ID A0A1X0P3X4_9TRYP Unreviewed; 563 AA.
AC A0A1X0P3X4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=ribonuclease P {ECO:0000256|ARBA:ARBA00012179};
DE EC=3.1.26.5 {ECO:0000256|ARBA:ARBA00012179};
GN ORFNames=TM35_000051340 {ECO:0000313|EMBL:ORC91538.1};
OS Trypanosoma theileri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=67003 {ECO:0000313|EMBL:ORC91538.1, ECO:0000313|Proteomes:UP000192257};
RN [1] {ECO:0000313|EMBL:ORC91538.1, ECO:0000313|Proteomes:UP000192257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Edinburgh {ECO:0000313|EMBL:ORC91538.1};
RA Kelly S., Ivens A., Mott A., O'Neill E., Emms D., Macleod O., Voorheis P.,
RA Matthews J., Matthews K., Carrington M.;
RT "An alternative strategy for trypanosome survival in the mammalian
RT bloodstream revealed through genome and transcriptome analysis of the
RT ubiquitous bovine parasite Trypanosoma (Megatrypanum) theileri.";
RL Submitted (MAR-2017) 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 -!- SIMILARITY: Belongs to the PPR family. P subfamily.
CC {ECO:0000256|ARBA:ARBA00007626}.
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:ORC91538.1}.
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DR EMBL; NBCO01000005; ORC91538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0P3X4; -.
DR STRING; 67003.A0A1X0P3X4; -.
DR VEuPathDB; TriTrypDB:TM35_000051340; -.
DR OrthoDB; 47419at2759; -.
DR Proteomes; UP000192257; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
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:SF19; RIBONUCLEASE P; 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 Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000192257};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 362..518
FT /note="PRORP"
FT /evidence="ECO:0000259|Pfam:PF16953"
FT REGION 508..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 63951 MW; 0761D88DA0B74799 CRC64;
MRRISTAVAL QWFSLGHPLC SFQTRWKSCS PAEELQRRVG QLVSKRNVDQ VSHEIRDALG
KSIFSMKAFA SALFLCEQTQ NEVVGIELVR QVQASNLVES WDDESVLSVV LRLQCSVGDA
AAATQMFSFL VSKKLLRLRS TSVFLGFWCK RLDRSMAFAV YAEALRQGIE LRALDYVELG
RLCVALQEPI STLHYILREM QEHVLSVPAV MLTDVLSPWA QRAGLRVESV SFPHSDPTRP
PGTCSCCGAL LKGHRFTTAQ KTRLLKDVVE VALVAQRKKS ARVRIGFEAW RRFVALHGQR
IDVLIDGANL GYYGLSSWYA DAKRALLLKR GKREEDIKPQ DIVWSKQGSV DVGVNFHLID
LAVQEARRRG MRPLIILHER HCETKNMTSS DEVLAAQWRR DGILYCTPSG LNDDLCWLYA
ALELTTPTDA VAGTVEKTVW VLTNDLMRDH HFKLLSPRFF ARWRDRHRIA FKCSRKDNCT
LLHWELPVPY AQCIQEVEPL KWHIPIATEK EEGEEVEENK EEEEKKKDAV DENSNLQENQ
EGNDNNGMAV VPSQVSHTWA CIG
//
