GTPase ObgE [Burkholderiales bacterium GJ-E10]
Protein Classification
GTPase Obg( domain architecture ID 11425313)
GTPase Obg is a P-loop small G protein that is implicated in a variety of functions including bacterial ribosomal biogenesis, the cell cycle, and stress response
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| Obg | COG0536 | GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ... |
3-343 | 0e+00 | ||||||
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, chromosome partitioning, Replication, recombination, and repair]; : Pssm-ID: 440302 [Multi-domain] Cd Length: 343 Bit Score: 567.69 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| Obg | COG0536 | GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ... |
3-343 | 0e+00 | ||||||
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, chromosome partitioning, Replication, recombination, and repair]; Pssm-ID: 440302 [Multi-domain] Cd Length: 343 Bit Score: 567.69 E-value: 0e+00
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| obgE | PRK12299 | GTPase CgtA; Reviewed |
2-344 | 0e+00 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 555.84 E-value: 0e+00
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| Obg_CgtA | TIGR02729 | Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ... |
3-336 | 0e+00 | ||||||
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome GTP-binding protein that associates with ribosomal subunits and appears to play a role in ribosomal RNA maturation. This GTPase, related to the nucleolar protein Obg, is designated CgtA in bacteria. Mutations in this gene are pleiotropic, but it appears that effects on cellular functions such as chromosome partition may be secondary to the effect on ribosome structure. Recent work done in Vibrio cholerae shows an essential role in the stringent response, in which RelA-dependent ability to synthesize the alarmone ppGpp is required for deletion of this GTPase to be lethal. [Protein synthesis, Other] Pssm-ID: 274271 [Multi-domain] Cd Length: 328 Bit Score: 550.49 E-value: 0e+00
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| Obg | cd01898 | Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
160-336 | 1.57e-95 | ||||||
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain. Pssm-ID: 206685 [Multi-domain] Cd Length: 170 Bit Score: 282.01 E-value: 1.57e-95
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| GTP1_OBG | pfam01018 | GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ... |
4-158 | 3.62e-77 | ||||||
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three glycine-rich regions inserted into a small 8-stranded beta-sandwich these regions form six left-handed collagen-like helices packed and H-bonded together. Pssm-ID: 460027 [Multi-domain] Cd Length: 155 Bit Score: 234.55 E-value: 3.62e-77
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| Name | Accession | Description | Interval | E-value | ||||||
| Obg | COG0536 | GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ... |
3-343 | 0e+00 | ||||||
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, chromosome partitioning, Replication, recombination, and repair]; Pssm-ID: 440302 [Multi-domain] Cd Length: 343 Bit Score: 567.69 E-value: 0e+00
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| obgE | PRK12299 | GTPase CgtA; Reviewed |
2-344 | 0e+00 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 555.84 E-value: 0e+00
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| Obg_CgtA | TIGR02729 | Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ... |
3-336 | 0e+00 | ||||||
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome GTP-binding protein that associates with ribosomal subunits and appears to play a role in ribosomal RNA maturation. This GTPase, related to the nucleolar protein Obg, is designated CgtA in bacteria. Mutations in this gene are pleiotropic, but it appears that effects on cellular functions such as chromosome partition may be secondary to the effect on ribosome structure. Recent work done in Vibrio cholerae shows an essential role in the stringent response, in which RelA-dependent ability to synthesize the alarmone ppGpp is required for deletion of this GTPase to be lethal. [Protein synthesis, Other] Pssm-ID: 274271 [Multi-domain] Cd Length: 328 Bit Score: 550.49 E-value: 0e+00
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| obgE | PRK12298 | GTPase CgtA; Reviewed |
1-343 | 0e+00 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237047 [Multi-domain] Cd Length: 390 Bit Score: 524.82 E-value: 0e+00
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| obgE | PRK12297 | GTPase CgtA; Reviewed |
3-343 | 6.45e-172 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237046 [Multi-domain] Cd Length: 424 Bit Score: 485.38 E-value: 6.45e-172
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| obgE | PRK12296 | GTPase CgtA; Reviewed |
1-339 | 5.19e-117 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237045 [Multi-domain] Cd Length: 500 Bit Score: 348.78 E-value: 5.19e-117
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| Obg | cd01898 | Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
160-336 | 1.57e-95 | ||||||
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain. Pssm-ID: 206685 [Multi-domain] Cd Length: 170 Bit Score: 282.01 E-value: 1.57e-95
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| GTP1_OBG | pfam01018 | GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ... |
4-158 | 3.62e-77 | ||||||
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three glycine-rich regions inserted into a small 8-stranded beta-sandwich these regions form six left-handed collagen-like helices packed and H-bonded together. Pssm-ID: 460027 [Multi-domain] Cd Length: 155 Bit Score: 234.55 E-value: 3.62e-77
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| Obg_like | cd01881 | Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
163-336 | 2.62e-41 | ||||||
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified. Pssm-ID: 206668 [Multi-domain] Cd Length: 167 Bit Score: 142.92 E-value: 2.62e-41
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| MMR_HSR1 | pfam01926 | 50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
161-288 | 4.09e-32 | ||||||
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: 116.95 E-value: 4.09e-32
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| Era_like | cd00880 | E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
163-336 | 9.01e-26 | ||||||
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: 101.55 E-value: 9.01e-26
