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thrS thrS fmt fmt gatC gatC lysS lysS serS serS trpS trpS glyS glyS tyrS tyrS cysS cysS valS valS aspS aspS gltX1 gltX1 metS metS hisS hisS proS proS glyQ glyQ leuS leuS alaS alaS argS argS gatA gatA ileS ileS pheT pheT pheS pheS gatB gatB Cla_1233 Cla_1233 Cla_1236 Cla_1236 selA selA gltX2 gltX2 Cla_1312 Cla_1312 Cla_1323 Cla_1323
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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
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; 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). (603 aa)
fmt10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. (303 aa)
gatCglu-tRNAGln 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)
lysSlysyl-tRNA synthetase; Pfam matches to PF01336.16 tRNA_anti, and to PF00152.11 tRNA-synt_2; Belongs to the class-II aminoacyl-tRNA synthetase family. (500 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). (411 aa)
trpStryptophanyl-tRNA synthetase; Pfam match to PF00579.16 tRNA-synt_1b; Belongs to the class-I aminoacyl-tRNA synthetase family. (319 aa)
glySglycyl-tRNA synthetase, beta subunit; Pfam match to PF02092.8 tRNA_synt_2f. (664 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)
cysScysteinyl-tRNA synthetase; Pfam matches to PF01406.10 tRNA-synt_1e, and to PF09190.2 DALR_2; Belongs to the class-I aminoacyl-tRNA synthetase family. (460 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. (870 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. (583 aa)
gltX1glutamyl-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. (431 aa)
metSmethionyl-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. (629 aa)
hisShistidyl-tRNA synthetase; Pfam match to PF00587.16 tRNA-synt_2b. (408 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 [...] (565 aa)
glyQglycyl-tRNA synthetase, alpha chain; Pfam match to PF02091.6 tRNA-synt_2e. (286 aa)
leuSleucyl-tRNA synthetase; Pfam match to PF00133.13 tRNA-synt_1; Belongs to the class-I aminoacyl-tRNA synthetase family. (809 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. (845 aa)
argSarginyl-tRNA synthetase; Pfam matches to PF03485.7 Arg_tRNA_synt_N, and to PF00750.10 tRNA-synt_1d. (531 aa)
gatAglu-tRNAGln 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). (454 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. (921 aa)
pheTphenylalanyl-tRNA synthetase, beta subunit; Pfam matches to PF01588.11 tRNA_bind, and to PF03484.6 B5; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (776 aa)
pheSphenylalanyl-tRNA synthetase, alpha subunit; Pfam matches to PF02912.9 Phe_tRNA-synt_N, and to PF01409.11 tRNA-synt_2d; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (330 aa)
gatBglu-tRNAGln 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. (472 aa)
Cla_1233Conserved hypothetical protein, putative formyltransferase; Pfam match to PF00551.10 Formyl_trans_N. (297 aa)
Cla_1236Formyltransferase, putative; Pfam match to PF00551.10 Formyl_trans_N. (296 aa)
selAL-seryl-tRNA(SeC) selenium transferase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. (443 aa)
gltX2glutamyl-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. (463 aa)
Cla_1312Conserved hypothetical protein, formyltransferase domain protein; Pfam match to PF00551.10 Formyl_trans_N. (238 aa)
Cla_1323Conserved hypothetical protein, putative formyltransferase. (228 aa)
Your Current Organism:
Campylobacter lari
NCBI taxonomy Id: 306263
Other names: C. lari RM2100, Campylobacter lari RM2100, Campylobacter lari str. RM2100, Campylobacter lari strain RM2100
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