STRINGSTRING
SFS16242.1 SFS16242.1 thrS thrS birA birA hisZ hisZ alaS alaS aspS aspS asnA asnA asnS asnS hisS hisS aspS-2 aspS-2 proS proS SFS01473.1 SFS01473.1 glyQS glyQS pheS pheS pheT pheT lysS lysS
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:
SFS16242.1seryl-tRNA synthetase. (429 aa)
thrSSer-tRNA(Thr) hydrolase /threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (584 aa)
birABifunctional ligase/repressor BirA; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. (326 aa)
hisZATP phosphoribosyltransferase regulatory subunit; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. (421 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. (882 aa)
aspSNondiscriminating 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily. (443 aa)
asnAAspartate-ammonia ligase. (335 aa)
asnSasparaginyl-tRNA synthetase. (463 aa)
hisShistidyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (421 aa)
aspS-2aspartyl-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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (600 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). (479 aa)
SFS01473.1Lipoate-protein ligase. (335 aa)
glyQSglycyl-tRNA synthetase; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family. (462 aa)
pheSphenylalanyl-tRNA synthetase, alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (339 aa)
pheTphenylalanyl-tRNA synthetase beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (810 aa)
lysSlysyl-tRNA synthetase, class II; Belongs to the class-II aminoacyl-tRNA synthetase family. (649 aa)
Your Current Organism:
Clostridium citroniae
NCBI taxonomy Id: 358743
Other names: CCUG 52203, Clostridium citroniae Warren et al. 2007, DSM 19261, [. citroniae, [Clostridium] citroniae, strain RMA 16102
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