STRINGSTRING
serS serS lipB lipB Sros_1326 Sros_1326 aspS aspS proS proS glyQS glyQS lipB-2 lipB-2 lysS lysS glyS glyS Sros_4299 Sros_4299 Sros_4302 Sros_4302 pheT pheT pheS pheS alaS alaS aspS-2 aspS-2 hisS hisS thrS thrS glyS-2 glyS-2 lysS-2 lysS-2
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
Node Content
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:
serSSerine--tRNA ligase; 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). (420 aa)
lipBLipoyl(octanoyl) transferase; 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. (215 aa)
Sros_1326KEGG: afw:Anae109_1479 biotin--acetyl-CoA- carboxylase ligase. (274 aa)
aspSAspartate--tRNA ligase; 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 2 subfamily. (428 aa)
proSProline--tRNA ligase; 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 deacy [...] (580 aa)
glyQSAnticodon binding domain protein; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family. (461 aa)
lipB-2Lipoyl(octanoyl) transferase; 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. (225 aa)
lysSLysyl-tRNA synthetase (class II)-like protein; KEGG: lysine--tRNA ligase class II, chloroplast or mitochondrial; K04567 lysyl-tRNA synthetase, class II; Belongs to the class-II aminoacyl-tRNA synthetase family. (1098 aa)
glySGlycine--tRNA ligase; KEGG: hypothetical protein; K01878 glycyl-tRNA synthetase alpha chain. (1024 aa)
Sros_4299Asparaginase like protein 1-like protein; KEGG: similar to asparaginase like 1. (343 aa)
Sros_4302Prolyl-tRNA synthetase-like protein; KEGG: Prolyl-tRNA synthetase; K01881 prolyl-tRNA synthetase. (474 aa)
pheTPhenylalanine--tRNA ligase; KEGG: ank:AnaeK_1907 phenylalanyl-tRNA synthetase, beta subunit. (838 aa)
pheSPhenylalanine--tRNA ligase; KEGG: cja:CJA_2526 phenylalanyl-tRNA synthetase, alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (365 aa)
alaSAlanine--tRNA ligase; 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. (890 aa)
aspS-2aspartyl-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. (578 aa)
hisSHistidine--tRNA ligase; KEGG: noc:Noc_0902 histidyl-tRNA synthetase, class IIA. (421 aa)
thrSKEGG: mgm:Mmc1_0363 threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (659 aa)
glyS-2Glycine--tRNA ligase; KEGG: hypothetical protein; K01878 glycyl-tRNA synthetase alpha chain. (991 aa)
lysS-2KEGG: bsu:BSU00820 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (500 aa)
Your Current Organism:
Streptosporangium roseum
NCBI taxonomy Id: 479432
Other names: S. roseum DSM 43021, Streptosporangium roseum DSM 43021, Streptosporangium roseum str. DSM 43021, Streptosporangium roseum strain DSM 43021
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