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| DRG | cd01896 | Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ... |
160-291 | 8.16e-23 | ||||||
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding protein (DRG) subfamily is an uncharacterized member of the Obg family, an evolutionary branch of GTPase superfamily proteins. GTPases act as molecular switches regulating diverse cellular processes. DRG2 and DRG1 comprise the DRG subfamily in eukaryotes. In view of their widespread expression in various tissues and high conservation among distantly related species in eukaryotes and archaea, DRG proteins may regulate fundamental cellular processes. It is proposed that the DRG subfamily proteins play their physiological roles through RNA binding. Pssm-ID: 206683 [Multi-domain] Cd Length: 233 Bit Score: 95.31 E-value: 8.16e-23
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| Rbg1 | COG1163 | Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; |
160-328 | 1.09e-21 | ||||||
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440777 [Multi-domain] Cd Length: 368 Bit Score: 94.87 E-value: 1.09e-21
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| Ras_like_GTPase | cd00882 | Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
163-334 | 4.86e-21 | ||||||
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: 88.67 E-value: 4.86e-21
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| Ygr210 | cd01899 | Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ... |
162-248 | 2.49e-20 | ||||||
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They are characterized by a distinct glycine-rich motif immediately following the Walker B motif. The Ygr210 and YyaF/YchF subfamilies appear to form one major branch of the Obg-like family. Among eukaryotes, the Ygr210 subfamily is represented only in fungi. These fungal proteins form a tight cluster with their archaeal orthologs, which suggests the possibility of horizontal transfer from archaea to fungi. Pssm-ID: 206686 [Multi-domain] Cd Length: 318 Bit Score: 90.37 E-value: 2.49e-20
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| PRK09602 | PRK09602 | translation-associated GTPase; Reviewed |
162-248 | 1.25e-19 | ||||||
translation-associated GTPase; Reviewed Pssm-ID: 236584 [Multi-domain] Cd Length: 396 Bit Score: 89.48 E-value: 1.25e-19
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| PTZ00258 | PTZ00258 | GTP-binding protein; Provisional |
162-274 | 3.15e-18 | ||||||
GTP-binding protein; Provisional Pssm-ID: 240334 [Multi-domain] Cd Length: 390 Bit Score: 85.00 E-value: 3.15e-18
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| GTP1 | COG0012 | Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ... |
162-270 | 8.29e-18 | ||||||
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis]; Pssm-ID: 439783 [Multi-domain] Cd Length: 362 Bit Score: 83.53 E-value: 8.29e-18
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| Nog1 | COG1084 | GTP-binding protein, GTP1/Obg family [General function prediction only]; |
166-344 | 4.42e-17 | ||||||
GTP-binding protein, GTP1/Obg family [General function prediction only]; Pssm-ID: 440701 [Multi-domain] Cd Length: 330 Bit Score: 81.03 E-value: 4.42e-17
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| Era | COG1159 | GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
162-341 | 2.00e-16 | ||||||
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 78.49 E-value: 2.00e-16
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| YchF | cd01900 | YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ... |
162-271 | 5.90e-16 | ||||||
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of GTPases: Obg, DRG, Ygr210, and NOG1. Obg is an essential gene that is involved in DNA replication in C. crescentus and Streptomyces griseus and is associated with the ribosome. Several members of the family, including YchF, possess the TGS domain related to the RNA-binding proteins. Experimental data and genomic analysis suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translational factor. Pssm-ID: 206687 [Multi-domain] Cd Length: 274 Bit Score: 77.11 E-value: 5.90e-16
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| HflX | cd01878 | HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
147-336 | 7.01e-15 | ||||||
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: 72.49 E-value: 7.01e-15
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| Era | cd04163 | E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
162-329 | 8.04e-15 | ||||||
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: 71.34 E-value: 8.04e-15
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| HflX | COG2262 | 50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
162-336 | 4.99e-14 | ||||||
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 72.81 E-value: 4.99e-14
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| era | PRK00089 | GTPase Era; Reviewed |
162-341 | 6.96e-14 | ||||||
GTPase Era; Reviewed Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 71.23 E-value: 6.96e-14
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| GTP_HflX | TIGR03156 | GTP-binding protein HflX; This protein family is one of a number of homologous small, ... |
162-336 | 1.81e-13 | ||||||
GTP-binding protein HflX; This protein family is one of a number of homologous small, well-conserved GTP-binding proteins with pleiotropic effects. Bacterial members are designated HflX, following the naming convention in Escherichia coli where HflX is encoded immediately downstream of the RNA chaperone Hfq, and immediately upstream of HflKC, a membrane-associated protease pair with an important housekeeping function. Over large numbers of other bacterial genomes, the pairing with hfq is more significant than with hflK and hlfC. The gene from Homo sapiens in this family has been named PGPL (pseudoautosomal GTP-binding protein-like). [Unknown function, General] Pssm-ID: 274455 [Multi-domain] Cd Length: 351 Bit Score: 70.58 E-value: 1.81e-13
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| NOG | cd01897 | Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ... |
166-329 | 8.56e-13 | ||||||
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins. Pssm-ID: 206684 [Multi-domain] Cd Length: 167 Bit Score: 65.66 E-value: 8.56e-13
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| Gem1 | COG1100 | GTPase SAR1 family domain [General function prediction only]; |
162-340 | 2.43e-11 | ||||||
GTPase SAR1 family domain [General function prediction only]; Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 61.92 E-value: 2.43e-11
