ID G3T4I4_LOXAF Unreviewed; 395 AA.
AC G3T4I4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=ribonuclease P {ECO:0000256|ARBA:ARBA00012179};
DE EC=3.1.26.5 {ECO:0000256|ARBA:ARBA00012179};
GN Name=PRORP {ECO:0000313|Ensembl:ENSLAFP00000008272.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000008272.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000008272.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000008272.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000008272.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000008272.3};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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 AlphaFoldDB; G3T4I4; -.
DR Ensembl; ENSLAFT00000009871.3; ENSLAFP00000008272.3; ENSLAFG00000009871.3.
DR GeneTree; ENSGT00390000002201; -.
DR HOGENOM; CLU_033070_0_0_1; -.
DR Proteomes; UP000007646; 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:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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:UP000007646};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 343..390
FT /note="PRORP"
FT /evidence="ECO:0000259|Pfam:PF16953"
FT REGION 95..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 45568 MW; 5163D37C62C17EE9 CRC64;
MTFCLSGFRS FSKLWKNNPY LGLVPGYSPH SLFLVDSYGI WNRQRWFSLK TVSPQNTKAL
NLLKAKTRYH RKGDEGSNKQ VSSDSPHLFA AGAARKRAEM NPQSKEPVSS PVRDTIQLPT
RPLNSEEWDK LKEDFKGKGN FENWISSQIT YSRSSIDVAK SLLAWVAAKN NGIVSYDLLV
KYLYLCVFHK QKSEIIDVYE IMKVRYKILE PAGYSLLIRG LIHTDRWREA LLLLEDFEKV
MIPSKRNYDD CIQGALLHQD VNTAWNLYQK LLGHDLIPML ETLEAFFDFG KDIKDHQYAN
KLLDILLYLR NNQLYPGESF AHSIKAWFES VPGEQWKGQF TTIRKSGRCS GCGKTMESIY
LSPEEYEFLK ENIMRNVIDG GDQYKKTTPE SGIAW
//