STRINGSTRING
rimO rimO pqqE pqqE Daro_1855 Daro_1855 Daro_1884 Daro_1884 Daro_1969 Daro_1969 Daro_1996 Daro_1996 lipA lipA Daro_0409 Daro_0409 Daro_0417 Daro_0417 Daro_1048 Daro_1048 Daro_1454 Daro_1454 moaA-2 moaA-2 Daro_2577 Daro_2577 moaA moaA Daro_4199 Daro_4199 Daro_4163 Daro_4163 Daro_3853 Daro_3853 miaB miaB Daro_3325 Daro_3325 Daro_3261 Daro_3261 rlmN rlmN
Nodes:
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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 to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
rimOSSU ribosomal protein S12P methylthiotransferase; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (440 aa)
pqqECoenzyme PQQ biosynthesis protein E; Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ). (375 aa)
Daro_1855Radical SAM. (638 aa)
Daro_1884Radical SAM. (296 aa)
Daro_1969Radical SAM. (370 aa)
Daro_1996Radical SAM. (740 aa)
lipALipoate synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. (314 aa)
Daro_0409Radical SAM. (474 aa)
Daro_0417Radical SAM. (457 aa)
Daro_1048Coproporphyrinogen III oxidase, anaerobic; Belongs to the anaerobic coproporphyrinogen-III oxidase family. (471 aa)
Daro_1454Nitrogenase cofactor biosynthesis protein NifB. (500 aa)
moaA-2GTP cyclohydrolase subunit MoaA; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. (327 aa)
Daro_2577Radical SAM:Molybdenum cofactor synthesis C-terminal; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. (323 aa)
moaAGTP cyclohydrolase subunit MoaA; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. (357 aa)
Daro_4199Cobalamin B12-binding:Radical SAM. (548 aa)
Daro_4163Radical SAM. (524 aa)
Daro_3853Putative oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (399 aa)
miaBtRNA-i(6)A37 thiotransferase enzyme MiaB; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. (445 aa)
Daro_3325Radical SAM. (368 aa)
Daro_3261Radical SAM. (379 aa)
rlmN23S rRNA m(2)A-2503 methyltransferase; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. (364 aa)
Your Current Organism:
Dechloromonas aromatica
NCBI taxonomy Id: 159087
Other names: D. aromatica RCB, Dechloromonas aromatica RCB, Dechloromonas aromatica str. RCB, Dechloromonas sp. RCB
Server load: low (24%) [HD]