GTPase HflX [Candidatus Shapirobacteria bacterium CG08_land_8_20_14_0_20_39_18]
Protein Classification
HflX GTPase family protein( domain architecture ID 11455136)
HflX GTPase family protein similar to GTPase HflX, which is a GTP-binding protein with a GTP hydrolysis activity that is stimulated by binding to the 50S ribosome subunit, and it may play a role during protein synthesis or ribosome biogenesis
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| HflX | COG2262 | 50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
16-372 | 2.00e-116 | ||||||
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; : Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 344.38 E-value: 2.00e-116
|
||||||||||
| Name | Accession | Description | Interval | E-value | ||||||
| HflX | COG2262 | 50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
16-372 | 2.00e-116 | ||||||
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 344.38 E-value: 2.00e-116
|
||||||||||
| GTP_HflX | TIGR03156 | GTP-binding protein HflX; This protein family is one of a number of homologous small, ... |
20-370 | 1.81e-101 | ||||||
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: 304.01 E-value: 1.81e-101
|
||||||||||
| HflX | cd01878 | HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
165-370 | 1.16e-65 | ||||||
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: 206.93 E-value: 1.16e-65
|
||||||||||
| PRK11058 | PRK11058 | GTPase HflX; Provisional |
22-366 | 2.52e-57 | ||||||
GTPase HflX; Provisional Pssm-ID: 182934 [Multi-domain] Cd Length: 426 Bit Score: 192.63 E-value: 2.52e-57
|
||||||||||
| GTP-bdg_N | pfam13167 | GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. ... |
27-118 | 9.53e-25 | ||||||
GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. The full-length members bind and interact with the 50S ribosome and are GTPases, hydrolysing GTP/GDP/ATP/ADP. This N-terminal region is necessary for stability of the whole protein. Pssm-ID: 463797 [Multi-domain] Cd Length: 87 Bit Score: 96.27 E-value: 9.53e-25
|
||||||||||
| Name | Accession | Description | Interval | E-value | ||||||
| HflX | COG2262 | 50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
16-372 | 2.00e-116 | ||||||
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 344.38 E-value: 2.00e-116
|
||||||||||
| GTP_HflX | TIGR03156 | GTP-binding protein HflX; This protein family is one of a number of homologous small, ... |
20-370 | 1.81e-101 | ||||||
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: 304.01 E-value: 1.81e-101
|
||||||||||
| HflX | cd01878 | HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
165-370 | 1.16e-65 | ||||||
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: 206.93 E-value: 1.16e-65
|
||||||||||
| PRK11058 | PRK11058 | GTPase HflX; Provisional |
22-366 | 2.52e-57 | ||||||
GTPase HflX; Provisional Pssm-ID: 182934 [Multi-domain] Cd Length: 426 Bit Score: 192.63 E-value: 2.52e-57
|
||||||||||
| GTP-bdg_N | pfam13167 | GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. ... |
27-118 | 9.53e-25 | ||||||
GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. The full-length members bind and interact with the 50S ribosome and are GTPases, hydrolysing GTP/GDP/ATP/ADP. This N-terminal region is necessary for stability of the whole protein. Pssm-ID: 463797 [Multi-domain] Cd Length: 87 Bit Score: 96.27 E-value: 9.53e-25
|
||||||||||
| MMR_HSR1 | pfam01926 | 50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
207-327 | 7.56e-17 | ||||||
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: 75.73 E-value: 7.56e-17
|
||||||||||
| Era_like | cd00880 | E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
210-366 | 5.17e-15 | ||||||
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: 71.89 E-value: 5.17e-15
|
||||||||||
| Ras_like_GTPase | cd00882 | Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
210-366 | 9.50e-14 | ||||||
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: 68.25 E-value: 9.50e-14
|
||||||||||
| Obg_like | cd01881 | Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
210-366 | 1.16e-12 | ||||||
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: 65.49 E-value: 1.16e-12
|
||||||||||
| EngA1 | cd01894 | EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
210-366 | 1.40e-11 | ||||||
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: 62.07 E-value: 1.40e-11
|
||||||||||
| GTP-bdg_M | pfam16360 | GTP-binding GTPase Middle Region; This family locates between the N-terminal domain and ... |
122-200 | 1.13e-10 | ||||||
GTP-binding GTPase Middle Region; This family locates between the N-terminal domain and MMR_HSR1 50S ribosome-binding GTPase of GTP-binding HflX-like proteins. The full-length members bind and interact with the 50S ribosome and are GTPases, hydrolysing GTP/GDP/ATP/ADP. This region is unknown for its function. Pssm-ID: 465103 [Multi-domain] Cd Length: 79 Bit Score: 57.06 E-value: 1.13e-10
