ID A0A074Z987_9TREM Unreviewed; 492 AA.
AC A0A074Z987;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 41.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=T265_14937 {ECO:0000313|EMBL:KER22137.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER22137.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER22137.1, 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; KL596917; KER22137.1; -; Genomic_DNA.
DR RefSeq; XP_009174131.1; XM_009175867.1.
DR AlphaFoldDB; A0A074Z987; -.
DR GeneID; 20329103; -.
DR KEGG; ovi:T265_14937; -.
DR CTD; 20329103; -.
DR OrthoDB; 615305at2759; -.
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; 2.40.70.10; 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:SF1; ASPARTYL PROTEINASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000054324}.
FT DOMAIN 73..485
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 440..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 54613 MW; C9E1628662D88D83 CRC64;
MIIGLHRNAR VHLMQHIQLE RTTSSRWIET DCSKDKVTKL VQGRKPFAAK FFIRKHQIGK
YKLFGQESER PGFYVVVGFG KPRQNFRLLI DTGSSTLWVP SDKCEPGLFV NNNKFKGTSK
TFQKKAGALC EIYGDGSSIE GTLGTDTLDV RSYEGTELIF VPSDQWHKGG RCDVWSGASR
ERPTFTQCDG NLGLAVNETA ESFDQTLLEY LFTQELISQL VFTIVYPRIG QPGSIPALVL
PSGETAARHR KSVTAASTLI HGKITFGGVN HDDYRGEISY ATVLPGKFWR VQFHRRPACL
SSHLSICLSV HLPIYLSVCP PIYCLSVSCL SLRLSYSSSV SLSVYYISVC LMEVSGNTVA
HNFIAIADTG TYLVMCPYGT LLNLISQLGV YLEPEEQVDC EEADEFPEII FTLDGFQLGF
PRDLYVERKL TTRTPLTSVG SHSLQPLQPG TVRTTRSPPW KASSTDSTQA FCDPLHTPLP
SQGLAISLFT PL
//