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
//