ID   RNP1_METKA              Reviewed;         107 AA.
AC   Q8TGY6;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=MK1216;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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}.
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   -!- 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; AE009439; AAM02429.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TGY6; -.
DR   SMR; Q8TGY6; -.
DR   STRING; 190192.MK1216; -.
DR   EnsemblBacteria; AAM02429; AAM02429; MK1216.
DR   KEGG; mka:MK1216; -.
DR   HOGENOM; CLU_107020_2_1_2; -.
DR   OMA; WHELIGL; -.
DR   Proteomes; UP000001826; 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   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..107
FT                   /note="Ribonuclease P protein component 1"
FT                   /id="PRO_0000128430"
SQ   SEQUENCE   107 AA;  12135 MW;  8C0A1618430EBB42 CRC64;
     MPITPRNIVR HELIGLECRV VKSLGPPYEG LEGRIVDETK NTLVLKTESG EKVIVKDQVL
     LELKLPSGER VRVDGALLVG RPEERLSKRI KYAEVVRGRF DPEDYLD