STRINGSTRING
rpsJ rpsJ rnpA rnpA gluQ gluQ trmU trmU EEU97970.1 EEU97970.1 rpsG rpsG rpsL rpsL pheT pheT pheS pheS rplA rplA EEU97124.1 EEU97124.1 EEU96860.1 EEU96860.1 rlmN rlmN thiI thiI metG metG alaS alaS dtd dtd ileS ileS typA typA tmcAL tmcAL gltX gltX thrS thrS rpsM rpsM rplE rplE EEU95590.1 EEU95590.1 rplP rplP
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.
Node Color
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:
rpsJRibosomal protein S10; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family. (103 aa)
rnpARibonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. (152 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. (314 aa)
trmUtRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. (371 aa)
EEU97970.1Hypothetical protein; Psort location: Cytoplasmic, score: 8.96. (1222 aa)
rpsGRibosomal protein S7; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family. (156 aa)
rpsLRibosomal protein S12; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. (142 aa)
pheTKEGG: tte:TTE1688 6.2e-155 pheT; phenylalanyl-tRNA synthetase beta subunit K01890; Psort location: Cytoplasmic, score: 9.97. (803 aa)
pheSKEGG: tte:TTE1689 4.4e-99 pheS; phenylalanyl-tRNA synthetase alpha subunit K01889; Psort location: Cytoplasmic, score: 10.00. (340 aa)
rplARibosomal protein L1; Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release. (230 aa)
EEU97124.1Hypothetical protein; KEGG: cno:NT01CX_2281 4.8e-13 trmU; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase K00566; Psort location: Cytoplasmic, score: 8.96. (170 aa)
EEU96860.1TIGR00255 family protein; Psort location: CytoplasmicMembrane, score: 9.82. (305 aa)
rlmN23S rRNA m2A2503 methyltransferase; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family. (346 aa)
thiIThiamine biosynthesis/tRNA modification protein ThiI; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. (399 aa)
metGmethionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (666 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. (886 aa)
dtdD-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. (153 aa)
ileSisoleucine--tRNA ligase; 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. (930 aa)
typAGTP-binding protein TypA; KEGG: bur:Bcep18194_A4648 3.1e-160 typA; GTP-binding protein TypA K06207; Psort location: Cytoplasmic, score: 9.97. (607 aa)
tmcALHypothetical protein; Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac- AMP) and then transfers the acetyl group to tRNA to form ac(4)C34. (417 aa)
gltXglutamate--tRNA ligase; 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). (472 aa)
thrSthreonine--tRNA ligase; KEGG: gka:GK2719 4.0e-167 thrS; threonyl-tRNA synthetase K01868; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family. (611 aa)
rpsM30S ribosomal protein S13; Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. Belongs to the universal ribosomal protein uS13 family. (130 aa)
rplERibosomal protein L5; This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. (182 aa)
EEU95590.1Putative fibronectin-binding protein; Psort location: Cytoplasmic, score: 8.96. (585 aa)
rplPRibosomal protein L16; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs; Belongs to the universal ribosomal protein uL16 family. (146 aa)
Your Current Organism:
Faecalibacterium prausnitzii A2165
NCBI taxonomy Id: 411483
Other names: F. prausnitzii A2-165, Faecalibacterium prausnitzii A2-165
Server load: low (38%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.