RNPA_THEMA
ID RNPA_THEMA Reviewed; 117 AA.
AC Q9X1H4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Ribonuclease P protein component {ECO:0000255|HAMAP-Rule:MF_00227};
DE Short=RNase P protein {ECO:0000255|HAMAP-Rule:MF_00227};
DE Short=RNaseP protein {ECO:0000255|HAMAP-Rule:MF_00227};
DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00227};
DE AltName: Full=Protein C5 {ECO:0000255|HAMAP-Rule:MF_00227};
GN Name=rnpA {ECO:0000255|HAMAP-Rule:MF_00227}; OrderedLocusNames=TM_1463;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
RX PubMed=12799461; DOI=10.1073/pnas.0932597100;
RA Kazantsev A.V., Krivenko A.A., Harrington D.J., Carter R.J., Holbrook S.R.,
RA Adams P.D., Pace N.R.;
RT "High-resolution structure of RNase P protein from Thermotoga maritima.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7497-7502(2003).
CC -!- FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from
CC pre-tRNA to produce the mature 5'-terminus. It can also cleave other
CC RNA substrates such as 4.5S RNA. The protein component plays an
CC auxiliary but essential role in vivo by binding to the 5'-leader
CC sequence and broadening the substrate specificity of the ribozyme.
CC {ECO:0000255|HAMAP-Rule:MF_00227}.
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_00227};
CC -!- SUBUNIT: Consists of a catalytic RNA component (M1 or rnpB) and a
CC protein subunit. {ECO:0000255|HAMAP-Rule:MF_00227}.
CC -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00227}.
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DR EMBL; AE000512; AAD36531.1; -; Genomic_DNA.
DR PIR; H72251; H72251.
DR RefSeq; NP_229262.1; NC_000853.1.
DR RefSeq; WP_004081756.1; NZ_CP011107.1.
DR PDB; 1NZ0; X-ray; 1.20 A; A/B/C/D=1-117.
DR PDB; 3Q1Q; X-ray; 3.80 A; A=3-117.
DR PDB; 3Q1R; X-ray; 4.21 A; A=3-117.
DR PDB; 6CQC; X-ray; 1.54 A; A/B/C/D=2-117.
DR PDB; 6MAX; X-ray; 1.42 A; A=9-117.
DR PDBsum; 1NZ0; -.
DR PDBsum; 3Q1Q; -.
DR PDBsum; 3Q1R; -.
DR PDBsum; 6CQC; -.
DR PDBsum; 6MAX; -.
DR AlphaFoldDB; Q9X1H4; -.
DR BMRB; Q9X1H4; -.
DR SMR; Q9X1H4; -.
DR STRING; 243274.THEMA_07000; -.
DR PRIDE; Q9X1H4; -.
DR EnsemblBacteria; AAD36531; AAD36531; TM_1463.
DR KEGG; tma:TM1463; -.
DR eggNOG; COG0594; Bacteria.
DR InParanoid; Q9X1H4; -.
DR OMA; RWVREIF; -.
DR OrthoDB; 2014742at2; -.
DR BRENDA; 3.1.26.5; 6331.
DR EvolutionaryTrace; Q9X1H4; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0030677; C:ribonuclease P complex; IBA:GO_Central.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0004526; F:ribonuclease P activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034414; P:tRNA 3'-trailer cleavage, endonucleolytic; IBA:GO_Central.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_00227; RNase_P; 1.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR000100; RNase_P.
DR InterPro; IPR020539; RNase_P_CS.
DR PANTHER; PTHR33992; PTHR33992; 1.
DR Pfam; PF00825; Ribonuclease_P; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00188; rnpA; 1.
DR PROSITE; PS00648; RIBONUCLEASE_P; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW RNA-binding; tRNA processing.
FT CHAIN 1..117
FT /note="Ribonuclease P protein component"
FT /id="PRO_0000198555"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:1NZ0"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:1NZ0"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:1NZ0"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1NZ0"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1NZ0"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1NZ0"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:1NZ0"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1NZ0"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1NZ0"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:1NZ0"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1NZ0"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:1NZ0"
SQ SEQUENCE 117 AA; 14317 MW; 0E68A9B25D023C64 CRC64;
MTESFTRRER LRLRRDFLLI FKEGKSLQNE YFVVLFRKNG LDYSRLGIVV KRKFGKATRR
NKLKRWVREI FRRNKGVIPK GFDIVVIPRK KLSEEFERVD FWTVREKLLN LLKRIEG
