tRNA modification GTPase MnmE [Geothrix oryzae]
Protein Classification
tRNA modification GTPase( domain architecture ID 11480540)
tRNA modification GTPase is involved in the modification of the wobble position of certain tRNAs and is one of the G proteins activated by nucleotide-dependent dimerization, such as bacterial MnmE and mitochondrial GTP-binding protein 3
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| trmE | PRK05291 | tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
6-439 | 1.79e-134 | |||||||
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; : Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 394.09 E-value: 1.79e-134
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| Name | Accession | Description | Interval | E-value | |||||||
| trmE | PRK05291 | tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
6-439 | 1.79e-134 | |||||||
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 394.09 E-value: 1.79e-134
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| MnmE | COG0486 | tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
7-439 | 3.20e-133 | |||||||
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: 390.96 E-value: 3.20e-133
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| MnmE_helical | pfam12631 | MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
120-436 | 8.17e-82 | |||||||
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: 255.10 E-value: 8.17e-82
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| mnmE_trmE_thdF | TIGR00450 | tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF ... |
12-439 | 4.76e-71 | |||||||
tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF (thiophene and furan oxidation protein), is a GTPase involved in tRNA modification to create 5-methylaminomethyl-2-thiouridine in the wobble position of some tRNAs. This protein and GidA form an alpha2/beta2 heterotetramer. [Protein synthesis, tRNA and rRNA base modification] Pssm-ID: 273083 [Multi-domain] Cd Length: 442 Bit Score: 230.83 E-value: 4.76e-71
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| trmE | cd04164 | trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
210-360 | 4.47e-55 | |||||||
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: 180.00 E-value: 4.47e-55
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| Name | Accession | Description | Interval | E-value | |||||||
| trmE | PRK05291 | tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
6-439 | 1.79e-134 | |||||||
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 394.09 E-value: 1.79e-134
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| MnmE | COG0486 | tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
7-439 | 3.20e-133 | |||||||
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: 390.96 E-value: 3.20e-133
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| MnmE_helical | pfam12631 | MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
120-436 | 8.17e-82 | |||||||
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: 255.10 E-value: 8.17e-82
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| mnmE_trmE_thdF | TIGR00450 | tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF ... |
12-439 | 4.76e-71 | |||||||
tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF (thiophene and furan oxidation protein), is a GTPase involved in tRNA modification to create 5-methylaminomethyl-2-thiouridine in the wobble position of some tRNAs. This protein and GidA form an alpha2/beta2 heterotetramer. [Protein synthesis, tRNA and rRNA base modification] Pssm-ID: 273083 [Multi-domain] Cd Length: 442 Bit Score: 230.83 E-value: 4.76e-71
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| trmE | cd04164 | trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
210-360 | 4.47e-55 | |||||||
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: 180.00 E-value: 4.47e-55
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| TrmE_N | cd14858 | N-terminal domain of TrmE, a tRNA modification GTPase; This family contains the N-terminal ... |
6-116 | 9.46e-41 | |||||||
N-terminal domain of TrmE, a tRNA modification GTPase; This family contains the N-terminal domain of TrmE (also known as MnmE, ThdF, MSS1), a guanine nucleotide-binding protein conserved in all three kingdoms of life. It is involved in the modification of uridine bases (U34) at the first anticodon (wobble) position of tRNAs decoding two-family box triplets. TrmE is a three-domain protein comprising an N-terminal alpha/beta domain, a helical domain, and the GTPase domain which is nested within the helical domain. The N-terminal domain induces dimerization for self-assembly and is topologically homologous to the tetrahydrofolate (THF)-binding domain of N,N-dimethylglycine oxidase (DMGO). However, the THF-binding site in DMGO is encoded on a single polypeptide, while homodimerization would be required to create a similar THF-binding site in TrmE. Dimerization also creates a second, symmetry-related THF-binding site. Biochemical and structural studies show that TrmE indeed binds formyl-THF. A cysteine residue, necessary for modification of U34, is located close to the C1-group donor 5-formyl-tetrahydrofolate, suggesting a direct role of TrmE in the modification analogous to DNA modification enzymes. Pssm-ID: 410986 [Multi-domain] Cd Length: 117 Bit Score: 140.95 E-value: 9.46e-41
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| TrmE_N | pfam10396 | GTP-binding protein TrmE N-terminus; This family represents the shorter, B, chain of the ... |
7-117 | 7.24e-36 | |||||||
GTP-binding protein TrmE N-terminus; This family represents the shorter, B, chain of the homo-dimeric structure which is a guanine nucleotide-binding protein that binds and hydrolyses GTP. TrmE is homologous to the tetrahydrofolate-binding domain of N,N-dimethylglycine oxidase and indeed binds formyl-tetrahydrofolate. TrmE actively participates in the formylation reaction of uridine and regulates the ensuing hydrogenation reaction of a Schiff's base intermediate. This B chain is the N-terminal portion of the protein consisting of five beta-strands and three alpha helices and is necessary for mediating dimer formation within the protein. Pssm-ID: 463072 [Multi-domain] Cd Length: 117 Bit Score: 128.24 E-value: 7.24e-36
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| Der | COG1160 | Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
212-296 | 3.01e-31 | |||||||
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 124.37 E-value: 3.01e-31
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| EngA2 | cd01895 | EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
211-298 | 1.66e-30 | |||||||
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: 115.61 E-value: 1.66e-30
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| PRK00093 | PRK00093 | GTP-binding protein Der; Reviewed |
210-298 | 1.83e-30 | |||||||
GTP-binding protein Der; Reviewed Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 122.08 E-value: 1.83e-30
