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Database: UniProt
Entry: A0A059ABV5_EUCGR
LinkDB: A0A059ABV5_EUCGR
Original site: A0A059ABV5_EUCGR 
ID   A0A059ABV5_EUCGR        Unreviewed;       447 AA.
AC   A0A059ABV5;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE            EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN   ORFNames=EUGRSUZ_J00874 {ECO:0000313|EMBL:KCW51318.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW51318.1};
RN   [1] {ECO:0000313|EMBL:KCW51318.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW51318.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) 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; KK198762; KCW51318.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059ABV5; -.
DR   MEROPS; S10.A39; -.
DR   EnsemblPlants; KCW51318; KCW51318; EUGRSUZ_J00874.
DR   Gramene; KCW51318; KCW51318; EUGRSUZ_J00874.
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:SF31; SERINE CARBOXYPEPTIDASE-LIKE 34; 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   3: Inferred from homology;
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..29
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT   CHAIN           30..447
FT                   /note="Carboxypeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT                   /id="PRO_5006511868"
SQ   SEQUENCE   447 AA;  50795 MW;  A99100C1838F22EF CRC64;
     MGHHCSSSSS PSMLSLKCLL MLTATFVASS LPSGTANWAS EQEADRVYRL PGQPDVKFKQ
     YAGYVTVNET HGRALFYWFF EATDKPQDKP LLLWLNGGPG CSSIGYGQSE ELGPFFPQKD
     QPKLKFNRYT WNKAANLLFV ESPVGVGFSY TNTSSDIGQL GDTITAQDSY VFLVNWFRRF
     PQFKSHDFYL AGESYAGHYV PQLSELILDN NKKLSKEDYI NLKGLMIGNA LLDDDTDQRG
     MIDYAWDHAV VSDRLYHDIK ATCNFSQENL TSDCTSNLNK YFAVYRIIDM YSLYVSKCVN
     SNFSSTRQRP VIDGVIAPRL LSKFAGWHKR PAGYDPCASD YTEVYFNRPD VQEALHANVT
     NIPYPWTHCS NNISFWSDAP ASILPIIRKL IQGGLRVWVY SGDTDGRIPV TSTRYTLNKL
     GLDIVQDWTP WYNYQQVIFD LFLLIYL
//
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