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
Igag_1247COGs: COG0143 Methionyl-tRNA synthetase; InterPro IPR014758:IPR015413:IPR001412:IPR002304; KEGG: smr:Smar_1511 methionyl-tRNA synthetase; PFAM: tRNA synthetase class I (M); SPTR: A3DPP0 Methionyl-tRNA synthetase; TIGRFAM: methionyl-tRNA synthetase; PFAM: tRNA synthetases class I (M); Anticodon-binding domain; TIGRFAM: methionyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (501 aa)    
Predicted Functional Partners:
Igag_1895
methionyl-tRNA synthetase, beta subunit; COGs: COG0073 EMAP domain; InterPro IPR002547:IPR004495; KEGG: ape:APE_0675.1 tRNA-binding protein; PFAM: t-RNA-binding domain protein; SPTR: Q9YE98 TRNA-binding protein; TIGRFAM: methionyl-tRNA synthetase, beta subunit; PFAM: Putative tRNA binding domain; TIGRFAM: methionyl-tRNA synthetase C-terminal region/beta chain.
 
  
 0.950
Igag_0284
COGs: COG0620 Methionine synthase II (cobalamin-independent); InterPro IPR002629; KEGG: smr:Smar_0416 methionine synthase II (cobalamin-independent)-like protein; PFAM: Methionine synthase vitamin-B12 independent; SPTR: A3DLL7 Methionine synthase II (Cobalamin-independent)-like protein; PFAM: Cobalamin-independent synthase, Catalytic domain.
    
 0.903
metE
Methionine synthase (B12-independent); Catalyzes the transfer of a methyl group to L-homocysteine resulting in methionine formation. The physiological methyl donor is unknown.
    
 0.903
Igag_0650
Cobalamin-independent synthase MetE domain protein; COGs: COG0620 Methionine synthase II (cobalamin-independent); InterPro IPR013215:IPR002629; KEGG: pab:PAB2361 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; PFAM: Cobalamin-independent synthase MetE domain protein; Methionine synthase vitamin-B12 independent; SPTR: Q9V086 MetE-like1 B12-independent methionine synthase homolog; PFAM: Cobalamin-independent synthase, N-terminal domain.
    
 0.903
leuS
COGs: COG0495 Leucyl-tRNA synthetase; InterProIPR015413:IPR013155:IPR002300:IPR001412:IPR 004493; KEGG: pcl:Pcal_0691 leucyl-tRNA synthetase; PFAM: aminoacyl-tRNA synthetase class Ia; tRNA synthetase class I (M); tRNA synthetase valyl/leucyl anticodon-binding; SPTR: A3MU00 Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, archaeal and cytosolic family.
  
0.895
ileS
Isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.
  
 0.874
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
  
 0.859
argS
COGs: COG0018 Arginyl-tRNA synthetase; InterPro IPR015945:IPR005148:IPR008909:IPR001278; KEGG: hbu:Hbut_1178 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SPTR: A2BM01 Arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 0.845
gltX
glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
  
 0.818
proS
prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
 
 0.810
Your Current Organism:
Ignisphaera aggregans
NCBI taxonomy Id: 583356
Other names: I. aggregans DSM 17230, Ignisphaera aggregans DSM 17230, Ignisphaera aggregans str. DSM 17230, Ignisphaera aggregans strain DSM 17230
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