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Conserved domains on  [gi|752296346|ref|WP_041152374|]
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MULTISPECIES: ribosome biogenesis GTP-binding protein YihA/YsxC [Lactobacillaceae]

Protein Classification

GTP-binding protein( domain architecture ID 10785093)

GTP-binding protein similar to YsxC/EngB, a GTPase associated with ribosome biogenesis; belongs to the large superfamily of translation factor-related (TRAFAC) GTPases

CATH:  3.40.50.300
Gene Ontology:  GO:0046872|GO:0005525
PubMed:  16333325|11916378|11489118
SCOP:  4004043

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 1-191 3.47e-102

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 292.75  E-value: 3.47e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346   1 MDVHNVNIDISAVEPKQYPSNGYPEIALVGRSNVGKSSLTNVLINRNGYARTSNKPGKTQTLNFYNLDEKLFFVDIPGYG 80
Cdd:COG0218    1 MKIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  81 YAKISKAQRAKWGEMIETYLTTRRQLKGVVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMDKTPKSKWNKEVSILN 160
Cdd:COG0218   81 YAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIK 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 752296346 161 KTVDLNDG-DEIQLFSALSKYGKEEVWNWIES 191
Cdd:COG0218  161 KALGKDPAaPEVILFSSLKKEGIDELRAAIEE 192
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 1-191 3.47e-102

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 292.75  E-value: 3.47e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346   1 MDVHNVNIDISAVEPKQYPSNGYPEIALVGRSNVGKSSLTNVLINRNGYARTSNKPGKTQTLNFYNLDEKLFFVDIPGYG 80
Cdd:COG0218    1 MKIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  81 YAKISKAQRAKWGEMIETYLTTRRQLKGVVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMDKTPKSKWNKEVSILN 160
Cdd:COG0218   81 YAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIK 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 752296346 161 KTVDLNDG-DEIQLFSALSKYGKEEVWNWIES 191
Cdd:COG0218  161 KALGKDPAaPEVILFSSLKKEGIDELRAAIEE 192
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 10-183 3.22e-94

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 272.04  E-value: 3.22e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346   10 ISAVEPKQYPSNGYPEIALVGRSNVGKSSLTNVLINRNGYARTSNKPGKTQTLNFYNLDEKLFFVDIPGYGYAKISKAQR 89
Cdd:TIGR03598   5 KSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVSKEEK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346   90 AKWGEMIETYLTTRRQLKGVVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMDKTPKSKWNKEVSILNKTVDLNDGD 169
Cdd:TIGR03598  85 EKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKKDADD 164

                         170
                  ....*....|....*
gi 752296346  170 -EIQLFSALSKYGKE 183
Cdd:TIGR03598 165 pSVQLFSSLKKTGID 179
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 25-193 6.25e-84

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: 245.50  E-value: 6.25e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  25 EIALVGRSNVGKSSLTNVLINRNGYARTSNKPGKTQTLNFYNLDEKLFFVDIPGYGYAKISKAQRAKWGEMIETYLTTRR 104
Cdd:cd01876    1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346 105 QLKGVVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMDKTPKSKWNKEVSILNKTVDL-NDGDEIQLFSALSKYGKE 183
Cdd:cd01876   81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLfNILPPVILFSSKKGTGID 160

                        170
                 ....*....|
gi 752296346 184 EVWNWIESKT 193
Cdd:cd01876  161 ELRALIAEWL 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 25-143 1.15e-25

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: 95.38  E-value: 1.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346   25 EIALVGRSNVGKSSLTNVLINRNgyARTSNKPGKTQTLNFYNL---DEKLFFVDIPGygyakISKAQRAKWGeMIETYLT 101
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLelkGKQIILVDTPG-----LIEGASEGEG-LGRAFLA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 752296346  102 TRRQlKGVVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATK 143
Cdd:pfam01926  73 IIEA-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK04213 PRK04213
GTP-binding protein EngB;
24-146 8.89e-19

