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
msrCFree methionine-R-sulfoxide reductase; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern. (155 aa)    
Predicted Functional Partners:
dapL
LL-diaminopimelate aminotransferase; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern.
     
  0.900
ARQ06060.1
Hypothetical protein; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern.
     
  0.900
metK
S-adenosylmethionine synthase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
    
  0.900
fdtC
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose 3-N-acetyltransferase; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern.
      0.740
msrA1
Peptide methionine sulfoxide reductase MsrA 1; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
 
    
 0.585
ezrA
Septation ring formation regulator EzrA; Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization; Belongs to the EzrA family.
       0.571
msrAB
Peptide methionine sulfoxide reductase msrA/msrB; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern.
 
    
 0.495
valS
Valine--tRNA ligase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
     
 0.492
rpsD
30S ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
       0.489
thiI
Putative tRNA sulfurtransferase; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
       0.434
Your Current Organism:
Macrococcus canis
NCBI taxonomy Id: 1855823
Other names: CCM 8748, CCOS 969, CCOS:969, CCUG 68920, DSM 101690, M. canis, Macrococcus canis Gobeli Brawand et al. 2017, Macrococcus sp. KM45013, strain KM 45013
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