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Database: UniProt
Entry: A0A061DEM2_BABBI
LinkDB: A0A061DEM2_BABBI
Original site: A0A061DEM2_BABBI 
ID   A0A061DEM2_BABBI        Unreviewed;       469 AA.
AC   A0A061DEM2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   08-NOV-2023, entry version 46.
DE   SubName: Full=Aspartyl protease, putative {ECO:0000313|EMBL:CDR97525.1};
GN   ORFNames=BBBOND_0400170 {ECO:0000313|EMBL:CDR97525.1};
OS   Babesia bigemina.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Babesiidae; Babesia.
OX   NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR97525.1, ECO:0000313|Proteomes:UP000033188};
RN   [1] {ECO:0000313|Proteomes:UP000033188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RX   PubMed=24799432; DOI=10.1093/nar/gku322;
RA   Jackson A.P., Otto T.D., Darby A., Ramaprasad A., Xia D., Echaide I.E.,
RA   Farber M., Gahlot S., Gamble J., Gupta D., Gupta Y., Jackson L.,
RA   Malandrin L., Malas T.B., Moussa E., Nair M., Reid AJ., Sanders M.,
RA   Sharma J., Tracey A., Quail M.A., Weir W., Wastling J.M., Hall N.,
RA   Willadsen P., Lingelbach K., Shiels B., Tait A., Berriman M., Allred D.R.,
RA   Pain A.;
RT   "The evolutionary dynamics of variant antigen genes in Babesia reveal a
RT   history of genomic innovation underlying host-parasite interaction.";
RL   Nucleic Acids Res. 42:7113-7131(2014).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; LK391710; CDR97525.1; -; Genomic_DNA.
DR   RefSeq; XP_012769711.1; XM_012914257.1.
DR   AlphaFoldDB; A0A061DEM2; -.
DR   STRING; 5866.A0A061DEM2; -.
DR   MEROPS; A01.A95; -.
DR   EnsemblProtists; CDR97525; CDR97525; BBBOND_0400170.
DR   GeneID; 24566066; -.
DR   KEGG; bbig:BBBOND_0400170; -.
DR   VEuPathDB; PiroplasmaDB:BBBOND_0400170; -.
DR   OMA; VAFSECL; -.
DR   OrthoDB; 46443at2759; -.
DR   Proteomes; UP000033188; Chromosome 4.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034164; Pepsin-like_dom.
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:CDR97525.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033188};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..469
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001595765"
FT   DOMAIN          148..459
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        355
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        179..184
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        380..413
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   469 AA;  52198 MW;  B06135D853DAC603 CRC64;
     MVSWKRCGIT TAVVFLTALR LSVCDIDSSS SEAITGERCL RFDEGGCSVW LHKGNPAEHS
     ISLERYQIPG SVSALQMASS NHELFKKGKI SFAKRGEGVF GSIGYDGNKN RRPAFSTMKN
     KLNKRIAMLK RCDRANYIPI KQTKDSLYVG EIKIGTPPQT FHPIFDTGST NLWVVGSTCK
     EPSCSKVCRY DASRSTTFKM MDTPIKIHIK FGTGEIEGYP AKDTVVLGKI AIPDQSLAVV
     VSEKSAGGDN IFDKIHFEGI VGLAFPEMSS VPGMPIFDHM ALLKNMKHKE FAFYIDENDK
     ESRIMLGGID PQYYLGEIQM FPVVREHYWE VKLDAFYVGN EKLCCDGQSS YLIFDSGTSL
     NTIPSSYFGH FMSYFESKTC DVGADYPTIT YVLEGERITL EPHQYMLRQG KRCVPAFMQL
     DVPSEFGNAF IVGSNAFMKH YVTVYHRGTG GKASMVGIAK SNHSATQHD
//
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