ID A0A074ZX50_9TREM Unreviewed; 409 AA.
AC A0A074ZX50;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=T265_01821 {ECO:0000313|EMBL:KER32043.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER32043.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER32043.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KL596638; KER32043.1; -; Genomic_DNA.
DR RefSeq; XP_009164195.1; XM_009165931.1.
DR AlphaFoldDB; A0A074ZX50; -.
DR STRING; 6198.A0A074ZX50; -.
DR GeneID; 20316009; -.
DR KEGG; ovi:T265_01821; -.
DR CTD; 20316009; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000054324; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1960; -; 1.
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:UP000054324}.
FT DOMAIN 92..406
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 110
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 296
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 123..130
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 287..291
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 330..367
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 409 AA; 45128 MW; 700B191602B718D6 CRC64;
MSPFFVVFHS PLDLEVDISS KEYPLDSLHL LKFCRNIPGT TYLGVPLKPL RSTRRTVQDA
QSALDRVRTK WTRRLSNEPF PEKLDNYMDS QYYGEITIGT PPQPFKVVFD TGSSNLWVPS
KRCSFWNEAC RTHQKYDSER SSTYRANGQP FSIQYGTGSV SGVLSTDVVT VSSAKVQDQT
FGEAINEPGS VFVAAKFDGI LGLAFQSIAV DNVVPVFDNM ISQGLVDKQL FSVWLDCGDV
QDIGGEIMFG GVDKGRYTGD MFFVPLSAET YWQIDMAGIQ LTSLTLCAQG CQAIVDTGTS
LIVGPTDDVK QLNDAIGAVP IEGGLNLLDC LQIHTLPPIE FSINGEKLTL QATDYVREMS
YWGRTVCTSG FSGMEVPGVP MWILGDVFIG AYYTVFDKEQ SRVGFARST
//