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Database: UniProt
Entry: A0A0B2QRJ0_GLYSO
LinkDB: A0A0B2QRJ0_GLYSO
Original site: A0A0B2QRJ0_GLYSO 
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}.
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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
//
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