STRINGSTRING
lysS lysS ileS ileS tyrS tyrS glnS glnS serS serS proS proS pheS pheS pheT pheT gatB gatB gatA gatA gatC gatC aspS aspS metG metG valS valS hisS hisS gluQ gluQ argS argS leuS leuS
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
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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:
lysSTIGRFAM: Lysyl-tRNA synthetase, class II; HAMAP: Lysyl-tRNA synthetase; KEGG: nit:NAL212_0716 lysyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; Belongs to the class-II aminoacyl-tRNA synthetase family. (502 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. (935 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 2 subfamily. (400 aa)
glnSTIGRFAM: Glutaminyl-tRNA synthetase, class Ic; HAMAP: Glutaminyl-tRNA synthetase; KEGG: nit:NAL212_2802 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain. (584 aa)
serSSeryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). (438 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] (569 aa)
pheSTIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, alpha subunit; HAMAP: Phenylalanyl-tRNA synthetase alpha chain; KEGG: nit:NAL212_2129 phenylalanyl-tRNA synthetase, alpha subunit; PFAM: Phenylalanyl-tRNA synthetase alpha chain; Phenylalanyl-tRNA synthetase, class II, N-terminal; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (339 aa)
pheTTIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: nit:NAL212_2128 phenylalanyl-tRNA synthetase, beta subunit. (790 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. (479 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). (482 aa)
gatCAspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; 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 GatC family. (95 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (595 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. (702 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 1 subfamily. (939 aa)
hisSTIGRFAM: Histidyl-tRNA synthetase, class IIa, subgroup; HAMAP: Histidyl-tRNA synthetase, class IIa, subgroup; KEGG: nit:NAL212_1228 histidyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Anticodon-binding. (422 aa)
gluQGlutamyl-Q tRNA(Asp) synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. (297 aa)
argSTIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic; KEGG: nit:NAL212_1355 arginyl-tRNA synthetase. (585 aa)
leuSTIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG: nit:NAL212_0261 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (866 aa)
Your Current Organism:
Nitrosomonas sp. Is79A3
NCBI taxonomy Id: 261292
Other names: N. sp. Is79A3
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