ID A0DEH8_PARTE Unreviewed; 425 AA.
AC A0DEH8;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE SubName: Full=Chromosome undetermined scaffold_48, whole genome shotgun sequence {ECO:0000313|EMBL:CAK81445.1};
GN ORFNames=GSPATT00016271001 {ECO:0000313|EMBL:CAK81445.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK81445.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK81445.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK81445.1,
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; CT868407; CAK81445.1; -; Genomic_DNA.
DR RefSeq; XP_001448842.1; XM_001448805.1.
DR AlphaFoldDB; A0DEH8; -.
DR STRING; 5888.A0DEH8; -.
DR MEROPS; A01.058; -.
DR EnsemblProtists; CAK81445; CAK81445; GSPATT00016271001.
DR GeneID; 5034627; -.
DR KEGG; ptm:GSPATT00016271001; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_2_1; -.
DR InParanoid; A0DEH8; -.
DR OMA; GVHDAAC; -.
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; 2.
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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..425
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002623770"
FT DOMAIN 100..421
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 116
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 299
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 129..134
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 290..294
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 425 AA; 47987 MW; 9862FABDD1A909B8 CRC64;
MNQFLFSLLI VTIHCGQEQG SFLQEKQDNQ IFTIKLKETQ KIVTAKEMYD FLSTKQTYFR
QHIPIDISEI EFGGYVPKLQ ENENRKKTSL KLHNFRNTQF TGPITVGDQE FQVIFDTGSA
NFWIDSTKCK NEGCRQHTQY QPSLRSKHLG YALNVEFGTG DLNGEINSDV VRLGEIEVED
QNIAEIIEEN GSVFQNAGFD GIVGLGYPSM AAYNFNPLFD NIMQEKKLKS NQFSFYMSNQ
VNSYESQITF GGYDAAKLDG EVHYHPVIDQ YYWMIQADNI LVNGKDEGFC PKGCKVVADT
GTSLITGPFE DLMKLLDLTN INDDCSNLNE LPKLTFRIGG VDYDLDSKDY IMELRDDGTE
IPLNNDVSAS AFIQGTSSRC IGAFMPLDIP DPQGPAWILG DIFLTKYLSI YDRDANMVGF
GKAKH
//