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 79.96  E-value: 8.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  24 PEIALVGRSNVGKSSLTNVLINRNgyARTSNKPGKTQTLNFYNLDEKLfFVDIPGYGY-AKISKAQRAKWGEMIETYL-T 101
Cdd:PRK04213  10 PEIVFVGRSNVGKSTLVRELTGKK--VRVGKRPGVTRKPNHYDWGDFI-LTDLPGFGFmSGVPKEVQEKIKDEIVRYIeD 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 752296346 102 TRRQLKGVVLLIDGRRAP-------SQD----DLQMYEFLKYYDIPTLVLATKMDK 146
Cdd:PRK04213  87 NADRILAAVLVVDGKSFIeiierweGRGeipiDVEMFDFLRELGIPPIVAVNKMDK 142
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 1-191 3.47e-102

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 292.75  E-value: 3.47e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346   1 MDVHNVNIDISAVEPKQYPSNGYPEIALVGRSNVGKSSLTNVLINRNGYARTSNKPGKTQTLNFYNLDEKLFFVDIPGYG 80
Cdd:COG0218    1 MKIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  81 YAKISKAQRAKWGEMIETYLTTRRQLKGVVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMDKTPKSKWNKEVSILN 160
Cdd:COG0218   81 YAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIK 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 752296346 161 KTVDLNDG-DEIQLFSALSKYGKEEVWNWIES 191
Cdd:COG0218  161 KALGKDPAaPEVILFSSLKKEGIDELRAAIEE 192
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 10-183 3.22e-94

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 272.04  E-value: 3.22e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346   10 ISAVEPKQYPSNGYPEIALVGRSNVGKSSLTNVLINRNGYARTSNKPGKTQTLNFYNLDEKLFFVDIPGYGYAKISKAQR 89
Cdd:TIGR03598   5 KSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVSKEEK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346   90 AKWGEMIETYLTTRRQLKGVVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMDKTPKSKWNKEVSILNKTVDLNDGD 169
Cdd:TIGR03598  85 EKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKKDADD 164

                         170
                  ....*....|....*
gi 752296346  170 -EIQLFSALSKYGKE 183
Cdd:TIGR03598 165 pSVQLFSSLKKTGID 179
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 25-193 6.25e-84

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: 245.50  E-value: 6.25e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  25 EIALVGRSNVGKSSLTNVLINRNGYARTSNKPGKTQTLNFYNLDEKLFFVDIPGYGYAKISKAQRAKWGEMIETYLTTRR 104
Cdd:cd01876    1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346 105 QLKGVVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMDKTPKSKWNKEVSILNKTVDL-NDGDEIQLFSALSKYGKE 183
Cdd:cd01876   81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLfNILPPVILFSSKKGTGID 160

                        170
                 ....*....|
gi 752296346 184 EVWNWIESKT 193
Cdd:cd01876  161 ELRALIAEWL 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 25-143 1.15e-25

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: 95.38  E-value: 1.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346   25 EIALVGRSNVGKSSLTNVLINRNgyARTSNKPGKTQTLNFYNL---DEKLFFVDIPGygyakISKAQRAKWGeMIETYLT 101
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLelkGKQIILVDTPG-----LIEGASEGEG-LGRAFLA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 752296346  102 TRRQlKGVVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATK 143
Cdd:pfam01926  73 IIEA-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK04213 PRK04213
GTP-binding protein EngB;
24-146 8.89e-19

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 79.96  E-value: 8.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  24 PEIALVGRSNVGKSSLTNVLINRNgyARTSNKPGKTQTLNFYNLDEKLfFVDIPGYGY-AKISKAQRAKWGEMIETYL-T 101
Cdd:PRK04213  10 PEIVFVGRSNVGKSTLVRELTGKK--VRVGKRPGVTRKPNHYDWGDFI-LTDLPGFGFmSGVPKEVQEKIKDEIVRYIeD 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 752296346 102 TRRQLKGVVLLIDGRRAP-------SQD----DLQMYEFLKYYDIPTLVLATKMDK 146
Cdd:PRK04213  87 NADRILAAVLVVDGKSFIeiierweGRGeipiDVEMFDFLRELGIPPIVAVNKMDK 142
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 27-189 4.28e-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: 74.80  E-value: 4.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  27 ALVGRSNVGKSSLTNVLINRNgYARTSNKPGKTQTLNFYNL-----DEKLFFVDIPGygyakISKAQRAKWGEMIETYLt 101
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGE-VGEVSDVPGTTRDPDVYVKeldkgKVKLVLVDTPG-----LDEFGGLGREELARLLL- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346 102 trRQLKGVVLLIDGRRAPSQDDLQMY--EFLKYYDIPTLVLATKMDKtpKSKWNKEVSILNKTVDLNDGDEIQLFSALSK 179
Cdd:cd00882   74 --RGADLILLVVDSTDRESEEDAKLLilRRLRKEGIPIILVGNKIDL--LEEREVEELLRLEELAKILGVPVFEVSAKTG 149

