ID A0A183N489_9TREM Unreviewed; 543 AA.
AC A0A183N489;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 22-FEB-2023, entry version 32.
DE SubName: Full=Peptidase A1 domain-containing protein {ECO:0000313|WBParaSite:SMRZ_0002311501-mRNA-1};
GN ORFNames=SMRZ_LOCUS23114 {ECO:0000313|EMBL:VDP45891.1};
OS Schistosoma margrebowiei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=48269 {ECO:0000313|Proteomes:UP000050790, ECO:0000313|WBParaSite:SMRZ_0002311501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMRZ_0002311501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP45891.1, ECO:0000313|Proteomes:UP000277204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zambia {ECO:0000313|EMBL:VDP45891.1,
RC ECO:0000313|Proteomes:UP000277204};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UZAI01019518; VDP45891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183N489; -.
DR STRING; 48269.A0A183N489; -.
DR WBParaSite; SMRZ_0002311501-mRNA-1; SMRZ_0002311501-mRNA-1; SMRZ_0002311501.
DR Proteomes; UP000050790; Unplaced.
DR Proteomes; UP000277204; 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; 3.
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; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 2.
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:UP000277204}.
FT DOMAIN 200..538
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 218
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 398
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 231..238
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 431..499
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 543 AA; 61949 MW; E7228269FE984324 CRC64;
MINDIEFCNG CTAFIDTGTS TIIGGREQVT RINTMLGISF QFGRSFLDCK RIDMLPPIEF
IFRKKKYILE PHDYVIKENL SLLYSNVNLT SILKSPTSIA GYSPSMIGLI EDAGDSGQSQ
MGGMHVLKPI SMILFIIVGF LPYLYGEIVR IPLHPVKRSD SLLGLGATYF KPLTRKWKYE
WNKQNTSTPE QLINYENLQY YGEISVGTPP QKLRVMFDTG STDTWFASRR CWFLDIFCWM
FSFYDSSKSS TYVADGSSFH VSYLDGDYSG FWSVDTIRIR NQSFAEVRSI FNLDYLFDKC
DGIIGMSPSR ISDDGSIPMF PNILANGVNM NPIFSFYLNR ENGAGIGGEL VLGGVNPKYF
KGDFEYVPTI QNYMWTIQML SLQINGINFC NICSALIDTG TSLIIGPNEQ VERINSLLHA
FDNFGRNVID CDRIDMLPSI EFIFHRKKYI LKPQHYVVKV HTIIFHTVTI QTNKMETICF
HTNVFFVQLQ ETEFFKTICL SPFDSRFSLS PNYWILGDVF MGKFYTVFDF GQRRIGLADA
VGT
//