RNP1_PYRFU
ID RNP1_PYRFU Reviewed; 127 AA.
AC Q8U007;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Ribonuclease P protein component 1 {ECO:0000255|HAMAP-Rule:MF_00754};
DE Short=RNase P component 1 {ECO:0000255|HAMAP-Rule:MF_00754};
DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00754};
DE AltName: Full=Rpp29 {ECO:0000255|HAMAP-Rule:MF_00754};
GN Name=rnp1 {ECO:0000255|HAMAP-Rule:MF_00754}; OrderedLocusNames=PF1816;
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 INTERACTION WITH RNP1, AND SUBUNIT.
RX PubMed=18922021; DOI=10.1021/bi8015982;
RA Amero C.D., Boomershine W.P., Xu Y., Foster M.;
RT "Solution structure of Pyrococcus furiosus RPP21, a component of the
RT archaeal RNase P holoenzyme, and interactions with its RPP29 protein
RT partner.";
RL Biochemistry 47:11704-11710(2008).
RN [4]
RP FUNCTION, INTERACTION WITH RNP4, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP 1-MET--GLN-17; 1-MET--ILE-24 AND 1-MET--ARG-31.
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 [5]
RP FUNCTION, INTERACTION WITH RNP4, 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 [6]
RP STRUCTURE BY NMR, INTERACTION WITH RNP4, AND SUBUNIT.
RX PubMed=19733182; DOI=10.1016/j.jmb.2009.08.068;
RA Xu Y., Amero C.D., Pulukkunat D.K., Gopalan V., Foster M.P.;
RT "Solution structure of an archaeal RNase P binary protein complex:
RT formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29
RT is accompanied by coupled protein folding and highlights critical features
RT for protein-protein and protein-RNA interactions.";
RL J. Mol. Biol. 393:1043-1055(2009).
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_00754,
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_00754, 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 protein
CC subunits. Forms a subcomplex with Rnp4 which stimulates the catalytic
CC RNA. {ECO:0000269|PubMed:17053064, ECO:0000269|PubMed:18922021,
CC ECO:0000269|PubMed:19733182, ECO:0000269|PubMed:21683084,
CC ECO:0000269|PubMed:22298511}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00754}.
CC -!- DOMAIN: Interaction with Rnp4 is mediated by the N-terminus; short
CC deletion mutants are still able to reconstitute RNase P activity.
CC {ECO:0000269|PubMed:21683084}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 1 family. {ECO:0000255|HAMAP-Rule:MF_00754}.
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DR EMBL; AE009950; AAL81940.1; -; Genomic_DNA.
DR PDB; 2KI7; NMR; -; A=1-127.
DR PDBsum; 2KI7; -.
DR AlphaFoldDB; Q8U007; -.
DR BMRB; Q8U007; -.
DR SMR; Q8U007; -.
DR STRING; 186497.PF1816; -.
DR EnsemblBacteria; AAL81940; AAL81940; PF1816.
DR KEGG; pfu:PF1816; -.
DR PATRIC; fig|186497.12.peg.1887; -.
DR eggNOG; arCOG00784; Archaea.
DR HOGENOM; CLU_107020_1_0_2; -.
DR OMA; WHELIGL; -.
DR PhylomeDB; Q8U007; -.
DR EvolutionaryTrace; Q8U007; -.
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:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.30.210; -; 1.
DR HAMAP; MF_00754; RNase_P_1; 1.
DR InterPro; IPR036980; RNase_P/MRP_Rpp29_sf.
DR InterPro; IPR023538; RNP1.
DR InterPro; IPR023534; Rof/RNase_P-like.
DR InterPro; IPR002730; Rpp29/RNP1.
DR Pfam; PF01868; RNase_P-MRP_p29; 1.
DR SMART; SM00538; POP4; 1.
DR SUPFAM; SSF101744; SSF101744; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Nuclease;
KW Reference proteome; tRNA processing.
FT CHAIN 1..127
FT /note="Ribonuclease P protein component 1"
FT /id="PRO_0000128436"
FT MUTAGEN 1..31
FT /note="Missing: No interaction with Rnp4, does not
FT reconstitute RNase P activity."
FT /evidence="ECO:0000269|PubMed:21683084"
FT MUTAGEN 1..24
FT /note="Missing: No interaction with Rnp4, reconstitutes
FT RNase P activity."
FT /evidence="ECO:0000269|PubMed:21683084"
FT MUTAGEN 1..17
FT /note="Missing: Interacts normally with Rnp4, reconstitutes
FT RNase P activity."
FT /evidence="ECO:0000269|PubMed:21683084"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:2KI7"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:2KI7"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:2KI7"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:2KI7"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:2KI7"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:2KI7"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:2KI7"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:2KI7"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:2KI7"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:2KI7"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:2KI7"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:2KI7"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:2KI7"
SQ SEQUENCE 127 AA; 14953 MW; 3CBBA84DD7AE7E4C CRC64;
MWRNSEEREN RTSGRSQGSY QEIIGRTWIF RGAHRGRVNK KNIVWHELIG LKVRVVNSTH
PGYVGIEGYV IDETRNMLVI AGENKVWKVP KDVCIFEFET WDGTKIKISG EKLVGRPEMR
LKKRWRK