                        170
                 ....*....|
gi 752296346 180 YGKEEVWNWI 189
Cdd:cd00882  150 EGVDELFEKL 159
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 26-192 2.94e-16

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: 72.49  E-value: 2.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  26 IALVGRSNVGKSSLTNVLINRNgYARTSNKPGKT--QTLNFYNLDE-KLFFVDIPGygyakISKAQRAKWGEMIETYLTT 102
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQK-ISIVSPKPQTTrnRIRGIYTDDDaQIIFVDTPG-----IHKPKKKLGERMVKAAWSA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346 103 rrqLKG---VVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMDK-TPKSKWNKEVSILNKtvdLNDGDEIQLFSALS 178
Cdd:cd04163   80 ---LKDvdlVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLvKDKEDLLPLLEKLKE---LHPFAEIFPISALK 153

                        170
                 ....*....|....
gi 752296346 179 KYGKEEVWNWIESK 192
Cdd:cd04163  154 GENVDELLEYIVEY 167
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 27-185 3.04e-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: 69.58  E-value: 3.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  27 ALVGRSNVGKSSLTNVLINRNgYARTSNKPGKTQTLNFYNL----DEKLFFVDIPgyGYAKISKAQRakwgEMIETYLTT 102
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQN-VGIVSPIPGTTRDPVRKEWellpLGPVVLIDTP--GLDEEGGLGR----ERVEEARQV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346 103 RRQLKGVVLLIDGRRAPSqDDLQMYEFLKYYDIPTLVLATKMDKTPKSKwnKEVSILNKTVDLNDGDEIQLFSALSKYGK 182
Cdd:cd00880   74 ADRADLVLLVVDSDLTPV-EEEAKLGLLRERGKPVLLVLNKIDLVPESE--EEELLRERKLELLPDLPVIAVSALPGEGI 150


                 ...
gi 752296346 183 EEV 185
Cdd:cd00880  151 DEL 153
era PRK00089
GTPase Era; Reviewed
 26-191 5.16e-14

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 68.54  E-value: 5.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  26 IALVGRSNVGKSSLTNVLInrnGY--ARTSNKPgktQT-----LNFYNLDE-KLFFVDIPGygyakISKAQRaKWGE-MI 96
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALV---GQkiSIVSPKP---QTtrhriRGIVTEDDaQIIFVDTPG-----IHKPKR-ALNRaMN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  97 ETYLTTrrqLKGV---VLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMDK-TPKSKWNKEVSILNKTVdlnDGDEIQ 172
Cdd:PRK00089  76 KAAWSS---LKDVdlvLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLvKDKEELLPLLEELSELM---DFAEIV 149

                        170
                 ....*....|....*....
gi 752296346 173 LFSALSKYGKEEVWNWIES 191
Cdd:PRK00089 150 PISALKGDNVDELLDVIAK 168
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
26-191 1.05e-13

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 67.71  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  26 IALVGRSNVGKSSLTNVLInrnGY--ARTSNKPgktQT-----LNFYNLDE-KLFFVDIPGygyakISKAQRaKWGE-MI 96
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALV---GQkvSIVSPKP---QTtrhriRGIVTREDaQIVFVDTPG-----IHKPKR-KLGRrMN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  97 ETYLTTrrqLKGV---VLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMDKTPKSKWNKEVSILNKTVDLndgDEIQL 173
Cdd:COG1159   74 KAAWSA---LEDVdviLFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSELLDF---AEIVP 147

                        170
                 ....*....|....*...
gi 752296346 174 FSALSKYGKEEVWNWIES 191
Cdd:COG1159  148 ISALKGDNVDELLDEIAK 165
YeeP COG3596
Predicted GTPase [General function prediction only];
10-155 4.77e-11