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| trmE | cd04164 | trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
164-336 | 7.75e-09 | ||||||
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: 54.04 E-value: 7.75e-09
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| era | TIGR00436 | GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ... |
162-342 | 1.61e-08 | ||||||
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other] Pssm-ID: 129528 [Multi-domain] Cd Length: 270 Bit Score: 55.09 E-value: 1.61e-08
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| TIGR00092 | TIGR00092 | GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in ... |
163-280 | 2.65e-08 | ||||||
GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in every complete bacterial genome, and is found in Eukaryotes. A more distantly related protein, separated from this model, is found in the archaea. It is known to bind GTP and double-stranded nucleic acid. It is suggested to belong to a nucleoprotein complex and act as a translation factor. [Unknown function, General] Pssm-ID: 129200 [Multi-domain] Cd Length: 368 Bit Score: 55.17 E-value: 2.65e-08
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| small_GTP | TIGR00231 | small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
162-324 | 8.63e-08 | ||||||
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General] Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 51.22 E-value: 8.63e-08
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| PRK11058 | PRK11058 | GTPase HflX; Provisional |
162-336 | 1.92e-07 | ||||||
GTPase HflX; Provisional Pssm-ID: 182934 [Multi-domain] Cd Length: 426 Bit Score: 52.41 E-value: 1.92e-07
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| trmE | PRK05291 | tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
164-336 | 7.57e-07 | ||||||
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 50.88 E-value: 7.57e-07
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| FeoB | cd01879 | Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
164-329 | 8.43e-07 | ||||||
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent. Pssm-ID: 206667 [Multi-domain] Cd Length: 159 Bit Score: 48.22 E-value: 8.43e-07
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| MnmE | COG0486 | tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
164-324 | 1.55e-06 | ||||||
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: 49.67 E-value: 1.55e-06
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| YihA_EngB | cd01876 | YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
162-332 | 2.00e-06 | ||||||
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: 47.51 E-value: 2.00e-06
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| PRK00093 | PRK00093 | GTP-binding protein Der; Reviewed |
162-334 | 3.08e-06 | ||||||
GTP-binding protein Der; Reviewed Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 48.89 E-value: 3.08e-06
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| EngA2 | cd01895 | EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
162-334 | 1.22e-05 | ||||||
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: 45.12 E-value: 1.22e-05
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| SelB_euk | cd01889 | SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
284-324 | 6.40e-05 | ||||||
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea. Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 43.51 E-value: 6.40e-05
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| FeoB | COG0370 | Fe2+ transporter FeoB [Inorganic ion transport and metabolism]; |
162-344 | 7.63e-05 | ||||||
Fe2+ transporter FeoB [Inorganic ion transport and metabolism]; Pssm-ID: 440139 [Multi-domain] Cd Length: 662 Bit Score: 44.73 E-value: 7.63e-05
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| DLP_2 | cd09912 | Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
169-319 | 1.32e-04 | ||||||
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: 42.15 E-value: 1.32e-04
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| Der | COG1160 | Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
162-334 | 2.83e-04 | ||||||
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 42.70 E-value: 2.83e-04
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| SelB | COG3276 | Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
284-343 | 7.33e-04 | ||||||
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 41.44 E-value: 7.33e-04
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| YeeP | COG3596 | Predicted GTPase [General function prediction only]; |
162-299 | 9.07e-04 | ||||||
Predicted GTPase [General function prediction only]; Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 40.90 E-value: 9.07e-04
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| cobW | pfam02492 | CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ... |
217-315 | 1.28e-03 | ||||||
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans. Pssm-ID: 396860 Cd Length: 179 Bit Score: 39.16 E-value: 1.28e-03
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| YqeH | cd01855 | Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
161-217 | 1.73e-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: 39.17 E-value: 1.73e-03
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| YjeQ_EngC | cd01854 | Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
284-328 | 1.89e-03 | ||||||
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ 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. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain. Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.30 E-value: 1.89e-03
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| MMR_HSR1_Xtn | pfam16897 | C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ... |
271-330 | 3.96e-03 | ||||||
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of the MMR_HSR1 family. Pssm-ID: 465301 [Multi-domain] Cd Length: 105 Bit Score: 36.64 E-value: 3.96e-03
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| Arl10_like | cd04159 | Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ... |
161-339 | 8.76e-03 | ||||||
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from a human cancer-derived EST dataset. No functional information about the subfamily is available at the current time, but crystal structures of human Arl10b and Arl10c have been solved. Pssm-ID: 206724 [Multi-domain] Cd Length: 159 Bit Score: 36.53 E-value: 8.76e-03
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