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
//