(data stored in SCRATCH zone)

SWISSPROT: A8FP44_SHESH

ID   A8FP44_SHESH            Unreviewed;       120 AA.
AC   A8FP44;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 69.
DE   RecName: Full=Ribonuclease P protein component {ECO:0000256|HAMAP-Rule:MF_00227, ECO:0000256|SAAS:SAAS00413173};
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:SAAS00413184};
DE   AltName: Full=Protein C5 {ECO:0000256|HAMAP-Rule:MF_00227};
GN   Name=rnpA {ECO:0000256|HAMAP-Rule:MF_00227};
GN   OrderedLocusNames=Ssed_0004 {ECO:0000313|EMBL:ABV34617.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34617.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34617.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34617.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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:SAAS00413102}.
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing 5'-
CC       extranucleotides from tRNA precursor. {ECO:0000256|HAMAP-
CC       Rule:MF_00227, ECO:0000256|SAAS:SAAS00413156}.
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; CP000821; ABV34617.1; -; Genomic_DNA.
DR   RefSeq; WP_012004144.1; NC_009831.1.
DR   ProteinModelPortal; A8FP44; -.
DR   STRING; 425104.Ssed_0004; -.
DR   EnsemblBacteria; ABV34617; ABV34617; Ssed_0004.
DR   KEGG; sse:Ssed_0004; -.
DR   eggNOG; ENOG4105NVJ; Bacteria.
DR   eggNOG; COG0594; LUCA.
DR   HOGENOM; HOG000266301; -.
DR   KO; K03536; -.
DR   OMA; LHQHELP; -.
DR   OrthoDB; POG091H011Y; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-HAMAP.
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; A8FP44.
DR   SWISS-2DPAGE; A8FP44.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00227,
KW   ECO:0000256|SAAS:SAAS00492370};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00227,
KW   ECO:0000256|SAAS:SAAS00492336};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00227,
KW   ECO:0000256|SAAS:SAAS00492415};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00227,
KW   ECO:0000256|SAAS:SAAS00143798};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00227,
KW   ECO:0000256|SAAS:SAAS00143791}.
SQ   SEQUENCE   120 AA;  14121 MW;  8CB7FFD9AA93DE87 CRC64;
     MQVTSYTFTR ELRLLTPAQF KSVFTKPIKA SSAEITLLAI PNSEQHPRLG LTVAKRFVKK
     AHQRNRIKRI IRDNFRLHQH ELPPIDIVVL VRNGVVEMEN TDLHKLVEKL WRKLNRRYNG
//

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