ID D7MVI3_ARALL Unreviewed; 473 AA.
AC D7MVI3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN ORFNames=ARALYDRAFT_333040 {ECO:0000313|EMBL:EFH39462.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR EMBL; GL348721; EFH39462.1; -; Genomic_DNA.
DR RefSeq; XP_002863203.1; XM_002863157.1.
DR AlphaFoldDB; D7MVI3; -.
DR STRING; 81972.D7MVI3; -.
DR MEROPS; S10.004; -.
DR EnsemblPlants; fgenesh1_pm.C_scaffold_9000068; fgenesh1_pm.C_scaffold_9000068; fgenesh1_pm.C_scaffold_9000068.
DR GeneID; 9299279; -.
DR Gramene; fgenesh1_pm.C_scaffold_9000068; fgenesh1_pm.C_scaffold_9000068; fgenesh1_pm.C_scaffold_9000068.
DR KEGG; aly:9299279; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR OrthoDB; 1203831at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; IEA:EnsemblPlants.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.12670; -; 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:SF254; SERINE CARBOXYPEPTIDASE-LIKE 20; 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 Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|RuleBase:RU361156}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT CHAIN 24..473
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT /id="PRO_5006523652"
SQ SEQUENCE 473 AA; 52915 MW; B09169704B90A488 CRC64;
MVWLMKVFVF VTLVSLLFVI TESAPESALI TKLPGFEGTF PSKHYSGYVT IDKDHGKNLW
YYFVESEKDP SKDPVVLWLN GGPGCSSMDG FVYEHGPFNF ELPKKNNSLP LLHLNPYSWS
KVSNIIYLDS PVGVGFSYSN NISDYITGDT KTAVDSHAFL LKWFQMFPEF QSNPFFISGE
SYAGVYVPTL ASEVVKGIKN GVKPALNFKG YLVGNGVADQ VFDGNALVPF AHGMGLISDE
LFENVTKACH GNFYEIEGLE CEEQYTKVSD DTDRLNIYNI LEPCYHGTSL SAFDIRSLPS
SLLELGKTER PLAIRKRMFG RAWPVRAPVR PGIVPSWSQL LADVSVPCID DRVATAWLND
PAIRKAIHTK EESEIGRWEL CSGKLSFDHD AGSMIKFHRN LTLSGYRALI YSGDHDMCVP
FTGSEAWTKS LGYKVIDEWR AWISNDQVAG YTQGYANNLT FLTIKANIES QLK
//
