ID   RNP3_PYRFU              Reviewed;         214 AA.
AC   Q8TZS0;
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 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=PF1914;
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   INTERACTION WITH RNP2.
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).
RN   [3]
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   [4]
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   [5]
RP   FUNCTION, INTERACTION WITH RNP2, 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).
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_00756,
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_00756, 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 Rnp2 which stimulates the catalytic
CC       RNA. {ECO:0000255|HAMAP-Rule:MF_00756, ECO:0000269|PubMed:17053064,
CC       ECO:0000269|PubMed:21683084, ECO:0000269|PubMed:22298511}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009950; AAL82038.1; -; Genomic_DNA.
DR   RefSeq; WP_011013054.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8TZS0; -.
DR   BMRB; Q8TZS0; -.
DR   SMR; Q8TZS0; -.
DR   IntAct; Q8TZS0; 1.
DR   STRING; 186497.PF1914; -.
DR   EnsemblBacteria; AAL82038; AAL82038; PF1914.
DR   GeneID; 41713735; -.
DR   KEGG; pfu:PF1914; -.
DR   PATRIC; fig|186497.12.peg.1985; -.
DR   eggNOG; arCOG00307; Archaea.
DR   HOGENOM; CLU_1302679_0_0_2; -.
DR   OMA; WFDEVVF; -.
DR   OrthoDB; 66325at2157; -.
DR   PhylomeDB; Q8TZS0; -.
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   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   1: Evidence at protein level;
KW   Cytoplasm; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..214
FT                   /note="Ribonuclease P protein component 3"
FT                   /id="PRO_0000140045"
SQ   SEQUENCE   214 AA;  24495 MW;  A915506635C02CFB CRC64;
     MAGGRNGVKF VEMDIRSREA YELAEEWFDD VVFSYEIPPG VLDKERLKEI KKEYGNVAIT
     LINPKPSLVK EAVQRFKQNY LIYVESSDLR VVRYSIERGV DAVISPWANR KDQGIDHVLA
     RMMNKRGVAL GFSLRPLLHQ NPYERANALK FMRKAWTLVN KYKVPRFISS SAKGKFQVRG
     VKELISLGIA IGMEEVQAKA SLSFYPLGIL ERLK