ID   A0A0V1HSR7_9BILA        Unreviewed;       755 AA.
AC   A0A0V1HSR7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Carboxypeptidase B {ECO:0000313|EMBL:KRZ13344.1};
GN   ORFNames=T11_7862 {ECO:0000313|EMBL:KRZ13344.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ13344.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ13344.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ13344.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ13344.1}.
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DR   EMBL; JYDP01000033; KRZ13344.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1HSR7; -.
DR   Proteomes; UP000055024; 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; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR029033; His_PPase_superfam.
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; SSF53254; Phosphoglycerate mutase-like; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:KRZ13344.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          165..187
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
FT   DOMAIN          312..322
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
SQ   SEQUENCE   755 AA;  86372 MW;  0B69BB0AB8BE308E CRC64;
     MCLLAQSKQG RSGSAATHAQ SVYKVMRTVP TNESQLKFLQ IMYQHADGDQ IDFWRPPAFL
     NSTVDIMVND ISMDKFLFQC KEHNISLNIS IPDVEKSKGR VRRFNYLTTP YFDISVYHSY
     NEIQNYMRNL EKQYPHIAKV HTIGYTHENR EINLLQIGRF YSSQPAIWID AGIHAREWIA
     PSTALYIINY LVTRYDYDME VQKYVNGLTW YILPVVNPDG YEFSRSSLNP RVRLWRKNRS
     PANCQPFKNS FCCRGVDLNR NFDFKWNQQG GSQDPCQETY SGRSAFSEPE TQAIERFILQ
     RANQLGAFLT LHSYSQIWMY PYGNQRYSYP KDVHDLREVA LAACQSLYNV YGTRYHPASG
     GSEDWAKAVA GIKYSFLVEL RPEEDNQDGF ILDESHIIPT GKETLEGIKQ VAMVLLPGNH
     NSYFPNTDAS SVCQDFHPMC KIWAVFGACL NDTEVRRLCV KSCELCSELN NQVEKLFLAI
     GAAESAKDIY KNTDWLPGIE EKKGTFGSIS RLMSKVKNES IRVHENSVCQ IGNANLPQTL
     KWRRGEKSAW LADPPLTIVG CNTAKLYAEG LVSANLLNPE LLGSCVYAAP NFRCVQTADI
     ILKVVDPSGR IKIRIEPGLE ADPQPMDKNI CWYIKADQFT AHKIHRVDAA YKPKRQIKDF
     PQRNEILDEI QENHVGNIAL LIVSDWKINE LCNAICNCKI SSENNTVRNN ETVSLLRAFS
     FKLQDNEWKL LNSSVPPFTY TANSQLPWNA WHILE
//