(data stored in SCRATCH zone)

HOGENOM: PSEPG_1_PE1

ID   PSEPG_1_PE1                          STANDARD;      PRT;   134 AA.
AC   PSEPG_1_PE1; B0KEU7;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Ribonuclease P protein component; Short=RNase P protein;
DE   Short=RNaseP protein; EC=3.1.26 5;AltName: Full=Protein C5;
DE   (PSEPG_1.PE1).
GN   Name=rnpA; OrderedLocusNames=PputGB1_0001;
OS   PSEUDOMONAS PUTIDA GB-1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PSEPG_1.PE1.
CC       Pseudomonas putida GB-1 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:RNPA_PSEPG
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing 5'-
CC       extranucleotides from tRNA precursor.
CC   -!- SUBUNIT: Consists of a catalytic RNA component (M1 or rnpB) and a
CC       protein subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the rnpA family.
CC   -!- GENE_FAMILY: HOG000266301 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0KEU7; -.
DR   EMBL; CP000926; ABY95917.1; -; Genomic_DNA.
DR   RefSeq; YP_001666253.1; NC_010322.1.
DR   ProteinModelPortal; B0KEU7; -.
DR   STRING; B0KEU7; -.
DR   GeneID; 5873260; -.
DR   GenomeReviews; CP000926_GR; PputGB1_0001.
DR   KEGG; ppg:PputGB1_0001; -.
DR   OMA; LVIGKKS; -.
DR   ProtClustDB; PRK00396; -.
DR   BioCyc; PPUT76869:PPUTGB1_0001-MON; -.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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   Gene3D; G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 1.
DR   Pfam; PF00825; Ribonuclease_P; 1.
DR   ProDom; PD003629; Ribonuclease_P; 1.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   TIGRFAMs; TIGR00188; RnpA; 1.
DR   PROSITE; PS00648; RIBONUCLEASE_P; 1.
DR   HOGENOMDNA; PSEPG_1.PE1; -.
KW   ribonuclease P;
KW   Complete proteome; Endonuclease; Hydrolase; Nuclease; RNA-binding;
KW   tRNA processing.
SQ   SEQUENCE   134 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVSQDFSREK RLLTPRHFKA VFDSPTGKVP GKNLLILARE NGLDHPRLGL VIGKKSVKLA
     VQRNRLKRLM RDSFRLNQQS LAGLDIVIVA RKGLGEIENP ELHQHFGKLW KRLARSRPTP
     AATANSAGVD SQDA
//

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