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   27-MAR-2024, entry version 114.
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}.
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; 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.gene:9378459; -.
DR   EnsemblBacteria; BAA30588; BAA30588; BAA30588.
DR   KEGG; pho:PH1481; -.
DR   eggNOG; arCOG01365; Archaea.
DR   OrthoDB; 19261at2157; -.
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; Ribonuclease P, Pop5 subunit; 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   PANTHER; PTHR15441; RIBONUCLEASE P PROTEIN SUBUNIT P14; 1.
DR   PANTHER; PTHR15441:SF2; RIBONUCLEASE P_MRP PROTEIN SUBUNIT POP5; 1.
DR   Pfam; PF01900; RNase_P_Rpp14; 1.
DR   PIRSF; PIRSF004952; RNase_P_2; 1.
DR   SUPFAM; SSF160350; Rnp2-like; 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
//