MULTISPECIES: ribosome biogenesis GTP-binding protein YihA/YsxC [Vibrio]
Protein Classification
GTP-binding protein( domain architecture ID 1905333)
GTP-binding protein similar to YsxC/EngB, a GTPase associated with ribosome biogenesis; belongs to the large superfamily of translation factor-related (TRAFAC) GTPases
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| EngB | COG0218 | GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ... |
5-198 | 2.86e-115 | ||||
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning]; : Pssm-ID: 439988 [Multi-domain] Cd Length: 194 Bit Score: 326.64 E-value: 2.86e-115
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| Name | Accession | Description | Interval | E-value | ||||
| EngB | COG0218 | GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ... |
5-198 | 2.86e-115 | ||||
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 439988 [Multi-domain] Cd Length: 194 Bit Score: 326.64 E-value: 2.86e-115
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| GTPase_YsxC | TIGR03598 | ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ... |
10-188 | 3.96e-108 | ||||
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other] Pssm-ID: 274670 [Multi-domain] Cd Length: 179 Bit Score: 307.86 E-value: 3.96e-108
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| YihA_EngB | cd01876 | YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
29-198 | 1.03e-86 | ||||
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target. Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 253.59 E-value: 1.03e-86
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| MMR_HSR1 | pfam01926 | 50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
29-147 | 5.12e-22 | ||||
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide. Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 86.52 E-value: 5.12e-22
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| era | PRK00089 | GTPase Era; Reviewed |
30-209 | 4.19e-15 | ||||
GTPase Era; Reviewed Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 72.39 E-value: 4.19e-15
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| Name | Accession | Description | Interval | E-value | ||||
| EngB | COG0218 | GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ... |
5-198 | 2.86e-115 | ||||
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 439988 [Multi-domain] Cd Length: 194 Bit Score: 326.64 E-value: 2.86e-115
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| GTPase_YsxC | TIGR03598 | ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ... |
10-188 | 3.96e-108 | ||||
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other] Pssm-ID: 274670 [Multi-domain] Cd Length: 179 Bit Score: 307.86 E-value: 3.96e-108
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| YihA_EngB | cd01876 | YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
29-198 | 1.03e-86 | ||||
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target. Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 253.59 E-value: 1.03e-86
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| MMR_HSR1 | pfam01926 | 50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
29-147 | 5.12e-22 | ||||
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide. Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 86.52 E-value: 5.12e-22
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| Era_like | cd00880 | E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
31-198 | 8.08e-22 | ||||
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 87.69 E-value: 8.08e-22
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| era | PRK00089 | GTPase Era; Reviewed |
30-209 | 4.19e-15 | ||||
GTPase Era; Reviewed Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 72.39 E-value: 4.19e-15
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| Ras_like_GTPase | cd00882 | Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
31-194 | 8.58e-15 | ||||
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions. Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 69.02 E-value: 8.58e-15
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| Era | COG1159 | GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
30-211 | 6.83e-14 | ||||
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 68.86 E-value: 6.83e-14
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| Era | cd04163 | E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
30-194 | 3.32e-13 | ||||
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA. Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 64.79 E-value: 3.32e-13
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| PRK04213 | PRK04213 | GTP-binding protein EngB; |
23-85 | 1.50e-09 | ||||
GTP-binding protein EngB; Pssm-ID: 179790 [Multi-domain] Cd Length: 201 Bit Score: 55.69 E-value: 1.50e-09
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| trmE | cd04164 | trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
26-199 | 5.20e-07 | ||||
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance. Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 47.87 E-value: 5.20e-07
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| DLP_2 | cd09912 | Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
30-213 | 2.19e-06 | ||||
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner. Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 46.39 E-value: 2.19e-06
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| YeeP | COG3596 | Predicted GTPase [General function prediction only]; |
20-211 | 3.42e-06 | ||||
Predicted GTPase [General function prediction only]; Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 46.68 E-value: 3.42e-06
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| YlqF | cd01856 | Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ... |
37-82 | 1.56e-05 | ||||
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga). Pssm-ID: 206749 [Multi-domain] Cd Length: 171 Bit Score: 43.67 E-value: 1.56e-05
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| EngA2 | cd01895 | EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
26-196 | 1.47e-04 | ||||
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability. Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 40.88 E-value: 1.47e-04
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| MnmE | COG0486 | tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
26-198 | 1.77e-04 | ||||
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 440253 [Multi-domain] Cd Length: 448 Bit Score: 41.59 E-value: 1.77e-04
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| PRK00093 | PRK00093 | GTP-binding protein Der; Reviewed |
23-190 | 2.79e-04 | ||||
GTP-binding protein Der; Reviewed Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 41.19 E-value: 2.79e-04
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| YfjP | cd11383 | YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
31-150 | 3.18e-04 | ||||
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 39.63 E-value: 3.18e-04
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| HSR1_MMR1 | cd01857 | A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ... |
30-82 | 3.30e-04 | ||||
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC class I region and is highly homologous to a putative GTP-binding protein, MMR1 from mouse. These proteins represent a new subfamily of GTP-binding proteins that has only eukaryote members. This subfamily shows a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with sequence NKXD) are relocated to the N-terminus. Pssm-ID: 206750 [Multi-domain] Cd Length: 140 Bit Score: 39.52 E-value: 3.30e-04
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| HflX | cd01878 | HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
30-198 | 1.14e-03 | ||||
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms. Pssm-ID: 206666 [Multi-domain] Cd Length: 204 Bit Score: 38.59 E-value: 1.14e-03
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| YqeH | cd01855 | Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
32-83 | 1.14e-03 | ||||
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. Pssm-ID: 206748 [Multi-domain] Cd Length: 191 Bit Score: 38.40 E-value: 1.14e-03
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| Der | COG1160 | Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
23-50 | 1.49e-03 | ||||
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 38.85 E-value: 1.49e-03
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| MnmE_helical | pfam12631 | MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
26-198 | 1.67e-03 | ||||
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain. Pssm-ID: 463649 [Multi-domain] Cd Length: 326 Bit Score: 38.62 E-value: 1.67e-03
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| YlqF_related_GTPase | cd01849 | Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ... |
25-82 | 1.86e-03 | ||||
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases. Pssm-ID: 206746 [Multi-domain] Cd Length: 146 Bit Score: 37.36 E-value: 1.86e-03
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| PRK09518 | PRK09518 | bifunctional cytidylate kinase/GTPase Der; Reviewed |
30-196 | 2.67e-03 | ||||
bifunctional cytidylate kinase/GTPase Der; Reviewed Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 38.24 E-value: 2.67e-03
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| MJ1464 | cd01859 | An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ... |
19-82 | 2.89e-03 | ||||
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus. Pssm-ID: 206752 [Multi-domain] Cd Length: 157 Bit Score: 36.91 E-value: 2.89e-03
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| trmE | PRK05291 | tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
26-199 | 2.96e-03 | ||||
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 38.17 E-value: 2.96e-03
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| EngA1 | cd01894 | EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
34-198 | 6.40e-03 | ||||
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability. Pssm-ID: 206681 [Multi-domain] Cd Length: 157 Bit Score: 35.87 E-value: 6.40e-03
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