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Database: UniProt
Entry: A0A095CFT6_SCHHA
LinkDB: A0A095CFT6_SCHHA
Original site: A0A095CFT6_SCHHA 
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
//
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