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rpsQ rpsQ ligA ligA aspS aspS Rmag_0436 Rmag_0436 pnp pnp rho rho Rmag_0510 Rmag_0510 rnr rnr rsgA rsgA Rmag_0592 Rmag_0592 lysS lysS pheT pheT ccmE ccmE Rmag_0680 Rmag_0680 infA infA Rmag_0922 Rmag_0922 Rmag_0928 Rmag_0928 Rmag_0944 Rmag_0944 rplB rplB rpsL rpsL efp efp nusA nusA
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:
rpsQSSU ribosomal protein S17P; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. (88 aa)
ligADNA ligase (NAD(+)); DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. (614 aa)
aspSaspartyl-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. (583 aa)
Rmag_0436TIGRFAM: ribonuclease, Rne/Rng family; PFAM: RNA binding S1 domain protein; KEGG: tcx:Tcr_0703 ribonuclease, Rne/Rng family. (584 aa)
pnpPolyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction. (695 aa)
rhoTranscription termination factor Rho; Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA- dependent ATPase activity, and release of the mRNA from the DNA template. (424 aa)
Rmag_0510Single-strand binding protein; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. (163 aa)
rnrRNAse R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. (705 aa)
rsgARibosome small subunit-dependent GTPase A; One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit; Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA subfamily. (318 aa)
Rmag_0592SSU ribosomal protein S1P; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. (558 aa)
lysSTIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetase, class II (D, K and N); nucleic acid binding, OB-fold, tRNA/helicase-type; KEGG: tcx:Tcr_0726 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (497 aa)
pheTTIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: sde:Sde_1582 phenylalanine--tRNA ligase. (780 aa)
ccmECcmE/CycJ protein; Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH. Belongs to the CcmE/CycJ family. (139 aa)
Rmag_0680PFAM: Cold-shock protein, DNA-binding; SMART: Cold shock protein. (104 aa)
infABacterial translation initiation factor 1 (bIF-1); One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. (72 aa)
Rmag_0922PFAM: ribonuclease II; KEGG: ftu:FTT0257 ribonuclease II family protein. (601 aa)
Rmag_0928ATP-dependent DNA helicase RecG; PFAM: helicase domain protein; nucleic acid binding, OB-fold, tRNA/helicase-type; DEAD/DEAH box helicase domain protein; KEGG: csa:Csal_3245 ATP-dependent DNA helicase RecG. (686 aa)
Rmag_0944PFAM: Cold-shock protein, DNA-binding; SMART: Cold shock protein; KEGG: bca:BCE5298 cold shock protein CspC. (67 aa)
rplBLSU ribosomal protein L2P; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family. (276 aa)
rpsLSSU ribosomal protein S12P; With S4 and S5 plays an important role in translational accuracy. (124 aa)
efpTranslation elongation factor P (EF-P); Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation; Belongs to the elongation factor P family. (187 aa)
nusANusA antitermination factor; Participates in both transcription termination and antitermination. (491 aa)
Your Current Organism:
Ruthia magnifica
NCBI taxonomy Id: 413404
Other names: C. Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica strain Cm (Calyptogena magnifica), Ruthia magnifica str. Cm (Calyptogena magnifica)
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