STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
AEE96457.1(SSU ribosomal protein S18P)-alanine acetyltransferase; COGs: COG0456 Acetyltransferase; InterPro IPR000182: IPR006464; KEGG: tte:TTE0537 acetyltransferase; PFAM: GCN5-related N-acetyltransferase; SPTR: Acetyltransferases; TIGRFAM: ribosomal-protein-alanine acetyltransferase; PFAM: Acetyltransferase (GNAT) family; TIGRFAM: ribosomal-protein-alanine acetyltransferase. (157 aa)    
Predicted Functional Partners:
AEE96456.1
Peptidase M22 glycoprotease; COGs: COG1214 Inactive homolog of metal-dependent protease putative molecular chaperone; InterPro IPR000905; KEGG: cce:Ccel_0800 peptidase M22 glycoprotease; PFAM: peptidase M22 glycoprotease; SPTR: Peptidase M22 glycoprotease; PFAM: Glycoprotease family.
 
 
 0.996
tsaD
O-sialoglycoprotein endopeptidase; 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; Belongs to the KAE1 / TsaD family.
  
 0.960
AEE96455.1
Uncharacterized protein family UPF0079, ATPase; COGs: COG0802 ATPase or kinase; InterPro IPR003442; KEGG: tpd:Teth39_1745 hypothetical protein; PFAM: Uncharacterised protein family UPF0079, ATPase; SPTR: Putative uncharacterized protein; PFAM: Uncharacterised P-loop hydrolase UPF0079; TIGRFAM: ATPase, YjeE family.
  
  
 0.914
AEE95267.1
COGs: COG0394 Protein-tyrosine-phosphatase; InterPro IPR017867: IPR000106; KEGG: aoe:Clos_2574 protein tyrosine phosphatase; PFAM: Protein-tyrosine phosphatase, low molecular weight; SMART: Protein-tyrosine phosphatase, low molecular weight; SPTR: Protein tyrosine phosphatase; PFAM: Low molecular weight phosphotyrosine protein phosphatase.
 
  
 0.705
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
 
   
 0.696
ribBA
3,4-dihydroxy-2-butanone 4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the C-terminal section; belongs to the GTP cyclohydrolase II family.
  
  
 0.541
pheT
COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterPro IPR002547: IPR005121: IPR004532: IPR005146: IPR 005147; KEGG: cth:Cthe_0215 phenylalanyl-tRNA synthetase subunit beta; PFAM: B3/4 domain protein; t-RNA-binding domain-containing protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; PRIAM: Phenylalanine--tRNA ligase; SPTR: Phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA sy [...]
     
 0.450
nnrE
Carbohydrate kinase, YjeF related 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. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow t [...]
  
    0.441
ispDF
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D- erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4- diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C- methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
     
 0.416
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
  
    0.404
Your Current Organism:
Mahella australiensis
NCBI taxonomy Id: 697281
Other names: M. australiensis 50-1 BON, Mahella australiensis 50-1 BON, Mahella australiensis DSM 15567, Mahella australiensis str. 50-1 BON, Mahella australiensis strain 50-1 BON
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