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 60.55  E-value: 4.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  10 ISAVEPKQYPSNGYPEIALVGRSNVGKSSLTNVLINRNGYARTSNKPGkTQTLNFYNL----DEKLFFVDIPGYGyakiS 85
Cdd:COG3596   26 LAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPC-TREIQRYRLesdgLPGLVLLDTPGLG----E 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752296346  86 KAQRAKWGEMIETYLTtrrQLKGVVLLIDGRRAPSQDDLQMYEFLK--YYDIPTLVLATKMDKT-PKSKWNKE 155
Cdd:COG3596  101 VNERDREYRELRELLP---EADLILWVVKADDRALATDEEFLQALRaqYPDPPVLVVLTQVDRLePEREWDPP 170
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 27-145 1.92e-10

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: 56.67  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  27 ALVGRSNVGKSSLTNVLINRNgYARTSNKPGKT---QTLNFYNLDEKLFFVDIPGYGYAK--ISKAQRAKwgemietylt 101
Cdd:cd01894    1 AIVGRPNVGKSTLFNRLTGRR-DAIVSDTPGVTrdrKYGEAEWGGREFILIDTGGIEPDDegISKEIREQ---------- 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 752296346 102 TRRQLKG---VVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMD 145
Cdd:cd01894   70 AEIAIEEadvILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKID 116
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 22-155 1.10e-09

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: 55.13  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  22 GYPEIALVGRSNVGKSSLTNVLINRNgyaR--TSNKPGKTQ----TLNFYNlDEKLFFVDIPGygyakISKaqRAKWGEM 95
Cdd:cd01895    1 DPIKIAIIGRPNVGKSSLLNALLGEE---RviVSDIAGTTRdsidVPFEYD-GQKYTLIDTAG-----IRK--KGKVTEG 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752296346  96 IETY--LTTRRQLKG---VVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMDKTPKSKWNKE 155
Cdd:cd01895   70 IEKYsvLRTLKAIERadvVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEKDEKTMK 134
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 26-78 3.01e-08

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: 50.99  E-value: 3.01e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 752296346  26 IALVGRSNVGKSSLTNVLINRNgYARTSNKPGKTQTLNFYNLDEKLFFVDIPG 78
Cdd:cd01856  118 AMVVGIPNVGKSTLINRLRGKK-VAKVGNKPGVTRGQQWIRIGPNIELLDTPG 169
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 25-184 2.03e-07

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: 50.06  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  25 EIALVGRSNVGKSSLTNVLINRNgyaR--TSNKPGKT-----QTLnfyNLDEKLF-FVD-------------IpgyG--- 80
Cdd:COG0486  215 KVVIVGRPNVGKSSLLNALLGEE---RaiVTDIAGTTrdvieERI---NIGGIPVrLIDtaglretedevekI---Gier 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  81 -YAKISKAQRakwgemietylttrrqlkgVVLLIDGRRAPSQDDLQMYEFLKyyDIPTLVLATKMDKTPKSKWNKEvsil 159
Cdd:COG0486  286 aREAIEEADL-------------------VLLLLDASEPLTEEDEEILEKLK--DKPVIVVLNKIDLPSEADGELK---- 340

                        170       180
                 ....*....|....*....|....*
gi 752296346 160 nktvDLNDGDEIQLfSALSKYGKEE 184
Cdd:COG0486  341 ----SLPGEPVIAI-SAKTGEGIDE 360
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 24-146 2.20e-07

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 50.05  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  24 PEIALVGRSNVGKSSLTNVLINRNgYARTSNKPGKTQTLNfY---NLDEKLF-FVDIPGYGYAK--ISKAQRAKwgemie 97
Cdd:PRK00093   2 PVVAIVGRPNVGKSTLFNRLTGKR-DAIVADTPGVTRDRI-YgeaEWLGREFiLIDTGGIEPDDdgFEKQIREQ------ 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 752296346  98 tyltTRRQLKG---VVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMDK 146
Cdd:PRK00093  74 ----AELAIEEadvILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDG 121
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
14-125 6.55e-07

Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 48.48  E-value: 6.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  14 EPKQYPSNGYPEIALVGRSNVGKSSLTNVLInrnGYAR--TSNKPGKT----QTLnfYNLDEKLF-FVDIPGygyakISK 86
Cdd:COG1160  166 EEEEEEEDDPIKIAIVGRPNVGKSSLINALL---GEERviVSDIAGTTrdsiDTP--FERDGKKYtLIDTAG-----IRR 235

