STRINGSTRING
alaS alaS lipB lipB lysS lysS pheS pheS aspS aspS serS serS hisS hisS AsnS AsnS proS proS thrS thrS pheT pheT CAZ94757.1 CAZ94757.1 glyQS glyQS
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
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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:
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. (871 aa)
lipBLipoyltransferase; 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. (239 aa)
lysSLysyl-tRNA synthetase catalyzes the attachment of L-lysine to the tRNA(Lys) in a highly specific two-step reaction. LysS is an homodimer and binds 3 magnesium ions per subunit; Belongs to the class II of the aminoacyl-tRNA synthetases; Localized in the cytoplasm; High confidence in function and specificity. (562 aa)
pheSPheS encodes the alpha subunit of Phenylalanyl-tRNA synthetase. the Phenylalanyl-tRNA synthetase is an alpha2/beta2 tetramer that catalyzes the attachment of phenylalanine to its cognate transfer RNA molecule in a highly specific two-step reaction; Binds 2 magnesium ions per tetramer; Belongs to class II aminoacyl-tRNA synthetases; Localized in the cytoplasm; High confidence in function and specificity. (339 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. (584 aa)
serSSeryl-tRNA synthetase, class IIa; Seryl-tRNA synthetase is responsible for the attachment of serine to the 3' OH group of ribose of its cognate transfer RNA molecule (tRNA(Ser)) in a highly specific two-step reaction. It is a homodimer; Belongs to the class-IIa aminoacyl-tRNA synthetase family; Localized in the cytoplasm; High confidence in function and specificity. (423 aa)
hisSHistidyl-tRNA synthetase is responsible for the attachment of histidine to the 3' OH group of ribose of its cognate transfer RNA molecule (tRNA(His)) in a highly specific two-step reaction. It is a homodimer; Belongs to the class-IIa aminoacyl-tRNA synthetase family; Localized in the cytoplasm; High confidence in function and specificity. (458 aa)
AsnSAsparaginyltRNA synthetase catalyse the attachment of the aminoacid asparagine to the 3'-hydroxyl of the tRNA. It is an homodimer; Belongs to the class-II aminoacyl-tRNA synthetase family; Localized in the cytoplasm; High confidence in function and specificity. (477 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). (491 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). (648 aa)
pheTPhenylalanyl-tRNA synthetase catalyzes the attachment of phenylalanyl to its cognate transfer RNA molecule in a highly specific two-step reaction. It is an alpha2/beta2 tetramer composed of 2 subunits that belongs to class II aminoacyl-tRNA synthetases. PheT codes the beta subunit and folds as an anti-parallel beta-sheet flanked by alpha-helices. Phenylalanyl-tRNA synthetase binds 2 magnesium ions per tetramer. Localized in the cytoplasm; High confidence in function and specificity. (809 aa)
CAZ94757.1Biotin-[acetyl-CoA-carboxylase]ligase is responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. These enzymes usually transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Localized in the cytoplasm; High confidence in function and specificity. (243 aa)
glyQSGlycyl-tRNA synthetase; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family. (516 aa)
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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