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
Deba_0755Methyltransferase; COGs: COG0742 N6-adenine-specific methylase; InterPro IPR004398:IPR016065:IPR002052; KEGG: scl:sce8059 putative methylase; PFAM: Protein of unknown function methylase putative; SPTR: A9FHL8 Putative methylase; TIGRFAM: methyltransferase; PFAM: Conserved hypothetical protein 95; TIGRFAM: RNA methyltransferase, RsmD family. (189 aa)    
Predicted Functional Partners:
coaD
Pantetheine-phosphate adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family.
 
  
 0.963
Deba_0274
Protein of unknown function DUF37; Could be involved in insertion of integral membrane proteins into the membrane; Belongs to the UPF0161 family.
  
  
 0.769
asd
Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family.
       0.723
rsmI
Phosphocarrier, HPr family; Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
 
   
 0.663
rnpA
Ribonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
   
    0.585
der
Ribosome-associated GTPase EngA; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family.
 
    0.535
pyrH
Uridylate kinase; Catalyzes the reversible phosphorylation of UMP to UDP.
 
   
 0.509
Deba_1209
Polynucleotide adenylyltransferase region; COGs: COG0617 tRNA nucleotidyltransferase/poly(A) polymerase; InterPro IPR001667:IPR003156:IPR000644:IPR002646; KEGG: sfu:Sfum_0679 polynucleotide adenylyltransferase region; PFAM: Polynucleotide adenylyltransferase region; CBS domain containing protein; phosphoesterase RecJ domain protein; phosphoesterase DHHA1; SMART: CBS domain containing protein; SPTR: A0LG26 Polynucleotide adenylyltransferase region; PFAM: DHH family; DHHA1 domain; CBS domain; Poly A polymerase head domain; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
  
    0.500
rlmH
Protein of unknown function DUF163; Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA; Belongs to the RNA methyltransferase RlmH family.
 
   
 0.498
Deba_0352
Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
     
 0.496
Your Current Organism:
Desulfarculus baarsii
NCBI taxonomy Id: 644282
Other names: D. baarsii DSM 2075, Desulfarculus baarsii 2st 14, Desulfarculus baarsii DSM 2075, Desulfarculus baarsii str. DSM 2075, Desulfarculus baarsii strain DSM 2075
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.