|
||||||||||
| Der | COG1160 | Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
205-372 | 1.57e-09 | ||||||
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 59.27 E-value: 1.57e-09
|
||||||||||
| PRK00093 | PRK00093 | GTP-binding protein Der; Reviewed |
206-372 | 2.00e-09 | ||||||
GTP-binding protein Der; Reviewed Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 58.91 E-value: 2.00e-09
|
||||||||||
| trmE | cd04164 | trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
207-367 | 3.58e-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: 55.19 E-value: 3.58e-09
|
||||||||||
| MnmE | COG0486 | tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
176-370 | 7.56e-08 | ||||||
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: 53.91 E-value: 7.56e-08
|
||||||||||
| era | PRK00089 | GTPase Era; Reviewed |
208-371 | 2.21e-07 | ||||||
GTPase Era; Reviewed Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 51.97 E-value: 2.21e-07
|
||||||||||
| Arf_Arl | cd00878 | ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
208-367 | 2.55e-07 | ||||||
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: 49.88 E-value: 2.55e-07
|
||||||||||
| Obg | cd01898 | Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
288-370 | 3.20e-07 | ||||||
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: 49.73 E-value: 3.20e-07
|
||||||||||
| Gem1 | COG1100 | GTPase SAR1 family domain [General function prediction only]; |
208-370 | 7.15e-07 | ||||||
GTPase SAR1 family domain [General function prediction only]; Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 48.82 E-value: 7.15e-07
|
||||||||||
| trmE | PRK05291 | tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
176-367 | 7.40e-07 | ||||||
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 50.88 E-value: 7.40e-07
|
||||||||||
| Era | COG1159 | GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
208-371 | 1.56e-06 | ||||||
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 49.22 E-value: 1.56e-06
|
||||||||||
| obgE | PRK12299 | GTPase CgtA; Reviewed |
288-370 | 4.99e-06 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 47.76 E-value: 4.99e-06
|
||||||||||
| Era | cd04163 | E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
208-366 | 6.69e-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: 45.92 E-value: 6.69e-06
|
||||||||||
| MnmE_helical | pfam12631 | MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
176-370 | 1.32e-05 | ||||||
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: 46.70 E-value: 1.32e-05
|
||||||||||
| small_GTP | TIGR00231 | small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
205-358 | 3.15e-05 | ||||||
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: 43.90 E-value: 3.15e-05
|
||||||||||
| EngA2 | cd01895 | EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
204-369 | 3.81e-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: 43.58 E-value: 3.81e-05
|
||||||||||
| PRK00093 | PRK00093 | GTP-binding protein Der; Reviewed |
186-369 | 1.52e-04 | ||||||
GTP-binding protein Der; Reviewed Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 43.50 E-value: 1.52e-04
|
||||||||||
| YeeP | COG3596 | Predicted GTPase [General function prediction only]; |
177-371 | 2.61e-04 | ||||||
Predicted GTPase [General function prediction only]; Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 42.45 E-value: 2.61e-04
|
||||||||||
| GTP_translation_factor | cd00881 | GTP translation factor family primarily contains translation initiation, elongation and ... |
207-372 | 3.62e-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: 41.13 E-value: 3.62e-04
|
||||||||||
| MMR_HSR1_Xtn | pfam16897 | C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ... |
285-366 | 8.31e-04 | ||||||
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: 38.56 E-value: 8.31e-04
|
||||||||||
| obgE | PRK12298 | GTPase CgtA; Reviewed |
288-370 | 4.22e-03 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237047 [Multi-domain] Cd Length: 390 Bit Score: 38.70 E-value: 4.22e-03
|
||||||||||
| GTP_EFTU | pfam00009 | Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
206-372 | 5.47e-03 | ||||||
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: 37.50 E-value: 5.47e-03
|
||||||||||
| infB | CHL00189 | translation initiation factor 2; Provisional |
177-366 | 8.64e-03 | ||||||
translation initiation factor 2; Provisional Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 38.27 E-value: 8.64e-03
|
||||||||||
| LepA | cd01890 | LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
313-372 | 9.98e-03 | ||||||
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype. Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 36.74 E-value: 9.98e-03
|
||||||||||
| Blast search parameters | ||||
|
