GTP-binding protein, HflX [Arabidopsis thaliana]
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]; ... |
5-372 | 0e+00 | ||||||
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; : Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 568.18 E-value: 0e+00
|
||||||||||
| Name | Accession | Description | Interval | E-value | ||||||
| HflX | COG2262 | 50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
5-372 | 0e+00 | ||||||
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 568.18 E-value: 0e+00
|
||||||||||
| GTP_HflX | TIGR03156 | GTP-binding protein HflX; This protein family is one of a number of homologous small, ... |
5-318 | 1.10e-167 | ||||||
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: 472.73 E-value: 1.10e-167
|
||||||||||
| HflX | cd01878 | HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
115-318 | 1.28e-112 | ||||||
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: 327.11 E-value: 1.28e-112
|
||||||||||
| PRK11058 | PRK11058 | GTPase HflX; Provisional |
8-357 | 2.68e-110 | ||||||
GTPase HflX; Provisional Pssm-ID: 182934 [Multi-domain] Cd Length: 426 Bit Score: 329.37 E-value: 2.68e-110
|
||||||||||
| GTP-bdg_M | pfam16360 | GTP-binding GTPase Middle Region; This family locates between the N-terminal domain and ... |
73-150 | 1.01e-34 | ||||||
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: 122.93 E-value: 1.01e-34
|
||||||||||
| Name | Accession | Description | Interval | E-value | ||||||
| HflX | COG2262 | 50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
5-372 | 0e+00 | ||||||
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 568.18 E-value: 0e+00
|
||||||||||
| GTP_HflX | TIGR03156 | GTP-binding protein HflX; This protein family is one of a number of homologous small, ... |
5-318 | 1.10e-167 | ||||||
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: 472.73 E-value: 1.10e-167
|
||||||||||
| HflX | cd01878 | HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
115-318 | 1.28e-112 | ||||||
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: 327.11 E-value: 1.28e-112
|
||||||||||
| PRK11058 | PRK11058 | GTPase HflX; Provisional |
8-357 | 2.68e-110 | ||||||
GTPase HflX; Provisional Pssm-ID: 182934 [Multi-domain] Cd Length: 426 Bit Score: 329.37 E-value: 2.68e-110
|
||||||||||
| GTP-bdg_M | pfam16360 | GTP-binding GTPase Middle Region; This family locates between the N-terminal domain and ... |
73-150 | 1.01e-34 | ||||||
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: 122.93 E-value: 1.01e-34
|
||||||||||
| GTP-bdg_N | pfam13167 | GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. ... |
5-70 | 4.60e-32 | ||||||
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: 115.91 E-value: 4.60e-32
|
||||||||||
| MMR_HSR1 | pfam01926 | 50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
158-276 | 1.78e-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: 101.93 E-value: 1.78e-26
|
||||||||||
| Era_like | cd00880 | E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
160-310 | 7.32e-23 | ||||||
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: 93.85 E-value: 7.32e-23
|
||||||||||
| Obg_CgtA | TIGR02729 | Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ... |
158-318 | 5.61e-20 | ||||||
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: 89.79 E-value: 5.61e-20
|
||||||||||
| Obg | cd01898 | Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
158-318 | 2.32e-19 | ||||||
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: 84.40 E-value: 2.32e-19
|
||||||||||
| MnmE | COG0486 | tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
74-329 | 2.60e-19 | ||||||
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: 88.96 E-value: 2.60e-19
|
||||||||||
| Ras_like_GTPase | cd00882 | Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
160-314 | 3.96e-18 | ||||||
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: 80.96 E-value: 3.96e-18
|
||||||||||
| trmE | PRK05291 | tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
74-322 | 6.34e-18 | ||||||
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 84.78 E-value: 6.34e-18
|
||||||||||
