ID   A0A0S4J9X5_BODSA        Unreviewed;       563 AA.
AC   A0A0S4J9X5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Peptidase, putative {ECO:0000313|EMBL:CUG88276.1};
GN   ORFNames=BSAL_14695 {ECO:0000313|EMBL:CUG88276.1};
OS   Bodo saltans (Flagellated protozoan).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Eubodonida; Bodonidae; Bodo.
OX   NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG88276.1, 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.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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DR   EMBL; CYKH01001630; CUG88276.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4J9X5; -.
DR   VEuPathDB; TriTrypDB:BSAL_14695; -.
DR   OrthoDB; 2899215at2759; -.
DR   Proteomes; UP000051952; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00433; Peptidase_M17; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR   Pfam; PF00883; Peptidase_M17; 2.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 2.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051952}.
FT   DOMAIN          349..356
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
FT   REGION          479..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   563 AA;  59302 MW;  903F01A55DCA3EAE CRC64;
     MKASSLFPQV VCSSVGCVAS TAAKKSAGFA VSFVRKGTKF EVPDASFKGE VGQLYVDYAK
     ETVTAGVGSE SIGEIQRATH AVVSSARARK ISALDFHLPD AHKANIGKEP SANSLFLHDA
     SAKERNKPAI AQAVACSAVM GTYQYSRMKT SAADKTDAPA LSIRSRGSKS DTAIEAGVVI
     GNAVNDARTL GNLRPDEGNP RFYEAWMRKN IAGMPNVHVR HVIRGRALKE HGLGLMHAVG
     RAAVHEPVLV VLEYRGDKRS DESIGLVGKG LTFDCGGMNV KPYGSMESMH QDMMGAAAVM
     ATMRAVAKLK LPVNVVAVAA FAENAIGPDA YLPSTIIKSL NGKSVEILNT DAEGRLVLAD
     ALTFLQRKAK VTVKPTTVVD LATLTGAILI GLGTERAGLF ANNAKLMNDL MISGARTNEL
     LWPMPIGAEH TKAMKGGIAD LINAAEGRSG GSCTAAAFLQ EFIEKDVNWA HLDIAGTGMG
     KDKATPNQPA GTPGFGKKKS GSCTAAAFLQ EFIEKDVSWA HLDIAGTGMG KDKATPNQPA
     GTPGFGVRLL VDLLQRRCKA FSL
//