STRINGSTRING
thrS thrS argS argS leuS leuS Abm4_0120 Abm4_0120 alaS alaS metG metG hisS hisS pheS pheS valS valS pheT pheT gltX gltX glyS glyS tyrS tyrS Abm4_1672 Abm4_1672 ileS ileS
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.
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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:
thrSthreonyl-tRNA synthetase ThrS; Belongs to the class-II aminoacyl-tRNA synthetase family. (611 aa)
argSarginyl-tRNA synthetase ArgS; Belongs to the class-I aminoacyl-tRNA synthetase family. (574 aa)
leuSleucyl-tRNA synthetase LeuS; Belongs to the class-I aminoacyl-tRNA synthetase family. (955 aa)
Abm4_0120Translation-associated GTPase. (395 aa)
alaSalanyl-tRNA synthetase AlaS; 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. (906 aa)
metGmethionyl-tRNA synthetase MetG; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (671 aa)
hisShistidyl-tRNA synthetase HisS; Belongs to the class-II aminoacyl-tRNA synthetase family. (431 aa)
pheSphenylalanyl-tRNA synthetase alpha subunit PheS; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily. (520 aa)
valSvalyl-tRNA synthetase ValS; 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. (909 aa)
pheTphenylalanyl-tRNA synthetase subunit beta PheT. (552 aa)
gltXglutamyl-tRNA synthetase GltX; 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). (557 aa)
glySglycyl-tRNA synthetase GlyS. (568 aa)
tyrStyrosyl-tRNA synthetase TyrS; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 3 subfamily. (320 aa)
Abm4_1672Peptidyl-prolyl cis-trans isomerase. (142 aa)
ileSisoleucyl-tRNA synthetase IleS; 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. (1107 aa)
Your Current Organism:
Methanobrevibacter sp. AbM4
NCBI taxonomy Id: 224719
Other names: M. sp. AbM4
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