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Database: UniProt
Entry: A0A074Z987_9TREM
LinkDB: A0A074Z987_9TREM
Original site: A0A074Z987_9TREM 
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
//
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