STRINGSTRING
glyS glyS glyQ glyQ asnS asnS serS serS thrS thrS aspS aspS pheT pheT pheS pheS metG metG Sps_01471 Sps_01471 cysS cysS glnS glnS proS proS ileS ileS tyrS tyrS Sps_02817 Sps_02817 Sps_02818 Sps_02818 gltX gltX hisS hisS alaS alaS Sps_04165 Sps_04165 leuS leuS Sps_04511 Sps_04511 valS valS lysS lysS gluQ gluQ argS argS trpS trpS
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
Edges:
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:
glySPFAM: Glycyl-tRNA synthetase beta subunit; DALR anticodon binding domain; 'TIGRFAM: glycyl-tRNA synthetase, tetrameric type, beta subunit'. (689 aa)
glyQPFAM: Glycyl-tRNA synthetase alpha subunit; 'TIGRFAM: glycyl-tRNA synthetase, tetrameric type, alpha subunit'. (287 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)
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)
pheTphenylalanyl-tRNA synthetase beta subunit; PFAM: tRNA synthetase B5 domain; Ferredoxin-fold anticodon binding domain; B3/4 domain; Putative tRNA binding domain; 'TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial'; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (795 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)
metGmethionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (694 aa)
Sps_01471Hypothetical protein. (920 aa)
cysSPFAM: tRNA synthetases class I (C) catalytic domain; DALR domain; TIGRFAM: cysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (459 aa)
glnS'PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain'; TIGRFAM: glutaminyl-tRNA synthetase. (556 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)
ileSIsoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. (924 aa)
tyrStyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily. (398 aa)
Sps_02817Hypothetical protein. (112 aa)
Sps_02818Hypothetical protein; PFAM: tRNA synthetases class I (W and Y); TIGRFAM: tryptophanyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (257 aa)
gltXglutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). (469 aa)
hisSPFAM: Anticodon binding domain; Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase. (424 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. (874 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)
leuS'PFAM: Leucyl-tRNA synthetase, Domain 2; tRNA synthetases class I (I, L, M and V); Anticodon-binding domain of tRNA'; 'TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family'; Belongs to the class-I aminoacyl-tRNA synthetase family. (863 aa)
Sps_04511Hypothetical protein. (835 aa)
valSvalyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. (973 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)
gluQGlutamyl-queuosine tRNA(Asp) synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. (290 aa)
argSarginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. (581 aa)
trpStryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (335 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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