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Database: UniProt
Entry: A0A0L9V7W4_PHAAN
LinkDB: A0A0L9V7W4_PHAAN
Original site: A0A0L9V7W4_PHAAN 
ID   A0A0L9V7W4_PHAAN        Unreviewed;       390 AA.
AC   A0A0L9V7W4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE            EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN   ORFNames=LR48_Vigan08g190000 {ECO:0000313|EMBL:KOM51073.1};
OS   Phaseolus angularis (Azuki bean) (Vigna angularis).
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; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM51073.1, ECO:0000313|Proteomes:UP000053144};
RN   [1] {ECO:0000313|Proteomes:UP000053144}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX   PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA   Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA   Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA   Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA   Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT   "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT   high starch and low fat accumulation and domestication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR   EMBL; CM003378; KOM51073.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L9V7W4; -.
DR   STRING; 3914.A0A0L9V7W4; -.
DR   EnsemblPlants; KOM51073; KOM51073; LR48_Vigan08g190000.
DR   Gramene; KOM51073; KOM51073; LR48_Vigan08g190000.
DR   OMA; GYDPCTS; -.
DR   Proteomes; UP000053144; Chromosome 8.
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; IPR033124; Ser_caboxypep_his_AS.
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; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|RuleBase:RU361156};
KW   Protease {ECO:0000256|RuleBase:RU361156};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
SQ   SEQUENCE   390 AA;  44805 MW;  36202C1136A39F50 CRC64;
     MVGYFTFLLT QKLMFCTINI NITVNLLFLE SPVGVGFSYT NTSSDIIELG DSITAKDSHI
     FIIKWFRRFP QFRSHKFYIA GESYAGINIR FILKFDFSGH YVPQLSELIF DNNLNHAEKD
     YINFKGFLIG NALLDDETDQ KGMIDYAWDH AVISDALYHN ITAICDFNHP IQNQTDECNT
     ELNKYFDVYK IIDMYSLYTP RCFSNLSSTS TNEASQTSSR IILQKISEQN RWQRKRAGYD
     PCASDYTEVY LNRPEVQKAL HANVTKIPYP WTHCSDNITF WNDSPQSILP VLKKLVAGGL
     RIWVYSGDTD GRIPVTATRY TLRKLGLGIV EDWSPWYTSR QVGGWSIVYD GLTFVTIRGA
     GHQVPTFTPK QALQLLQHFI DNKKLPSRPI
//
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