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aspS aspS Sps_04165 Sps_04165 pheS pheS proS proS asnS asnS serS serS thrS thrS hisS hisS lysS lysS
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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
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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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Your Input:
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. (595 aa)
Sps_04165'PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T)'; TIGRFAM: threonyl-tRNA synthetase. (392 aa)
pheSphenylalanyl-tRNA synthetase, alpha subunit; 'PFAM: tRNA synthetases class II core domain (F); Aminoacyl tRNA synthetase class II, N-terminal domain'; 'TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit'; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (327 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)
asnS'PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain'; TIGRFAM: asparaginyl-tRNA synthetase. (466 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). (428 aa)
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). (642 aa)
hisSPFAM: Anticodon binding domain; Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase. (424 aa)
lysS'PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain'; 'TIGRFAM: lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial'; Belongs to the class-II aminoacyl-tRNA synthetase family. (500 aa)
Your Current Organism:
Shewanella psychrophila
NCBI taxonomy Id: 225848
Other names: CGMCC 1.6159, JCM 13876, S. psychrophila, Shewanella psychrophila Xiao et al. 2007 emend. Thorell et al. 2019, Shewanella sp. WP2, strain WP2
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