ID A0A022RDL3_ERYGU Unreviewed; 510 AA.
AC A0A022RDL3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=ribonuclease P {ECO:0000256|ARBA:ARBA00012179};
DE EC=3.1.26.5 {ECO:0000256|ARBA:ARBA00012179};
GN ORFNames=MIMGU_mgv1a004795mg {ECO:0000313|EMBL:EYU36960.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU36960.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU36960.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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}.
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DR EMBL; KI630578; EYU36960.1; -; Genomic_DNA.
DR RefSeq; XP_012837970.1; XM_012982516.1.
DR AlphaFoldDB; A0A022RDL3; -.
DR STRING; 4155.A0A022RDL3; -.
DR GeneID; 105958516; -.
DR KEGG; egt:105958516; -.
DR eggNOG; KOG1347; Eukaryota.
DR OMA; ASHGCEQ; -.
DR OrthoDB; 47419at2759; -.
DR PhylomeDB; A0A022RDL3; -.
DR Proteomes; UP000030748; 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; IBA:GO_Central.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IBA:GO_Central.
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:SF13; PROTEINACEOUS RNASE P 2; 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 Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 7..216
FT /note="Pentacotripeptide-repeat region of PRORP"
FT /evidence="ECO:0000259|Pfam:PF17177"
FT DOMAIN 258..485
FT /note="PRORP"
FT /evidence="ECO:0000259|Pfam:PF16953"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 57092 MW; 2BE168ABA9DD6AEE CRC64;
MDHHNTRRKK QKLSPESQFR STLDQCSKTK DLTAAISLYE SSPSPTLTLG NLNSFLYICS
NSLSDPETRQ PAIEFGFKLF HHHSDGDNFK PNEATLTALS RLAAARGDGD YAFELAKSVK
KYGVAPKLRT FSPALICFCG GAAAAADKAY EVEEYVESVG LHLEEPELAA LLKVSIESGK
EKKVYEYLHK LRATLREVDE STVAIIESWF SGKNAADVSV VSLDSDRIRE ANTRNGGGWH
GLGFLGNGEW ALQRSKIASY GQCCACNEQL VCVDTDTEET EKFAQSVASL AMERELHSNF
KEFQDWLEKH SEYETVVDGA NIGLYQQNFA EGGFSVTQLD AVVKETHSKS KKWPLVVMHK
KRVRSILEDA SKRELIEEWL DQGVLYGTPY GSNDDWYWLY AAVKLKCLLV TNDEMRDHIF
ELIGSNFFSR WKERHQVRYT FTKGGGLKLI MPPSYSLVIQ ESEKGSWHVP IAGEISDESS
RTWLCVTRSG SIDAEEVSGN LIRNGSNNTS
//
