ID   I3SRN4_MEDTR            Unreviewed;       488 AA.
AC   I3SRN4;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE            EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:AFK42926.1};
RN   [1] {ECO:0000313|EMBL:AFK42926.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Krishnakumar V., Cheung F., Xiao Y., Chan A., Moskal W.A., Town C.D.;
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR   EMBL; BT143132; AFK42926.1; -; mRNA.
DR   AlphaFoldDB; I3SRN4; -.
DR   MEROPS; S10.005; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.11320; -; 1.
DR   Gene3D; 6.10.250.940; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802:SF505; 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; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
KW   Hydrolase {ECO:0000256|RuleBase:RU361156};
KW   Protease {ECO:0000256|RuleBase:RU361156};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|RuleBase:RU361156}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT   CHAIN           29..488
FT                   /note="Carboxypeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT                   /id="PRO_5006526149"
SQ   SEQUENCE   488 AA;  55127 MW;  971B856ED5D41358 CRC64;
     MDNLIFKIRN LYTLVLLLFV LCFKPSFSSR SHRHYSGGDG RKLRSSGDNV SDLVTHLPGQ
     PQVDFQHYAG YVTVNKTNGR ALFYWFYEAM AKPEEKPLVL WLNGGPGCSS VGYGATQEIG
     PFLVDNNNDG QGLKFNNFSW NKEANMLFLE SPVGVGFSYS NTTSDYQQLG DDFTANDAYN
     FLHNWFLKFP SYRSKTFYIA GESYAGKYVP ELAELIHDRN KDPSLYIDLK GILLGNPETS
     DAEDWMGLVD YAWSHAVISD ETHKTIKTSC DFNSSDPWKN EDCDQAVDEV LKQYNEIDIY
     SLYTSVCFAS TARSNGHSMQ TSTKRSSKMM PRMMGGYDPC LDDYAKAFYS RPDVQKALHA
     SDGHNLKNWS ICNNKIFTDW ADSKPTVIPI YKKLISAGLR IWVYSGDTDG RVPVLSTRYS
     LSTLALPVTK PWSPWYHENE VSGWYEEYQG LTFATFRGAG HAVPCFKPSN SLAFFTSFLH
     GETPPSTK
//