ID A0BIH6_PARTE Unreviewed; 420 AA.
AC A0BIH6;
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_11, whole genome shotgun sequence {ECO:0000313|EMBL:CAK58343.1};
GN ORFNames=GSPATT00004715001 {ECO:0000313|EMBL:CAK58343.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK58343.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK58343.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK58343.1,
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; CT867997; CAK58343.1; -; Genomic_DNA.
DR RefSeq; XP_001425741.1; XM_001425704.1.
DR AlphaFoldDB; A0BIH6; -.
DR STRING; 5888.A0BIH6; -.
DR MEROPS; A01.058; -.
DR EnsemblProtists; CAK58343; CAK58343; GSPATT00004715001.
DR GeneID; 5011525; -.
DR KEGG; ptm:GSPATT00004715001; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_2_1; -.
DR InParanoid; A0BIH6; -.
DR OMA; TEDHIID; -.
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..420
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002622889"
FT DOMAIN 89..416
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 107
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 293
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 120..125
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 420 AA; 47812 MW; 5D428B204AE66F93 CRC64;
MIKSTLFLCL IIFLSDAVNI QNEQKFLEPE KKKVIHIQLQ ERETKVQDKQ NFYKLIAINQ
DKLSDSSFAQ TQQSGPQYMR MHNYKNIQYT ADLGIGQPGN TFKVVLDTGS ANLWIDSTRC
QEEGCMRHKQ YNHEDSQSFL PLNQELSVEF GSGDLKGVVN ADTVYFGDVT LPRQNLAEIT
SENGAIFRDL DFDGILGLAY PKMAPKNFNP VFDNLMDQRV LERNQFSFYF AKDANDIAHS
EFTLGGYNPA HVDGDIHYHD VIDKYYWMIK ADNILVDNKD IGLCNGSCRL IVDTGTSIMS
GPFDDLGTLL RTLNVKSHCH EINTLPTITF KIDDVDYTLD PEEYVKPTNF DAAQLTEVNE
GDDLQALIEV NNWDCIAAFM PLDIQQPQGP AWILGDIFLR KYYSIYDRDN NQVGFAKAKK
//