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 752296346  87 aqRAKWGEMIETY--LTTRRQLKG---VVLLIDGRRAPSQDDLQ 125
Cdd:COG1160  236 --KGKVDEGIEKYsvLRTLRAIERadvVLLVIDATEGITEQDLK 277
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 26-78 6.83e-07

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: 46.84  E-value: 6.83e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 752296346  26 IALVGRSNVGKSSLTNVLINRNgYARTSNKPGKTQTLNFYNLDEKLFFVDIPG 78
Cdd:cd01857   85 IGLVGYPNVGKSSLINALVGSK-KVSVSSTPGKTKHFQTIFLEPGITLCDCPG 136
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 26-160 9.58e-07

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: 46.72  E-value: 9.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  26 IALVGRSNVGKSSLTNVLINRNGyARTSNKPGKT-----QTLNFYNLdeKLFFVDIpgygyA-------KISKA--QRAK 91
Cdd:cd04164    6 VVIAGKPNVGKSSLLNALAGRDR-AIVSDIAGTTrdvieEEIDLGGI--PVRLIDT-----AglretedEIEKIgiERAR 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752296346  92 wgEMIEtylttRRQLkgVVLLIDGRRAPSQDDLQMYEFLKyyDIPTLVLATKMDKTPKSKWNKEVSILN 160
Cdd:cd04164   78 --EAIE-----EADL--VLLVVDASEGLDEEDLEILELPA--KKPVIVVLNKSDLLSDAEGISELNGKP 135
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
29-78 1.07e-06

Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 47.41  E-value: 1.07e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 752296346  29 VGRSNVGKSSLTNVLINRNGyARTSNKPGKTQTLNFYNLDEKLFFVDIPG 78
Cdd:COG1161  119 VGIPNVGKSTLINRLAGKKV-AKTGNKPGVTKGQQWIKLDDGLELLDTPG 167
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
26-185 1.11e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 46.90  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  26 IALVGRSNVGKSSLTNVLINR----NGYArTSNKPGKTQT-LNFYNLDEKLFFVDIPG-YGYAKISkaqrakwgemiETY 99
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDifslEKYL-STNGVTIDKKeLKLDGLDVDLVIWDTPGqDEFRETR-----------QFY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346 100 LTTRRQLKGVVLLIDGRRAPSQDDL-QMYEFLK--YYDIPTLVLATKMDKTPKSKWNKEVSILNKTVDLNDGDEIQLfSA 176
Cdd:COG1100   74 ARQLTGASLYLFVVDGTREETLQSLyELLESLRrlGKKSPIILVLNKIDLYDEEEIEDEERLKEALSEDNIVEVVAT-SA 152


                 ....*....
gi 752296346 177 LSKYGKEEV 185
Cdd:COG1100  153 KTGEGVEEL 161
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 16-78 1.73e-06

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: 45.77  E-value: 1.73e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752296346  16 KQYPSNGYPEI-ALVGRSNVGKSSLTNVLINRNGyARTS---NKPGKTQTLNFYNLDEKLFFVDIPG 78
Cdd:cd01859   91 KELAIDGKPVIvGVVGYPKVGKSSIINALKGRHS-ASTSpipGSPGYTKGIQLVRIDSKIYLIDTPG 156
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
26-181 4.75e-06

tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 45.87  E-value: 4.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  26 IALVGRSNVGKSSLTNVLINRNgYARTSNKPGKT-----QTLnfyNLDEKLF-FVDIPGygyakISKA---------QRA 90
Cdd:PRK05291 218 VVIAGRPNVGKSSLLNALLGEE-RAIVTDIAGTTrdvieEHI---NLDGIPLrLIDTAG-----IRETddevekigiERS 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  91 KwgEMIEtylttrrQLKGVVLLIDGRRAPSQDDLQMYEFLKyyDIPTLVLATKMDKTPKSkwnkevsilnKTVDLNDGDE 170
Cdd:PRK05291 289 R--EAIE-------EADLVLLVLDASEPLTEEDDEILEELK--DKPVIVVLNKADLTGEI----------DLEEENGKPV 347

                        170
                 ....*....|.
gi 752296346 171 IQLfSALSKYG 181
Cdd:PRK05291 348 IRI-SAKTGEG 357
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 28-79 8.11e-06

