ID   A0A0S4IT05_BODSA        Unreviewed;       541 AA.
AC   A0A0S4IT05;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=ribonuclease P {ECO:0000256|ARBA:ARBA00012179};
DE            EC=3.1.26.5 {ECO:0000256|ARBA:ARBA00012179};
GN   ORFNames=BSAL_54975 {ECO:0000313|EMBL:CUE73241.1};
OS   Bodo saltans (Flagellated protozoan).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Eubodonida; Bodonidae; Bodo.
OX   NCBI_TaxID=75058 {ECO:0000313|EMBL:CUE73241.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC         from tRNA precursor.; EC=3.1.26.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00000928};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the PPR family. P subfamily.
CC       {ECO:0000256|ARBA:ARBA00007626}.
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DR   EMBL; CYKH01000145; CUE73241.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4IT05; -.
DR   VEuPathDB; TriTrypDB:BSAL_54975; -.
DR   OMA; QLVRWKS; -.
DR   OrthoDB; 47419at2759; -.
DR   Proteomes; UP000051952; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.11980; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR031595; PRORP_C.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR13547:SF1; MITOCHONDRIAL RIBONUCLEASE P CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR13547; UNCHARACTERIZED; 1.
DR   Pfam; PF16953; PRORP; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051952};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          366..539
FT                   /note="PRORP"
FT                   /evidence="ECO:0000259|Pfam:PF16953"
SQ   SEQUENCE   541 AA;  60509 MW;  CC4017C60A3F1BBB CRC64;
     MRLWLRLWRV APISTHCTLR FSCEKLNQGI APPEGKSKKR VRHPIDGFIA AGDMTAAFAA
     LQSIPANELN PKHVAAVLHM TEKEGHRDMT AVIVERIVRS NSSMWDENIL SVWLRHQCHS
     GDFQAAWATA SMIASRSGGL WKKRNLSPLL AFACLSGQRA NVMELLHHAR TCSVPLDVDD
     VHVLVRYFSS THEPLTTLHH LLQLVVEYLP HINGETASFL EHWCKAVGGV TAATTCVDPS
     SGMCACCGTQ MHGLPFTAEH KEKVLEGIRV AAGVTRRNDA ALAARRKRSF EAWTKSMITF
     APLQTADILI DGANVGYYGL SSWYHIVKEE MVKHCTAHFP DRLARLHKGT TWSKKLPFVD
     VPVSMELIDE AMSQAKAAGL RPLLLLHERH VEPHNMFPKA HAILNKWKAA NEVITTPGGL
     NDDVCWLHAA ITRCTPTDVG ATTGQRPDLL VLTNDAMRDH HFQLLHQRSF VAWRGRHQVK
     FSCVRENECT RVQMTPPSTF TSCIQHNVAR CAWHLPVIEA TVGETVPELE DKNTTQWLCI
     R
//