| Era | cd04163 | E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
158-318 | 1.36e-17 | ||||||
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: 79.43 E-value: 1.36e-17
|
||||||||||
| Obg_like | cd01881 | Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
160-318 | 3.59e-17 | ||||||
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: 78.20 E-value: 3.59e-17
|
||||||||||
| obgE | PRK12299 | GTPase CgtA; Reviewed |
158-319 | 5.04e-17 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 81.27 E-value: 5.04e-17
|
||||||||||
| era | PRK00089 | GTPase Era; Reviewed |
158-321 | 8.87e-17 | ||||||
GTPase Era; Reviewed Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 79.71 E-value: 8.87e-17
|
||||||||||
| obgE | PRK12297 | GTPase CgtA; Reviewed |
158-319 | 9.71e-17 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237046 [Multi-domain] Cd Length: 424 Bit Score: 81.30 E-value: 9.71e-17
|
||||||||||
| trmE | cd04164 | trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
158-319 | 1.30e-16 | ||||||
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: 76.38 E-value: 1.30e-16
|
||||||||||
| Era | COG1159 | GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
158-318 | 9.63e-15 | ||||||
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 73.87 E-value: 9.63e-15
|
||||||||||
| MnmE_helical | pfam12631 | MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
118-318 | 2.54e-14 | ||||||
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: 73.28 E-value: 2.54e-14
|
||||||||||
| obgE | PRK12298 | GTPase CgtA; Reviewed |
158-320 | 3.81e-14 | ||||||
GTPase CgtA; Reviewed Pssm-ID: 237047 [Multi-domain] Cd Length: 390 Bit Score: 72.98 E-value: 3.81e-14
|
||||||||||
| EngA2 | cd01895 | EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
158-316 | 7.68e-14 | ||||||
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: 69.00 E-value: 7.68e-14
|
||||||||||
| PRK09518 | PRK09518 | bifunctional cytidylate kinase/GTPase Der; Reviewed |
131-318 | 5.13e-13 | ||||||
bifunctional cytidylate kinase/GTPase Der; Reviewed Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 70.59 E-value: 5.13e-13
|
||||||||||
| Der | COG1160 | Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
156-320 | 6.21e-12 | ||||||
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 66.59 E-value: 6.21e-12
|
||||||||||
| YihA_EngB | cd01876 | YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
158-309 | 7.02e-12 | ||||||
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: 63.30 E-value: 7.02e-12
|
||||||||||
| NOG | cd01897 | Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ... |
156-319 | 1.66e-10 | ||||||
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: 59.11 E-value: 1.66e-10
|
||||||||||
| PRK03003 | PRK03003 | GTP-binding protein Der; Reviewed |
149-318 | 3.07e-10 | ||||||
GTP-binding protein Der; Reviewed Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 61.52 E-value: 3.07e-10
|
||||||||||
| PRK00093 | PRK00093 | GTP-binding protein Der; Reviewed |
156-318 | 6.70e-10 | ||||||
GTP-binding protein Der; Reviewed Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 60.45 E-value: 6.70e-10
|
||||||||||
| YeeP | COG3596 | Predicted GTPase [General function prediction only]; |
143-281 | 9.03e-10 | ||||||
Predicted GTPase [General function prediction only]; Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 59.39 E-value: 9.03e-10
|
||||||||||
| EngA1 | cd01894 | EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
160-309 | 1.80e-09 | ||||||
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: 55.90 E-value: 1.80e-09
|
||||||||||
| PRK00093 | PRK00093 | GTP-binding protein Der; Reviewed |
158-316 | 9.38e-09 | ||||||
GTP-binding protein Der; Reviewed Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 56.60 E-value: 9.38e-09
|
||||||||||
| small_GTP | TIGR00231 | small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
156-309 | 1.66e-08 | ||||||
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General] Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 53.53 E-value: 1.66e-08
|
||||||||||
