STRINGSTRING
leuS leuS argS argS gltX gltX proS proS guaA-2 guaA-2 gltX-2 gltX-2 metG metG AFG35343.1 AFG35343.1 pheS pheS pheT pheT lysS lysS ileS ileS tyrS tyrS
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:
leuSPFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; Belongs to the class-I aminoacyl-tRNA synthetase family. (818 aa)
argSarginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R). (542 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (472 aa)
proSprolyl-tRNA synthetase, family II; 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 i [...] (572 aa)
guaA-2GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. (514 aa)
gltX-2glutamyl-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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (456 aa)
metGProtein containing C-terminal region/beta chain of methionyl-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. (653 aa)
AFG35343.1Putative GTPase, probable translation factor; PFAM: Protein of unknown function (DUF933). (354 aa)
pheSphenylalanyl-tRNA synthetase, alpha subunit; PFAM: tRNA synthetases class II core domain (F); Aminoacyl tRNA synthetase class II, N-terminal domain; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (333 aa)
pheTphenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (780 aa)
lysSlysyl-tRNA synthetase (class II); PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; Belongs to the class-II aminoacyl-tRNA synthetase family. (505 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. (912 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. (404 aa)
Your Current Organism:
Fervidobacterium pennivorans
NCBI taxonomy Id: 771875
Other names: F. pennivorans DSM 9078, Fervidobacterium pennivorans DSM 9078, Fervidobacterium pennivorans str. DSM 9078, Fervidobacterium pennivorans strain DSM 9078
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