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Conserved domains on  [gi|24307899|ref|NP_005693|]
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GTPase Era, mitochondrial isoform 1 [Homo sapiens]

Protein Classification

GTPase Era family protein( domain architecture ID 1000189)

GTPase Era family protein similar to bacterial GTPase Era and plant GTP-binding protein ERG that has a crucial role in plant growth and development, possibly by influencing mitochondrial division

CATH:  3.30.300.20|3.40.50.300
Gene Ontology:  GO:0000028|GO:0003924|GO:0043024|GO:0019843|GO:0005525
SCOP:  4004038|4001200

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
era super family cl35062
GTPase Era; Reviewed
 116-434 5.49e-54

GTPase Era; Reviewed


The actual alignment was detected with superfamily member PRK00089:

Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 181.78  E-value: 5.49e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899  116 VVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGIISPgkqkRHHLELSLLEDPWKSME 195
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIHKP----KRALNRAMNKAAWSSLK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899  196 SADLVVVLVDVSDKWTR------NQLspqllrcltKYSQIPSVLVMNKVDCLKQKSVLLELTAALTEGVvngkklkmrqa 269
Cdd:PRK00089  84 DVDLVLFVVDADEKIGPgdefilEKL---------KKVKTPVILVLNKIDLVKDKEELLPLLEELSELM----------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899  270 fhshpgthcpspavkdpntqsvgnpqrigwpHFKEIFMLSALSQEDVKTLKQYLLTQAQPGPWEYHSAVLTSQTPEEICA 349
Cdd:PRK00089 144 -------------------------------DFAEIVPISALKGDNVDELLDVIAKYLPEGPPYYPEDQITDRPERFLAA 192

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899  350 NIIREKLLEHLPQEVPYNVqqktAV----WEEgpGGELVIQQKLLVPKESYVKLLIGPKGHVISQIAQEAGHDLMDIFLC 425
Cdd:PRK00089 193 EIIREKLLRLLGDELPYSV----AVeiekFEE--RGLVRIEATIYVERDSQKGIIIGKGGAMLKKIGTEARKDIEKLLGK 266


                 ....*....
gi 24307899  426 DVDIRLSVK 434
Cdd:PRK00089 267 KVFLELWVK 275
 
Name Accession Description Interval E-value
era PRK00089
GTPase Era; Reviewed
 116-434 5.49e-54

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 181.78  E-value: 5.49e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899  116 VVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGIISPgkqkRHHLELSLLEDPWKSME 195
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIHKP----KRALNRAMNKAAWSSLK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899  196 SADLVVVLVDVSDKWTR------NQLspqllrcltKYSQIPSVLVMNKVDCLKQKSVLLELTAALTEGVvngkklkmrqa 269
Cdd:PRK00089  84 DVDLVLFVVDADEKIGPgdefilEKL---------KKVKTPVILVLNKIDLVKDKEELLPLLEELSELM----------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899  270 fhshpgthcpspavkdpntqsvgnpqrigwpHFKEIFMLSALSQEDVKTLKQYLLTQAQPGPWEYHSAVLTSQTPEEICA 349
Cdd:PRK00089 144 -------------------------------DFAEIVPISALKGDNVDELLDVIAKYLPEGPPYYPEDQITDRPERFLAA 192

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899  350 NIIREKLLEHLPQEVPYNVqqktAV----WEEgpGGELVIQQKLLVPKESYVKLLIGPKGHVISQIAQEAGHDLMDIFLC 425
Cdd:PRK00089 193 EIIREKLLRLLGDELPYSV----AVeiekFEE--RGLVRIEATIYVERDSQKGIIIGKGGAMLKKIGTEARKDIEKLLGK 266


                 ....*....
gi 24307899  426 DVDIRLSVK 434
Cdd:PRK00089 267 KVFLELWVK 275
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
116-434 6.23e-51

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 173.64  E-value: 6.23e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 116 VVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGIISPgkqkRHHLELSLLEDPWKSME 195
Cdd:COG1159   6 VAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIHKP----KRKLGRRMNKAAWSALE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 196 SADLVVVLVDVSDKWTR------NQLspqllrcltKYSQIPSVLVMNKVDCLKqKSVLLELTAALTEgvvngkklKMrqa 269
Cdd:COG1159  82 DVDVILFVVDATEKIGEgdefilELL---------KKLKTPVILVINKIDLVK-KEELLPLLAEYSE--------LL--- 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 270 fhshpgthcpspavkdpntqsvgnpqrigwpHFKEIFMLSALSQEDVKTLKQYLLTQAQPGPWEYHSAVLTSQTPEEICA 349
Cdd:COG1159 141 -------------------------------DFAEIVPISALKGDNVDELLDEIAKLLPEGPPYYPEDQITDRPERFLAA 189

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 350 NIIREKLLEHLPQEVPYNVqqktAV----WEEGPGGeLVIQQKLLVPKESYVKLLIGPKGHVISQIAQEAGHDLMDIFLC 425
Cdd:COG1159 190 EIIREKILRLLRDELPYSV----AVeieeFEEREGL-LRIRATIYVERDSQKGIIIGKGGSMLKKIGTEARKDIEKLLGK 264