| DLP_2 | cd09912 | Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
158-306 | 1.82e-08 | ||||||
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: 53.70 E-value: 1.82e-08
|
||||||||||
| Der | COG1160 | Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
147-316 | 3.08e-08 | ||||||
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 55.03 E-value: 3.08e-08
|
||||||||||
| Rbg1 | COG1163 | Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; |
125-192 | 1.10e-07 | ||||||
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440777 [Multi-domain] Cd Length: 368 Bit Score: 53.26 E-value: 1.10e-07
|
||||||||||
| IF2_eIF5B | cd01887 | Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
156-309 | 1.54e-07 | ||||||
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: 50.55 E-value: 1.54e-07
|
||||||||||
| PTZ00258 | PTZ00258 | GTP-binding protein; Provisional |
158-264 | 3.70e-07 | ||||||
GTP-binding protein; Provisional Pssm-ID: 240334 [Multi-domain] Cd Length: 390 Bit Score: 51.48 E-value: 3.70e-07
|
||||||||||
| PRK03003 | PRK03003 | GTP-binding protein Der; Reviewed |
154-318 | 9.81e-07 | ||||||
GTP-binding protein Der; Reviewed Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 50.35 E-value: 9.81e-07
|
||||||||||
| FeoB_N | pfam02421 | Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ... |
157-314 | 5.78e-06 | ||||||
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: 45.90 E-value: 5.78e-06
|
||||||||||
| PRK04213 | PRK04213 | GTP-binding protein EngB; |
156-286 | 9.87e-06 | ||||||
GTP-binding protein EngB; Pssm-ID: 179790 [Multi-domain] Cd Length: 201 Bit Score: 46.06 E-value: 9.87e-06
|
||||||||||
| PRK09518 | PRK09518 | bifunctional cytidylate kinase/GTPase Der; Reviewed |
154-320 | 2.96e-05 | ||||||
bifunctional cytidylate kinase/GTPase Der; Reviewed Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 45.94 E-value: 2.96e-05
|
||||||||||
| YfjP | cd11383 | YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
160-310 | 3.15e-05 | ||||||
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: 43.48 E-value: 3.15e-05
|
||||||||||
| GTP_EFTU | pfam00009 | Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
154-318 | 5.00e-05 | ||||||
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: 43.67 E-value: 5.00e-05
|
||||||||||
| Arf_Arl | cd00878 | ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
160-309 | 9.40e-05 | ||||||
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: 42.56 E-value: 9.40e-05
|
||||||||||
| FeoB | COG0370 | Fe2+ transporter FeoB [Inorganic ion transport and metabolism]; |
156-320 | 1.02e-04 | ||||||
Fe2+ transporter FeoB [Inorganic ion transport and metabolism]; Pssm-ID: 440139 [Multi-domain] Cd Length: 662 Bit Score: 44.34 E-value: 1.02e-04
|
||||||||||
| YlqF | cd01856 | Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ... |
93-212 | 1.24e-04 | ||||||
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: 42.13 E-value: 1.24e-04
|
||||||||||
| DRG | cd01896 | Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ... |
158-192 | 1.75e-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: 42.53 E-value: 1.75e-04
|
||||||||||
| HflX_C | pfam19275 | HflX C-terminal domain; This entry represents the C-terminal domain of the HflX protein. HflX ... |
286-356 | 1.82e-04 | ||||||
HflX C-terminal domain; This entry represents the C-terminal domain of the HflX protein. HflX binds to the intersubunit face of the 50S subunit. Its C-terminal domain (CTD) predominantly interacts with the NTD of uL11 at the bL12 stalk base. Truncation of the CTD rendered HflX inactive in 70S splitting. Pssm-ID: 437107 Cd Length: 102 Bit Score: 40.37 E-value: 1.82e-04
|
||||||||||
| Arl6 | cd04157 | Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ... |
158-309 | 2.55e-04 | ||||||
