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thrS thrS hisS hisS glyQ glyQ alaS alaS asnA asnA b4155 b4155 asuD asuD drpA drpA serS serS asnS asnS pheS pheS aspS aspS lplA lplA pheT pheT lipB lipB
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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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). (642 aa)
hisSSimilar to Escherichia coli histidyl-tRNA synthetase HisS SW:SYH_ECOLI (P04804) (423 aa) fasta scores: E(): 0,82.0% id in 423 aa, and to Salmonella typhimurium histidyl-tRNA synthetase HisS SW:SYH_SALTY (O52765) (423 aa) fasta scores: E(): 0, 82.0% id in 423 aa. (424 aa)
glyQSimilar to Escherichia coli glycyl-tRNA synthetase alpha subunit GlyQ SW:SYGA_ECOLI (P00960) (303 aa) fasta scores: E(): 0, 93.7% id in 303 aa, and to Vibrio cholerae glycyl-tRNA synthetase alpha subunit GlyQ TR:Q9KVW7 (EMBL:AE004094) (330 aa) fasta scores: E(): 0, 88.8% id in 303 aa. (304 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; Belongs to the class-II aminoacyl-tRNA synthetase family. (875 aa)
asnASimilar to Escherichia coli aspartate-ammonia ligase AsnA SW:ASNA_ECOLI (P00963) (330 aa) fasta scores: E(): 0,78.5% id in 330 aa. (330 aa)
b4155Putative lysyl-tRNA synthetase; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P; Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. (325 aa)
asuDSimilar to Escherichia coli lysyl-tRNA synthetase LysS SW:SYK1_ECOLI (P13030) (504 aa) fasta scores: E(): 0,85.9% id in 504 aa, and to Haemophilus influenzae lysyl-tRNA synthetase LysS SW:SYK_HAEIN (P43825) (502 aa) fasta scores: E(): 0, 68.5% id in 504 aa; Belongs to the class-II aminoacyl-tRNA synthetase family. (505 aa)
drpAprolyl-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 [...] (572 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). (430 aa)
asnSSimilar to Escherichia coli asparaginyl-tRNA synthetase AsnS SW:SYN_ECOLI (P17242) (465 aa) fasta scores: E(): 0, 87.3% id in 465 aa, and to Haemophilus influenzae asparaginyl-tRNA synthetase AsnS SW:SYN_HAEIN (P43829) (477 aa) fasta scores: E(): 0, 79.5% id in 464 aa. (466 aa)
pheSSimilar to Escherichia coli phenylalanyl-tRNA synthetase alpha chain PheS SW:SYFA_ECOLI (P08312) (327 aa) fasta scores: E(): 0, 90.2% id in 327 aa, and to Vibrio cholerae phenylalanyl-tRNA synthetase alpha chain PheS TR:Q9KSN7 (EMBL:AE004202) (327 aa) fasta scores: E(): 0,76.1% id in 327 aa; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (327 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. (598 aa)
lplAConserved hypothetical protein (pseudogene); Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. (338 aa)
pheTSimilar to Escherichia coli phenylalanyl-tRNA synthetase beta chain PheT SW:SYFB_ECOLI (P07395) (795 aa) fasta scores: E(): 0, 83.4% id in 795 aa, and to Haemophilus influenzae phenylalanyl-tRNA synthetase beta chain PheT SW:SYFB_HAEIN (P43820) (795 aa) fasta scores: E(): 0, 64.7% id in 795 aa; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (795 aa)
lipBLipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. (233 aa)
Your Current Organism:
Yersinia pestis
NCBI taxonomy Id: 214092
Other names: Y. pestis CO92, Yersinia pestis CO92, Yersinia pestis str. CO92, Yersinia pestis strain CO92
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