ID A0CSE4_PARTE Unreviewed; 452 AA.
AC A0CSE4;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN ORFNames=GSPATT00009983001 {ECO:0000313|EMBL:CAK73711.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK73711.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK73711.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK73711.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR EMBL; CT868163; CAK73711.1; -; Genomic_DNA.
DR RefSeq; XP_001441108.1; XM_001441071.1.
DR AlphaFoldDB; A0CSE4; -.
DR MEROPS; S10.005; -.
DR EnsemblProtists; CAK73711; CAK73711; GSPATT00009983001.
DR GeneID; 5026893; -.
DR KEGG; ptm:GSPATT00009983001; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_1_1; -.
DR InParanoid; A0CSE4; -.
DR OMA; WQVEYGE; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802:SF201; CARBOXYPEPTIDASE; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000000600};
KW Signal {ECO:0000256|RuleBase:RU361156}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT CHAIN 17..452
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT /id="PRO_5006521598"
SQ SEQUENCE 452 AA; 52069 MW; BAC036E7B13D1610 CRC64;
MMKCVILGML LLSVSCIDIV ADEFRWPDWP VYRFKTWSGL IEIDDDGVTR NLHYVFVESQ
TEDAEVATQP VILWLNGGPG CSSLLGLMQE IGPYVIDNGE TEYKYNPWSW NKNAHLLILE
SPFGVGFSQP SPDKDYKFTD EKTGRFNYEA IREWFNTFTY YRGRDFYIAG ESYAGMYIPY
TAKALLEGEK TVDQKEKINF KGVLIGNGVL INNEKFRAQT SIKFLARRSF IDYTNQFILN
HNCALQPNSA SCRQAKKSLD SAIAEINPYG VYSYCWGDST LKQYKVERES KHRFSYTPWL
KLTEDDDDSS APCIDFGPLA NKLNTDEYKE ALHVDKNIVW SGCSDPVYLQ YTKSEGSYQI
LPELFQAGIQ ILLYSGDQDL AVSIVETYES IKQIQGIKEI KGWTPYLNTN DGELKKLISR
MDCRIQLFQI PSYQRCWTYG PIRLKRELMV YD
//
