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Database: UniProt
Entry: A0DS31_PARTE
LinkDB: A0DS31_PARTE
Original site: A0DS31_PARTE 
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
//
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