STRINGSTRING
nrdI nrdI CEW89_07510 CEW89_07510 msrQ msrQ CEW89_12095 CEW89_12095 CEW89_17210 CEW89_17210 lldD lldD pdxH pdxH CEW89_08855 CEW89_08855 CEW89_05770 CEW89_05770 CEW89_01450 CEW89_01450 dusA dusA fadH fadH GCA_001550095_02551 GCA_001550095_02551 CEW89_06665 CEW89_06665 CEW89_04570 CEW89_04570 CEW89_04060 CEW89_04060 CEW89_17745 CEW89_17745
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:
nrdIUnannotated protein; Probably involved in ribonucleotide reductase function. (151 aa)
CEW89_07510Unannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (432 aa)
msrQUnannotated protein; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the [...] (207 aa)
CEW89_12095Unannotated protein. (159 aa)
CEW89_17210Unannotated protein. (508 aa)
lldDUnannotated protein. (387 aa)
pdxHUnannotated protein; Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). (205 aa)
CEW89_08855Unannotated protein. (172 aa)
CEW89_05770Unannotated protein. (698 aa)
CEW89_01450Unannotated protein. (370 aa)
dusAUnannotated protein; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs; Belongs to the Dus family. DusA subfamily. (335 aa)
fadHUnannotated protein. (672 aa)
GCA_001550095_02551Unannotated protein. (122 aa)
CEW89_06665Unannotated protein. (205 aa)
CEW89_04570Unannotated protein. (170 aa)
CEW89_04060Unannotated protein. (161 aa)
CEW89_17745Unannotated protein. (194 aa)
Your Current Organism:
Celeribacter ethanolicus
NCBI taxonomy Id: 1758178
Other names: C. ethanolicus, CGMCC 1.15406, Celeribacter ethanolicus Jian et al. 2016, Celeribacter sp. NH195, JCM 31095, strain NH195
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