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hisS hisS tyrS tyrS leuS leuS thrS thrS valS valS gltX gltX prfA prfA
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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
hisSPFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase. (458 aa)
tyrStyrosyl-tRNA synthetase; 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. (447 aa)
leuSPFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; tRNA synthetases class I (M); TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; Belongs to the class-I aminoacyl-tRNA synthetase family. (835 aa)
thrSthreonyl-tRNA synthetase /Ser-tRNA(Thr) hydrolase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). (672 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. (894 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. (525 aa)
prfABacterial peptide chain release factor 1 (bRF-1); Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. (369 aa)
Your Current Organism:
Micrococcus luteus NCTC 2665
NCBI taxonomy Id: 465515
Other names: M. luteus NCTC 2665, Micrococcus luteus ATCC 4698, Micrococcus luteus CCM 169, Micrococcus luteus DSM 20030, Micrococcus luteus Fleming 2665, Micrococcus luteus NCIB 9278, Micrococcus luteus str. NCTC 2665, Micrococcus luteus strain NCTC 2665
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