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Database: UniProt
Entry: A0A0V1L2W8_9BILA
LinkDB: A0A0V1L2W8_9BILA
Original site: A0A0V1L2W8_9BILA 
ID   A0A0V1L2W8_9BILA        Unreviewed;       647 AA.
AC   A0A0V1L2W8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Carboxypeptidase A2 {ECO:0000313|EMBL:KRZ53602.1};
GN   Name=Cpa2 {ECO:0000313|EMBL:KRZ53602.1};
GN   ORFNames=T02_15475 {ECO:0000313|EMBL:KRZ53602.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ53602.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ53602.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ53602.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular metalloprotease that contributes to
CC       pathogenicity. {ECO:0000256|ARBA:ARBA00003091}.
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:KRZ53602.1}.
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DR   EMBL; JYDW01000160; KRZ53602.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1L2W8; -.
DR   STRING; 6335.A0A0V1L2W8; -.
DR   Proteomes; UP000054721; 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; 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.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:KRZ53602.1};
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:UP000054721};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          177..467
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   647 AA;  74515 MW;  A7642B94F07D0C46 CRC64;
     MVYISTNVLV KKQSFTIVEQ MMHEKHSFLF DKQYISHSFR KAELNIMMLL VRTIFAIGLL
     RIGSGYSNNA LEIYQGHILL EAVPRTEQQL ITLQQLIHYN NSEIDVWTLS PSIWKKSLIL
     VAPQHHYDIY KRMLDDGIKV KIAIDHLKSM FATHANIIER RIHKCNFSSN DFDISEYHTY
     DEIAEYMKMI SSQHPNWTEL ISVGYSYEGR ELLAIKIGTA SSSFWIDAGI HSREWISVSS
     AVFIIGQLHK QYNLDINLRR LLSETVSWII LPVFNPDGYE FTWNKDRLWR KSRSKYKIPL
     FKSCIGVDLN RNFDMDFGGW LRKRSGSSSN PCSNVYHGKY SFSEPETRAV MRYLSKMQDK
     IKACISLHSF GQLWLMPYGN KKGHYPTNYR EMVKLANGAV KELRTVHRSI YKVLKASDLY
     LSTGVAADWI LNATSIKYAF TVELRPETPE KGGFVLPEKE IVPTGEEISL PCLALKTCSR
     TEACRIVEYH KLIIENGNME AVDENISGAG GSLQKETNSS IQELRDEASF TIASEQLCAC
     PSTDSPCAFD NETDNSENVI QINSGTMLIL CQSKERLPSC RDFRRPVVRL FKDLEVSSDL
     QGTFNRRYTK ARIWCRCTRG EFKKSKLTEI WMYGMQHADT FTCNRLF
//
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