OBG-type G domain-containing protein [Caenorhabditis elegans]
Protein Classification
Obg family GTPase( domain architecture ID 1004071)
Obg family GTPase is a P-loop small G protein that may be 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_CgtA super family | cl37158 | Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ... |
27-310 | 7.43e-66 | |||||
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] The actual alignment was detected with superfamily member TIGR02729: Pssm-ID: 274271 [Multi-domain] Cd Length: 328 Bit Score: 212.28 E-value: 7.43e-66
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| Name | Accession | Description | Interval | E-value | ||||||
| Obg_CgtA | TIGR02729 | Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ... |
27-310 | 7.43e-66 | ||||||
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: 212.28 E-value: 7.43e-66
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| Obg | COG0536 | GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ... |
27-380 | 1.75e-61 | ||||||
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: 201.36 E-value: 1.75e-61
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| obgE | PRK12297 | GTPase CgtA; Reviewed |
27-311 | 2.80e-59 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237046 [Multi-domain] Cd Length: 424 Bit Score: 198.02 E-value: 2.80e-59
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| Obg | cd01898 | Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
163-369 | 5.37e-58 | ||||||
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: 186.48 E-value: 5.37e-58
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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 ... |
27-160 | 7.46e-31 | ||||||
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: 115.13 E-value: 7.46e-31
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| Name | Accession | Description | Interval | E-value | ||||||
| Obg_CgtA | TIGR02729 | Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ... |
27-310 | 7.43e-66 | ||||||
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: 212.28 E-value: 7.43e-66
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| Obg | COG0536 | GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ... |
27-380 | 1.75e-61 | ||||||
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: 201.36 E-value: 1.75e-61
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| obgE | PRK12297 | GTPase CgtA; Reviewed |
27-311 | 2.80e-59 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237046 [Multi-domain] Cd Length: 424 Bit Score: 198.02 E-value: 2.80e-59
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| obgE | PRK12299 | GTPase CgtA; Reviewed |
27-310 | 4.03e-58 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 192.59 E-value: 4.03e-58
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| Obg | cd01898 | Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
163-369 | 5.37e-58 | ||||||
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: 186.48 E-value: 5.37e-58
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| obgE | PRK12298 | GTPase CgtA; Reviewed |
27-367 | 8.26e-48 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237047 [Multi-domain] Cd Length: 390 Bit Score: 166.97 E-value: 8.26e-48
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| obgE | PRK12296 | GTPase CgtA; Reviewed |
27-304 | 6.40e-39 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237045 [Multi-domain] Cd Length: 500 Bit Score: 145.40 E-value: 6.40e-39
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| Obg_like | cd01881 | Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
165-310 | 2.00e-31 | ||||||
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: 117.11 E-value: 2.00e-31
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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 ... |
27-160 | 7.46e-31 | ||||||
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: 115.13 E-value: 7.46e-31
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| MMR_HSR1 | pfam01926 | 50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
163-302 | 1.52e-23 | ||||||
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: 94.22 E-value: 1.52e-23
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| Ygr210 | cd01899 | Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ... |
164-368 | 1.52e-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: 91.14 E-value: 1.52e-20
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| Era_like | cd00880 | E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
165-331 | 4.69e-19 | ||||||
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: 83.45 E-value: 4.69e-19
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| PRK09602 | PRK09602 | translation-associated GTPase; Reviewed |
164-294 | 1.62e-17 | ||||||
translation-associated GTPase; Reviewed Pssm-ID: 236584 [Multi-domain] Cd Length: 396 Bit Score: 83.32 E-value: 1.62e-17
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| Rbg1 | COG1163 | Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; |
145-266 | 5.89e-17 | ||||||
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440777 [Multi-domain] Cd Length: 368 Bit Score: 81.38 E-value: 5.89e-17
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| DRG | cd01896 | Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ... |
164-295 | 2.89e-16 | ||||||
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: 77.20 E-value: 2.89e-16
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| Gem1 | COG1100 | GTPase SAR1 family domain [General function prediction only]; |
164-377 | 6.57e-15 | ||||||
GTPase SAR1 family domain [General function prediction only]; Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 72.32 E-value: 6.57e-15
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| Ras_like_GTPase | cd00882 | Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
165-322 | 2.66e-13 | ||||||
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: 67.10 E-value: 2.66e-13
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| small_GTP | TIGR00231 | small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
161-312 | 9.42e-12 | ||||||
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: 62.77 E-value: 9.42e-12
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| Nog1 | COG1084 | GTP-binding protein, GTP1/Obg family [General function prediction only]; |
168-318 | 4.40e-11 | ||||||
GTP-binding protein, GTP1/Obg family [General function prediction only]; Pssm-ID: 440701 [Multi-domain] Cd Length: 330 Bit Score: 63.31 E-value: 4.40e-11
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| NOG | cd01897 | Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ... |
162-310 | 4.42e-11 | ||||||
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: 61.04 E-value: 4.42e-11
