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Database: UniProt
Entry: A0E8W2_PARTE
LinkDB: A0E8W2_PARTE
Original site: A0E8W2_PARTE 
ID   A0E8W2_PARTE            Unreviewed;       397 AA.
AC   A0E8W2;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   SubName: Full=Chromosome undetermined scaffold_83, whole genome shotgun sequence {ECO:0000313|EMBL:CAK91729.1};
GN   ORFNames=GSPATT00024460001 {ECO:0000313|EMBL:CAK91729.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK91729.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK91729.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK91729.1,
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 A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; CT868664; CAK91729.1; -; Genomic_DNA.
DR   RefSeq; XP_001459126.1; XM_001459089.1.
DR   AlphaFoldDB; A0E8W2; -.
DR   STRING; 5888.A0E8W2; -.
DR   MEROPS; A01.058; -.
DR   EnsemblProtists; CAK91729; CAK91729; GSPATT00024460001.
DR   GeneID; 5044911; -.
DR   KEGG; ptm:GSPATT00024460001; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_3_0_1; -.
DR   InParanoid; A0E8W2; -.
DR   OMA; GADSAHY; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000600}.
FT   DOMAIN          66..393
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        84
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        97..102
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   397 AA;  45023 MW;  28636F2881AA61B4 CRC64;
     MPSIYWKSKP PFRHLRLNEK VVNVKDSQDF YKFVALNQKR LFENQFIQKS SASENLRLHN
     FKNIQYTADL GIGQAGNVFK VVLDTGSANL WIDSNRCSEQ GCMRHKQYKH EESHSFLPLN
     QELTVEFGSG ELKGLVNSDT IYFGDITLPR QNLAEITSEN GIIFKSLDFD GILGLAYPQM
     APKNFNPVFD NMMQQHALEK NQFAFYFAKD PNDITHSEFT LGGYNQAHVD GEINYHNVID
     KYYWMIKADS ILVGGKDIGL CNDGSCKLIV DTGTSIMSGP MDDVGTLLRN LNVKDHCSEV
     KSLPNITFKI DGIDYTLEPE EYVKPTTADS SAFAEMNSSE DQSMVEVNSW DCIASFIPLD
     IQEPQGPAWI LGDVFLRKYY SIYDRDNDRV GFAKAKQ
//
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