STRING allows inspection of the interaction evidence for any given network. Choose any of the viewers above (disabled if not applicable in your network).
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
colored nodes: query proteins and first shell of interactors
white nodes: second shell of interactors
empty nodes: proteins of unknown 3D structure
filled nodes: some 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
from curated databases
Leucyl aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (498 aa)
Predicted Functional Partners:
Hypothetical protein (198 aa)
Cysteine synthase A (337 aa)
Cysteine synthase (298 aa)
Class I and II aminotransferase (401 aa)
AMP-dependent synthetase and ligase (501 aa)
Molybdenum cofactor biosynthesis protein A; Catalyzes, together with MoaC, the conversion of 5’-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z) (329 aa)
MOSC domain-containing protein (147 aa)
Molybdenum cofactor biosynthesis protein C; Together with MoaA, is involved in the conversion of 5’- GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z) (159 aa)
valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a "posttransfer" editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner (880 aa)
DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5’-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3’-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA super [...] (698 aa)
Your Current Organism:
NCBI taxonomy Id: 552811 Other names: Chloroflexi bacterium BL-DC-8, Chloroflexi bacterium BL-DC-9, D. lykanthroporepellens, D. lykanthroporepellens BL-DC-9, Dehalogenimonas, Dehalogenimonas lykanthroporepellens, Dehalogenimonas lykanthroporepellens BL-DC-9, Dehalogenimonas lykanthroporepellens str. BL-DC-9, Dehalogenimonas lykanthroporepellens strain BL-DC-9