ID C5YE82_SORBI Unreviewed; 492 AA.
AC C5YE82;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN ORFNames=SORBI_3006G044400 {ECO:0000313|EMBL:EES11974.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EES11974.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EES11974.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR EMBL; CM000765; EES11974.1; -; Genomic_DNA.
DR RefSeq; XP_002447646.1; XM_002447601.1.
DR AlphaFoldDB; C5YE82; -.
DR MEROPS; S10.004; -.
DR EnsemblPlants; EES11974; EES11974; SORBI_3006G044400.
DR GeneID; 8070920; -.
DR Gramene; EES11974; EES11974; SORBI_3006G044400.
DR KEGG; sbi:8070920; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; C5YE82; -.
DR OMA; RIDYYHD; -.
DR OrthoDB; 1203831at2759; -.
DR Proteomes; UP000000768; Chromosome 6.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019748; P:secondary metabolic process; IBA:GO_Central.
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; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802:SF346; OS04G0321700 PROTEIN; 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:UP000000768};
KW Signal {ECO:0000256|RuleBase:RU361156}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT CHAIN 23..492
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT /id="PRO_5005125340"
SQ SEQUENCE 492 AA; 55214 MW; AA70A0CA5F7AE98A CRC64;
MASPFVLLVV VAALLLPPAV FAAPEEHLVT GLPGFHGAFP SKHYSGYVTV DERSERSLFY
YLVLSERDPA TDPVVIWLNG GPGCSSFDGF VYGNGPFNFE PGSSPGSLPK LQLNPYSWSK
VSNIMYLDSP AGVGMSYSLN KSDYITGDLK TAADAHKFLL KWFELYPEFQ LNPFYISGES
YAGVYIPTIT DEVVKGIERG VKPRINFKGY LIGNPATDVD YDFNSFVPFA HGMGLISTDM
YEDVKASCRG TFFGTLDNLC QEKIDRVRWE LKDLNKYNIL APCYHHPEIQ ELEFSKSSLP
QSFRRLGETD RPFPVRKRMA GRSWPLRLAL KDGHVPMWPG LGGRSLPCTS DEVATTWLDD
EDVRAAIHAK PKSLIGSWEL YTARIDFTHD TGTMLTYHKK LTGLGYRVLI YSGDHDLCIP
YPGTEAWVKS IGYQVVDRWR PWYFGDQVAG YTEGYGHNLT FLTIKGAGHA VPEYKPKEAL
AFYSRWLAGE KF
//
