(data stored in ACNUC7421 zone)

SWISSPROT: Q13F31_RHOPS

ID   Q13F31_RHOPS            Unreviewed;       242 AA.
AC   Q13F31;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 79.
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   OrderedLocusNames=RPD_0068 {ECO:0000313|EMBL:ABE37308.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37308.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37308.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37308.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-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: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; CP000283; ABE37308.1; -; Genomic_DNA.
DR   STRING; 316057.RPD_0068; -.
DR   EnsemblBacteria; ABE37308; ABE37308; RPD_0068.
DR   KEGG; rpd:RPD_0068; -.
DR   eggNOG; ENOG41087PG; Bacteria.
DR   eggNOG; COG0594; LUCA.
DR   KO; K03536; -.
DR   OMA; NDIAFAE; -.
DR   Proteomes; UP000001818; 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   ProDom; PD003629; Ribonuclease_P; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR00188; rnpA; 1.
DR   PROSITE; PS00648; RIBONUCLEASE_P; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13F31.
DR   SWISS-2DPAGE; Q13F31.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
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};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00227,
KW   ECO:0000256|SAAS:SAAS00143761};
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   242 AA;  27127 MW;  937BDB00CB99DB1C CRC64;
     MPNAGLARIG GPIRQKRRRA QLTRPGRSRI SRANCPRWPG STGAVHFLGC LRLICEPHHR
     AYLNLLNNLP GLRRTTREAD LSTEQIGAQA PSRLSCPSCH RWWPKGAGGA PRPRTQASER
     LSGPSRDQIM DRLRQRADFI AVAGGLRISG PAFVLQGRRR DDEGPVRVGF TVTKKIGTAT
     ERNRIRRRMR ELVKRADRSF MLPNSDYVLV GRRAALSRDF AVMLGDLRSA LDRIARRSSK
     PD
//

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