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Conserved domains on  [gi|1576636033|gb|RZO84872|]
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YihA family ribosome biogenesis GTP-binding protein [OM182 bacterium]

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
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, ...
12-200 1.62e-94

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: 273.87  E-value: 1.62e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  12 DATFLTSAPDLKRCPPIVSAEVAFAGRSNAGKSSVLNQLTGNRRTAKVSKTPGRTQLMNFFDVRSGGRLVDLPGYGYAKA 91
Cdd:COG0218     5 KAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYGYAKV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  92 GKEAQKNWQNAVNHYLSYRDALVGIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKLSFGAQKQTLSRVQQRYA 171
Cdd:COG0218    85 SKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIKKALG 164
                         170       180       190
                  ....*....|....*....|....*....|
gi 1576636033 172 KHPTA-SFQTFSAARGEGKAALMEQLLDWL 200
Cdd:COG0218   165 KDPAApEVILFSSLKKEGIDELRAAIEEWL 194
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
12-200 1.62e-94

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: 273.87  E-value: 1.62e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  12 DATFLTSAPDLKRCPPIVSAEVAFAGRSNAGKSSVLNQLTGNRRTAKVSKTPGRTQLMNFFDVRSGGRLVDLPGYGYAKA 91
Cdd:COG0218     5 KAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYGYAKV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  92 GKEAQKNWQNAVNHYLSYRDALVGIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKLSFGAQKQTLSRVQQRYA 171
Cdd:COG0218    85 SKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIKKALG 164
                         170       180       190
                  ....*....|....*....|....*....|
gi 1576636033 172 KHPTA-SFQTFSAARGEGKAALMEQLLDWL 200
Cdd:COG0218   165 KDPAApEVILFSSLKKEGIDELRAAIEEWL 194
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
13-189 9.47e-90

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: 261.25  E-value: 9.47e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  13 ATFLTSAPDLKRCPPIVSAEVAFAGRSNAGKSSVLNQLTGNRRTAKVSKTPGRTQLMNFFDVRSGGRLVDLPGYGYAKAG 92
Cdd:TIGR03598   1 AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  93 KEAQKNWQNAVNHYLSYRDALVGIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKLSFGAQKQTLSRVQQRYAK 172
Cdd:TIGR03598  81 KEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKK 160
                         170
                  ....*....|....*...
gi 1576636033 173 HPT-ASFQTFSAARGEGK 189
Cdd:TIGR03598 161 DADdPSVQLFSSLKKTGI 178
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
32-200 4.57e-77

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: 228.93  E-value: 4.57e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  32 EVAFAGRSNAGKSSVLNQLTGNRRTAKVSKTPGRTQLMNFFDVRSGGRLVDLPGYGYAKAGKEAQKNWQNAVNHYLSYRD 111
Cdd:cd01876     1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033 112 ALVGIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKLSFGAQKQTLSRVQQRYAKHPTA-SFQTFSAARGEGKA 190
Cdd:cd01876    81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNILpPVILFSSKKGTGID 160
                         170
                  ....*....|
gi 1576636033 191 ALMEQLLDWL 200
Cdd:cd01876   161 ELRALIAEWL 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
32-150 3.53e-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: 94.61  E-value: 3.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  32 EVAFAGRSNAGKSSVLNQLTGNRrtAKVSKTPGRTQLMNFFDVRSGGR---LVDLPGYgYAKAGKEAQKnwqnaVNHYLS 108
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLELKGKqiiLVDTPGL-IEGASEGEGL-----GRAFLA 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1576636033 109 YRDALVgIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNK 150
Cdd:pfam01926  73 IIEADL-ILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK04213 PRK04213
GTP-binding protein EngB;
26-146 6.41e-16

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 73.03  E-value: 6.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  26 PPIVSAEVAFAGRSNAGKSSVLNQLTGnrRTAKVSKTPGRTQLMNFFDVRSgGRLVDLPGYGY-AKAGKEAQKNWQNAVN 104
Cdd:PRK04213    5 RPDRKPEIVFVGRSNVGKSTLVRELTG--KKVRVGKRPGVTRKPNHYDWGD-FILTDLPGFGFmSGVPKEVQEKIKDEIV 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1576636033 105 HYL-SYRDALVGIVLVMDIRhpcqAFDEQMLDWAGASELPIRI 146
Cdd:PRK04213   82 RYIeDNADRILAAVLVVDGK----SFIEIIERWEGRGEIPIDV 120
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
12-200 1.62e-94

