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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
MCA1744Acetyltransferase, GNAT family; Identified by similarity to GP:1652538; match to protein family HMM PF00583. (282 aa)    
Predicted Functional Partners:
MCA1742
Rhodanese-like domain protein; Identified by match to protein family HMM PF00581.
       0.601
dtD
D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family.
       0.601
dusB
TIM-barrel protein, yjbN family; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the Dus family. DusB subfamily.
       0.541
fis
DNA-binding protein Fis; Activates ribosomal RNA transcription. Plays a direct role in upstream activation of rRNA promoters; Belongs to the transcriptional regulatory Fis family.
       0.541
purH
Phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Identified by match to protein family HMM PF01808; match to protein family HMM PF02142; match to protein family HMM TIGR00355.
       0.486
MCA2158
Transcriptional regulator, AraC family; Identified by match to protein family HMM PF00165; match to protein family HMM PF06445.
  
     0.473
MCA1748
Iron-sulfur cluster binding protein; Identified by match to protein family HMM PF00037; match to protein family HMM PF02754.
       0.467
sucC-2
succinyl-CoA synthase, beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
       0.452
sucD-2
succinyl-CoA synthase, alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
       0.452
MCA0647
Identified by match to protein family HMM PF07885.
  
     0.433
Your Current Organism:
Methylococcus capsulatus
NCBI taxonomy Id: 243233
Other names: M. capsulatus str. Bath, Methylococcus capsulatus ATCC 33009, Methylococcus capsulatus Bath, Methylococcus capsulatus MC, Methylococcus capsulatus NCIB 11132, Methylococcus capsulatus str. Bath
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