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rimI protein (Synechocystis sp. PCC6803) - STRING interaction network
"rimI" - Ribosomal-protein-alanine acetyltransferase in Synechocystis sp. PCC6803
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
rimIRibosomal-protein-alanine acetyltransferase (158 aa)    
Predicted Functional Partners:
slr0852
Hypothetical protein (142 aa)
              0.859
argB
N-acetylglutamate kinase (297 aa)
   
 
    0.777
argD
N-acetylornithine aminotransferase (429 aa)
 
 
    0.720
cysS
cysteinyl-tRNA synthetase (483 aa)
   
 
  0.694
phrA
Deoxyribopyrimidine photolyase; Involved in repair of UV radiation-induced DNA damage. Exhibits specific, light-dependent repair activity for a cyclobutyl pyrimidine dimer by catalyzing the light-dependent monomerization (300-600 nm) of the dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. It has been shown that photorepair is more important than excision repair for UV-induced DNA lesions in Synechocystis. Its disruption does not affect circadian rhythm (479 aa)
   
        0.691
nnr
Hypothetical protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (By similarity) (524 aa)
   
   
  0.659
thiL
Thiamine monophosphate kinase; Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1 (364 aa)
         
  0.641
SYNGTS_1211
NADH dehydrogenase (445 aa)
              0.606
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3’ to 5’ and 5’ to 3’ exonuclease activity (986 aa)
   
 
  0.592
tsaD
Metalloendopeptidase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction (348 aa)
   
 
  0.557
Your Current Organism:
Synechocystis sp. PCC6803
NCBI taxonomy Id: 1148
Other names: Aphanocapsa sp. (strain N-1), Aphanocapsa sp. N-1, S. sp. PCC 6803, Synechocystis, Synechocystis PCC6803, Synechocystis sp. (ATCC 27184), Synechocystis sp. (PCC 6803), Synechocystis sp. (strain PCC 6803), Synechocystis sp. ATCC 27184, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 A, Synechocystis sp. PCC 6803 B, Synechocystis sp. PCC6803
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