(data stored in SCRATCH zone)

SWISSPROT: C3MF50_SINFN

ID   C3MF50_SINFN            Unreviewed;       128 AA.
AC   C3MF50;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=Ribonuclease P protein component {ECO:0000256|HAMAP-Rule:MF_00227, ECO:0000256|SAAS:SAAS00143752};
DE            Short=RNase P protein {ECO:0000256|HAMAP-Rule:MF_00227};
DE            Short=RNaseP protein {ECO:0000256|HAMAP-Rule:MF_00227};
DE            EC=3.1.26.5 {ECO:0000256|HAMAP-Rule:MF_00227, ECO:0000256|SAAS:SAAS00143815};
DE   AltName: Full=Protein C5 {ECO:0000256|HAMAP-Rule:MF_00227};
GN   Name=rnpA {ECO:0000256|HAMAP-Rule:MF_00227,
GN   ECO:0000313|EMBL:ACP23887.1};
GN   OrderedLocusNames=NGR_c00830 {ECO:0000313|EMBL:ACP23887.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23887.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23887.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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:0000256|HAMAP-Rule:MF_00227,
CC       ECO:0000256|SAAS:SAAS00143774}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing 5'-
CC         extranucleotides from tRNA precursor.; EC=3.1.26.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00227,
CC         ECO:0000256|SAAS:SAAS01128988};
CC   -!- SUBUNIT: Consists of a catalytic RNA component (M1 or rnpB) and a
CC       protein subunit. {ECO:0000256|HAMAP-Rule:MF_00227,
CC       ECO:0000256|SAAS:SAAS00598021}.
CC   -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00227, ECO:0000256|SAAS:SAAS00598027}.
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DR   EMBL; CP001389; ACP23887.1; -; Genomic_DNA.
DR   RefSeq; WP_012706672.1; NC_012587.1.
DR   RefSeq; YP_002824640.1; NC_012587.1.
DR   STRING; 394.NGR_c00830; -.
DR   EnsemblBacteria; ACP23887; ACP23887; NGR_c00830.
DR   GeneID; 7790662; -.
DR   KEGG; rhi:NGR_c00830; -.
DR   PATRIC; fig|394.7.peg.2876; -.
DR   eggNOG; ENOG4105KK3; Bacteria.
DR   eggNOG; COG0594; LUCA.
DR   HOGENOM; HOG000266302; -.
DR   KO; K03536; -.
DR   OMA; GFTCSKK; -.
DR   OrthoDB; 2014742at2; -.
DR   Proteomes; UP000001054; 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; C3MF50.
DR   SWISS-2DPAGE; C3MF50.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00227,
KW   ECO:0000256|SAAS:SAAS00143784};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00227,
KW   ECO:0000256|SAAS:SAAS00143780, ECO:0000313|EMBL:ACP23887.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00227,
KW   ECO:0000256|SAAS:SAAS00143761};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00227,
KW   ECO:0000256|SAAS:SAAS00492429};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00227,
KW   ECO:0000256|SAAS:SAAS00492455}.
SQ   SEQUENCE   128 AA;  14450 MW;  24C016B4D9BFACE0 CRC64;
     MTSEKDKSTV GRLKSRPQFL AVRAGEARKG PHFLLEVLDR KDPEGEARVG FTVTKKHGNA
     VERNRMRRRL KEAVRLSAGF AMKPGHDYVI VARRDLLNAP FDALTRGLQD RIENKPKPKR
     PPAGSRKP
//

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