RNP3_THEGJ
ID RNP3_THEGJ Reviewed; 214 AA.
AC C5A1N9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=TGAM_1806;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
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; CP001398; ACS34308.1; -; Genomic_DNA.
DR RefSeq; WP_015859417.1; NC_012804.1.
DR AlphaFoldDB; C5A1N9; -.
DR SMR; C5A1N9; -.
DR STRING; 593117.TGAM_1806; -.
DR PaxDb; C5A1N9; -.
DR EnsemblBacteria; ACS34308; ACS34308; TGAM_1806.
DR GeneID; 7987633; -.
DR KEGG; tga:TGAM_1806; -.
DR PATRIC; fig|593117.10.peg.1815; -.
DR eggNOG; arCOG00307; Archaea.
DR HOGENOM; CLU_1302679_0_0_2; -.
DR OMA; WFDEVVF; -.
DR OrthoDB; 66325at2157; -.
DR Proteomes; UP000001488; 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 Pfam; PF01876; RNase_P_p30; 1.
DR SUPFAM; SSF89550; SSF89550; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Nuclease; tRNA processing.
FT CHAIN 1..214
FT /note="Ribonuclease P protein component 3"
FT /id="PRO_1000212861"
SQ SEQUENCE 214 AA; 24783 MW; 5A80B2DCB7833547 CRC64;
MSEREYFVEM DVRSVEAYEL AKEWFDEVVF TKKLILDTEP DWDSLKEELR ELRRTYGKVA
VLLVTRKPSL IRTFKARNLK ALLYVQGGDM RVNRMAIEAK VDALISPWLG RKDYGFDHTL
AGMAGRRGVA IGFSLSPLLR ANPYERALTL RFMAKVWELV RKYRVPRFIT SSAESKWEVR
GPRDLMSLGI NIGMEIPEAR ASLNFHPRSL LSRL