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ADU65029.1 ADU65029.1 rpsL rpsL rplB rplB rpsQ rpsQ infA infA ADU65172.1 ADU65172.1 metG metG ADU65388.1 ADU65388.1 ADU65397.1 ADU65397.1 ADU65471.1 ADU65471.1 aspS aspS ligA ligA ADU65762.1 ADU65762.1 asnS asnS rnr rnr ruvA ruvA rimO rimO lysS lysS ADU66204.1 ADU66204.1 ADU66244.1 ADU66244.1 nusA nusA efp efp ADU66828.1 ADU66828.1 ADU66883.1 ADU66883.1 pnp pnp rho rho pheT pheT
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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
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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
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textmining
co-expression
protein homology
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ADU65029.1PFAM: (Uracil-5)-methyltransferase; KEGG: dap:Dacet_0891 (uracil-5)-methyltransferase; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. (385 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. (124 aa)
rplBRibosomal protein L2; 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. (274 aa)
rpsQ30S ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. (87 aa)
infATranslation initiation factor IF-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)
ADU65172.1KEGG: glo:Glov_1954 ATP-dependent DNA helicase RecG; PFAM: DEAD/DEAH box helicase domain protein; nucleic acid binding OB-fold tRNA/helicase-type; helicase domain protein; SMART: DEAD-like helicase; helicase domain protein. (675 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. (629 aa)
ADU65388.1Tex-like protein; KEGG: cth:Cthe_1955 RNA binding S1; PFAM: Tex-like protein-like; RNA binding S1 domain protein; SMART: Resolvase RNase H domain protein fold. (729 aa)
ADU65397.1Single-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. (152 aa)
ADU65471.1RNA binding S1 domain protein; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. (544 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. (592 aa)
ligADNA ligase, NAD-dependent; 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; Belongs to the NAD-dependent DNA ligase family. LigA subfamily. (660 aa)
ADU65762.1TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase HD sub domain; nucleic acid binding OB-fold tRNA/helicase-type; KEGG: sat:SYN_02192 HD-superfamily hydrolase; SMART: metal-dependent phosphohydrolase HD region. (375 aa)
asnSKEGG: pca:Pcar_0586 asparaginyl-tRNA synthetase; TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type. (448 aa)
rnrRibonuclease R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. (747 aa)
ruvAHolliday junction DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. (202 aa)
rimOMiaB-like tRNA modifying enzyme YliG; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (440 aa)
lysSKEGG: ddf:DEFDS_1155 lysyl-tRNA synthetase; TIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; Belongs to the class-II aminoacyl-tRNA synthetase family. (498 aa)
ADU66204.1KEGG: plm:Plim_2626 single-strand binding protein; TIGRFAM: single-strand binding protein; PFAM: single-strand binding protein/Primosomal replication protein n. (107 aa)
ADU66244.1Ribonuclease, Rne/Rng family; KEGG: gur:Gura_0301 ribonuclease; TIGRFAM: ribonuclease, Rne/Rng family; PFAM: RNA-binding protein AU-1/Ribonuclease E/G; RNA binding S1 domain protein. (501 aa)
nusATranscription termination factor NusA; Participates in both transcription termination and antitermination. (382 aa)
efpTranslation elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. (186 aa)
ADU66828.1PFAM: protein of unknown function DUF107; KEGG: nhl:Nhal_3157 protein of unknown function DUF107. (462 aa)
ADU66883.1KEGG: rca:Rcas_1237 spermidine/putrescine ABC transporter ATPase subunit; PFAM: ABC transporter related; SMART: AAA ATPase; Belongs to the ABC transporter superfamily. (365 aa)
pnpPolyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction. (722 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. (416 aa)
pheTKEGG: mxa:MXAN_3595 phenylalanyl-tRNA synthetase subunit beta; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (793 aa)
Your Current Organism:
Desulfurispirillum indicum
NCBI taxonomy Id: 653733
Other names: D. indicum S5, Desulfurispirillum indicum S5, Desulfurispirillum indicum str. S5, Desulfurispirillum indicum strain S5, bacterium S5, dissimilatory selenate-respiring bacterium S5
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