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Database: UniProt
Entry: R7TBR3_CAPTE
LinkDB: R7TBR3_CAPTE
Original site: R7TBR3_CAPTE 
ID   R7TBR3_CAPTE            Unreviewed;       421 AA.
AC   R7TBR3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00132};
GN   ORFNames=CAPTEDRAFT_215633 {ECO:0000313|EMBL:ELT88927.1};
OS   Capitella teleta (Polychaete worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Sedentaria; Scolecida; Capitellidae; Capitella.
OX   NCBI_TaxID=283909 {ECO:0000313|EMBL:ELT88927.1};
RN   [1] {ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ELT88927.1, ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELT88927.1,
RC   ECO:0000313|Proteomes:UP000014760};
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:CapteP215633}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) 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   EMBL; AMQN01015107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB311612; ELT88927.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7TBR3; -.
DR   EnsemblMetazoa; CapteT215633; CapteP215633; CapteG215633.
DR   HOGENOM; CLU_019326_0_0_1; -.
DR   OMA; SHGISYE; -.
DR   Proteomes; UP000014760; 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; CARBOXYPEPTIDASE A1 (PANCREATIC)-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.
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: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:UP000014760};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..421
FT                   /note="Peptidase M14 carboxypeptidase A domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008786846"
FT   DOMAIN          171..193
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
SQ   SEQUENCE   421 AA;  48227 MW;  85A2E7B3AA11758E CRC64;
     MAWWRSIWLC NLSFLLAVAA TGVDYNGYRV YRLEPKTRLQ VDQVIALETE FDFWKECRSI
     GQPCDVIVSG EQNNDLLQYL QDREVPHSIM IGDVGQLILE QEIERAARIS SKHRDLDFDY
     GVYHTLADIE QWMVDIEDAY PDLLESFHVA TSYEGREIRA FKISTGTTEK PKIWLDGGIH
     SREWVAIANM LYMTNEIVSQ YGVDPEVTAI LDEVDIYLLP VFNVDGYEYT WTADRFWRKT
     RSINDDFPSC VGCDPNRNFD VNWGMNGTSS NPCSDLYPGP SPFSEIEVRM VADYIAGLFD
     VRALIAYHSY GQMYMTPYGF TYEYPPDFED QMEACNKGNE ALYAVHGMEY TCDTLINLVG
     PNSGSSADYT YTALKIKYSF GAELRDKGQF GFVLPDNQII PTGEENWAFF KAFARHVIDD
     V
//
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