ID   RNP1_PYRHO              Reviewed;         127 AA.
AC   O59425;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 123.
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=PH1771;
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, SUBUNIT, AND RNA-BINDING.
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) OF 32-127.
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=15317976; DOI=10.1261/rna.7560904;
RA   Numata T., Ishimatsu I., Kakuta Y., Tanaka I., Kimura M.;
RT   "Crystal structure of archaeal ribonuclease P protein Ph1771p from
RT   Pyrococcus horikoshii OT3: an archaeal homolog of eukaryotic ribonuclease P
RT   protein Rpp29.";
RL   RNA 10:1423-1432(2004).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) IN COMPLEX WITH RNP4, FUNCTION,
RP   SUBUNIT, AND MUTAGENESIS OF 1-MET--ARG-31; GLU-47; GLU-73; ARG-75; LYS-90;
RP   PHE-95; ARG-115; 118-MET--TRP-127; LYS-121; 121-LYS-LYS-122; LYS-122 AND
RP   124-TRP--TRP-127.
RX   PubMed=18929577; DOI=10.1016/j.jmb.2008.09.056;
RA   Honda T., Kakuta Y., Kimura K., Saho J., Kimura M.;
RT   "Structure of an archaeal homolog of the human protein complex Rpp21-Rpp29
RT   that is a key core component for the assembly of active ribonuclease P.";
RL   J. Mol. Biol. 384:652-662(2008).
CC   -!- FUNCTION: Part of ribonuclease P (RNase P), a protein complex that
CC       generates mature tRNA molecules by cleaving their 5'-ends. Binds RNase
CC       P RNA. {ECO:0000269|PubMed:12810070, ECO:0000269|PubMed:16574071,
CC       ECO:0000269|PubMed:16829535, ECO:0000269|PubMed:18929577}.
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};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius.
CC         {ECO:0000269|PubMed:12810070, ECO:0000269|PubMed:16574071};
CC   -!- SUBUNIT: Consists of a catalytic RNA component and at least 5 protein
CC       subunits. Forms a heterodimeric subcomplex with Rnp4. Reconstituted
CC       enzyme missing individual protein subunits is suboptimally active,
CC       showing each subunit contributes to optimization of activity.
CC       {ECO:0000269|PubMed:12810070, ECO:0000269|PubMed:16574071,
CC       ECO:0000269|PubMed:16829535, ECO:0000269|PubMed:18929577}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00754}.
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; BA000001; BAA30886.1; -; Genomic_DNA.
DR   PIR; G71186; G71186.
DR   PDB; 1V76; X-ray; 2.00 A; A/B=32-127.
DR   PDB; 2ZAE; X-ray; 2.21 A; A/C=1-127.
DR   PDBsum; 1V76; -.
DR   PDBsum; 2ZAE; -.
DR   AlphaFoldDB; O59425; -.
DR   SMR; O59425; -.
DR   IntAct; O59425; 1.
DR   STRING; 70601.gene:9378769; -.
DR   EnsemblBacteria; BAA30886; BAA30886; BAA30886.
DR   KEGG; pho:PH1771; -.
DR   eggNOG; arCOG00784; Archaea.
DR   OrthoDB; 39019at2157; -.
DR   BRENDA; 3.1.26.5; 5244.
DR   EvolutionaryTrace; O59425; -.
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:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IDA:UniProtKB.
DR   Gene3D; 2.30.30.210; Ribonuclease P/MRP, subunit p29; 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; Rof/RNase P subunit-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Endonuclease; Hydrolase; Nuclease;
KW   tRNA processing.
FT   CHAIN           1..127
FT                   /note="Ribonuclease P protein component 1"
FT                   /id="PRO_0000128437"
FT   MUTAGEN         1..31
FT                   /note="Missing: Does not reconstitute RNase P activity, no
FT                   longer interacts with Rnp4."
FT                   /evidence="ECO:0000269|PubMed:18929577"
FT   MUTAGEN         47
FT                   /note="E->A: Fully reconstitutes RNase P activity."
FT                   /evidence="ECO:0000269|PubMed:18929577"
FT   MUTAGEN         73
FT                   /note="E->A: 40% reconstituted RNase P activity."
FT                   /evidence="ECO:0000269|PubMed:18929577"
FT   MUTAGEN         75
FT                   /note="R->A: 40% reconstituted RNase P activity."
FT                   /evidence="ECO:0000269|PubMed:18929577"
FT   MUTAGEN         90
FT                   /note="K->A: 10% reconstituted RNase P activity."
FT                   /evidence="ECO:0000269|PubMed:18929577"
FT   MUTAGEN         95
FT                   /note="F->A: 75% reconstituted RNase P activity."
FT                   /evidence="ECO:0000269|PubMed:18929577"
FT   MUTAGEN         115
FT                   /note="R->A: 75% reconstituted RNase P activity."
FT                   /evidence="ECO:0000269|PubMed:18929577"
FT   MUTAGEN         118..127
FT                   /note="Missing: Does not reconstitute RNase P activity."
FT                   /evidence="ECO:0000269|PubMed:18929577"
FT   MUTAGEN         121..122
FT                   /note="KK->AA: 60% reconstituted RNase P activity."
FT                   /evidence="ECO:0000269|PubMed:18929577"
FT   MUTAGEN         121
FT                   /note="K->A: 90% reconstituted RNase P activity."
FT                   /evidence="ECO:0000269|PubMed:18929577"
FT   MUTAGEN         122
FT                   /note="K->A: Fully reconstitutes RNase P activity."
FT                   /evidence="ECO:0000269|PubMed:18929577"
FT   MUTAGEN         124..127
FT                   /note="Missing: Fully reconstitutes RNase P activity."
FT                   /evidence="ECO:0000269|PubMed:18929577"
FT   HELIX           21..23
FT                   /evidence="ECO:0007829|PDB:2ZAE"
FT   HELIX           27..30
FT                   /evidence="ECO:0007829|PDB:2ZAE"
FT   TURN            31..33
FT                   /evidence="ECO:0007829|PDB:2ZAE"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:1V76"
FT   STRAND          52..60
FT                   /evidence="ECO:0007829|PDB:1V76"
FT   HELIX           61..63
FT                   /evidence="ECO:0007829|PDB:1V76"
FT   STRAND          67..73
FT                   /evidence="ECO:0007829|PDB:1V76"
FT   STRAND          75..90
FT                   /evidence="ECO:0007829|PDB:1V76"
FT   STRAND          93..98
FT                   /evidence="ECO:0007829|PDB:1V76"
FT   STRAND          104..108
FT                   /evidence="ECO:0007829|PDB:1V76"
FT   HELIX           109..112
FT                   /evidence="ECO:0007829|PDB:1V76"
FT   HELIX           116..119
FT                   /evidence="ECO:0007829|PDB:1V76"
FT   HELIX           120..123
FT                   /evidence="ECO:0007829|PDB:1V76"
SQ   SEQUENCE   127 AA;  15054 MW;  840FE2A1234FF0AD CRC64;
     MRRNSKERKN RATRRSQGSY QEIIGRTWIF RGAHRGRVTR RNIIWHELIG LRVRIVGSTH
     PAFVGIEGYV IDETRNMLVI AGDRIWKVPK DVCIFEFEAD DGTKIKIPGE RLVGRPEMRL
     KKRWKKW
//