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: 273.87  E-value: 1.62e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  12 DATFLTSAPDLKRCPPIVSAEVAFAGRSNAGKSSVLNQLTGNRRTAKVSKTPGRTQLMNFFDVRSGGRLVDLPGYGYAKA 91
Cdd:COG0218     5 KAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYGYAKV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  92 GKEAQKNWQNAVNHYLSYRDALVGIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKLSFGAQKQTLSRVQQRYA 171
Cdd:COG0218    85 SKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIKKALG 164
                         170       180       190
                  ....*....|....*....|....*....|
gi 1576636033 172 KHPTA-SFQTFSAARGEGKAALMEQLLDWL 200
Cdd:COG0218   165 KDPAApEVILFSSLKKEGIDELRAAIEEWL 194
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
13-189 9.47e-90

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: 261.25  E-value: 9.47e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  13 ATFLTSAPDLKRCPPIVSAEVAFAGRSNAGKSSVLNQLTGNRRTAKVSKTPGRTQLMNFFDVRSGGRLVDLPGYGYAKAG 92
Cdd:TIGR03598   1 AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  93 KEAQKNWQNAVNHYLSYRDALVGIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKLSFGAQKQTLSRVQQRYAK 172
Cdd:TIGR03598  81 KEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKK 160
                         170
                  ....*....|....*...
gi 1576636033 173 HPT-ASFQTFSAARGEGK 189
Cdd:TIGR03598 161 DADdPSVQLFSSLKKTGI 178
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
32-200 4.57e-77

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: 228.93  E-value: 4.57e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  32 EVAFAGRSNAGKSSVLNQLTGNRRTAKVSKTPGRTQLMNFFDVRSGGRLVDLPGYGYAKAGKEAQKNWQNAVNHYLSYRD 111
Cdd:cd01876     1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033 112 ALVGIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKLSFGAQKQTLSRVQQRYAKHPTA-SFQTFSAARGEGKA 190
Cdd:cd01876    81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNILpPVILFSSKKGTGID 160
                         170
                  ....*....|
gi 1576636033 191 ALMEQLLDWL 200
Cdd:cd01876   161 ELRALIAEWL 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
32-150 3.53e-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: 94.61  E-value: 3.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  32 EVAFAGRSNAGKSSVLNQLTGNRrtAKVSKTPGRTQLMNFFDVRSGGR---LVDLPGYgYAKAGKEAQKnwqnaVNHYLS 108
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLELKGKqiiLVDTPGL-IEGASEGEGL-----GRAFLA 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1576636033 109 YRDALVgIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNK 150
Cdd:pfam01926  73 IIEADL-ILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
34-198 4.22e-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: 75.19  E-value: 4.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  34 AFAGRSNAGKSSVLNQLTGnRRTAKVSKTPGRTQLMNFFDVRSGG-----RLVDLPGYGYAKAGKEAQKNWqnavnHYLS 108
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLG-GEVGEVSDVPGTTRDPDVYVKELDKgkvklVLVDTPGLDEFGGLGREELAR-----LLLR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033 109 YRDalvGIVLVMDIRHPCQAFDEQ--MLDWAGASELPIRILLNKADKLSFGAQKQTLSRvqQRYAKHPTASFQTFSAARG 186
Cdd:cd00882    75 GAD---LILLVVDSTDRESEEDAKllILRRLRKEGIPIILVGNKIDLLEEREVEELLRL--EELAKILGVPVFEVSAKTG 149
                         170
                  ....*....|..
gi 1576636033 187 EGKAALMEQLLD 198
Cdd:cd00882   150 EGVDELFEKLIE 161
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
34-200 1.21e-16

