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
pcmProtein-L-isoaspartate O-methyltransferase; Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. (244 aa)    
Predicted Functional Partners:
surE
Multifunctional protein surE; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family.
  
 0.783
trmH
tRNA/rRNA methyltransferase (SpoU); Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
 
     0.657
ispE
4-diphosphocytidyl-2-C-methyl-D- erythritolkinase; Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
   
    0.594
AEJ61797.1
Carbohydrate-binding CenC domain protein; PFAM: Carbohydrate binding domain; InterPro IPR003305; KEGG: sta:STHERM_c13980 hypothetical protein; PFAM: Carbohydrate-binding, CenC-like; SPTR: Carbohydrate-binding CenC domain protein.
       0.546
AEJ61798.1
PFAM: Family 4 glycosyl hydrolase; Family 4 glycosyl hydrolase C-terminal domain; COGs: COG1486 Alpha-galactosidase/6-phospho-beta-glucosidase family 4 of glycosyl hydrolase; InterPro IPR001088; KEGG: sta:STHERM_c13990 alpha-glucosidase; PFAM: Glycoside hydrolase, family 4; SPTR: Glycoside hydrolase family 4.
       0.546
AEJ61136.1
PFAM: FliG C-terminal domain; TIGRFAM: flagellar motor switch protein FliG; COGs: COG1536 Flagellar motor switch protein; InterPro IPR000090; KEGG: sta:STHERM_c12950 flagellar motor switch protein FliG; PFAM: Flagellar motor switch protein FliG; SPTR: Flagellar motor switch protein FliG.
   
   0.465
AEJ61210.1
Flagellar motor switch protein FliG; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.
   
   0.465
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.
   
    0.432
AEJ60747.1
Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.
   
   0.409
Your Current Organism:
Spirochaeta thermophila
NCBI taxonomy Id: 869211
Other names: S. thermophila DSM 6578, Spirochaeta thermophila DSM 6578, Spirochaeta thermophila str. DSM 6578, Spirochaeta thermophila strain DSM 6578
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.