GenomeNet

Database: UniProt
Entry: S5VQL7_STRC3
LinkDB: S5VQL7_STRC3
Original site: S5VQL7_STRC3 
ID   S5VQL7_STRC3            Unreviewed;       123 AA.
AC   S5VQL7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Ribonuclease P protein component {ECO:0000256|HAMAP-Rule:MF_00227};
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};
DE   AltName: Full=Protein C5 {ECO:0000256|HAMAP-Rule:MF_00227};
GN   Name=rnpA {ECO:0000256|HAMAP-Rule:MF_00227};
GN   ORFNames=B446_19155 {ECO:0000313|EMBL:AGS70645.1};
OS   Streptomyces collinus (strain DSM 40733 / Tue 365).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS70645.1, ECO:0000313|Proteomes:UP000015423};
RN   [1] {ECO:0000313|Proteomes:UP000015423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RA   Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA   Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT   "The complete genome sequence of Streptomyces collinus Tu 365.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGS70645.1, ECO:0000313|Proteomes:UP000015423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RX   PubMed=24140291; DOI=10.1016/j.jbiotec.2013.10.004;
RA   Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Iftime D.,
RA   Musiol E.M., Blin K., Wohlleben W., Puhler A., Kalinowski J., Weber T.;
RT   "Complete genome sequence of the kirromycin producer Streptomyces collinus
RT   Tu 365 consisting of a linear chromosome and two linear plasmids.";
RL   J. Biotechnol. 168:739-740(2013).
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:0000256|ARBA:ARBA00002663, ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_00227};
CC   -!- SUBUNIT: Consists of a catalytic RNA component (M1 or rnpB) and a
CC       protein subunit. {ECO:0000256|HAMAP-Rule:MF_00227}.
CC   -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00227}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP006259; AGS70645.1; -; Genomic_DNA.
DR   AlphaFoldDB; S5VQL7; -.
DR   STRING; 1214242.B446_19155; -.
DR   KEGG; sci:B446_19155; -.
DR   eggNOG; COG0594; Bacteria.
DR   HOGENOM; CLU_117179_4_1_11; -.
DR   Proteomes; UP000015423; 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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR000100; RNase_P.
DR   InterPro; IPR020539; RNase_P_CS.
DR   NCBIfam; TIGR00188; rnpA; 1.
DR   PANTHER; PTHR33992; RIBONUCLEASE P PROTEIN COMPONENT; 1.
DR   PANTHER; PTHR33992:SF1; RIBONUCLEASE P PROTEIN COMPONENT; 1.
DR   Pfam; PF00825; Ribonuclease_P; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00648; RIBONUCLEASE_P; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_00227};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00227};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00227};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015423};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00227};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00227}.
SQ   SEQUENCE   123 AA;  13243 MW;  5B4372281A5578DF CRC64;
     MLPTEHRLRR REDFATAVRR GRRAGRPTLV VHLRSGATDP HAPGESAPPT RAGFVVSKAV
     GGAVVRNQVK RRLRHLMRDR VALFPPGSLV VVRALPGAGD ADHAQLARDL DAAVQRLLGG
     GAR
//
DBGET integrated database retrieval system