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Database: UniProt
Entry: A0A182FDU5_ANOAL
LinkDB: A0A182FDU5_ANOAL
Original site: A0A182FDU5_ANOAL 
ID   A0A182FDU5_ANOAL        Unreviewed;      1300 AA.
AC   A0A182FDU5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|SMART:SM00631};
OS   Anopheles albimanus (New world malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7167 {ECO:0000313|EnsemblMetazoa:AALB004686-PA, ECO:0000313|Proteomes:UP000069272};
RN   [1] {ECO:0000313|EnsemblMetazoa:AALB004686-PA}
RP   IDENTIFICATION.
RC   STRAIN=STECLA/ALBI9_A {ECO:0000313|EnsemblMetazoa:AALB004686-PA};
RG   EnsemblMetazoa;
RL   Submitted (AUG-2022) 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   STRING; 7167.A0A182FDU5; -.
DR   EnsemblMetazoa; AALB004686-RA; AALB004686-PA; AALB004686.
DR   VEuPathDB; VectorBase:AALB004686; -.
DR   VEuPathDB; VectorBase:AALB20_028582; -.
DR   VEuPathDB; VectorBase:AALB20_030240; -.
DR   Proteomes; UP000069272; Chromosome 3L.
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; 3.
DR   Gene3D; 3.40.630.10; Zn peptidases; 3.
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; 3.
DR   Pfam; PF02244; Propep_M14; 3.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 3.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 3.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 3.
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          125..404
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
FT   DOMAIN          531..809
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
FT   DOMAIN          1005..1282
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   1300 AA;  146943 MW;  BAB74E9FBAB70C4F CRC64;
     MKYCGVAFVL LAALAMLSQG STAEQVSYRN YKVYDIQVDT IEKHTVLKRW EEVKGVDFWD
     RAGKRVMIAP MLQDTFERFL TLNGFTFVRS IEDVEATIEA ERQYDQEYRR RKAASGRATV
     DFEHFWTIDE VETYLESLAR EYPSLVKVET IGTSHLGRRI KSITISTNNG VAGTKPVVFI
     DGGIHAREWA GVMSVLYLIH ELVEHSSDYA DMLAKDWIII PVANPDGYEF SHTSNRMWRK
     NRFPATVLCT GVDLNRNWDY MWVFTSNACS DSYAGATAFS ELETQALNRV MLRYQSDIVL
     YLAVHTYGDM ILYPYGHSWP FVPVTNQAAH IALAEQAREA VTAVGGPRYI VGNSAEILYT
     ANGCSDDYAV GVIGTRYGYT LELTGGGSNG FDLPASQIQA VATQTFQIYL MMKLLPVLLL
     LGVACLAHAQ FYENYKLYEL LVKDSDHVDE LNFWYDQGTL DFWSHAAPNR SVTVMISPRV
     RRRFEQMLQE EDIAFKVMME NVQEMLDAEQ AWRKEQERLR PTNGAIDFNH FWTLDEINSY
     LEKLSLAYPK LVTLVEIGRT SLNRPINAVT ISTKGRISQK RPVVLIDAGL QAREWASHMA
     VMHLIHQLVV NSEANKEMLK NTDWVIVPVA NPDGYAYSHE MNRLWRKNRS AGKTICPGAD
     LSHNFPFRWH YTSNSCTEGY SGSAPASESE TRALMLMMAQ YARSLKVYLT VHACGEYILY
     PYGYDKVQAP NAAVLQMLGE QAARAARDVR GTVYQVGSAG SLLTPQTGSA DFVYGSYGAE
     FTYTLELPCG RGGSAFLLET DRLPQVLAEA FEMFKVYGKF AGSTTVGRPY DASKVKDVKV
     KDTKAVADTV DSSSSSAAEE SQENDDDDEK RTRTVVAMKS LAAVCCWFLV TLAFAKAGSY
     HGFELYTVRP ETQEQLMELL RWPVPMAEVD FWDAPKLNRD TRMMVARTDR KAVVTFLERH
     DIDYELVVED VQELLTKEER RNAEHLRRRV RRDSNSRATI DFEHFWTLEE IYDYLDELAT
     AYTGLVRVTE VGTTHEGRPI KAITISTNGE IDQRRPIVFI DGGIHAREWA GVMSVMYMIH
     EFVEHSEEYA AQLTNTDYVI IPVLNPDGYV YTHDQNRLWR KNRSQVNVLC YGVDLNRNFP
     YQWDWTSSEC TNNFAGTAQA SEKETQTMMA LMDQYKSAIR VYLAVHTYGE LILWPWGYDF
     IRSDNEIELQ RLGEQARDAL VAAGGPTYEV GNSAEILYTA SGATDDYAHS LGVPYAYTLE
     LTGGGLEGFD LPASELAKVA ADTFELFKVF GQHAGTLTVP
//
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