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
//