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Database: UniProt
Entry: A0A022Q1Y0_ERYGU
LinkDB: A0A022Q1Y0_ERYGU
Original site: A0A022Q1Y0_ERYGU 
ID   A0A022Q1Y0_ERYGU        Unreviewed;       457 AA.
AC   A0A022Q1Y0;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE            EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN   ORFNames=MIMGU_mgv1a006099mg {ECO:0000313|EMBL:EYU21824.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU21824.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU21824.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR   EMBL; KI632223; EYU21824.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A022Q1Y0; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
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:SF435; SERINE CARBOXYPEPTIDASE-LIKE 45; 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:UP000030748};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|RuleBase:RU361156}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT   CHAIN           19..457
FT                   /note="Carboxypeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT                   /id="PRO_5006511620"
SQ   SEQUENCE   457 AA;  51441 MW;  1F4E81001FDD91F3 CRC64;
     MSAALFLVFS CFICIASCLP THHHPDRIAR LPGQPPVDFQ QFSGYVSVDE KREKALFYYF
     VEAEIDPPSK PLVLWLNGGP GCSSIGVGAF SENGPFRPNV EVLLRNEYSW NREANMLYLD
     TPVGVGFSYS TGASSYETVN DEITAKDNLV FLQKWFLDFP QYRNSSLFIT GESYAGHYVP
     QLANLIIQLN KKKKIINLTG IALGNPLLEF STDYNSRAEY FWSHGLISDS TYNVFTSGCN
     YSRYVSEYYR DSVSVLCSRV MSLVNRESSR FVDKYDVTLD VCIPSVLSQS KIIAPHQNSE
     RIDVCVEDEI TKYLNRRDVQ MALHARLVGV RKWDVCSNIL DYDMLDLEIP TISIIGSLVK
     EGIPVLIYSG DQDSVIPLTG TRTLVHKLAK QLGLNTTVTY RVWFEGQQVG GWTQVYGNIL
     SFGTVRGASH EAPFSQPERS FVLFKSFLSG KPLPLEF
//
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