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| GTPase_EngA | TIGR03594 | ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase ... |
211-298 | 3.70e-29 | |||||||
ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase with a duplication of its GTP-binding domain. It is broadly to universally distributed among bacteria. It appears to function in ribosome biogenesis or stability. [Protein synthesis, Other] Pssm-ID: 274667 [Multi-domain] Cd Length: 428 Bit Score: 118.32 E-value: 3.70e-29
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| MMR_HSR1 | pfam01926 | 50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
214-298 | 1.09e-26 | |||||||
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: 103.47 E-value: 1.09e-26
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| PRK00093 | PRK00093 | GTP-binding protein Der; Reviewed |
216-298 | 2.56e-24 | |||||||
GTP-binding protein Der; Reviewed Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 104.36 E-value: 2.56e-24
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| Era_like | cd00880 | E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
216-388 | 9.16e-24 | |||||||
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: 96.93 E-value: 9.16e-24
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| EngA1 | cd01894 | EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
216-296 | 1.03e-23 | |||||||
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: 96.74 E-value: 1.03e-23
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| GTPase_EngA | TIGR03594 | ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase ... |
215-298 | 4.23e-23 | |||||||
ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase with a duplication of its GTP-binding domain. It is broadly to universally distributed among bacteria. It appears to function in ribosome biogenesis or stability. [Protein synthesis, Other] Pssm-ID: 274667 [Multi-domain] Cd Length: 428 Bit Score: 100.60 E-value: 4.23e-23
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| Der | COG1160 | Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
215-296 | 2.06e-22 | |||||||
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 98.94 E-value: 2.06e-22
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| Ras_like_GTPase | cd00882 | Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
216-305 | 3.52e-17 | |||||||
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: 78.65 E-value: 3.52e-17
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| small_GTP | TIGR00231 | small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
214-305 | 1.45e-15 | |||||||
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: 73.95 E-value: 1.45e-15
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| PRK03003 | PRK03003 | GTP-binding protein Der; Reviewed |
214-271 | 1.45e-13 | |||||||
GTP-binding protein Der; Reviewed Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 72.31 E-value: 1.45e-13
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| PRK09518 | PRK09518 | bifunctional cytidylate kinase/GTPase Der; Reviewed |
214-304 | 3.58e-13 | |||||||
bifunctional cytidylate kinase/GTPase Der; Reviewed Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 71.36 E-value: 3.58e-13
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| Era | COG1159 | GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
216-359 | 9.79e-13 | |||||||
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 68.48 E-value: 9.79e-13
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| YeeP | COG3596 | Predicted GTPase [General function prediction only]; |
197-304 | 2.43e-12 | |||||||
Predicted GTPase [General function prediction only]; Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 67.48 E-value: 2.43e-12
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| Era | cd04163 | E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
216-303 | 9.70e-12 | |||||||
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: 63.25 E-value: 9.70e-12
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| era | PRK00089 | GTPase Era; Reviewed |
216-298 | 2.06e-11 | |||||||
GTPase Era; Reviewed Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 64.30 E-value: 2.06e-11
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| era | TIGR00436 | GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ... |
213-330 | 2.35e-10 | |||||||
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: 60.87 E-value: 2.35e-10
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| PRK09518 | PRK09518 | bifunctional cytidylate kinase/GTPase Der; Reviewed |
215-296 | 2.63e-10 | |||||||
bifunctional cytidylate kinase/GTPase Der; Reviewed Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 62.50 E-value: 2.63e-10
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| YlqF | cd01856 | Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ... |
197-269 | 4.71e-10 | |||||||
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: 58.31 E-value: 4.71e-10
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| YfjP | cd11383 | YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
216-304 | 6.42e-10 | |||||||
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: 56.96 E-value: 6.42e-10
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| PRK03003 | PRK03003 | GTP-binding protein Der; Reviewed |
215-296 | 1.08e-09 | |||||||
GTP-binding protein Der; Reviewed Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 59.98 E-value: 1.08e-09
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| FeoB_N | pfam02421 | Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ... |
213-269 | 2.04e-09 | |||||||
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (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: 460552 [Multi-domain] Cd Length: 156 Bit Score: 55.92 E-value: 2.04e-09
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| YqeH | cd01855 | Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
217-270 | 3.14e-09 | |||||||
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: 56.50 E-value: 3.14e-09
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| FeoB | cd01879 | Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
216-269 | 2.06e-08 | |||||||
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: 53.23 E-value: 2.06e-08
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| RbgA | COG1161 | Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis]; |
212-269 | 1.07e-07 | |||||||
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440775 [Multi-domain] Cd Length: 279 Bit Score: 52.80 E-value: 1.07e-07
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| feoB | TIGR00437 | ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ... |
219-297 | 2.36e-07 | |||||||
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane protein required for iron(II) update, is encoded in an operon with FeoA (75 amino acids), which is also required, and is regulated by Fur. There appear to be two copies in Archaeoglobus fulgidus and Clostridium acetobutylicum. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273077 [Multi-domain] Cd Length: 591 Bit Score: 52.82 E-value: 2.36e-07