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small GTPases. Arl6 expression is limited to the brain and kidney in adult mice, but it is expressed in the neural plate and somites during embryogenesis, suggesting a possible role for Arl6 in early development. Arl6 is also believed to have a role in cilia or flagella function. Several proteins have been identified that bind Arl6, including Arl6 interacting protein (Arl6ip), and SEC61beta, a subunit of the heterotrimeric conducting channel SEC61p. Based on Arl6 binding to these effectors, Arl6 is also proposed to play a role in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. At least three specific homozygous Arl6 mutations in humans have been found to cause Bardet-Biedl syndrome, a disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, and hypogenitalism. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily. Pssm-ID: 206722 [Multi-domain] Cd Length: 162 Bit Score: 41.26 E-value: 2.55e-04
|
||||||||||
| feoB | TIGR00437 | ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ... |
162-333 | 2.70e-04 | ||||||
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: 42.81 E-value: 2.70e-04
|
||||||||||
| FeoB | cd01879 | Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
160-309 | 2.78e-04 | ||||||
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: 40.90 E-value: 2.78e-04
|
||||||||||
| InfB | COG0532 | Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
275-309 | 9.21e-04 | ||||||
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 41.15 E-value: 9.21e-04
|
||||||||||
| Arfrp1 | cd04160 | Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ... |
158-309 | 9.67e-04 | ||||||
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a membrane-associated Arf family member that lacks the N-terminal myristoylation motif. Arfrp1 is mainly associated with the trans-Golgi compartment and the trans-Golgi network, where it regulates the targeting of Arl1 and the GRIP domain-containing proteins, golgin-97 and golgin-245, onto Golgi membranes. It is also involved in the anterograde transport of the vesicular stomatitis virus G protein from the Golgi to the plasma membrane, and in the retrograde transport of TGN38 and Shiga toxin from endosomes to the trans-Golgi network. Arfrp1 also inhibits Arf/Sec7-dependent activation of phospholipase D. Deletion of Arfrp1 in mice causes embryonic lethality at the gastrulation stage and apoptosis of mesodermal cells, indicating its importance in development. Pssm-ID: 206725 [Multi-domain] Cd Length: 168 Bit Score: 39.63 E-value: 9.67e-04
|
||||||||||
| GBP | cd01851 | Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
149-213 | 1.09e-03 | ||||||
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach. Pssm-ID: 206650 Cd Length: 224 Bit Score: 40.00 E-value: 1.09e-03
|
||||||||||
| RsgA_GTPase | pfam03193 | RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
157-213 | 2.03e-03 | ||||||
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern. Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 38.68 E-value: 2.03e-03
|
||||||||||
| PRK09602 | PRK09602 | translation-associated GTPase; Reviewed |
158-192 | 3.29e-03 | ||||||
translation-associated GTPase; Reviewed Pssm-ID: 236584 [Multi-domain] Cd Length: 396 Bit Score: 39.41 E-value: 3.29e-03
|
||||||||||
| GTP_translation_factor | cd00881 | GTP translation factor family primarily contains translation initiation, elongation and ... |
158-310 | 4.29e-03 | ||||||
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: 38.04 E-value: 4.29e-03
|
||||||||||
| SR_beta | cd04105 | Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ... |
156-291 | 4.30e-03 | ||||||
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer. Pssm-ID: 206691 [Multi-domain] Cd Length: 202 Bit Score: 38.07 E-value: 4.30e-03
|
||||||||||
| Ygr210 | cd01899 | Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ... |
158-192 | 5.16e-03 | ||||||
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: 38.36 E-value: 5.16e-03
|
||||||||||
| YqeH | cd01855 | Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
225-325 | 8.81e-03 | ||||||
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. Pssm-ID: 206748 [Multi-domain] Cd Length: 191 Bit Score: 36.86 E-value: 8.81e-03
|
||||||||||
| LepA | cd01890 | LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
234-318 | 9.80e-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: 9.80e-03
|
||||||||||
| Blast search parameters | ||||
|
