(data stored in ACNUC7421 zone)

SWISSPROT: A1AXY3_PARDP

ID   A1AXY3_PARDP            Unreviewed;       241 AA.
AC   A1AXY3;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 85.
DE   RecName: Full=Ribonuclease PH {ECO:0000256|HAMAP-Rule:MF_00564, ECO:0000256|SAAS:SAAS00104182};
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:SAAS01092908};
DE   AltName: Full=tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00564};
GN   Name=rph {ECO:0000256|HAMAP-Rule:MF_00564};
GN   OrderedLocusNames=Pden_0010 {ECO:0000313|EMBL:ABL68127.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68127.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) 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:SAAS01092914}.
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,
CC         ChEBI:CHEBI:83401; EC=2.7.7.56; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00564, ECO:0000256|SAAS:SAAS01125748};
CC   -!- SUBUNIT: Homohexameric ring arranged as a trimer of dimers.
CC       {ECO:0000256|HAMAP-Rule:MF_00564, ECO:0000256|SAAS:SAAS01092913}.
CC   -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000256|HAMAP-
CC       Rule:MF_00564, ECO:0000256|SAAS:SAAS00578435}.
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DR   EMBL; CP000489; ABL68127.1; -; Genomic_DNA.
DR   STRING; 318586.Pden_0010; -.
DR   PRIDE; A1AXY3; -.
DR   EnsemblBacteria; ABL68127; ABL68127; Pden_0010.
DR   KEGG; pde:Pden_0010; -.
DR   eggNOG; ENOG4105ED0; Bacteria.
DR   eggNOG; COG0689; LUCA.
DR   HOGENOM; HOG000229516; -.
DR   KO; K00989; -.
DR   OMA; KGKGQGW; -.
DR   Proteomes; UP000000361; Chromosome 1.
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; A1AXY3.
DR   SWISS-2DPAGE; A1AXY3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS01092912, ECO:0000313|EMBL:ABL68127.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   RNA-binding {ECO:0000256|SAAS:SAAS01092910};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS01092909};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS01092911, ECO:0000313|EMBL:ABL68127.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS00469605};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS01092906}.
FT   DOMAIN       12    140       RNase_PH. {ECO:0000259|Pfam:PF01138}.
FT   DOMAIN      160    224       RNase_PH_C. {ECO:0000259|Pfam:PF03725}.
FT   REGION      125    127       Phosphate (substrate) binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00564}.
FT   BINDING      87     87       Phosphate (substrate) binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00564}.
SQ   SEQUENCE   241 AA;  25563 MW;  1F33C39958A9F759 CRC64;
     MMRPSGRNLS DMRPISIETG IMRHAEGSCL ISCGDTRVLC SASIEEKAPP FLKGSGQGWV
     TAEYGMLPRA TNTRNRREAA AGKQSGRTQE IQRLIGRALR AGVDRRALGE RQIVVDCDVI
     QADGGTRCAA ITGGWVALRL AMNKLLKAGI VTADPIMDHV AAVSCGIYAG QPILDLDYAE
     DSEAGTDGNF IMTGAGRLIE VQMSAEGATF SRPEMNQLLD LAEAGIAELV RAQNEAVACA
     G
//

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