ID A0A095CFT6_SCHHA Unreviewed; 323 AA.
AC A0A095CFT6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 41.
DE SubName: Full=Lysosomal aspartic protease {ECO:0000313|EMBL:KGB41738.1};
GN ORFNames=MS3_10282 {ECO:0000313|EMBL:KGB41738.1};
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB41738.1};
RN [1] {ECO:0000313|EMBL:KGB41738.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22246508; DOI=10.1038/ng.1065;
RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA Wang J., Gasser R.B.;
RT "Whole-genome sequence of Schistosoma haematobium.";
RL Nat. Genet. 44:221-225(2012).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KL252078; KGB41738.1; -; Genomic_DNA.
DR RefSeq; XP_012801526.1; XM_012946072.1.
DR AlphaFoldDB; A0A095CFT6; -.
DR STRING; 6185.A0A095CFT6; -.
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; 1.
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, ECO:0000313|EMBL:KGB41738.1}.
FT DOMAIN 19..318
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DISULFID 242..279
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 323 AA; 36515 MW; FBAEAEFFE11FD671 CRC64;
MVDIYSKVYI TSKENLPLLY SNVNLTSILK SPTSIAGHSP SMIGLIEDAG DSGQSQMGGM
QVINFNVQYL DSNYSGFWSM DTIRINPLEI RNQAFAEMRS IFNLDYLSDK YDGIIGMSNR
RISEYGNIPM FPNILANGVN MNPIFSFYLN RENGEGIGGE MVLGGVNPKY FKGDFEYVPT
IQNYMWTIQM LSLQINGINF CNICSAVIDT GTSLIIGPNE QVERINSLLH AFDNFGRNVI
DCGRIDMLPS IEFIFHRKKY ILKPQHYVVK ETDFFKTICL SPFQSHFSLP PNYWVLGDVF
MGKFYTVFDF GQRRIGLADA VGA
//