STRINGSTRING
valS valS argS argS tyrS tyrS ileS ileS hisS hisS aspS aspS serS serS metG metG gltX gltX asnC asnC cysS cysS leuS leuS glyS glyS proS proS lysS lysS alaS alaS pheT pheT pheS pheS gatA gatA gatB gatB trpS trpS thrS thrS
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:
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 1 subfamily. (824 aa)
argSarginyl-tRNA synthetase; Identified by sequence similarity; putative. (533 aa)
tyrSTyrosyl tRNA synthetase 1; 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 1 subfamily. (418 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 1 subfamily. (892 aa)
hisShistidyl-tRNA synthetase; Identified by sequence similarity; putative. (438 aa)
aspSaspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (573 aa)
serSseryl-tRNA synthetase; Identified by sequence similarity; putative. (422 aa)
metGmethionyl-tRNA synthetase; Identified by sequence similarity; putative. (510 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (481 aa)
asnCasparaginyl-tRNA synthetase; Identified by sequence similarity; putative. (446 aa)
cysSCysteinyl-tRNA synthetase; Identified by sequence similarity; putative. (400 aa)
leuSleucyl-tRNA synthetase; Identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family. (788 aa)
glySGlycyl-tRNA synthetase; Identified by sequence similarity; putative. (458 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). (480 aa)
lysSlysyl-tRNA synthetase; Identified by sequence similarity; putative; Belongs to the class-II aminoacyl-tRNA synthetase family. (492 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. (887 aa)
pheTphenylalanyl-tRNA synthetase, beta subunit; Identified by sequence similarity; putative; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (728 aa)
pheSphenylalanyl-tRNA synthetase subunit alpha; Identified by sequence similarity; putative; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (318 aa)
gatAAsp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit; Identified by sequence similarity; putative. (458 aa)
gatBAsp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit; 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. (474 aa)
trpStryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (327 aa)
thrSThreonyl-tRNA synthetase; Identified by sequence similarity; putative; Belongs to the class-II aminoacyl-tRNA synthetase family. (581 aa)
Your Current Organism:
Mycoplasma hyorhinis
NCBI taxonomy Id: 2100
Other names: ATCC 17981, ATCC 23234, Asterococcus hyorhinis, CIP 104968, DSM 25591, IFO 14858, M. hyorhinis, NBRC 14858, NCTC 10130, strain BTS 7, strain BTS-7, strain BTS7, strain PG42
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