR   EnsemblMetazoa; SCAU005301-RB; SCAU005301-PB; SCAU005301.
DR   GeneID; 106085896; -.
DR   VEuPathDB; VectorBase:SCAU005301; -.
DR   OrthoDB; 3540647at2759; -.
DR   Proteomes; UP000095300; 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:SF149; FI01817P-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   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};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          263..285
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
SQ   SEQUENCE   507 AA;  57212 MW;  A492F7C778F57AC8 CRC64;
     MTSNTRWNVV ALVVVLATVI ALIMPSHFAT AFDVSRMTPV ADRNIRTGNK MLIEKEIIEE
     RQVVSENDSN STQAEVALDE DMSFLDEDDG DSDDGVLDVN EIPVRYDEAQ LWRVYNISNA
     MSRRNMLPLG DILESKYGGT IWKENSKFLD VSIDKKHVKA ARAFLEDHNL NTEVLNYNIQ
     EMIDNEAAVG ANLTQSEAGQ RTKKAARSGI HWKDYHDLDT IYAFMREIRG KFPNICRLYT
     IGKTAEGRDL KVLSISENLT ANKKIWIDGG IHAREWVSPA TVTYIINQLL TNWEKQPSYI
     RNKSWYIMPV MNPDGYMYSR RSNRLWRKNR KPHKTSSCVG VDLNRNFNIG WGTVGSSKNP
     CHETYHGTSA NSELETQAVV NYIKSIKANL EAYLTYHSYS QALVYPYGYK SAKSKYATAL
     QRVGKEAARL IKNKTGKTYD VGVTYKVLSL AAGGSDDWSC SVMGIKYVYT IELRDRGQYG
     FILPPAQIEG TASEGLILAQ QVAKDIS
//