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pheT pheT texA texA metG metG ligC ligC AsnS AsnS nusA nusA ruvA ruvA rpsL rpsL rplB rplB rpsQ rpsQ infA infA rho rho cspA3 cspA3 csaA csaA rumA rumA ligA ligA rpsA rpsA rimO rimO pnpA pnpA engC engC lysS lysS recG recG efp efp cspA5 cspA5 cspA4 cspA4 CAZ98159.1 CAZ98159.1 cspA1 cspA1 CAZ95386.1 CAZ95386.1 ssb1 ssb1 rngA rngA CAZ95437.1 CAZ95437.1 recO recO vacB vacB cspA2 cspA2 aspS aspS ssb2 ssb2
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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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pheTPhenylalanyl-tRNA synthetase catalyzes the attachment of phenylalanyl to its cognate transfer RNA molecule in a highly specific two-step reaction. It is an alpha2/beta2 tetramer composed of 2 subunits that belongs to class II aminoacyl-tRNA synthetases. PheT codes the beta subunit and folds as an anti-parallel beta-sheet flanked by alpha-helices. Phenylalanyl-tRNA synthetase binds 2 magnesium ions per tetramer. Localized in the cytoplasm; High confidence in function and specificity. (809 aa)
texAThe protein Tex is a transcriptional accessory protein, but its exact function is not known. Contains a central RNAse H-like domain and a C-terminal S1 RNA binding domain; Localized in the cytoplasm; High confidence in function and specificity. (707 aa)
metGMethionyl-tRNA synthetase, class Ia; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (692 aa)
ligCDNA ligase (polydeoxyribonucleotide synthase) joins two DNA fragments by catalysing the formation of an internucleotide phosphodiester bond between 5-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using ATP as a coenzyme and as the energy source. It is essential for DNA replication, DNA recombination and DNA repair; Belongs to the ATP-dependent DNA ligase family; Localized in the cytoplasm; High confidence in function and specificity. (554 aa)
AsnSAsparaginyltRNA synthetase catalyse the attachment of the aminoacid asparagine to the 3'-hydroxyl of the tRNA. It is an homodimer; Belongs to the class-II aminoacyl-tRNA synthetase family; Localized in the cytoplasm; High confidence in function and specificity. (477 aa)
nusATranscription termination factor NusA; Participates in both transcription termination and antitermination. (410 aa)
ruvAHolliday junction DNA helicase; 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. (193 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. (152 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)
rpsQRibosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. (86 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. (71 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. (557 aa)
cspA3Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. (64 aa)
csaACsaA could serves as a molecular chaperone for exported proteins or alternatively acts by stabilizing the secA protein. Belongs to a putative tRNA binding domain family. Localized in the cytoplasm; Function unclear. (112 aa)
rumA23S rRNA (uracil-5-)-methyltransferase RumA; The RumA protein catalyzes the formation of 5-methyl-uridine at position 1939 (M-5-U1939) in 23S rRNA; Contains two structural domains: an N-terminal TRAM domain predicted to bind RNA and deliver the RNA-modifying enzymatic domain to their targets, and a C-terminal tRNA (Uracil-5-)-methyltransferase domain that displays the typical SAM-dependent methyltransferase fold; Belongs to the RNA M5U methyltransferase family; Localized in the cytoplasm; High confidence in function and specificity. (478 aa)
ligADNA ligase; 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. (665 aa)
rpsARibosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. (610 aa)
rimOMiaB-like tRNA modifying protein; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (433 aa)
pnpAPolyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction. (740 aa)
engCGTPase engC; 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. (322 aa)
lysSLysyl-tRNA synthetase catalyzes the attachment of L-lysine to the tRNA(Lys) in a highly specific two-step reaction. LysS is an homodimer and binds 3 magnesium ions per subunit; Belongs to the class II of the aminoacyl-tRNA synthetases; Localized in the cytoplasm; High confidence in function and specificity. (562 aa)
recGATP-dependent DNA helicase RecG; Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y- DNA); Belongs to the helicase family. RecG subfamily. (701 aa)
efpElongation 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. (188 aa)
cspA5Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. (63 aa)
cspA4Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. (151 aa)
CAZ98159.1Conserved hypothetical protein; Seems to contains a C-terminal OB motif involved in the oligonucleotide/oligosaccharide binding; Localized in the cytoplasm; Belongs to the CvfB family. (276 aa)
cspA1Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. (63 aa)
CAZ95386.1Conserved hypothetical protein; Localized in the cytoplasm. (125 aa)
ssb1Single-stranded DNA-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. (154 aa)
rngARibonuclease G is involved in the processing of the 5'-end of 16S rRNA. Could be involved in chromosome segregation and cell division. It may be one of the components of the cytoplasmic axial filaments bundles or merely regulate the formation of this structure; Contains a S1 motif domain; Belongs to the RNase E/G family, RNase G subfamily; Localized in the cytoplasm; High confidence in function and specificity. (515 aa)
CAZ95437.1Conserved hypothetical membrane protein; Contains three transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. (192 aa)
recODNA repair protein RecO; Involved in DNA repair and RecF pathway recombination. (239 aa)
vacBRibonuclease R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. (731 aa)
cspA2Cold shock proteins (CSPs) help the cell to survive in temperatures lower than optimum growth temperature. CSPs may act as RNA chaperones by destabilizing RNA secondary structures, regulating ribosomal translation, rate of mRNA degradation and termination of transcription; Contains a 'cold-shock domain' (CSD) involved in the single-strand nucleic-acid binding; Localized in the cytoplasm; High confidence in function and specificity. (64 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. (584 aa)
ssb2Single-stranded DNA-binding protein (SSB) is essential for replication of the chromosome. It is also involved in DNA recombination and repair. This protein forms a homotetramer. Localized in the cytoplasm; High confidence in function and specificity. (110 aa)
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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