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| FeoB | COG0370 | Fe2+ transporter FeoB [Inorganic ion transport and metabolism]; |
213-266 | 3.07e-07 | |||||||
Fe2+ transporter FeoB [Inorganic ion transport and metabolism]; Pssm-ID: 440139 [Multi-domain] Cd Length: 662 Bit Score: 52.81 E-value: 3.07e-07
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| Rbg1 | COG1163 | Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; |
215-296 | 1.52e-06 | |||||||
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440777 [Multi-domain] Cd Length: 368 Bit Score: 49.80 E-value: 1.52e-06
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| HflX | cd01878 | HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
197-236 | 4.07e-06 | |||||||
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: 47.45 E-value: 4.07e-06
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| PksD | COG3321 | Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
44-429 | 8.45e-06 | |||||||
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 48.33 E-value: 8.45e-06
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| HflX | COG2262 | 50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
197-236 | 1.75e-05 | |||||||
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 46.62 E-value: 1.75e-05
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| PRK09602 | PRK09602 | translation-associated GTPase; Reviewed |
213-270 | 3.35e-05 | |||||||
translation-associated GTPase; Reviewed Pssm-ID: 236584 [Multi-domain] Cd Length: 396 Bit Score: 45.95 E-value: 3.35e-05
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| GTP_HflX | TIGR03156 | GTP-binding protein HflX; This protein family is one of a number of homologous small, ... |
197-236 | 5.45e-05 | |||||||
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: 45.16 E-value: 5.45e-05
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| YihA_EngB | cd01876 | YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
216-248 | 6.67e-05 | |||||||
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: 43.27 E-value: 6.67e-05
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| DLP_2 | cd09912 | Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
213-298 | 1.72e-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: 1.72e-04
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| ABCF_EF-3 | cd03221 | ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
208-239 | 2.27e-04 | |||||||
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions. Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 41.28 E-value: 2.27e-04
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| Toc34_like | cd01853 | Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ... |
209-275 | 2.47e-04 | |||||||
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon. Pssm-ID: 206652 Cd Length: 248 Bit Score: 42.30 E-value: 2.47e-04
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| Ygr210 | cd01899 | Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ... |
215-270 | 2.48e-04 | |||||||
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: 42.99 E-value: 2.48e-04
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| Obg_like | cd01881 | Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
216-309 | 2.50e-04 | |||||||
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: 41.61 E-value: 2.50e-04
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| YlqF_related_GTPase | cd01849 | Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ... |
212-254 | 3.84e-04 | |||||||
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: 40.45 E-value: 3.84e-04
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| DRG | cd01896 | Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ... |
214-296 | 5.24e-04 | |||||||
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: 41.38 E-value: 5.24e-04
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| GTP1 | COG0012 | Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ... |
213-232 | 9.09e-04 | |||||||
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis]; Pssm-ID: 439783 [Multi-domain] Cd Length: 362 Bit Score: 41.16 E-value: 9.09e-04
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| ABC_tran | pfam00005 | ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
209-235 | 1.40e-03 | |||||||
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains. Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 39.17 E-value: 1.40e-03
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| HSR1_MMR1 | cd01857 | A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ... |
217-248 | 1.60e-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: 38.75 E-value: 1.60e-03
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| TagH | COG1134 | ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
185-234 | 2.50e-03 | |||||||
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism]; Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 39.29 E-value: 2.50e-03
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| PTZ00258 | PTZ00258 | GTP-binding protein; Provisional |
213-232 | 2.63e-03 | |||||||
GTP-binding protein; Provisional Pssm-ID: 240334 [Multi-domain] Cd Length: 390 Bit Score: 39.93 E-value: 2.63e-03
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| YchF | cd01900 | YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ... |
218-232 | 3.51e-03 | |||||||
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: 38.98 E-value: 3.51e-03
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| MJ1464 | cd01859 | An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ... |
214-269 | 5.16e-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: 37.68 E-value: 5.16e-03
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| Dynamin_N | pfam00350 | Dynamin family; |
215-254 | 5.79e-03 | |||||||
Dynamin family; Pssm-ID: 459775 [Multi-domain] Cd Length: 168 Bit Score: 37.60 E-value: 5.79e-03
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| Uup | COG0488 | ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
208-238 | 6.33e-03 | |||||||
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only]; Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 38.89 E-value: 6.33e-03
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| Obg | cd01898 | Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
215-245 | 6.39e-03 | |||||||
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: 37.40 E-value: 6.39e-03
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| ABCC_cytochrome_bd | cd03247 | ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
209-305 | 9.66e-03 | |||||||
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism. Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 36.91 E-value: 9.66e-03
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