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: 73.82  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  34 AFAGRSNAGKSSVLNQLTGnRRTAKVSKTPGRTQLMNFFDVRSGG----RLVDLPGYGYAKAGKEAQKnwQNAVNHyLSY 109
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLG-QNVGIVSPIPGTTRDPVRKEWELLPlgpvVLIDTPGLDEEGGLGRERV--EEARQV-ADR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033 110 RDalvGIVLVMDIRHPcQAFDEQMLDWAGASELPIRILLNKADKLSFGAQKQTLSrvQQRYAKHPTASFQTFSAARGEGK 189
Cdd:cd00880    77 AD---LVLLVVDSDLT-PVEEEAKLGLLRERGKPVLLVLNKIDLVPESEEEELLR--ERKLELLPDLPVIAVSALPGEGI 150
                         170
                  ....*....|.
gi 1576636033 190 AALMEQLLDWL 200
Cdd:cd00880   151 DELRKKIAELL 161
PRK04213 PRK04213
GTP-binding protein EngB;
26-146 6.41e-16

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 73.03  E-value: 6.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  26 PPIVSAEVAFAGRSNAGKSSVLNQLTGnrRTAKVSKTPGRTQLMNFFDVRSgGRLVDLPGYGY-AKAGKEAQKNWQNAVN 104
Cdd:PRK04213    5 RPDRKPEIVFVGRSNVGKSTLVRELTG--KKVRVGKRPGVTRKPNHYDWGD-FILTDLPGFGFmSGVPKEVQEKIKDEIV 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1576636033 105 HYL-SYRDALVGIVLVMDIRhpcqAFDEQMLDWAGASELPIRI 146
Cdd:PRK04213   82 RYIeDNADRILAAVLVVDGK----SFIEIIERWEGRGEIPIDV 120
era PRK00089
GTPase Era; Reviewed
33-200 3.55e-11

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 61.22  E-value: 3.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGnrrtAKVS----------------KTPGRTQLMnffdvrsggrLVDLPGYgyakagkeaQ 96
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVG----QKISivspkpqttrhrirgiVTEDDAQII----------FVDTPGI---------H 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  97 KNwQNAVNHYL------SYRDALVgIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKLSfgAQKQTLSRVQQRY 170
Cdd:PRK00089   65 KP-KRALNRAMnkaawsSLKDVDL-VLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVK--DKEELLPLLEELS 140
                         170       180       190
                  ....*....|....*....|....*....|
gi 1576636033 171 AKHPTASFQTFSAARGEGKAALMEQLLDWL 200
Cdd:PRK00089  141 ELMDFAEIVPISALKGDNVDELLDVIAKYL 170
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
33-200 6.39e-11

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: 58.63  E-value: 6.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGnrrtAKVS----------------KTPGRTQLMnffdvrsggrLVDLPgyGYAKAGKEAQ 96
Cdd:cd04163     6 VAIIGRPNVGKSTLLNALVG----QKISivspkpqttrnrirgiYTDDDAQII----------FVDTP--GIHKPKKKLG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  97 KNWQNAVNHylSYRDALVgIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKLSfgAQKQTLSRVQQRYAKHPTA 176
Cdd:cd04163    70 ERMVKAAWS--ALKDVDL-VLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVK--DKEDLLPLLEKLKELHPFA 144
                         170       180
                  ....*....|....*....|....
gi 1576636033 177 SFQTFSAARGEGKAALMEQLLDWL 200
Cdd:cd04163   145 EIFPISALKGENVDELLEYIVEYL 168
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
33-200 7.55e-11

