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   27-MAR-2024, entry version 69.
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};
GN   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; 593117-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   OrthoDB; 85765at2157; -.
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   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
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; PHP domain-like; 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
//