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Database: UniProt
Entry: B3S4P4_TRIAD
LinkDB: B3S4P4_TRIAD
Original site: B3S4P4_TRIAD 
ID   B3S4P4_TRIAD            Unreviewed;       498 AA.
AC   B3S4P4;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIADDRAFT_28971 {ECO:0000313|EMBL:EDV22249.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV22249.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV22249.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV22249.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431}.
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DR   EMBL; DS985250; EDV22249.1; -; Genomic_DNA.
DR   RefSeq; XP_002115404.1; XM_002115368.1.
DR   AlphaFoldDB; B3S4P4; -.
DR   MEROPS; S10.002; -.
DR   EnsemblMetazoa; TriadT28971; TriadP28971; TriadG28971.
DR   GeneID; 6756617; -.
DR   KEGG; tad:TRIADDRAFT_28971; -.
DR   CTD; 6756617; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_13_3_1; -.
DR   InParanoid; B3S4P4; -.
DR   OMA; GYDPCTS; -.
DR   OrthoDB; 1647009at2759; -.
DR   PhylomeDB; B3S4P4; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR033124; Ser_caboxypep_his_AS.
DR   PANTHER; PTHR11802:SF201; CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..498
FT                   /note="Carboxypeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002798459"
FT   TRANSMEM        478..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   498 AA;  56768 MW;  823013E0EAC02618 CRC64;
     MADHPFNFKL VWLSIAFSLL ITHSIPAVQC SNIVYTKEAL ADEVLSVPNL HGNITFRHFS
     GYLNSVDGDM LHYWFFESTK NPTSDPLALW LNGGPGCSSL HGLIAEHGPF HVSDNLQVHL
     REYTWNRLAN MLYIESPAGV GFSYNKYTRY RLNDSATAET NLVALQEFFR RFPTFKKNDF
     YITGESFASV YLSTLAVQLM KDPSIKLKGI AIGNGILDYA MNFNSLVYFA YYHGYFSTQL
     YQNLIKACCV GDICKFYEST NTTCKTLYQK LFNLVFFGGL NRYDLYQDCV YKSYKYSQNS
     INVSTSQTLL MELAYKSFAT PPCYDDTKDE KYLRLPQVRR ALNIHSQSLN WSLCRTFVQR
     TYKVQTFSSY KLFPLLLEKY RMLIFFGDSD GTCNYLGGEW VMKELGLQPI SAYTPWHVTN
     KNGQQIAGYK ITYPNLHFVT IKGAGHLVPE DKPQEAFIML QTWLEAKPAT SMVVSSSTAG
     FIVAVVFIAI TLLIEIIS
//
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