STRINGSTRING
leuS leuS ADZ08277.1 ADZ08277.1 gatA gatA thrS thrS argS argS ileS ileS gatB gatB hisS hisS ADZ08912.1 ADZ08912.1 gltX gltX valS valS pheT pheT proS proS pheS pheS ADZ09419.1 ADZ09419.1 metG metG aspS aspS alaS alaS gatE gatE gatD gatD
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
leuSTIGRFAM: Leucyl-tRNA synthetase, class Ia, archaeal/eukaryotic cytosolic; KEGG: mst:Msp_0171 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (958 aa)
ADZ08277.1PFAM: GTPase of unknown function C-terminal; GTP-binding protein, HSR1-related; TGS; KEGG: mth:MTH1515 translation-associated GTPase. (395 aa)
gatAGlutamyl-tRNA(Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). (459 aa)
thrSTIGRFAM: Threonyl-tRNA synthetase, class IIa; KEGG: mth:MTH1455 threonyl-tRNA synthetase; PFAM: Threonyl-tRNA synthetase, editing domain, archaea; Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain; Anticodon-binding; Belongs to the class-II aminoacyl-tRNA synthetase family. (614 aa)
argSKEGG: mth:MTH1447 arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic; Belongs to the class-I aminoacyl-tRNA synthetase family. (561 aa)
ileSIsoleucyl-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. (1060 aa)
gatBAspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. (452 aa)
hisSATP phosphoribosyltransferase regulatory subunit; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain; Anticodon-binding; TIGRFAM: Histidyl-tRNA synthetase, class IIa, subgroup; HAMAP: ATP phosphoribosyltransferase regulatory subunit; Histidyl-tRNA synthetase, class IIa, subgroup; KEGG: mth:MTH244 histidyl-tRNA synthetase. (429 aa)
ADZ08912.1KEGG: mmg:MTBMA_c04160 glycyl-tRNA synthetase; TIGRFAM: Glycyl-tRNA synthetase, alpha2 dimer; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain; Anticodon-binding. (575 aa)
gltXglutamyl-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). (564 aa)
valSValyl-tRNA synthetase; 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 2 subfamily. (887 aa)
pheTPhenylalanyl-tRNA synthetase beta chain; SMART: B3/B4 tRNA-binding domain; tRNA synthetase, B5; TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, archae/euk cytosolic; KEGG: mmg:MTBMA_c11660 phenylalanyl-tRNA synthetase, beta chain; HAMAP: Phenylalanyl-tRNA synthetase beta chain 2, bacterial/archaeal; PFAM: tRNA synthetase, B5; B3/B4 tRNA-binding domain. (553 aa)
proSProlyl-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). (469 aa)
pheSTIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, alpha subunit; HAMAP: Phenylalanyl-tRNA synthetase alpha chain 2, bacterial/archaeal; KEGG: mmg:MTBMA_c11370 phenylalanyl-tRNA synthetase, alpha subunit; PFAM: Phenylalanyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily. (522 aa)
ADZ09419.1TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mst:Msp_0489 aspartyl/glutamyl-tRNA amidotransferase subunit C. (71 aa)
metGMethionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (658 aa)
aspSaspartyl-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). (439 aa)
alaSalanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. (905 aa)
gatEGlutamyl-tRNA(Gln) amidotransferase subunit E; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. (626 aa)
gatDGlutamyl-tRNA(Gln) amidotransferase subunit D; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. (437 aa)
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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