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 60.00  E-value: 7.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGnrrtAKVS----------------KTPGRTQLMnffdvrsggrLVDLPGYgyakagkeaQ 96
Cdd:COG1159     6 VAIVGRPNVGKSTLLNALVG----QKVSivspkpqttrhrirgiVTREDAQIV----------FVDTPGI---------H 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  97 KNwQNAVNHYL------SYRDALVgIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKLSfgaQKQTLSRVQQRY 170
Cdd:COG1159    63 KP-KRKLGRRMnkaawsALEDVDV-ILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVK---KEELLPLLAEYS 137
                         170       180       190
                  ....*....|....*....|....*....|
gi 1576636033 171 AKHPTASFQTFSAARGEGKAALMEQLLDWL 200
Cdd:COG1159   138 ELLDFAEIVPISALKGDNVDELLDEIAKLL 167
YeeP COG3596
Predicted GTPase [General function prediction only];
32-169 1.01e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.00  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  32 EVAFAGRSNAGKSSVLNQLTGNRRtAKVSKTPGRTQLMNFFDVRSGG----RLVDLPGYGYAKAGKEAqknwqnavnhYL 107
Cdd:COG3596    41 VIALVGKTGAGKSSLINALFGAEV-AEVGVGRPCTREIQRYRLESDGlpglVLLDTPGLGEVNERDRE----------YR 109
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1576636033 108 SYRDALVG---IVLVMDIRHPCQAFDEQMLD--WAGASELPIRILLNKADKLSFGAQKQTLSRVQQR 169
Cdd:COG3596   110 ELRELLPEadlILWVVKADDRALATDEEFLQalRAQYPDPPVLVVLTQVDRLEPEREWDPPYNWPSP 176
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
33-169 3.21e-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: 51.39  E-value: 3.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGNR--------RTAKVSktpgrtqlMNFFDVRSGGRLVDLPGygyakagkeaqknwqnaVN 104
Cdd:cd09912     3 LAVVGEFSAGKSTLLNALLGEEvlptgvtpTTAVIT--------VLRYGLLKGVVLVDTPG-----------------LN 57
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1576636033 105 HYLSYRDALV--------GIVLVMDIRHPCQAFDEQML-DWAGASELPIRILLNKADKLSFGAQKQTLSRVQQR 169
Cdd:cd09912    58 STIEHHTEITesflpradAVIFVLSADQPLTESEREFLkEILKWSGKKIFFVLNKIDLLSEEELEEVLEYSREE 131
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
34-153 6.97e-08

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: 49.65  E-value: 6.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  34 AFAGRSNAGKSSVLNQLTGNRRTAKVSKTPGRTQLMNfFDVRSGGR---LVDLPGYGyakagkEAQKNWQNAVNHYLSYR 110
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQA-YVWQTGGDglvLLDLPGVG------ERGRRDREYEELYRRLL 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1576636033 111 DALVGIVLVMDIRHPCQAFDEQM-LDWAGASELPIRILLNKADK 153
Cdd:cd11383    74 PEADLVLWLLDADDRALAADHDFyLLPLAGHDAPLLFVLNQVDP 117
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
37-200 8.53e-08

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: 49.74  E-value: 8.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  37 GRSNAGKSSVLNQLTGnRRTAKVSKTPGRTQlmnffDVRSG-----GR---LVDLPGYGYAKAG--KEAQKNWQNAVNhy 106
Cdd:cd01894     4 GRPNVGKSTLFNRLTG-RRDAIVSDTPGVTR-----DRKYGeaewgGRefiLIDTGGIEPDDEGisKEIREQAEIAIE-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033 107 lsyrDALVgIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKLsfgaqkqtlsrvQQRYAKHPTASF-----QTF 181
Cdd:cd01894    76 ----EADV-ILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNI------------KEEEEAAEFYSLgfgepIPI 138
                         170
                  ....*....|....*....
gi 1576636033 182 SAARGEGKAALMEQLLDWL 200
Cdd:cd01894   139 SAEHGRGIGDLLDAILELL 157
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
30-85 2.78e-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: 48.00  E-value: 2.78e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1576636033  30 SAEVAFAGRSNAGKSSVLNQLTGNRRTaKVSKTPGRTQLMNFFDVRSGGRLVDLPG 85
Cdd:cd01857    82 EATIGLVGYPNVGKSSLINALVGSKKV-SVSSTPGKTKHFQTIFLEPGITLCDCPG 136
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
9-214 3.14e-07

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 50.18  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033   9 ERLDATFLtSAPDLKRCPPIVsAEVAFAGRSNAGKSSVLNQLTGnRRTAKVSKTPGRTQLMNFFDVRSGGR---LVDLPG 85
Cdd:PRK09518  256 DLLEGSGF-VAGDEKAGPKAV-GVVAIVGRPNVGKSTLVNRILG-RREAVVEDTPGVTRDRVSYDAEWAGTdfkLVDTGG 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  86 YGYAKAGKEAQKNWQNAVNHYLSyrDAlvgIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKAD------------K 153
Cdd:PRK09518  333 WEADVEGIDSAIASQAQIAVSLA--DA---VVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKIDdqaseydaaefwK 407
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033 154 LSFG-----------AQKQTLSRVQQRYAKHP-TASFQTFSAAR--------GEGKAALMEQLLDWLSIPLDDLAPQSNE 213
Cdd:PRK09518  408 LGLGepypisamhgrGVGDLLDEALDSLKVAEkTSGFLTPSGLRrvalvgrpNVGKSSLLNQLTHEERAVVNDLAGTTRD 487

