RNP2_PYRHO
ID RNP2_PYRHO Reviewed; 120 AA.
AC O59150;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 110.
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=PH1481;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=12810070; DOI=10.1016/s0006-291x(03)01034-9;
RA Kouzuma Y., Mizoguchi M., Takagi H., Fukuhara H., Tsukamoto M., Numata T.,
RA Kimura M.;
RT "Reconstitution of archaeal ribonuclease P from RNA and four protein
RT components.";
RL Biochem. Biophys. Res. Commun. 306:666-673(2003).
RN [3]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=16574071; DOI=10.1016/j.bbrc.2006.02.192;
RA Fukuhara H., Kifusa M., Watanabe M., Terada A., Honda T., Numata T.,
RA Kakuta Y., Kimura M.;
RT "A fifth protein subunit Ph1496p elevates the optimum temperature for the
RT ribonuclease P activity from Pyrococcus horikoshii OT3.";
RL Biochem. Biophys. Res. Commun. 343:956-964(2006).
RN [4]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=16829535; DOI=10.1093/jb/mvj144;
RA Terada A., Honda T., Fukuhara H., Hada K., Kimura M.;
RT "Characterization of the archaeal ribonuclease P proteins from Pyrococcus
RT horikoshii OT3.";
RL J. Biochem. 140:293-298(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RNP3, SUBUNIT, AND
RP MUTAGENESIS OF 43-LEU--GLU-48 AND CYS-72.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=16430919; DOI=10.1016/j.jmb.2005.12.086;
RA Kawano S., Nakashima T., Kakuta Y., Tanaka I., Kimura M.;
RT "Crystal structure of protein Ph1481p in complex with protein Ph1877p of
RT archaeal RNase P from Pyrococcus horikoshii OT3: implication of dimer
RT formation of the holoenzyme.";
RL J. Mol. Biol. 357:583-591(2006).
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, ECO:0000269|PubMed:12810070,
CC ECO:0000269|PubMed:16574071, ECO:0000269|PubMed:16829535}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:12810070, ECO:0000269|PubMed:16574071};
CC -!- SUBUNIT: Homodimer in solution. Component of RNase P which consists of
CC a catalytic RNA component and at least 5 protein subunits. Forms a
CC heterotetrameric subcomplex with Rnp3. Reconstituted enzyme missing
CC individual protein subunits is suboptimally active, showing each
CC subunit contributes to optimization of activity.
CC {ECO:0000269|PubMed:12810070, ECO:0000269|PubMed:16430919,
CC ECO:0000269|PubMed:16574071, ECO:0000269|PubMed:16829535}.
CC -!- INTERACTION:
CC O59150; O59543: rnp3; NbExp=2; IntAct=EBI-2603177, EBI-2603192;
CC O59150; O59248: rnp4; NbExp=3; IntAct=EBI-2603177, EBI-2641275;
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; BA000001; BAA30588.1; -; Genomic_DNA.
DR PIR; D71023; D71023.
DR PDB; 2CZV; X-ray; 2.00 A; C/D=1-120.
DR PDBsum; 2CZV; -.
DR AlphaFoldDB; O59150; -.
DR SMR; O59150; -.
DR IntAct; O59150; 2.
DR STRING; 70601.3257905; -.
DR EnsemblBacteria; BAA30588; BAA30588; BAA30588.
DR KEGG; pho:PH1481; -.
DR eggNOG; arCOG01365; Archaea.
DR OMA; NPWLIDY; -.
DR BRENDA; 3.1.26.5; 5244.
DR EvolutionaryTrace; O59150; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030677; C:ribonuclease P complex; IDA:UniProtKB.
DR GO; GO:0004526; F:ribonuclease P activity; IDA:UniProtKB.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:UniProtKB.
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 tRNA processing.
FT CHAIN 1..120
FT /note="Ribonuclease P protein component 2"
FT /id="PRO_0000140027"
FT MUTAGEN 43..48
FT /note="Missing: Forms heterodimer with Rnp3, but not
FT heterotetramer. Does not reconstitute RNase P activity."
FT /evidence="ECO:0000269|PubMed:16430919"
FT MUTAGEN 72
FT /note="C->S: Fully reconstitutes RNase P activity."
FT /evidence="ECO:0000269|PubMed:16430919"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:2CZV"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:2CZV"
FT HELIX 31..54
FT /evidence="ECO:0007829|PDB:2CZV"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:2CZV"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:2CZV"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:2CZV"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2CZV"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:2CZV"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:2CZV"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:2CZV"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2CZV"
SQ SEQUENCE 120 AA; 14044 MW; C78C9EF6C5380E53 CRC64;
MMRKLKTLPP TLRDKNRYIA FEIISDGDFT KDEVKELIWK SSLEVLGETG TAIVKPWLIK
FDPNTKTGIV RCDREYVEYL RFALMLVSEF NGKRLIIRTL GVSGTIKRLK RKFLAKYGWK
