ID A0DS31_PARTE Unreviewed; 418 AA.
AC A0DS31;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=Chromosome undetermined scaffold_61, whole genome shotgun sequence {ECO:0000313|EMBL:CAK85848.1};
GN ORFNames=GSPATT00019552001 {ECO:0000313|EMBL:CAK85848.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK85848.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK85848.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK85848.1,
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; CT868552; CAK85848.1; -; Genomic_DNA.
DR RefSeq; XP_001453245.1; XM_001453208.1.
DR AlphaFoldDB; A0DS31; -.
DR STRING; 5888.A0DS31; -.
DR MEROPS; A01.058; -.
DR EnsemblProtists; CAK85848; CAK85848; GSPATT00019552001.
DR GeneID; 5039030; -.
DR KEGG; ptm:GSPATT00019552001; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_2_1; -.
DR InParanoid; A0DS31; -.
DR OMA; VAFSECL; -.
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..418
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002624290"
FT DOMAIN 104..414
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 120
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 303
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 133..138
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 294..298
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 418 AA; 47129 MW; 24EBF3DD333B3327 CRC64;
MNIFLYSLLI VLVFCGQEQG TFLQDQSTTS QENKLYTIKL KETHTIVSAK EMYDFLTTKQ
TYFRQQTPID IQEIEFGGYV PKPQQTTEKR QADLKLHNFK NTQFTGPITV GDQEFQVIFD
TGSANFWIDS VKCKNEGCKQ HTQYKPSFRS KHLGYALNVQ FGTGDLNGEV NSDVVKLGEI
EVEDQNIAEI VEENGAVFQN SGFDGIVGLA YPSMAAYDLN PLFDNIMKQK KLQSNQFSFY
MSNKVNSYES QLTFGGYDVT KLDGPVHYHP VIDKYYWMIK AENILVNGQD QGFCPKGCKV
VADTGTSLIT GPYDDLMKLL DLTNIDDNCS NLKELPTLTF RIDGVNYDLE AKDYIMDNEV
SASAFIEGSA KQCIGAFMPL DIPDPQGPAW ILGDIFLTKY LSIYDRDVNM VGFGKAKH
//