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Database: UniProt
Entry: A0A0C1H468_9RHOB
LinkDB: A0A0C1H468_9RHOB
Original site: A0A0C1H468_9RHOB 
ID   A0A0C1H468_9RHOB        Unreviewed;       141 AA.
AC   A0A0C1H468;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=RA28_02625 {ECO:0000313|EMBL:KIC46688.1};
OS   Ruegeria sp. ANG-S4.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1577904 {ECO:0000313|EMBL:KIC46688.1, ECO:0000313|Proteomes:UP000031326};
RN   [1] {ECO:0000313|Proteomes:UP000031326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANG-S4 {ECO:0000313|Proteomes:UP000031326};
RX   PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA   Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT   "Comparative genomics of Roseobacter clade bacteria isolated from the
RT   accessory nidamental gland of Euprymna scolopes.";
RL   Front. Microbiol. 6:123-123(2015).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIC46688.1}.
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DR   EMBL; JWLK01000001; KIC46688.1; -; Genomic_DNA.
DR   RefSeq; WP_039523479.1; NZ_JWLK01000001.1.
DR   AlphaFoldDB; A0A0C1H468; -.
DR   STRING; 1577904.RA28_02625; -.
DR   OrthoDB; 9810867at2; -.
DR   Proteomes; UP000031326; Unassembled WGS sequence.
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:UP000031326};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00227};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00227}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   141 AA;  15499 MW;  2A3BEA351AB41990 CRC64;
     MTPPEAPEDG KRQPRETPPA ASVCAPVSLT VLTKRSDFLK AARARRQGTS SMMVQARKRA
     KGEADGIRVG FTCSKKVGNA VARNRAKRRL REAARAILPV KGQNGWDYVL IGRAQVTADR
     AFLDLLDDLS YALRKLHGDR T
//
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