(data stored in ACNUC29543 zone)

SWISSPROT: RNPH_ACIBT

ID   RNPH_ACIBT              Reviewed;         238 AA.
AC   A3M0U3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   11-DEC-2019, entry version 79.
DE   RecName: Full=Ribonuclease PH {ECO:0000255|HAMAP-Rule:MF_00564};
DE            Short=RNase PH {ECO:0000255|HAMAP-Rule:MF_00564};
DE            EC=2.7.7.56 {ECO:0000255|HAMAP-Rule:MF_00564};
DE   AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_00564};
GN   Name=rph {ECO:0000255|HAMAP-Rule:MF_00564}; OrderedLocusNames=A1S_0042;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS   KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT   density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
CC   -!- FUNCTION: Phosphorolytic 3'-5' exoribonuclease that plays an important
CC       role in tRNA 3'-end maturation. Removes nucleotide residues following
CC       the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of
CC       RNA molecules by using nucleoside diphosphates as substrates, but this
CC       may not be physiologically important. Probably plays a role in
CC       initiation of 16S rRNA degradation (leading to ribosome degradation)
CC       during starvation. {ECO:0000255|HAMAP-Rule:MF_00564}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate +
CC         tRNA(n); Xref=Rhea:RHEA:10628, Rhea:RHEA-COMP:11132, Rhea:RHEA-
CC         COMP:11133, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:83401;
CC         EC=2.7.7.56; Evidence={ECO:0000255|HAMAP-Rule:MF_00564};
CC   -!- SUBUNIT: Homohexameric ring arranged as a trimer of dimers.
CC       {ECO:0000255|HAMAP-Rule:MF_00564}.
CC   -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00564}.
DR   EMBL; CP000521; ABO10537.2; -; Genomic_DNA.
DR   RefSeq; WP_001217232.1; NZ_CP039028.2.
DR   SMR; A3M0U3; -.
DR   EnsemblBacteria; ABO10537; ABO10537; A1S_0042.
DR   GeneID; 31349879; -.
DR   KEGG; acb:A1S_0042; -.
DR   HOGENOM; HOG000229516; -.
DR   KO; K00989; -.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016075; P:rRNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR   CDD; cd11362; RNase_PH_bact; 1.
DR   Gene3D; 3.30.230.70; -; 1.
DR   HAMAP; MF_00564; RNase_PH; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR002381; RNase_PH_bac-type.
DR   InterPro; IPR018336; RNase_PH_CS.
DR   Pfam; PF01138; RNase_PH; 1.
DR   Pfam; PF03725; RNase_PH_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55666; SSF55666; 1.
DR   TIGRFAMs; TIGR01966; RNasePH; 1.
DR   PROSITE; PS01277; RIBONUCLEASE_PH; 1.
PE   3: Inferred from homology;
DR   PRODOM; A3M0U3.
DR   SWISS-2DPAGE; A3M0U3.
KW   Nucleotidyltransferase; RNA-binding; rRNA processing; Transferase;
KW   tRNA processing; tRNA-binding.
FT   CHAIN           1..238
FT                   /note="Ribonuclease PH"
FT                   /id="PRO_1000129310"
FT   REGION          124..126
FT                   /note="Phosphate (substrate) binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00564"
FT   BINDING         86
FT                   /note="Phosphate (substrate) binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00564"
SQ   SEQUENCE   238 AA;  26296 MW;  EF3216AD4D0B0BE6 CRC64;
     MRIDQRALDQ LREVKITRNY TRYAEGSVLV EFGHTKVLCT ASIDNSVPRF LKGQGQGWVT
     AEYGMLPRST HSRCDREAAR GKQTGRTQEI QRLIGRSLRA MVDLKKLGEN TITIDCDVIQ
     ADGGTRTASI TGAAVALVDA MNVLLAQKKI KQDPLKGLVA AISVGMYQDE VLLDLCYEED
     SNCQTDLNVV MTQAGEFIEI QGTAEDKPFT RAQSNAMLEM AEKGIAELIK KQQEALGW
//

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