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: 44.56  E-value: 8.11e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752296346  28 LVGRSNVGKSSLTNVLINRNGY----------ARTSNKPGKTQTLNFYNLDEKLFFVDIPGY 79
Cdd:cd01855  130 VVGATNVGKSTLINALLKSNGGkvqaqalvqrLTVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
24-145 8.68e-06

Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 45.40  E-value: 8.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  24 PEIALVGRSNVGKSSLTNVLINRNgYARTSNKPGKTQTLNFY--NLDEKLF-FVDIPGYGYAK---ISKAQRAKwgemie 97
Cdd:COG1160    3 PVVAIVGRPNVGKSTLFNRLTGRR-DAIVDDTPGVTRDRIYGeaEWGGREFtLIDTGGIEPDDddgLEAEIREQ------ 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 752296346  98 tyltTRRQLKG---VVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMD 145
Cdd:COG1160   76 ----AELAIEEadvILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVD 122
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 26-125 1.79e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 44.27  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  26 IALVGRSNVGKSSLTNVLINRNgyaR--TSNKPGKTQ----TLNFYNlDEKLFFVDIPGygyakISKaqRAKWGEMIEtY 99
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLGEE---RviVSDIAGTTRdsidTPFERD-GQKYTLIDTAG-----IRR--KGKVTEGVE-K 243

                         90       100       110
                 ....*....|....*....|....*....|..
gi 752296346 100 LTTRRQLKG------VVLLIDGRRAPSQDDLQ 125
Cdd:PRK00093 244 YSVIRTLKAieradvVLLVIDATEGITEQDLR 275
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 26-78 2.58e-05

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: 42.44  E-value: 2.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 752296346   26 IALVGRSNVGKSSLTNVLInrNGYARTSNKPGKT---QTLNFYNLDEKLFFVDIPG 78
Cdd:pfam02421   3 IALVGNPNVGKTTLFNALT--GANQHVGNWPGVTvekKEGKFKYKGYEIEIVDLPG 56
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 2-128 2.80e-05

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 44.01  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346   2 DVHNVNIDISAVEPKQY----PSnGYPEIALVGRSNVGKSSLTNVLINR-----NGYARTSNKPGKTqtlnFYNLDEKLF 72
Cdd:PRK09518 426 DLLDEALDSLKVAEKTSgfltPS-GLRRVALVGRPNVGKSSLLNQLTHEeravvNDLAGTTRDPVDE----IVEIDGEDW 500

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  73 -FVDIPGygyakISKAQRAKWGEMIETYLTTRRQLKG---VVLLIDGRRAPSQDDLQMYE 128
Cdd:PRK09518 501 lFIDTAG-----IKRRQHKLTGAEYYSSLRTQAAIERselALFLFDASQPISEQDLKVMS 555
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 23-146 3.58e-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: 42.36  E-value: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346   23 YPEIALVGRSNVGKSSLTNVLInRNGYARTSNKPGKTQTLNFYNLDE-----KLFFVDIPGygyakiSKAQRAKWGEMIE 97
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLL-GNKGSITEYYPGTTRNYVTTVIEEdgktyKFNLLDTAG------QEDYDAIRRLYYP 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 752296346   98 TYLTTRRQLKGVVLLIDGRRAPSQDDLQMYEFLKyYDIPTLVLATKMDK 146
Cdd:TIGR00231  74 QVERSLRVFDIVILVLDVEEILEKQTKEIIHHAD-SGVPIILVGNKIDL 121
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 3-78 7.19e-05

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: 41.22  E-value: 7.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346   3 VHNVNIDISAVEPKQYPSNGYPE----IALVGRSNVGKSSLTNVLINRNGyARTSNKPGKTQTLNFYNLDEKLFFVDIPG 78
Cdd:cd01849   67 TNGQGILKLKAEITKQKLKLKYKkgirVGVVGLPNVGKSSFINALLNKFK-LKVGSIPGTTKLQQDVKLDKEIYLYDTPG 145
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 27-78 7.88e-05

Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 41.29  E-value: 7.88e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 752296346  27 ALVGRSNVGKSSLTNVLInrNGYARTSNKPGKTQTLN---FYNLDEKLFFVDIPG 78
Cdd:cd01879    1 ALVGNPNVGKTTLFNALT--GARQKVGNWPGVTVEKKegeFKLGGKEIEIVDLPG 53
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 26-184 1.03e-04

