RNP1_METTH
ID RNP1_METTH Reviewed; 93 AA.
AC O26119;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 129.
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=MTH_11;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP FUNCTION, SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=12003490; DOI=10.1017/s1355838202028492;
RA Hall T.A., Brown J.W.;
RT "Archaeal RNase P has multiple protein subunits homologous to eukaryotic
RT nuclear RNase P proteins.";
RL RNA 8:296-306(2002).
RN [3]
RP STRUCTURE BY NMR OF 2-93, FUNCTION, AND RNA-BINDING.
RX PubMed=14673079; DOI=10.1073/pnas.2535887100;
RA Boomershine W.P., McElroy C.A., Tsai H.Y., Wilson R.C., Gopalan V.,
RA Foster M.P.;
RT "Structure of Mth11/Mth Rpp29, an essential protein subunit of archaeal and
RT eukaryotic RNase P.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15398-15403(2003).
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_00754, ECO:0000269|PubMed:12003490,
CC ECO:0000269|PubMed:14673079}.
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 -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC subunits. {ECO:0000255|HAMAP-Rule:MF_00754,
CC ECO:0000269|PubMed:12003490}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00754}.
CC -!- INDUCTION: Constitutively expressed (at protein level).
CC {ECO:0000269|PubMed:12003490}.
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; AE000666; AAB84512.1; -; Genomic_DNA.
DR PIR; B69013; B69013.
DR RefSeq; WP_010875653.1; NC_000916.1.
DR PDB; 1OQK; NMR; -; A=2-93.
DR PDBsum; 1OQK; -.
DR AlphaFoldDB; O26119; -.
DR BMRB; O26119; -.
DR SMR; O26119; -.
DR IntAct; O26119; 1.
DR STRING; 187420.MTH_11; -.
DR EnsemblBacteria; AAB84512; AAB84512; MTH_11.
DR GeneID; 1469973; -.
DR KEGG; mth:MTH_11; -.
DR PATRIC; fig|187420.15.peg.11; -.
DR HOGENOM; CLU_107020_2_1_2; -.
DR OMA; WHELIGL; -.
DR EvolutionaryTrace; O26119; -.
DR Proteomes; UP000005223; 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; IEA:InterPro.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.30.210; -; 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; SSF101744; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Nuclease;
KW Reference proteome; tRNA processing.
FT CHAIN 1..93
FT /note="Ribonuclease P protein component 1"
FT /id="PRO_0000128433"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:1OQK"
FT TURN 25..29
FT /evidence="ECO:0007829|PDB:1OQK"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1OQK"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1OQK"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1OQK"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1OQK"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:1OQK"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1OQK"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1OQK"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:1OQK"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1OQK"
SQ SEQUENCE 93 AA; 10740 MW; 9641D6240AAE7928 CRC64;
MITPRNIFRH ELIGLSVRIA RSVHRDIQGI SGRVVDETRN TLRIEMDDGR EITVPKGIAV
FHFRTPQGEL VEIDGRALVA RPEERIKKKF RKP