                  .
gi 1576636033 214 P 214
Cdd:PRK09518  488 P 488
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
33-155 2.97e-06

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: 45.89  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGNRRtAKVSKTPGRTQ-----LMNFFDVRSggRLVDLPgyGYAKAGKEAQKnwqnaVNHYl 107
Cdd:cd01895     5 IAIIGRPNVGKSSLLNALLGEER-VIVSDIAGTTRdsidvPFEYDGQKY--TLIDTA--GIRKKGKVTEG-----IEKY- 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1576636033 108 SYRDALVGI------VLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKLS 155
Cdd:cd01895    74 SVLRTLKAIeradvvLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVE 127
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
33-85 8.17e-06

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ 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. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 45.08  E-value: 8.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTG--NRRTAKVSKTPGR-------TQLmnfFDVRSGGRLVDLPG 85
Cdd:cd01854    88 SVLVGQSGVGKSTLLNALLPelVLATGEISEKLGRgrhttthREL---FPLPGGGLIIDTPG 146
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
33-85 8.76e-06

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: 44.45  E-value: 8.76e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGN--RRTAKVSKTPGR----TQLMNFFDVRSGGRLVDLPG 85
Cdd:pfam03193 109 TVLAGQSGVGKSTLLNALLPEldLRTGEISEKLGRgrhtTTHVELFPLPGGGLLIDTPG 167
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
33-200 2.29e-05

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 44.24  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGnRRTAKVSKTPGRTQLMNFFDVRSGGR---LVDLPGYGYAKAG---KEAQKNWQNAVNhy 106
Cdd:COG1160     5 VAIVGRPNVGKSTLFNRLTG-RRDAIVDDTPGVTRDRIYGEAEWGGReftLIDTGGIEPDDDDgleAEIREQAELAIE-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033 107 lsyrDALVgIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKlsfgaqKQTLSRVQQRYA---KHPTAsfqtFSA 183
Cdd:COG1160    82 ----EADV-ILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDG------PKREADAAEFYSlglGEPIP----ISA 146
                         170
                  ....*....|....*..
gi 1576636033 184 ARGEGKAALMEQLLDWL 200
Cdd:COG1160   147 EHGRGVGDLLDAVLELL 163
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
33-153 4.15e-05

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 42.36  E-value: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGNRRtAKVSKTPGRTQLMNFFDVRSGGR-----LVDLPGygyakagkeaqknwQNAVN--H 105
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKG-SITEYYPGTTRNYVTTVIEEDGKtykfnLLDTAG--------------QEDYDaiR 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1576636033 106 YLSYRDALVGI------VLVMDIRHPCQAFDEQMLDWAgASELPIRILLNKADK 153
Cdd:TIGR00231  69 RLYYPQVERSLrvfdivILVLDVEEILEKQTKEIIHHA-DSGVPIILVGNKIDL 121
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
33-66 4.57e-05

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: 42.10  E-value: 4.57e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGNRRtAKVSKTPGRT 66
Cdd:cd04164     6 VVIAGKPNVGKSSLLNALAGRDR-AIVSDIAGTT 38
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
33-200 4.72e-05

