| Tag | Content |
|---|
| CPLM ID | CPLM-007842 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | RNA 3'-terminal phosphate cyclase |
Protein Synonyms/Alias | RNA cyclase; RNA-3'-phosphate cyclase |
Gene Name | rtcA |
Gene Synonyms/Alias | yhgJ; yhgK; b4475; JW5688 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 255 | RFFVVGEKRVSAEVV | acetylation | [1] | | 268 | VVAAQLVKEVKRYLA | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Catalyzes the conversion of 3'-phosphate to a 2',3'- cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA- N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'- phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing. |
Sequence Annotation | NP_BIND 283 287 ATP.
ACT_SITE 308 308 Tele-AMP-histidine intermediate.
BINDING 103 103 ATP. |
Keyword | 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 338 AA |
Protein Sequence | MKRMIALDGA QGEGGGQILR SALSLSMITG QPFTITSIRA GRAKPGLLRQ HLTAVKAATE 60
ICGATVEGAE LGSQRLLFRP GTVRGGDYRF AIGSAGSCTL VLQTVLPALW FADGPSRVEV 120
SGGTDNPSAP PADFIRRVLE PLLAKIGIHQ QTTLLRHGFY PAGGGVVATE VSPVASFNTL 180
QLGERGNIVQ MRGEVLLAGV PRHVAEREIA TLAGSFSLHE QNIHNLPRDQ GPGNTVSLEV 240
ESENITERFF VVGEKRVSAE VVAAQLVKEV KRYLASTAAV GEYLADQLVL PMALAGAGEF 300
TVAHPSCHLL TNIAVVERFL PVRFSLIETD GVTRVSIE 338 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |