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Database: UniProt
Entry: G0MM29_CAEBE
LinkDB: G0MM29_CAEBE
Original site: G0MM29_CAEBE 
ID   G0MM29_CAEBE            Unreviewed;      1098 AA.
AC   G0MM29;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00133};
GN   ORFNames=CAEBREN_00188 {ECO:0000313|EMBL:EGT36562.1};
OS   Caenorhabditis brenneri (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN   [1] {ECO:0000313|Proteomes:UP000008068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG   Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA   Wilson R.K.;
RL   Submitted (JUL-2011) 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}.
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DR   EMBL; GL379801; EGT36562.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0MM29; -.
DR   STRING; 135651.G0MM29; -.
DR   MEROPS; M14.A22; -.
DR   EnsemblMetazoa; CBN00188.1; CBN00188.1; WBGene00138913.
DR   eggNOG; KOG2650; Eukaryota.
DR   HOGENOM; CLU_283599_0_0_1; -.
DR   InParanoid; G0MM29; -.
DR   OMA; DPREINC; -.
DR   Proteomes; UP000008068; 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; 2.
DR   Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 2.
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; 2.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 2.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          774..784
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
FT   REGION          926..1013
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..1013
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1098 AA;  124871 MW;  33E939C1CD22A481 CRC64;
     MCFDLIELNF WKTGKDKHGF WDVMVEMKNE KFFLDYLQLN DISHMKTIED VERLITKHEN
     NQTLSKLFPR LWDDSSSAHY DFHTYGSYQR MTDWMKQLVQ KYPKMVQYIS IGKTTEGRNI
     DGVEIGGDSR TKKIFWIDGG IHAREWAAPH TALFFIHQLT SRANEPGIKK LLEEITFVVV
     PCLNPDGYEF TRSSTNPHVR LWRKNRSKMQ CRKDIWGRNR CCRGVDLNRN FDFHFRESGT
     SDDPCSEIYQ GPAPFSEPEA KAVRDALLSQ RYRGRTDAYI TLHTYSQIWI HPYGHKKDAY
     PGDIKDLYEV GKKAAQALKR VYGTKYVVGS GADTLYPASG GSEDWAKHEA KVKFVYLLEL
     RPDEKNWDGF ILDEKELIPT ARETWEGVRV VAEAVLDRIL AGRASTPRGG HPQREEEKGE
     KKRSLGVLTT LWSIFFCIRV CVCSSLVSDY CCTKMRYLLF LVLIFCDETV YGIHNTDENS
     AFHNFKLIRI NPETEGSVRY LRSLYEDPSP YELDFWQPPT HIGAIVDLTV APSDAPRFVK
     DLESKNINYI VAVNDLSKAI ENERGSDAFY NPVAGFAYDK YNSLDEIHSE MKRLKKEYPT
     MITLIDIGQS HENRTLLVMK ITGKRNPLGS KISMWIDGGI HAREWISPAT AMYIAHELIL
     GYENDATVAK LMDHIDFYIL PVMNPDGYEY SREKNRMWRK NRSPAKCHRQ TFSTVCCSGV
     DLNRNFDWFW ASTGSSSDPC HDTYHGSSAF SEPESQAVRD FLEQNTPEAF ISLHSYSQMW
     LIPYGHRKQS YPQDYHTGLR PLALRATKAL YELYGTKYQV GTGADLMYEA SGGSHDWAKG
     QLKVPYAYLI ELRPKNTMMG HGFLLPEREI VPTGLETSES IKVVADELVA QFVEPVIRAK
     MSTTSRPSIP PYRRGYSIID TTTTEPEDTV TEKRTTVVPS TVSTTTTVAP TTTTTVATTT
     TTEEPTTTTP TTTTTTTEAP TTTTETTTVP PTTTTTVTES TTTTTVSQET TTTISPEDAT
     ATVVLPTETY PPGTEEVSTI RPDEETEEIR VIEETSAPVK CLDYGDYCRL WGVLQLCYRD
     QVSKLCPKTC DSRCAFVN
//
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