RNPH_LEIXX
ID RNPH_LEIXX Reviewed; 251 AA.
AC Q6AEK9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Lxx13580;
OS Leifsonia xyli subsp. xyli (strain CTCB07).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia.
OX NCBI_TaxID=281090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTCB07;
RX PubMed=15305603; DOI=10.1094/mpmi.2004.17.8.827;
RA Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P.,
RA Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D.,
RA de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R.,
RA Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L.,
RA El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S.,
RA Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M.,
RA Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F.,
RA Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A.,
RA Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
RT "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli
RT subsp. xyli.";
RL Mol. Plant Microbe Interact. 17:827-836(2004).
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:17343, Rhea:RHEA-
CC COMP:17344, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:173114;
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}.
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DR EMBL; AE016822; AAT89187.1; -; Genomic_DNA.
DR RefSeq; WP_011186181.1; NC_006087.1.
DR AlphaFoldDB; Q6AEK9; -.
DR SMR; Q6AEK9; -.
DR STRING; 281090.Lxx13580; -.
DR PRIDE; Q6AEK9; -.
DR EnsemblBacteria; AAT89187; AAT89187; Lxx13580.
DR KEGG; lxx:Lxx13580; -.
DR eggNOG; COG0689; Bacteria.
DR HOGENOM; CLU_050858_0_0_11; -.
DR OMA; KGKGQGW; -.
DR OrthoDB; 1824064at2; -.
DR Proteomes; UP000001306; Chromosome.
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;
KW Nucleotidyltransferase; Reference proteome; RNA-binding; rRNA processing;
KW Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..251
FT /note="Ribonuclease PH"
FT /id="PRO_0000139903"
FT BINDING 90
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00564"
FT BINDING 128..130
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00564"
SQ SEQUENCE 251 AA; 26519 MW; 2518B883643ED2C5 CRC64;
MTDTIRADGR TADQLRPVTI ERAWNRKAEG SALVSFGGTR VLCTASFTNG VPRWMSGKGR
GWVTAEYAML PRSTNDRMDR ESVKGRIGGR THEISRLIGR SLRAVVDMKA LGENTIVLDC
DVLQADGGTR TAAITGAYVA LADALEWGRE HRFIGQKAAP LLDSVSAVSV GIVDGSPMLD
LAYTEDVRAE TDMNVVVTGR GLFVEVQGTA EGAPFDRSEL NGLLDLALAG TTALVAVQSA
ALAAPAPGCE G
