|rtcB||GTP-dependent RNA ligase that is involved in tRNA splicing and RNA repair (PubMed:21224389, PubMed:21757685, PubMed:22045815, PubMed:22730297, PubMed:22474365, PubMed:26858100). Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends (PubMed:21224389, PubMed:21757685, PubMed:22045815, PubMed:22730297, PubMed:22474365, PubMed:26858100). Also acts as a DNA ligase in case of DNA damage by splicing 'dirty' DNA breaks, characterized by 3'- phosphate (or cyclic-phosphate) and 5'-hydroxy ends that cannot be sealed by classical DNA ligases . ECO:0000269|PubMed:2 [...] (408 aa)|| |
Predicted Functional Partners:
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
| || || || ||0.998
Transcriptional repressor of the rtcAB genes. Interacts with sigma-54
| || || || || ||0.989
May be a nuclease involved in DNA recombination and repair.
| || || || || || ||0.771
Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''- cyclic phosphate (APPR>P). May function as an ADP-ribosylase.
| || || || ||0.757
Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'- phosphomonoester . In vitro, can also ligate 5' and 3' half-tRNA molecules with 2',3'-cyclic phosphate and 5'-hydroxyl termini, respectively, to the product containing the 2'-5' phosphodiester linkage. This reaction does not require ATP and is reversible .
| || || || || || ||0.648
Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific endoribonuclease it inhibits protein synthesis by cleaving mRNA and inducing bacterial stasis. It is stable, single- strand specific with mRNA cleavage independent of the ribosome, although translation enhances cleavage for some mRNAs . Cleavage occurs at the 5'-end of ACA sequences, yielding a 2',3'-cyclic phosphate and a free 5'-OH, although cleavage can also occur on the 3'-end of the first A (PubMed:15537630, PubMed:23280569). Digests 16S rRNA in vivo 43 nts upstream of the C- terminus; this removes the a [...]
| || || || || || || ||0.605
Catalyzes the hydrolysis of the N-glycosidic bond in the first two intermediates of riboflavin biosynthesis, which are highly reactive metabolites, yielding relatively innocuous products. Thus, can divert a surplus of harmful intermediates into relatively harmless products and pre-empt the damage these intermediates would otherwise do. Helps maintain flavin levels. May act on other substrates in vivo. Has no activity against GTP, nucleoside monophosphates or ADP-ribose . Is Required for swarming motility .
| || || || || || || ||0.530
SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity
| || || || || ||0.511
Uncharacterized protein YehL; Protein involved in ATP-binding cassette (ABC) transporter activity
| || || || || || ||0.485
To Synechocystis PCC 6803 sll0103
| || || || || ||0.484