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Database: UniProt
Entry: A0A0S4KGW0_BODSA
LinkDB: A0A0S4KGW0_BODSA
Original site: A0A0S4KGW0_BODSA 
ID   A0A0S4KGW0_BODSA        Unreviewed;       502 AA.
AC   A0A0S4KGW0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   13-SEP-2023, entry version 28.
DE   SubName: Full=Aspartate protease, putative {ECO:0000313|EMBL:CUI14930.1};
GN   ORFNames=BSAL_20410 {ECO:0000313|EMBL:CUI14930.1};
OS   Bodo saltans (Flagellated protozoan).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Eubodonida; Bodonidae; Bodo.
OX   NCBI_TaxID=75058 {ECO:0000313|EMBL:CUI14930.1, ECO:0000313|Proteomes:UP000051952};
RN   [1] {ECO:0000313|Proteomes:UP000051952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CYKH01001720; CUI14930.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4KGW0; -.
DR   VEuPathDB; TriTrypDB:BSAL_20410; -.
DR   OrthoDB; 1332686at2759; -.
DR   Proteomes; UP000051952; 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; cd05479; RP_DDI; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR15397:SF3; DNA DAMAGE-INDUCIBLE 1 HOMOLOG 2; 1.
DR   PANTHER; PTHR15397; SODIUM-GLUCOSE COTRANSPORTER REGULATORY PROTEIN -RELATED; 1.
DR   Pfam; PF09668; Asp_protease; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:CUI14930.1};
KW   Protease {ECO:0000313|EMBL:CUI14930.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051952}.
FT   DOMAIN          193..315
FT                   /note="Aspartic peptidase DDI1-type"
FT                   /evidence="ECO:0000259|Pfam:PF09668"
FT   REGION          90..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  55392 MW;  129FBF99842C5AB2 CRC64;
     MQLLCHITNA SNNRHDVTLS DIDASDPLAL VCALLEDSAG IEAADQRVTS TLANGGGELL
     LPHRSLKEQG VQGTMVELNV YHKDVYAQQR SNGAQTPAPT NTSASTGAAV ASQDDAARLI
     AQLFAGGGGQ QPQPQQQQQQ PSPDELIARL FQGGAASAAS AAPTHNAAAA APIPPDPEDP
     EYQRRLYEHI QRQNLEENLA NAMEYTPEAF ARVVMLYVPC TVNNVPLTAF VDSGAQMSVM
     SERMAEKCGI MRLLDRRMQG VAKGVGTCRI LGRVHMTMVS LGGLVLPFSI TVLERQDMDF
     LIGLDQLKRH QMQIDLKANC LRIDEHALPF LSEGELPIHL RKESAGENEE EEGEQQQQQT
     AESHAATKAK EEAQSHSAAA AIARNSAAPD AAKASKVATP PSQTQTASFF FLKTKKKRES
     SSSNRQQSRM QLRRQKKKRS LTLLLRPSPE IQQQHPMLHE RKLPRPHPKH RQLQHRHRLL
     LLSQRRLLQL LSTKKRWLGF KK
//
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