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RNPA_PSECP
ID   RNPA_PSECP              Reviewed;         136 AA.
AC   B8H8Z3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=Achl_3936;
OS   Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS   107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS   chlorophenolicus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Pseudarthrobacter.
OX   NCBI_TaxID=452863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB
RC   13794 / A6;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT   "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001341; ACL41888.1; -; Genomic_DNA.
DR   RefSeq; WP_015939080.1; NC_011886.1.
DR   AlphaFoldDB; B8H8Z3; -.
DR   SMR; B8H8Z3; -.
DR   STRING; 452863.Achl_3936; -.
DR   EnsemblBacteria; ACL41888; ACL41888; Achl_3936.
DR   KEGG; ach:Achl_3936; -.
DR   eggNOG; COG0594; Bacteria.
DR   HOGENOM; CLU_117179_4_1_11; -.
DR   OMA; THHVVIR; -.
DR   OrthoDB; 2014742at2; -.
DR   Proteomes; UP000002505; Chromosome.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Nuclease; RNA-binding; tRNA processing.
FT   CHAIN           1..136
FT                   /note="Ribonuclease P protein component"
FT                   /id="PRO_1000194599"
FT   REGION          116..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   136 AA;  14413 MW;  033D3D6B64BE6256 CRC64;
     MLATRNRLRT SADFSTTVRS GVRNGRRNVV LYTAAIAAGE PSRIGFIVSK SVGNAVVRNL
     VKRRLREAGA ASLREHGTGL AIVVRALPAS ASASWDQLRE DYDAALESTL NRLAGRPQRA
     AAKGSAGTTQ KGTPRA
 
 
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