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Database: UniProt
Entry: A7AS70_BABBO
LinkDB: A7AS70_BABBO
Original site: A7AS70_BABBO 
ID   A7AS70_BABBO            Unreviewed;       532 AA.
AC   A7AS70;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   SubName: Full=Aspartyl protease, putative {ECO:0000313|EMBL:EDO07389.1};
GN   ORFNames=BBOV_IV010360 {ECO:0000313|EMBL:EDO07389.1};
OS   Babesia bovis.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Babesiidae; Babesia.
OX   NCBI_TaxID=5865 {ECO:0000313|EMBL:EDO07389.1, ECO:0000313|Proteomes:UP000002173};
RN   [1] {ECO:0000313|EMBL:EDO07389.1, ECO:0000313|Proteomes:UP000002173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T2Bo {ECO:0000313|EMBL:EDO07389.1};
RX   PubMed=17953480; DOI=10.1371/journal.ppat.0030148;
RA   Brayton K.A., Lau A.O.T., Herndon D.R., Hannick L., Kappmeyer L.S.,
RA   Berens S.J., Bidwell S.L., Brown W.C., Crabtree J., Fadrosh D.,
RA   Feldblum T., Forberger H.A., Haas B.J., Howell J.M., Khouri H., Koo H.,
RA   Mann D.J., Norimine J., Paulsen I.T., Radune D., Ren Q., Smith R.K. Jr.,
RA   Suarez C.E., White O., Wortman J.R., Knowles D.P. Jr., McElwain T.F.,
RA   Nene V.M.;
RT   "Genome sequence of Babesia bovis and comparative analysis of apicomplexan
RT   hemoprotozoa.";
RL   PLoS Pathog. 3:1401-1413(2007).
RN   [2] {ECO:0000313|Proteomes:UP000002173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=33294524; DOI=10.1016/j.dib.2020.106533;
RA   Ueti M.W., Johnson W.C., Kappmeyer L.S., Herndon D.R., Mousel M.R.,
RA   Reif K.E., Taus N.S., Ifeonu O.O., Silva J.C., Suarez C.E., Brayton K.A.;
RT   "Transcriptome dataset of Babesia bovis life stages within vertebrate and
RT   invertebrate hosts.";
RL   Data Brief 33:106533-106533(2020).
RN   [3] {ECO:0000313|Proteomes:UP000002173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=33069745;
RA   Ueti M.W., Johnson W.C., Kappmeyer L.S., Herndon D.R., Mousel M.R.,
RA   Reif K.E., Taus N.S., Ifeonu O.O., Silva J.C., Suarez C.E., Brayton K.A.;
RT   "Comparative analysis of gene expression between Babesia bovis blood stages
RT   and kinetes allowed by improved genome annotation.";
RL   Int. J. Parasitol. 51:123-136(2021).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDO07389.1}.
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DR   EMBL; AAXT01000002; EDO07389.1; -; Genomic_DNA.
DR   RefSeq; XP_001610957.1; XM_001610907.1.
DR   AlphaFoldDB; A7AS70; -.
DR   STRING; 5865.A7AS70; -.
DR   EnsemblProtists; EDO07389; EDO07389; BBOV_IV010360.
DR   VEuPathDB; PiroplasmaDB:BBOV_IV010360; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   InParanoid; A7AS70; -.
DR   Proteomes; UP000002173; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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; 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; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000313|EMBL:EDO07389.1};
KW   Protease {ECO:0000313|EMBL:EDO07389.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002173};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..532
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002706882"
FT   DOMAIN          185..511
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        203
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        403
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        216..221
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   532 AA;  58573 MW;  50A2A496DDD5812B CRC64;
     MVIATLIAAI VWQACISKIC YPAWVLSVVD AAPIGKTPSG SLKDCPSHKI DVYKGPKPKI
     VLPMIPMQNN NTPGAFMQIG NTISLPPKSS VVKQHKDNIS KTKSGKVATV FPGRGPNGSM
     GVDMETKRRH EERIRKQSLE QLAAMDNNTS EKDEIPVTVT RQETAFPRVP ANACLDFASL
     RHTTFVVEAY IGKPGQKFLP ILDTGSTNVW AIHPECTSAG CMEAIKYDPA RSKTFKPLEA
     ADSIVRARFV SGVVLGTLGY DDFTIGGFTV KGQLFAMMRD IPDKSTNDIL TVSNGQNVDI
     FTQETPFNGM IGLGFKDLMV MNSEPLYQRY MKVVGAEPIF SFYYSRNGVG SAFLVGGADE
     RLHKGPMQMM PVVPGYYWQV ELEEVFVGKR KVCCDKQSYA VFDTGTAFNS MPHAAINTLL
     EEYPFYECNA ENMNRVYAAL PTIKYTFSNG VQAKLTPEQY TYESEGVCRP AFMQINVDVA
     GGEGYLLGSM AFMPHYYTVY YGGESPMIGI APSNHENAPK VVAEYTSKHK KA
//
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