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: 41.70  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346   26 IALVGRSNVGKSSLTNVLINRNgyaR--TSNKPGKT-----QTLNFYNLdeKLFFVDIPGygyakISKA---------QR 89
Cdd:pfam12631  97 VVIVGKPNVGKSSLLNALLGEE---RaiVTDIPGTTrdvieETINIGGI--PLRLIDTAG-----IRETddevekigiER 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346   90 AKwgEMIEtylttRRQLkgVVLLIDGRRAPSQDDLQMYEFLKyYDIPTLVLATKMDKTPKSKWNKEvsilnktvdlNDGD 169
Cdd:pfam12631 167 AR--EAIE-----EADL--VLLVLDASRPLDEEDLEILELLK-DKKPIIVVLNKSDLLGEIDELEE----------LKGK 226

                         170
                  ....*....|....*
gi 752296346  170 EIQLFSALSKYGKEE 184
Cdd:pfam12631 227 PVLAISAKTGEGLDE 241
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 26-146 1.71e-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: 40.61  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  26 IALVGRSNVGKSSLTNVLINRN----GYARTSNKPgktqTLNFYNLDEKLFFVDIPGYGyaKISKAQRAkwgemietylT 101
Cdd:cd09912    3 LAVVGEFSAGKSTLLNALLGEEvlptGVTPTTAVI----TVLRYGLLKGVVLVDTPGLN--STIEHHTE----------I 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 752296346 102 TRRQLK---GVVLLIDGRRAPSQDDLQ-MYEFLKYYDIPTLVLATKMDK 146
Cdd:cd09912   67 TESFLPradAVIFVLSADQPLTESEREfLKEILKWSGKKIFFVLNKIDL 115
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 26-184 2.05e-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: 40.36  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  26 IALVGRSNVGKSSLTNVLINRNG--YARTSNKPGKTQTL---------------NFYNLDEKLFFVDIPGYgyakiskaq 88
Cdd:cd00881    2 VGVIGHVDHGKTTLTGSLLYQTGaiDRRGTRKETFLDTLkeerergitiktgvvEFEWPKRRINFIDTPGH--------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  89 rAKWgemIETYLTTRRQLKGVVLLIDGRRAPsqdDLQMYEF---LKYYDIPTLVLATKMDKTPKSKWN---KEVS-ILNK 161
Cdd:cd00881   73 -EDF---SKETVRGLAQADGALLVVDANEGV---EPQTREHlniALAGGLPIIVAVNKIDRVGEEDFDevlREIKeLLKL 145

                        170       180
                 ....*....|....*....|....*.
gi 752296346 162 TVDLNDGDE---IQLFSALSKYGKEE 184
Cdd:cd00881  146 IGFTFLKGKdvpIIPISALTGEGIEE 171
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 26-79 2.92e-04

A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein that functions as a regulator of cell growth and proliferation in stem cells and in several types of cancer cells, but is not expressed in the differentiated cells of most mammalian adult tissues. NS shuttles between the nucleolus and nucleoplasm bidirectionally at a rate that is fast and independent of cell type. Lowering GTP levels decreases the nucleolar retention of NS, and expression of NS is abruptly down-regulated during differentiation prior to terminal cell division. Found only in eukaryotes, NS consists of an N-terminal basic domain, a coiled-coil domain, a GTP-binding domain, an intermediate domain, and a C-terminal acidic domain. Experimental evidence indicates that NS uses its GTP-binding property as a molecular switch to control the transition between the nucleolus and nucleoplasm, and this process involves interaction between the basic, GTP-binding, and intermediate domains of the protein.