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: 42.83  E-value: 4.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGNRRTAKvsktpgrTQLmnF---------FDVRSGGRLV---------DLPgygyakagke 94
Cdd:cd01878    44 VALVGYTNAGKSTLFNALTGADVLAE-------DQL--FatldpttrrIKLPGGREVLltdtvgfirDLP---------- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  95 aqknwqnavnHYL--SYR---------DALVgivLVMDIRHPCqaFDEQM------LDWAGASELPIRILLNKADKLSFG 157
Cdd:cd01878   105 ----------HQLveAFRstleevaeaDLLL---HVVDASDPD--REEQIetveevLKELGADDIPIILVLNKIDLLDDE 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1576636033 158 AQKQTLsrvqqrYAKHPTASFqtFSAARGEGKAALMEQLLDWL 200
Cdd:cd01878   170 ELEERL------RAGRPDAVF--ISAKTGEGLDLLKEAIEELL 204
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
33-214 6.71e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 43.11  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGNRRtAKVSKTPGRTQLMNFFDVRSGGR---LVDLPGYGYAKAG--KEAQKNWQNAVNhyl 107
Cdd:PRK00093    4 VAIVGRPNVGKSTLFNRLTGKRD-AIVADTPGVTRDRIYGEAEWLGRefiLIDTGGIEPDDDGfeKQIREQAELAIE--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033 108 syrDALVgIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKLSFGAQkqtlsrvqqryakhpTASFQTF------ 181
Cdd:PRK00093   80 ---EADV-ILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPDEEAD---------------AYEFYSLglgepy 140
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1576636033 182 --SAARGEGKAALMEQLLDWLsiPLDDLAPQSNEP 214
Cdd:PRK00093  141 piSAEHGRGIGDLLDAILEEL--PEEEEEDEEDEP 173
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
34-85 1.32e-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: 1.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1576636033  34 AFAGRSNAGKSSVLNQLTGNRrtAKVSKTPGRT--QLMNFFdvRSGGR---LVDLPG 85
Cdd:cd01879     1 ALVGNPNVGKTTLFNALTGAR--QKVGNWPGVTveKKEGEF--KLGGKeieIVDLPG 53
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
33-85 1.53e-04

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: 40.51  E-value: 1.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGNRrtAKVSKTPGRTqlmnfFDVRSG--------GRLVDLPG 85
Cdd:pfam02421   3 IALVGNPNVGKTTLFNALTGAN--QHVGNWPGVT-----VEKKEGkfkykgyeIEIVDLPG 56
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
37-201 1.57e-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: 40.88  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  37 GRSNAGKSSVLNQL-TGNRRTAKVSKTPG------RTQLMNF--FDVrSGgrlvdlpgygyakagkeaQKNWQNAVNHYL 107
Cdd:cd04157     6 GLDNSGKTTIINQLkPSNAQSQNIVPTVGfnvesfKKGNLSFtaFDM-SG------------------QGKYRGLWEHYY 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033 108 SYRDalvGIVLVMD----IRHpCQAFDE--QMLDWAG--ASELPIRILLNKAD-KLSFGAQKQTLSRVQQRYAKHPTASF 178
Cdd:cd04157    67 KNIQ---GIIFVIDssdrLRM-VVAKDEleLLLNHPDikHRRIPILFYANKMDlPDALTAVKITQLLCLENIKDKPWHIF 142
                         170       180
                  ....*....|....*....|...
gi 1576636033 179 QTfSAARGEGkaalMEQLLDWLS 201
Cdd:cd04157   143 AS-SALTGEG----LDEGVDWLQ 160
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
33-198 1.70e-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: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGNRRtAKVSKTPGRT-----QLMNFfdvrsGG---RLVDlpgygyaKAG---------KE- 94
Cdd:pfam12631  97 VVIVGKPNVGKSSLLNALLGEER-AIVTDIPGTTrdvieETINI-----GGiplRLID-------TAGiretddeveKIg 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  95 ---AQKNWQNAvnhylsyrDAlvgIVLVMDIRHPCQAFDEQMLDwAGASELPIRILLNKADklsfgaqkqtLSRVQQRYA 171
Cdd:pfam12631 164 ierAREAIEEA--------DL---VLLVLDASRPLDEEDLEILE-LLKDKKPIIVVLNKSD----------LLGEIDELE 221
                         170       180
                  ....*....|....*....|....*..
gi 1576636033 172 KHPTASFQTFSAARGEGKAALMEQLLD 198
Cdd:pfam12631 222 ELKGKPVLAISAKTGEGLDELEEAIKE 248
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
33-154 2.05e-04

