(data stored in ACNUC29543 zone)

SWISSPROT: RNPA_SYNR3

ID   RNPA_SYNR3              Reviewed;         127 AA.
AC   A5GRN3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 64.
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};
GN   OrderedLocusNames=SynRCC307_0639;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence
CC       from pre-tRNA to produce the mature 5'-terminus. It can also
CC       cleave other RNA substrates such as 4.5S RNA. The protein
CC       component plays an auxiliary but essential role in vivo by binding
CC       to the 5'-leader sequence and broadening the substrate specificity
CC       of the ribozyme. {ECO:0000255|HAMAP-Rule:MF_00227}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing 5'-
CC         extranucleotides from tRNA precursor.; EC=3.1.26.5;
CC         Evidence={ECO:0000255|HAMAP-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}.
DR   EMBL; CT978603; CAK27542.1; -; Genomic_DNA.
DR   RefSeq; WP_011935057.1; NC_009482.1.
DR   SMR; A5GRN3; -.
DR   STRING; 316278.SynRCC307_0639; -.
DR   EnsemblBacteria; CAK27542; CAK27542; SynRCC307_0639.
DR   KEGG; syr:SynRCC307_0639; -.
DR   eggNOG; ENOG4105UVI; Bacteria.
DR   eggNOG; ENOG410YT7G; LUCA.
DR   HOGENOM; HOG000266301; -.
DR   KO; K03536; -.
DR   OMA; MRLKGHR; -.
DR   OrthoDB; 2014742at2; -.
DR   BioCyc; SSP316278:G1GJL-632-MONOMER; -.
DR   Proteomes; UP000001115; 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   PANTHER; PTHR33992; PTHR33992; 1.
DR   Pfam; PF00825; Ribonuclease_P; 1.
DR   ProDom; PD003629; Ribonuclease_P; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR00188; rnpA; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GRN3.
DR   SWISS-2DPAGE; A5GRN3.
KW   Complete proteome; Endonuclease; Hydrolase; Nuclease;
KW   Reference proteome; RNA-binding; tRNA processing.
FT   CHAIN         1    127       Ribonuclease P protein component.
FT                                /FTId=PRO_1000021485.
SQ   SEQUENCE   127 AA;  14747 MW;  D39431DA7AF44433 CRC64;
     MVLPQRHRLR GRGVFDYIYQ RGQRFQQGLL QLRVADAATN LLREPPETLE GELRFGVVIS
     SKVSKRAVKR NRLRRLLHEA FLRQTFRSDL PPTWLLLNLR PGAVELSDDN LLEEWSTLIQ
     RAGLTDS
//

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