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 39.87  E-value: 2.92e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 752296346  26 IALVGRSNVGKSSLTNVLINRNGYArTSNKPGKTQTLNFYNLDEKLFFVDIPGY 79
Cdd:cd04178  119 VGVVGYPNVGKSSVINSLKRSRACN-VGATPGVTKSMQEVHLDKHVKLLDSPGV 171
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 26-145 3.95e-04

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 40.55  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  26 IALVGRSNVGKSSLTNVLINRNGyARTSNKPGKTQT----------LNFYNLDEKLFFVDIPGYGYAKISKAQRAkwgem 95
Cdd:PRK09518 278 VAIVGRPNVGKSTLVNRILGRRE-AVVEDTPGVTRDrvsydaewagTDFKLVDTGGWEADVEGIDSAIASQAQIA----- 351

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 752296346  96 IETylttrrqLKGVVLLIDGRRAPSQDDLQMYEFLKYYDIPTLVLATKMD 145
Cdd:PRK09518 352 VSL-------ADAVVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKID 394
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 27-146 4.91e-04

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 38.86  E-value: 4.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  27 ALVGRSNVGKSSLTNVLINRNGYARTSNKPGKT--QTLNFYNLDEKLFFVDIPGYGyakiSKAQRAKWGEmiETYLTTRR 104
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRaaQAYVWQTGGDGLVLLDLPGVG----ERGRRDREYE--ELYRRLLP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 752296346 105 QLKGVVLLIDGRRAPSQDDLQMYE-FLKYYDIPTLVLATKMDK 146
Cdd:cd11383   75 EADLVLWLLDADDRALAADHDFYLlPLAGHDAPLLFVLNQVDP 117
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
 26-78 9.50e-04

A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; Autoantigen NGP-1 (Nucleolar G-protein gene 1) has been shown to localize in the nucleolus and nucleolar organizers in all cell types analyzed, which is indicative of a function in ribosomal assembly. NGP-1 and its homologs show 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 NKXD motif) are relocated to the N terminus.


Pssm-ID: 206751 [Multi-domain]  Cd Length: 157  Bit Score: 38.05  E-value: 9.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 752296346  26 IALVGRSNVGKSSLTNVLINRNgYARTSNKPGKTQTLNFYNLDEKLFFVDIPG 78
Cdd:cd01858  105 VGFIGYPNVGKSSVINTLRSKK-VCKVAPIPGETKVWQYITLMKRIYLIDCPG 156
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 27-146 1.09e-03

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: 38.14  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296346  27 ALVGRSNVGKSSLTNVLINRNgyARTSNKPGKTQTLN---FYNLD-EKLFFVDIPGYgyakiskAQRAKWGE-MIETYLT 101
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAK--VEIASYPFTTLEPNvgvFEFGDgVDIQIIDLPGL-------LDGASEGRgLGEQILA 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 752296346 102 TRRQLKGVVLLIDGRRAPSQDDLQMYEFLKY---------YDIPTLVLATKMDK 146
Cdd:cd01881   72 HLYRSDLILHVIDASEDCVGDPLEDQKTLNEevsgsflflKNKPEMIVANKIDM 125
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
26-78 1.53e-03

Fe2+ transporter FeoB [Inorganic ion transport and metabolism];


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 38.56  E-value: 1.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 752296346  26 IALVGRSNVGKSSLTNVLINRNgyARTSNKPGKTQTL---NFYNLDEKLFFVDIPG 78
Cdd:COG0370    6 IALVGNPNVGKTTLFNALTGSR--QKVGNWPGVTVEKkegKFKLKGKEIELVDLPG 59
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 21-51 1.89e-03

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: 37.82  E-value: 1.89e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 752296346  21 NGYPEIALVGRSNVGKSSLTNVLINRNGYAR 51
Cdd:cd01878   39 SGVPTVALVGYTNAGKSTLFNALTGADVLAE 69
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 14-43 1.97e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 38.41  E-value: 1.97e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 752296346  14 EPKQYPSNGYP-EIALVGRSNVGKSSLTNVL 43
Cdd:PRK03003 201 VPRVGSASGGPrRVALVGKPNVGKSSLLNKL 231
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 24-46 2.72e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 37.64  E-value: 2.72e-03
                         10        20
                 ....*....|....*....|...
gi 752296346  24 PEIALVGRSNVGKSSLTNVLINR 46
Cdd:PRK03003  39 PVVAVVGRPNVGKSTLVNRILGR 61
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 21-43 6.61e-03

50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 36.60  E-value: 6.61e-03
                         10        20
                 ....*....|....*....|...
gi 752296346  21 NGYPEIALVGRSNVGKSSLTNVL 43
Cdd:COG2262  197 SGIPTVALVGYTNAGKSTLFNRL 219
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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