RNP2_PYRFU
ID RNP2_PYRFU Reviewed; 120 AA.
AC Q8U151;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=PF1378;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=17053064; DOI=10.1073/pnas.0608000103;
RA Tsai H.Y., Pulukkunat D.K., Woznick W.K., Gopalan V.;
RT "Functional reconstitution and characterization of Pyrococcus furiosus
RT RNase P.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16147-16152(2006).
RN [3]
RP FUNCTION, AND SUBUNIT.
RX PubMed=21683084; DOI=10.1016/j.jmb.2011.05.012;
RA Chen W.Y., Xu Y., Cho I.M., Oruganti S.V., Foster M.P., Gopalan V.;
RT "Cooperative RNP assembly: complementary rescue of structural defects by
RT protein and RNA subunits of archaeal RNase P.";
RL J. Mol. Biol. 411:368-383(2011).
RN [4]
RP FUNCTION, INTERACTION WITH RNP3, AND SUBUNIT.
RX PubMed=22298511; DOI=10.1093/nar/gks013;
RA Chen W.Y., Singh D., Lai L.B., Stiffler M.A., Lai H.D., Foster M.P.,
RA Gopalan V.;
RT "Fidelity of tRNA 5'-maturation: a possible basis for the functional
RT dependence of archaeal and eukaryal RNase P on multiple protein
RT cofactors.";
RL Nucleic Acids Res. 40:4666-4680(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS), INTERACTION WITH RNP3, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=16418270; DOI=10.1073/pnas.0508004103;
RA Wilson R.C., Bohlen C.J., Foster M.P., Bell C.E.;
RT "Structure of Pfu Pop5, an archaeal RNase P protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:873-878(2006).
CC -!- FUNCTION: Part of ribonuclease P, a protein complex that generates
CC mature tRNA molecules by cleaving their 5'-ends. The RNA is catalytic,
CC but its KM for pre-tRNA is 170-fold decreased in the presence of the 4
CC known protein subunits (Rnp1-4). The protein subunits also decrease the
CC amount of Mg(2+) needed for activity. {ECO:0000255|HAMAP-Rule:MF_00755,
CC ECO:0000269|PubMed:17053064, ECO:0000269|PubMed:21683084,
CC ECO:0000269|PubMed:22298511}.
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, ECO:0000269|PubMed:17053064};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.18 uM for E.coli pre-tRNA(Tyr) {ECO:0000269|PubMed:17053064};
CC Note=kcat is 9.5 min(-1). For enzyme reconstituted with RNA and 4
CC known subunits (Rnp1-4).;
CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC subunits. Forms a subcomplex with Rnp3 which stimulates the catalytic
CC RNA. {ECO:0000255|HAMAP-Rule:MF_00755, ECO:0000269|PubMed:16418270,
CC ECO:0000269|PubMed:17053064, ECO:0000269|PubMed:21683084,
CC ECO:0000269|PubMed:22298511}.
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; AE009950; AAL81502.1; -; Genomic_DNA.
DR RefSeq; WP_011012525.1; NZ_CP023154.1.
DR PDB; 2AV5; X-ray; 3.15 A; A/B/C/D/E=1-120.
DR PDBsum; 2AV5; -.
DR AlphaFoldDB; Q8U151; -.
DR BMRB; Q8U151; -.
DR SMR; Q8U151; -.
DR IntAct; Q8U151; 1.
DR STRING; 186497.PF1378; -.
DR EnsemblBacteria; AAL81502; AAL81502; PF1378.
DR GeneID; 41713186; -.
DR KEGG; pfu:PF1378; -.
DR PATRIC; fig|186497.12.peg.1441; -.
DR eggNOG; arCOG01365; Archaea.
DR HOGENOM; CLU_137733_1_0_2; -.
DR OMA; NPWLIDY; -.
DR OrthoDB; 89278at2157; -.
DR PhylomeDB; Q8U151; -.
DR BRENDA; 3.1.26.5; 5243.
DR EvolutionaryTrace; Q8U151; -.
DR Proteomes; UP000001013; 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; 3.30.70.3250; -; 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_0000140026"
FT STRAND 16..27
FT /evidence="ECO:0007829|PDB:2AV5"
FT HELIX 31..54
FT /evidence="ECO:0007829|PDB:2AV5"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:2AV5"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:2AV5"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:2AV5"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2AV5"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:2AV5"
FT STRAND 93..105
FT /evidence="ECO:0007829|PDB:2AV5"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:2AV5"
FT TURN 113..118
FT /evidence="ECO:0007829|PDB:2AV5"
SQ SEQUENCE 120 AA; 13839 MW; B690DF4C26299915 CRC64;
MSERPKTLPP TLRDKKRYIA FKVISENQFN KDEIKEAIWN ACLRTLGELG TAKAKPWLIK
FDETTQTGII RCDRNHVYDV IFSLTLVSDI NGNKAIIKVL GVSGTIKRLK RKFLSQFGWR
