ID   A0A1I7UEX8_9PELO        Unreviewed;      1068 AA.
AC   A0A1I7UEX8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Peptidase_M14 domain-containing protein {ECO:0000313|WBParaSite:Csp11.Scaffold629.g8630.t1};
OS   Caenorhabditis tropicalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold629.g8630.t1};
RN   [1] {ECO:0000313|WBParaSite:Csp11.Scaffold629.g8630.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) 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   AlphaFoldDB; A0A1I7UEX8; -.
DR   STRING; 1561998.A0A1I7UEX8; -.
DR   WBParaSite; Csp11.Scaffold629.g8630.t1; Csp11.Scaffold629.g8630.t1; Csp11.Scaffold629.g8630.
DR   eggNOG; KOG2650; Eukaryota.
DR   eggNOG; KOG3714; Eukaryota.
DR   Proteomes; UP000095282; Unplaced.
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; 2.
DR   Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
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; 2.
DR   Pfam; PF02244; Propep_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 2.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 2.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
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, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..1068
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009308837"
FT   DOMAIN          969..979
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
FT   REGION          64..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1068 AA;  119776 MW;  7F0E5BA8324FB685 CRC64;
     MKTSLVLILL VGIANAQDFL SMFKPFLGGG GGGGNPFANP QAIGGLFQQF AGGNGGGFGQ
     FLGAMAPKPP PAPASRGPAP VAPTNEDYNT DLDPVPAPPK PKAKARAAHH RPQADAPHTW
     LDAPQSFRQP RTKAEKIERW KNIARTFSPF LFTDDSQNTT PAPQFNNYIW QQNAPVTPEP
     FTFAPFSIPT LATVSPAGPT LEPFLPTTAS PKLLAHNTAR MIREIATFSD GGKSRDQDFG
     AVQTLMQAFF EAVSTGNNGA VATGPAVGTP LGDAPVLQAR RDGTELGANR ALTNKLFESD
     MVLTVPQMKA VYFVCAPGNA RSALILFGYQ ARRRSVKPIK PENPLPRPQK RSIREVKEVK
     VGDEIIGGDS RTKKIFWIDG GIHAREWAAP HTALFFIHQL TSRANEPGIK KLLDEITFVV
     VPCLNPDGYE FTRSSTNPHV RLWRKNRSKM QCRKDIWGRN RCCRGVDLNR NFDFHFRESG
     TSDDPCSEIY QGPAPFSEPE AKAVRDALLS QRYHGRTDAF ITLHTYSQIW IHPYGHKKDA
     YPGDIKDLYE VGKKAAQALK RVYGTKYVVG SGADTLYPAS GGSEDWAKHE AKVKFVYLLE
     LRPDEKNWDG FILDEKELIP TARETWEGVR VVAEAVLDRI GLLEETTLPH ETMRLLYLVG
     LVLGVQAIHN TDENSGFHNF KLIRINPETE ESVKYLRSLY EDPSPYELDF WQPPTHIGAI
     VDLTVAPSDA PKFVMDLESK RINYIVAVND LSKAIENERG SDKFYNPVAG FAYDKYNSLQ
     EIHSEMKRLK KEYSSMITLI DIGQSHENRT LLVMKITGKR NPLGSKISMW IDGGIHAREW
     ISPATAMYIA HELILGYEND ATVAKLMDHI DFYILPVMNP DGYEYSREKN RMWRKNRSPA
     KCHRHTFSTV CCSGVDLNRN FDWFWASTGS SSDPCHDTYH GSSAFSEPES QAVRDFLEQN
     TPEAFISLHS YSQMWLIPYG HRKQSYPQDY HTGLRPLALR ATKALYELYG TKYQVGTGAD
     LMYMSFHSDR NVHRWTCTMV HVQCDFSVLF PRPLLLLLHY SSSILRID
//