ID A0A2G5TMS4_9PELO Unreviewed; 447 AA.
AC A0A2G5TMS4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00132};
GN Name=Cni-F02D8.4 {ECO:0000313|EMBL:PIC28562.1};
GN Synonyms=Cnig_chr_V.g20432 {ECO:0000313|EMBL:PIC28562.1};
GN ORFNames=B9Z55_020432 {ECO:0000313|EMBL:PIC28562.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC28562.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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:PIC28562.1}.
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DR EMBL; PDUG01000005; PIC28562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5TMS4; -.
DR STRING; 1611254.A0A2G5TMS4; -.
DR Proteomes; UP000230233; Chromosome v.
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:InterPro.
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; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF146; PEPTIDASE_M14 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_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:ARBA00022645};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022645};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..447
FT /note="Peptidase M14 carboxypeptidase A domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013653733"
FT DOMAIN 167..189
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
SQ SEQUENCE 447 AA; 50671 MW; C1C7AD136BED40C8 CRC64;
MLLQLLSLSV VFIGGISAEY KNYDGFKILE VNFQNPRVRK YIQEIDKNLG FMPDFLGENW
KQKQAHYFID KDSVEKVKTN LASNNITYQL RDVNPQIFKV RRRRDINGAV TINDVNNKYL
SYDEQMQFLS SIAQQYPNDV KLQKIGNSYE GRSLTAVRIG DDGSSKPIVW IDAGVHAREW
ISYNVALYLV YTIVSQPAYR DLLNAVQLVV VPNTNPDGYE YSRTNDRMWR KTRSRFSNGR
CSGADANRNY PFFWGTQGVS HSQCSEIYCG SRPQSEPEVM ALTNAIQREE TRIKGYIALH
SYGQEILYPW GHTMRTYPSD VQDLIQVGKA MAAAIRAVNN TDYNVVNSGD GLYPAAGASD
DWAKSRGIKY SYTIELSPID DYTGFSLPED RINQVCREAF QAIQVLMIEV RSKFAIRQTT
SSASSTSAQS SLLLKRMRTA VRGSGRG
//