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: 40.77  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  33 VAFAGRSNAGKSSVLNQL-TGNRRTAKVSKTPGRTQlmnFFDVRSGG---RLVDLPGYgyakaGKEAQKNWQNavnhyls 108
Cdd:cd04105     3 VLLLGPSDSGKTALFTKLtTGKVRSTVTSIEPNVAS---FYSNSSKGkklTLVDVPGH-----EKLRDKLLEY------- 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1576636033 109 YRDALVGIVLVMDIrhpcQAFD-------EQMLDWAGASEL---PIRILL--NKADKL 154
Cdd:cd04105    68 LKASLKAIVFVVDS----ATFQknirdvaEFLYDILTDLEKiknKIPILIacNKQDLF 121
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
33-85 2.12e-04

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: 40.38  E-value: 2.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGNRR--TAKVSKTPGRTQLMNFFDVRSGGRLVDLPG 85
Cdd:cd01859   102 VGVVGYPKVGKSSIINALKGRHSasTSPIPGSPGYTKGIQLVRIDSKIYLIDTPG 156
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
35-86 3.03e-04

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 40.77  E-value: 3.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1576636033  35 FAGRSNAGKSSVLNQLTG--NRRTAKVSKTPGR----TQLMNFFDVRSGGRLVDLPGY 86
Cdd:PRK12289  177 VAGPSGVGKSSLINRLIPdvELRVGKVSGKLGRgrhtTRHVELFELPNGGLLADTPGF 234
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
33-85 3.51e-04

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 40.87  E-value: 3.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGNRrtAKVSKTPGRTqlmnfFDVRSG--------GRLVDLPG 85
Cdd:COG0370     6 IALVGNPNVGKTTLFNALTGSR--QKVGNWPGVT-----VEKKEGkfklkgkeIELVDLPG 59
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
32-201 4.15e-04

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: 40.43  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  32 EVAFAGRSNAGKSSVLNQLTGNRRtAKVSKTPGRT-----QLMNFfdvrsGG---RLVDlpgygyaKAG---------KE 94
Cdd:COG0486   215 KVVIVGRPNVGKSSLLNALLGEER-AIVTDIAGTTrdvieERINI-----GGipvRLID-------TAGlretedeveKI 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  95 A-QKNWQNAvnhylsyRDA-LVgiVLVMDIRHPCQAFDEQMLDWagASELPIRILLNKADKlsfgaqkqtLSRVQQRYAK 172
Cdd:COG0486   282 GiERAREAI-------EEAdLV--LLLLDASEPLTEEDEEILEK--LKDKPVIVVLNKIDL---------PSEADGELKS 341
                         170       180
                  ....*....|....*....|....*....
gi 1576636033 173 HPTASFQTFSAARGEGKAALMEQLLDWLS 201
Cdd:COG0486   342 LPGEPVIAISAKTGEGIDELKEAILELVG 370
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
33-200 5.29e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 40.34  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGnRRTAKVSKTPGRTQLMNFFDVRSGGR---LVDLPGYGYAKAGKEAQKNWQNAVNhyLSY 109
Cdd:PRK03003   41 VAVVGRPNVGKSTLVNRILG-RREAVVEDVPGVTRDRVSYDAEWNGRrftVVDTGGWEPDAKGLQASVAEQAEVA--MRT 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033 110 RDAlvgIVLVMDIRHPCQAFDEQMLDWAGASELPIRILLNKADKLSFGAQKQTLsrvqqrYA-----KHPTasfqtfSAA 184
Cdd:PRK03003  118 ADA---VLFVVDATVGATATDEAVARVLRRSGKPVILAANKVDDERGEADAAAL------WSlglgePHPV------SAL 182
                         170
                  ....*....|....*.
gi 1576636033 185 RGEGKAALMEQLLDWL 200
Cdd:PRK03003  183 HGRGVGDLLDAVLAAL 198
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
40-86 5.60e-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: 39.10  E-value: 5.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1576636033  40 NAGKSSVLNQLTgNRRTAKVSKTPGRTQLMNFFDVRSGGRLVDLPGY 86
Cdd:cd04178   126 NVGKSSVINSLK-RSRACNVGATPGVTKSMQEVHLDKHVKLLDSPGV 171
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
35-86 1.10e-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: 38.40  E-value: 1.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1576636033  35 FAGRSNAGKSSVLNQL----------TGNRRTAKVSKTPGRTQLMNFFDVRSGGRLVDLPGY 86
Cdd:cd01855   130 VVGATNVGKSTLINALlksnggkvqaQALVQRLTVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
33-66 1.26e-03

