(data stored in SCRATCH zone)

SWISSPROT: C6AZ81_RHILS

ID   C6AZ81_RHILS            Unreviewed;       133 AA.
AC   C6AZ81;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
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=Rleg_0096 {ECO:0000313|EMBL:ACS54407.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54407.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54407.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54407.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001622; ACS54407.1; -; Genomic_DNA.
DR   RefSeq; WP_003545005.1; NC_012850.1.
DR   ProteinModelPortal; C6AZ81; -.
DR   EnsemblBacteria; ACS54407; ACS54407; Rleg_0096.
DR   KEGG; rlg:Rleg_0096; -.
DR   HOGENOM; HOG000266302; -.
DR   KO; K03536; -.
DR   OMA; GFTCSKK; -.
DR   OrthoDB; POG091H01XK; -.
DR   Proteomes; UP000002256; 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   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.
PE   3: Inferred from homology;
DR   PRODOM; C6AZ81.
DR   SWISS-2DPAGE; C6AZ81.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
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   133 AA;  15178 MW;  2996F4F1E36C7617 CRC64;
     MAGELTISEK KHTVGRLKSR PQFLAAREGE KRRGGLFLLE VLDRKEPDSQ ARVGFTVTKK
     HGNAVERNRM RRRLKEAVRL HAGFAMQPGH DYVVVARRDV LDASFQELAA ELKSRVETRP
     KHRRSGDGRP RNV
//

If you have problems or comments...

PBIL Back to PBIL home page