| Tag | Content |
|---|
| CPLM ID | CPLM-015051 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ribonuclease PH |
Protein Synonyms/Alias | RNase PH; tRNA nucleotidyltransferase |
Gene Name | rph |
Gene Synonyms/Alias | RPA0329 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 52 | ERLPPWLKGQGRGWV | acetylation | [1] |
|
Reference | [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC. J Biol Chem. 2012 May 4;287(19):15590-601. [ PMID: 22416131] |
Functional Description | Phosphorolytic exoribonuclease that removes nucleotide residues following the -CCA terminus of tRNA and adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates (By similarity). |
Sequence Annotation | |
Keyword | Complete proteome; Nucleotidyltransferase; Transferase; tRNA processing. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 237 AA |
Protein Sequence | MRPSRRAPDE LRAVSLERGV VKYAEGSCLV KFGDTHVLVT ATLEERLPPW LKGQGRGWVT 60
AEYGMLPRAT LERTRREASA GKQNGRTVEI QRLIGRSLRT IVDLEALGER QITVDCDVLQ 120
ADGGTRTASI TGAWVALADC LNWMKARNMI KGQVLRDNVA AISCGIYNGT PVLDLDYAED 180
SEAETDANFV MTGDGRLVEV QGTAERTPFS QDEFLQLMAL AQKGVARLVD LQKMAVG 237 |
Gene Ontology | GO:0000049; F:tRNA binding; IEA:InterPro. GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:EC. GO:0004549; F:tRNA-specific ribonuclease activity; IEA:InterPro. GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |