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hisS hisS birA birA pheT pheT pheS pheS proS proS alaS alaS thrS thrS AEH23356.1 AEH23356.1 glyQ glyQ aspS aspS lysS lysS serS serS
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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
protein homology
Your Input:
hisSPFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Anticodon-binding; TIGRFAM: Histidyl-tRNA synthetase, class IIa, subgroup; HAMAP: Histidyl-tRNA synthetase, class IIa, subgroup; KEGG: has:Halsa_1638 histidyl-tRNA synthetase. (438 aa)
birAbiotin/acetyl-CoA-carboxylase ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. (316 aa)
pheTTIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: chy:CHY_1570 phenylalanyl-tRNA synthetase subunit beta. (800 aa)
pheSTIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, alpha subunit; HAMAP: Phenylalanyl-tRNA synthetase alpha chain; KEGG: dte:Dester_0632 phenylalanyl-tRNA synthetase alpha chain; 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. (337 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)
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. (866 aa)
thrSKEGG: tye:THEYE_A1229 threonyl-tRNA synthetase; TIGRFAM: Threonyl-tRNA synthetase, class IIa; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Threonyl/alanyl tRNA synthetase, SAD; Anticodon-binding; Belongs to the class-II aminoacyl-tRNA synthetase family. (645 aa)
AEH23356.1KEGG: dak:DaAHT2_0465 biotin/acetyl-CoA-carboxylase ligase; TIGRFAM: Biotin--acetyl-CoA-carboxylase ligase; PFAM: Biotin/lipoate A/B protein ligase. (260 aa)
glyQPFAM: Glycyl-tRNA synthetase, class IIc, alpha subunit; TIGRFAM: Glycyl-tRNA synthetase, class IIc, alpha subunit; HAMAP: Glycyl-tRNA synthetase, class IIc, alpha subunit; KEGG: cni:Calni_0744 glycyl-tRNA synthetase alpha chain. (281 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. (598 aa)
lysSPFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; TIGRFAM: Lysyl-tRNA synthetase, class II; HAMAP: Lysyl-tRNA synthetase; KEGG: dvl:Dvul_0888 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (497 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)
Your Current Organism:
Thermodesulfobacterium geofontis
NCBI taxonomy Id: 795359
Other names: T. geofontis OPF15, Thermodesulfobacterium geofontis OPF15, Thermodesulfobacterium sp. OPF15
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