RNP2_THEKO
ID RNP2_THEKO Reviewed; 120 AA.
AC Q5JJ62;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Ribonuclease P protein component 2 {ECO:0000255|HAMAP-Rule:MF_00755};
DE Short=RNase P component 2 {ECO:0000255|HAMAP-Rule:MF_00755};
DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00755};
DE AltName: Full=Pop5 {ECO:0000255|HAMAP-Rule:MF_00755};
GN Name=rnp2 {ECO:0000255|HAMAP-Rule:MF_00755}; OrderedLocusNames=TK1767;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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_00755}.
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_00755};
CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC subunits. {ECO:0000255|HAMAP-Rule:MF_00755}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00755}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 2 family. {ECO:0000255|HAMAP-Rule:MF_00755}.
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DR EMBL; AP006878; BAD85956.1; -; Genomic_DNA.
DR RefSeq; WP_011250718.1; NC_006624.1.
DR PDB; 3WZ0; X-ray; 2.79 A; A/C=1-120.
DR PDBsum; 3WZ0; -.
DR AlphaFoldDB; Q5JJ62; -.
DR SMR; Q5JJ62; -.
DR STRING; 69014.TK1767; -.
DR EnsemblBacteria; BAD85956; BAD85956; TK1767.
DR GeneID; 3235444; -.
DR KEGG; tko:TK1767; -.
DR PATRIC; fig|69014.16.peg.1723; -.
DR eggNOG; arCOG01365; Archaea.
DR HOGENOM; CLU_137733_1_0_2; -.
DR InParanoid; Q5JJ62; -.
DR OMA; NPWLIDY; -.
DR OrthoDB; 89278at2157; -.
DR PhylomeDB; Q5JJ62; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000172; C:ribonuclease MRP complex; IBA:GO_Central.
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:0006364; P:rRNA processing; IBA:GO_Central.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR Gene3D; 3.30.70.3250; -; 1.
DR HAMAP; MF_00755; RNase_P_2; 1.
DR InterPro; IPR002759; Pop5/Rpp14/Rnp2-like.
DR InterPro; IPR038085; Rnp2-like_sf.
DR InterPro; IPR016434; Rnp2_archaea.
DR Pfam; PF01900; RNase_P_Rpp14; 1.
DR PIRSF; PIRSF004952; RNase_P_2; 1.
DR SUPFAM; SSF160350; SSF160350; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Nuclease;
KW Reference proteome; tRNA processing.
FT CHAIN 1..120
FT /note="Ribonuclease P protein component 2"
FT /id="PRO_0000140028"
FT STRAND 16..27
FT /evidence="ECO:0007829|PDB:3WZ0"
FT HELIX 31..45
FT /evidence="ECO:0007829|PDB:3WZ0"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:3WZ0"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:3WZ0"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:3WZ0"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:3WZ0"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:3WZ0"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:3WZ0"
FT STRAND 93..105
FT /evidence="ECO:0007829|PDB:3WZ0"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:3WZ0"
FT TURN 113..118
FT /evidence="ECO:0007829|PDB:3WZ0"
SQ SEQUENCE 120 AA; 14047 MW; 2E6A1FF49BAC7239 CRC64;
MREKPKYLPP TLRDKNRYIA FQVIGERPFK KDEIKKAVWE ASLSALGYLG SARAKPWFIK
FDEKSQTGIV RVDRKHVEEL RFALTMLTEI NGSKVIFRTL GVSGTIKRLK RKFLAEYGWR