RNP3_METMA
ID RNP3_METMA Reviewed; 239 AA.
AC Q8PTU3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Ribonuclease P protein component 3 {ECO:0000255|HAMAP-Rule:MF_00756};
DE Short=RNase P component 3 {ECO:0000255|HAMAP-Rule:MF_00756};
DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00756};
DE AltName: Full=Rpp30 {ECO:0000255|HAMAP-Rule:MF_00756};
GN Name=rnp3 {ECO:0000255|HAMAP-Rule:MF_00756}; OrderedLocusNames=MM_2618;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC -!- FUNCTION: Part of ribonuclease P, a protein complex that generates
CC mature tRNA molecules by cleaving their 5'-ends. {ECO:0000255|HAMAP-
CC Rule:MF_00756}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00756};
CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC subunits. {ECO:0000255|HAMAP-Rule:MF_00756}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00756}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 3 family. {ECO:0000255|HAMAP-Rule:MF_00756}.
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DR EMBL; AE008384; AAM32314.1; -; Genomic_DNA.
DR RefSeq; WP_011034531.1; NC_003901.1.
DR AlphaFoldDB; Q8PTU3; -.
DR SMR; Q8PTU3; -.
DR STRING; 192952.MM_2618; -.
DR EnsemblBacteria; AAM32314; AAM32314; MM_2618.
DR GeneID; 44088070; -.
DR GeneID; 66134561; -.
DR KEGG; mma:MM_2618; -.
DR PATRIC; fig|192952.21.peg.3011; -.
DR eggNOG; arCOG00307; Archaea.
DR HOGENOM; CLU_074509_1_0_2; -.
DR OMA; INRAACE; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030677; C:ribonuclease P complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00756; RNase_P_3; 1.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR023539; RNase_P_comp-3_arc.
DR InterPro; IPR002738; RNase_P_p30.
DR PANTHER; PTHR13031; PTHR13031; 1.
DR Pfam; PF01876; RNase_P_p30; 1.
DR SUPFAM; SSF89550; SSF89550; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW tRNA processing.
FT CHAIN 1..239
FT /note="Ribonuclease P protein component 3"
FT /id="PRO_0000140041"
SQ SEQUENCE 239 AA; 26002 MW; 4753C3632EAA7063 CRC64;
MGKPEFYDFC VHAVPDGANA VEELSSLSRH LGYSGIALAN HSDKLPSKKP VLPSIEGFEV
FRGIELVEEN PSKLHGLVGK FRSSMDVLIV HGGSEAVNRA ALENPRVDIL NHPAFDKSSG
LNQVLAKAAA ENGVAIGITL RPLLHSRGSR RIRMLSDLKA NLELARKYDV PLVLCSDAMS
CYDLRSPMET LAFAEVCGLE EDEALDALST VPKKIIKKNR PGPGYVREGI EVLEGEDIF