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| PTZ00258 | PTZ00258 | GTP-binding protein; Provisional |
163-257 | 1.14e-10 | ||||||
GTP-binding protein; Provisional Pssm-ID: 240334 [Multi-domain] Cd Length: 390 Bit Score: 62.66 E-value: 1.14e-10
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| EngA2 | cd01895 | EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
164-367 | 9.97e-10 | ||||||
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: 57.06 E-value: 9.97e-10
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| HflX | cd01878 | HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
162-353 | 3.92e-09 | ||||||
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: 55.93 E-value: 3.92e-09
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| Era | COG1159 | GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
164-363 | 6.96e-08 | ||||||
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 53.45 E-value: 6.96e-08
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| Der | COG1160 | Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
161-365 | 1.36e-07 | ||||||
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 53.10 E-value: 1.36e-07
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| Arf | pfam00025 | ADP-ribosylation factor family; Pfam combines a number of different Prosite families together |
164-326 | 4.43e-07 | ||||||
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together Pssm-ID: 459636 [Multi-domain] Cd Length: 160 Bit Score: 49.14 E-value: 4.43e-07
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| FeoB | COG0370 | Fe2+ transporter FeoB [Inorganic ion transport and metabolism]; |
162-358 | 8.50e-07 | ||||||
Fe2+ transporter FeoB [Inorganic ion transport and metabolism]; Pssm-ID: 440139 [Multi-domain] Cd Length: 662 Bit Score: 50.89 E-value: 8.50e-07
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| YeeP | COG3596 | Predicted GTPase [General function prediction only]; |
161-307 | 1.29e-06 | ||||||
Predicted GTPase [General function prediction only]; Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 49.76 E-value: 1.29e-06
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| era | PRK00089 | GTPase Era; Reviewed |
164-363 | 2.36e-06 | ||||||
GTPase Era; Reviewed Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 48.89 E-value: 2.36e-06
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| Era | cd04163 | E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
164-363 | 2.97e-06 | ||||||
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: 47.07 E-value: 2.97e-06
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| GTP_EFTU | pfam00009 | Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
159-365 | 4.91e-06 | ||||||
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains. Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 46.75 E-value: 4.91e-06
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| MnmE_helical | pfam12631 | MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
166-378 | 7.83e-06 | ||||||
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: 47.48 E-value: 7.83e-06
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| GTP_HflX | TIGR03156 | GTP-binding protein HflX; This protein family is one of a number of homologous small, ... |
162-310 | 8.04e-06 | ||||||
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: 47.47 E-value: 8.04e-06
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| SelB_euk | cd01889 | SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
163-323 | 2.50e-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: 44.66 E-value: 2.50e-05
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| FeoB | cd01879 | Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
166-357 | 5.94e-05 | ||||||
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: 42.83 E-value: 5.94e-05
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| YfjP | cd11383 | YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
165-304 | 1.36e-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: 41.56 E-value: 1.36e-04
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| PRK11058 | PRK11058 | GTPase HflX; Provisional |
162-310 | 1.60e-04 | ||||||
GTPase HflX; Provisional Pssm-ID: 182934 [Multi-domain] Cd Length: 426 Bit Score: 43.55 E-value: 1.60e-04
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| GTP_translation_factor | cd00881 | GTP translation factor family primarily contains translation initiation, elongation and ... |
163-339 | 8.37e-04 | ||||||
GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function. Pssm-ID: 206647 [Multi-domain] Cd Length: 183 Bit Score: 39.97 E-value: 8.37e-04
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| Arf_Arl | cd00878 | ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
163-353 | 1.10e-03 | ||||||
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions. Pssm-ID: 206644 [Multi-domain] Cd Length: 158 Bit Score: 39.10 E-value: 1.10e-03
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| DLP_2 | cd09912 | Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
171-310 | 1.20e-03 | ||||||
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: 39.45 E-value: 1.20e-03
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| HSR1_MMR1 | cd01857 | A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ... |
245-308 | 1.66e-03 | ||||||
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: 38.37 E-value: 1.66e-03
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| ARLTS1 | cd04156 | Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ... |
166-326 | 1.81e-03 | ||||||
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in high-risk familial breast cancer. Pssm-ID: 133356 [Multi-domain] Cd Length: 160 Bit Score: 38.55 E-value: 1.81e-03
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| HSR1_MMR1 | cd01857 | A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ... |
159-189 | 1.84e-03 | ||||||
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: 38.37 E-value: 1.84e-03
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| era | TIGR00436 | GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ... |
164-362 | 1.96e-03 | ||||||
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: 39.68 E-value: 1.96e-03
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| IF2_eIF5B | cd01887 | Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
248-365 | 2.51e-03 | ||||||
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s. Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 38.22 E-value: 2.51e-03
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| feoB | PRK09554 | Fe(2+) transporter permease subunit FeoB; |
164-321 | 6.07e-03 | ||||||
Fe(2+) transporter permease subunit FeoB; Pssm-ID: 236563 [Multi-domain] Cd Length: 772 Bit Score: 38.93 E-value: 6.07e-03
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