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 39.24  E-value: 1.26e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGNRRtAKVSKTPGRT 66
Cdd:COG1160   178 IAIVGRPNVGKSSLINALLGEER-VIVSDIAGTT 210
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
40-201 1.52e-03

ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 37.94  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  40 NAGKSSVLNQLTGNrRTAKVSKTPGrTQL---------MNFFDVrsGGrlvdlpgygyakagkeaQKNWQNAVNHYLSYR 110
Cdd:cd00878     9 GAGKTTILYKLKLG-EVVTTIPTIG-FNVetveyknvkFTVWDV--GG-----------------QDKIRPLWKHYYENT 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033 111 DalvGIVLVMDIRHPCQaFDE------QMLDWAGASELPIRILLNKADKLSFGAQkQTLSRVQQRYAKHPTA-SFQTFSA 183
Cdd:cd00878    68 D---GLIFVVDSSDRER-IEEaknelhKLLNEEELKGAPLLILANKQDLPGALTE-SELIELLGLESIKGRRwHIQPCSA 142
                         170
                  ....*....|....*...
gi 1576636033 184 ARGEGkaalMEQLLDWLS 201
Cdd:cd00878   143 VTGDG----LDEGLDWLI 156
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
33-66 1.53e-03

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 38.94  E-value: 1.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGNRRtAKVSKTPGRT 66
Cdd:PRK05291  218 VVIAGRPNVGKSSLLNALLGEER-AIVTDIAGTT 250
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
33-66 1.65e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 38.88  E-value: 1.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGNRRtAKVSKTPGRT 66
Cdd:PRK00093  176 IAIIGRPNVGKSSLINALLGEER-VIVSDIAGTT 208
PRK00098 PRK00098
GTPase RsgA; Reviewed
35-85 2.64e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 37.88  E-value: 2.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1576636033  35 FAGRSNAGKSSVLNQLTG--NRRTAKVSKTPGR----TQLMNFFDVRSGGRLVDLPG 85
Cdd:PRK00098  169 LAGQSGVGKSTLLNALAPdlELKTGEISEALGRgkhtTTHVELYDLPGGGLLIDTPG 225
PRK12288 PRK12288
small ribosomal subunit biogenesis GTPase RsgA;
35-85 5.46e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237039 [Multi-domain]  Cd Length: 347  Bit Score: 37.14  E-value: 5.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1576636033  35 FAGRSNAGKSSVLNQLTG--NRRTAKVSKTPGRTQ-------LMNFfdvRSGGRLVDLPG 85
Cdd:PRK12288  210 FVGQSGVGKSSLINALLPeaEILVGDVSDNSGLGQhtttaarLYHF---PHGGDLIDSPG 266
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
33-85 5.52e-03

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: 36.21  E-value: 5.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTgNRRTAKVSKTPGRTQLMNFFDVRSGGRLVDLPG 85
Cdd:cd01849    94 VGVVGLPNVGKSSFINALL-NKFKLKVGSIPGTTKLQQDVKLDKEIYLYDTPG 145
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
33-66 6.33e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 36.87  E-value: 6.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1576636033  33 VAFAGRSNAGKSSVLNQLTGNRRtAKVSKTPGRT 66
Cdd:PRK03003  214 VALVGKPNVGKSSLLNKLAGEER-SVVDDVAGTT 246
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
37-85 8.72e-03

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 36.62  E-value: 8.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1576636033  37 GRSNAGKSSVLNQLTGNRRtaKVSKTPGRT---QLMNFFDVRSGGRLVDLPG 85
Cdd:PRK09554   10 GNPNSGKTTLFNQLTGARQ--RVGNWAGVTverKEGQFSTTDHQVTLVDLPG 59
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
40-85 9.87e-03

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: 35.58  E-value: 9.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1576636033  40 NAGKSSVLNQLTGnRRTAKVSKTPGRTQLMNFFDVRSGGRLVDLPG 85
Cdd:cd01856   125 NVGKSTLINRLRG-KKVAKVGNKPGVTRGQQWIRIGPNIELLDTPG 169
 
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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