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Database: UniProt/TrEMBL
Entry: B1Y0J9_LEPCP
LinkDB: B1Y0J9_LEPCP
Original site: B1Y0J9_LEPCP 
ID   B1Y0J9_LEPCP            Unreviewed;       241 AA.
AC   B1Y0J9;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   25-APR-2018, entry version 66.
DE   RecName: Full=Ribonuclease PH {ECO:0000256|HAMAP-Rule:MF_00564, ECO:0000256|SAAS:SAAS00654476};
DE            Short=RNase PH {ECO:0000256|HAMAP-Rule:MF_00564};
DE            EC=2.7.7.56 {ECO:0000256|HAMAP-Rule:MF_00564, ECO:0000256|SAAS:SAAS01026446};
DE   AltName: Full=tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00564};
GN   Name=rph {ECO:0000256|HAMAP-Rule:MF_00564};
GN   OrderedLocusNames=Lcho_0705 {ECO:0000313|EMBL:ACB32980.1};
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Leptothrix.
OX   NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB32980.1, ECO:0000313|Proteomes:UP000001693};
RN   [1] {ECO:0000313|EMBL:ACB32980.1, ECO:0000313|Proteomes:UP000001693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC   {ECO:0000313|Proteomes:UP000001693};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphorolytic 3'-5' exoribonuclease that plays an
CC       important role in tRNA 3'-end maturation. Removes nucleotide
CC       residues following the 3'-CCA terminus of tRNAs; can also add
CC       nucleotides to the ends of RNA molecules by using nucleoside
CC       diphosphates as substrates, but this may not be physiologically
CC       important. Probably plays a role in initiation of 16S rRNA
CC       degradation (leading to ribosome degradation) during starvation.
CC       {ECO:0000256|HAMAP-Rule:MF_00564, ECO:0000256|SAAS:SAAS01026451}.
CC   -!- CATALYTIC ACTIVITY: tRNA(n+1) + phosphate = tRNA(n) + a nucleoside
CC       diphosphate. {ECO:0000256|HAMAP-Rule:MF_00564,
CC       ECO:0000256|SAAS:SAAS01026442}.
CC   -!- SUBUNIT: Homohexameric ring arranged as a trimer of dimers.
CC       {ECO:0000256|HAMAP-Rule:MF_00564, ECO:0000256|SAAS:SAAS01026449}.
CC   -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000256|HAMAP-
CC       Rule:MF_00564, ECO:0000256|SAAS:SAAS00654479}.
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DR   EMBL; CP001013; ACB32980.1; -; Genomic_DNA.
DR   RefSeq; WP_012345742.1; NC_010524.1.
DR   ProteinModelPortal; B1Y0J9; -.
DR   STRING; 395495.Lcho_0705; -.
DR   EnsemblBacteria; ACB32980; ACB32980; Lcho_0705.
DR   KEGG; lch:Lcho_0705; -.
DR   eggNOG; ENOG4105ED0; Bacteria.
DR   eggNOG; COG0689; LUCA.
DR   HOGENOM; HOG000229516; -.
DR   KO; K00989; -.
DR   OMA; KGKGQGW; -.
DR   OrthoDB; POG091H03ML; -.
DR   BioCyc; LCHO395495:G1GBL-716-MONOMER; -.
DR   Proteomes; UP000001693; 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   Complete proteome {ECO:0000313|Proteomes:UP000001693};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS01026438, ECO:0000313|EMBL:ACB32980.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001693};
KW   RNA-binding {ECO:0000256|SAAS:SAAS01026448};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS01026453};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS01026444, ECO:0000313|EMBL:ACB32980.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS00654473};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS01026455}.
FT   DOMAIN       14    143       RNase_PH. {ECO:0000259|Pfam:PF01138}.
FT   DOMAIN      161    226       RNase_PH_C. {ECO:0000259|Pfam:PF03725}.
FT   REGION      127    129       Phosphate (substrate) binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00564}.
FT   BINDING      89     89       Phosphate (substrate) binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00564}.
SQ   SEQUENCE   241 AA;  25268 MW;  C060C982C26AA38A CRC64;
     MSSTRPLGRA ADALRPVRIT RSYTKHAEGS VLIEFGDTQV LCTASVEEKV PPHKKGSGEG
     WVTAEYGMLP RATHTRSARE AAKGKQSGRT QEIQRLIGRS LRCVFDLAAL GERSILIDCD
     VLQADGGTRT ASITGAFVAA HDAVQGLIAQ GKLKRSPIRD FVAAVSVGIL DGVALLDLEY
     VEDSACDTDM NIVMTGAGGF VEVQGTAEGV AFSRAEMDQL LALGSAGIAE LVAAQKAALG
     V
//
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