ID A0A0B2QRJ0_GLYSO Unreviewed; 420 AA.
AC A0A0B2QRJ0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=ribonuclease P {ECO:0000256|ARBA:ARBA00012179};
DE EC=3.1.26.5 {ECO:0000256|ARBA:ARBA00012179};
GN ORFNames=glysoja_041173 {ECO:0000313|EMBL:KHN22498.1};
OS Glycine soja (Wild soybean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN22498.1};
RN [1] {ECO:0000313|EMBL:KHN22498.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Root {ECO:0000313|EMBL:KHN22498.1};
RA Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT "Identification of a novel salt tolerance gene in wild soybean by whole-
RT genome sequencing.";
RL Submitted (JUL-2014) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN657291; KHN22498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2QRJ0; -.
DR Proteomes; UP000053555; 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 CDD; cd18671; PIN_PRORP-Zc3h12a-like; 1.
DR Gene3D; 3.40.50.11980; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR033443; PPR_long.
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; PF17177; PPR_long; 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 tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..131
FT /note="Pentacotripeptide-repeat region of PRORP"
FT /evidence="ECO:0000259|Pfam:PF17177"
FT DOMAIN 172..398
FT /note="PRORP"
FT /evidence="ECO:0000259|Pfam:PF16953"
SQ SEQUENCE 420 AA; 47039 MW; C0D7D3674420121A CRC64;
MLNDRVQPNE ATFTNAARLA AANEDPDMAF ELLKQMKNVA IAPKLRSYEP ALFGFCKRGD
AEKAYLVDAD MVESGIVAEE PELSALLEVS VNAKKEDKVY DILHRLRSTL RQVSESTLGI
VEDWFNSEYA AKIGKEKWDV KKVREGIAQG GGGWHGQGWL GSGRWKVANT QVNEDGVCPL
CGEKLVSIDI DPKETENFAA SLSKLACQKE AKANFVHFQT WLEQHGPFDA VVDGANVGLA
NGHNFSFSQL NTVVEQLRQI SPSKRLPLII LHISRVRGGP AQNPKNMRLI ENWKKNGALY
ATPQGSNDDW YWLYAAVSCK CLLLTNDEMR DHLFQLLGSN FFPRWKEKHQ VRTSASTCGH
SIIMPPRYSI VIQESANGSW HVPTVTTDDH EIPRKWLCAT RSRKDSLHNL WTSSSKSDCT
//