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
ADZ08838.1Sua5/YciO/YrdC/YwlC family protein; KEGG: mfv:Mfer_1131 translation factor SUA5; TIGRFAM: Sua5/YciO/YrdC/YwlC; PFAM: Sua5/YciO/YrdC, N-terminal. (204 aa)    
Predicted Functional Partners:
ADZ08354.1
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 a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function. In the N-terminal section; belongs to the KAE1 / TsaD family.
 
 
 0.954
tgtA
7-cyano-7-deazaguanine tRNA-ribosyltransferase; Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs; Belongs to the archaeosine tRNA-ribosyltransferase family.
 
   
 0.778
ADZ08837.1
PFAM: CDP-alcohol phosphatidyltransferase; KEGG: mru:mru_0503 phosphatidylglycerophosphate synthase PgsA; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
  
    0.752
rad50
SMC domain protein; Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex; Belongs to the SMC family. RAD50 subfamily.
 
 
 0.610
ADZ08440.1
Methylase; KEGG: mmg:MTBMA_c17150 methyltransferase; TIGRFAM: Putative methylase; PFAM: Methyltransferase small.
  
  
 0.609
ADZ09422.1
KEGG: mvn:Mevan_0177 serine O-acetyltransferase; TIGRFAM: Serine O-acetyltransferase.
       0.596
rsmA
Ribosomal RNA small subunit methyltransferase A; Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily.
 
  
 0.575
ADZ10146.1
Histone acetyltransferase, ELP3 family; SMART: Elongator protein 3/MiaB/NifB; TIGRFAM: Histone acetyltransferase ELP3; KEGG: mst:Msp_0372 histone acetyltransferase; PFAM: Radical SAM; GCN5-related N-acetyltransferase (GNAT) domain.
  
 
 0.560
ADZ09420.1
KEGG: mst:Msp_0490 putative asparagine synthetase; TIGRFAM: Asparagine synthase, glutamine-hydrolyzing; PFAM: Asparagine synthase; Glutamine amidotransferase, class-II.
  
  
 0.549
ADZ09791.1
SMC domain protein; PFAM: RecF/RecN/SMC; KEGG: rlg:Rleg_1580 SMC domain protein.
  
 
 0.547
Your Current Organism:
Methanobacterium lacus
NCBI taxonomy Id: 877455
Other names: DSM 24406, JCM 17760, M. lacus, Methanobacterium lacus Borrel et al. 2012, Methanobacterium sp. 17A1, Methanobacterium sp. AL-21, strain 17A1
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