ID A0BQJ6_PARTE Unreviewed; 446 AA.
AC A0BQJ6;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Chromosome undetermined scaffold_120, whole genome shotgun sequence {ECO:0000313|EMBL:CAK60813.1};
GN ORFNames=GSPATT00031042001 {ECO:0000313|EMBL:CAK60813.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK60813.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK60813.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK60813.1,
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CT868009; CAK60813.1; -; Genomic_DNA.
DR RefSeq; XP_001428211.1; XM_001428174.1.
DR AlphaFoldDB; A0BQJ6; -.
DR STRING; 5888.A0BQJ6; -.
DR EnsemblProtists; CAK60813; CAK60813; GSPATT00031042001.
DR GeneID; 5013995; -.
DR KEGG; ptm:GSPATT00031042001; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_1_1; -.
DR InParanoid; A0BQJ6; -.
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 CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, 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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..446
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002623057"
FT DOMAIN 97..441
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 115
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 321
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 446 AA; 51372 MW; 345AADE8FA48B418 CRC64;
MHIKVILFAL IISCTFSRQI RSRKSNLMHI PLVQKGQRVQ DAIKSTLHSD TKISFELSRE
DKQQIKNQNT LLDHLDRIQY AYQITYIPLR NSYNAQYFGK IELGSPEQTF DVLFDTGSSY
TWVASSDCHT CKKAGVKEFF DCEASYSCKY LQKKIKLQYG TGKAEAQFMV ENLKIGSLLI
RNQTMLILDE LTELKKFEGD GLAGLGFDTL SDGYPTLIDN LFSQNQIEKK EFSIFLTDEH
LKDEEQSKLI LGGQLDSLGD QSDQWHYCYV INNKYWAIQG DHVAFVSKDG NTKRTLKSIQ
PVHNAQDEKS DILYTSLFVV DSGTSLIVLY EKDHQRLVEY LQDFGIKCFD SLQFEGITQC
DQADVDEYPN FESTDFMFIL LVSLCGKVFT ITPDKYLLCS FFECYLMIAP FDQKVSILGD
LFIREYYTHF IQDEPRKVGF IKAVQN
//
