ID   RNP3_THEKO              Reviewed;         220 AA.
AC   Q5JH47;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=TK1450;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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_00756}.
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};
CC   -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00756}.
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; AP006878; BAD85639.1; -; Genomic_DNA.
DR   RefSeq; WP_011250401.1; NC_006624.1.
DR   PDB; 3WYZ; X-ray; 2.21 A; A=1-220.
DR   PDB; 3WZ0; X-ray; 2.79 A; E/F=1-220.
DR   PDBsum; 3WYZ; -.
DR   PDBsum; 3WZ0; -.
DR   AlphaFoldDB; Q5JH47; -.
DR   SMR; Q5JH47; -.
DR   STRING; 69014.TK1450; -.
DR   EnsemblBacteria; BAD85639; BAD85639; TK1450.
DR   GeneID; 78447973; -.
DR   KEGG; tko:TK1450; -.
DR   PATRIC; fig|69014.16.peg.1412; -.
DR   eggNOG; arCOG00307; Archaea.
DR   HOGENOM; CLU_1302679_0_0_2; -.
DR   InParanoid; Q5JH47; -.
DR   OrthoDB; 85765at2157; -.
DR   PhylomeDB; Q5JH47; -.
DR   Proteomes; UP000000536; 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; IBA:GO_Central.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
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   PANTHER; PTHR13031:SF0; RIBONUCLEASE P PROTEIN SUBUNIT P30; 1.
DR   PANTHER; PTHR13031; RIBONUCLEASE P SUBUNIT P30; 1.
DR   Pfam; PF01876; RNase_P_p30; 1.
DR   SUPFAM; SSF89550; PHP domain-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Endonuclease; Hydrolase; Nuclease;
KW   Reference proteome; tRNA processing.
FT   CHAIN           1..220
FT                   /note="Ribonuclease P protein component 3"
FT                   /id="PRO_0000140047"
FT   STRAND          14..18
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   HELIX           21..30
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   STRAND          32..41
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   HELIX           48..62
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   HELIX           74..83
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   STRAND          86..92
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   HELIX           96..104
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   TURN            113..116
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   HELIX           124..133
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   STRAND          136..141
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   HELIX           142..145
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   HELIX           149..168
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   STRAND          173..176
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   HELIX           182..184
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   HELIX           188..198
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   HELIX           202..209
FT                   /evidence="ECO:0007829|PDB:3WYZ"
FT   HELIX           211..217
FT                   /evidence="ECO:0007829|PDB:3WYZ"
SQ   SEQUENCE   220 AA;  25270 MW;  02EA82685C7B3EE0 CRC64;
     MSEEEVSFSR DYFVEMDVRD EEAHELASDW FDEVVFTKKL VLEDPPDWGS LKEELKELRG
     KYGKVALLLV TRKPSLIREV KSRNLKALLY VQGGDMRINR MAIESGVDAL ISPWFGRKDP
     GFDHTLAGMA ARRGVAIGFS LSPLLNANPY GRAQILRFMM KTWQLVKKYR VPRFITSSAE
     SRWEVRGPRD LMSLGINIGM EIPEARASLN FYPRTIVWKL
//