                ....*....
gi 24307899 426 DVDIRLSVK 434
Cdd:COG1159 265 KVFLELWVK 273
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 112-327 2.92e-45

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: 154.54  E-value: 2.92e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 112 RVLRVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGIISPgkqkRHHLELSLLEDPW 191
Cdd:cd04163   2 KSGFVAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIHKP----KKKLGERMVKAAW 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 192 KSMESADLVVVLVDVSDKWTRNqlSPQLLRCLtKYSQIPSVLVMNKVDCLKQKSVLLELTAALTEGVVngkklkmrqafh 271
Cdd:cd04163  78 SALKDVDLVLFVVDASEWIGEG--DEFILELL-KKSKTPVILVLNKIDLVKDKEDLLPLLEKLKELHP------------ 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24307899 272 shpgthcpspavkdpntqsvgnpqrigwphFKEIFMLSALSQEDVKTLKQYLLTQA 327
Cdd:cd04163 143 ------------------------------FAEIFPISALKGENVDELLEYIVEYL 168
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 114-434 1.23e-35

GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other]


Pssm-ID: 129528 [Multi-domain]  Cd Length: 270  Bit Score: 132.51  E-value: 1.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899   114 LRVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGIispgKQKRHHLELSLLEDPWKS 193
Cdd:TIGR00436   1 GFVAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGF----HEKKHSLNRLMMKEARSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899   194 MeSADLVVVLVDVSDKWtrNQLSPQLLRCLTKySQIPSVLVMNKVDcLKQKSVLLELTAALtEGVVNgkklkmrqafhsh 273
Cdd:TIGR00436  77 I-GGVDLILFVVDSDQW--NGDGEFVLTKLQN-LKRPVVLTRNKLD-NKFKDKLLPLIDKY-AILED------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899   274 pgthcpspavkdpntqsvgnpqrigwphFKEIFMLSALSQEDVKTLKQYLLTQAQPGPWEYHSAVLTSQTPEEICANIIR 353
Cdd:TIGR00436 138 ----------------------------FKDIVPISALTGDNTSFLAAFIEVHLPEGPFRYPEDYVTDQPDRFKISEIIR 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899   354 EKLLEHLPQEVPYNVQQKTAVWEEGPGGELVIQQKLLVPKESYVKLLIGPKGHVISQIAQEAGHDLMDIFLCDVDIRLSV 433
Cdd:TIGR00436 190 EKIIRYTKEEIPHSVRVEIERKSFNEKGLLKIHALISVERESQKKIIIGKNGSMIKAIGIAARKDILELFDCDVFLELFV 269


                  .
gi 24307899   434 K 434
Cdd:TIGR00436 270 K 270
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 115-237 9.91e-18

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: 78.43  E-value: 9.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899   115 RVVLLGAPNAGKSTLSNQLLGRKVfPVSRKVHTTRCQALGVITEKETQVILLDTPGIISPGKQKRHhlelslLEDPWKSM 194
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKA-IVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEG------LGRAFLAI 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 24307899   195 ESADLVVVLVDVSDKWTRNQLspQLLRCLTKySQIPSVLVMNK 237
Cdd:pfam01926  74 IEADLILFVVDSEEGITPLDE--ELLELLRE-NKKPIILVLNK 113
 
Name Accession Description Interval E-value
era PRK00089
GTPase Era; Reviewed
 116-434 5.49e-54

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 181.78  E-value: 5.49e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899  116 VVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGIISPgkqkRHHLELSLLEDPWKSME 195
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIHKP----KRALNRAMNKAAWSSLK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899  196 SADLVVVLVDVSDKWTR------NQLspqllrcltKYSQIPSVLVMNKVDCLKQKSVLLELTAALTEGVvngkklkmrqa 269
Cdd:PRK00089  84 DVDLVLFVVDADEKIGPgdefilEKL---------KKVKTPVILVLNKIDLVKDKEELLPLLEELSELM----------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899  270 fhshpgthcpspavkdpntqsvgnpqrigwpHFKEIFMLSALSQEDVKTLKQYLLTQAQPGPWEYHSAVLTSQTPEEICA 349
Cdd:PRK00089 144 -------------------------------DFAEIVPISALKGDNVDELLDVIAKYLPEGPPYYPEDQITDRPERFLAA 192

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899  350 NIIREKLLEHLPQEVPYNVqqktAV----WEEgpGGELVIQQKLLVPKESYVKLLIGPKGHVISQIAQEAGHDLMDIFLC 425
Cdd:PRK00089 193 EIIREKLLRLLGDELPYSV----AVeiekFEE--RGLVRIEATIYVERDSQKGIIIGKGGAMLKKIGTEARKDIEKLLGK 266


                 ....*....
gi 24307899  426 DVDIRLSVK 434
Cdd:PRK00089 267 KVFLELWVK 275
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
116-434 6.23e-51

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 173.64  E-value: 6.23e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 116 VVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGIISPgkqkRHHLELSLLEDPWKSME 195
Cdd:COG1159   6 VAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIHKP----KRKLGRRMNKAAWSALE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 196 SADLVVVLVDVSDKWTR------NQLspqllrcltKYSQIPSVLVMNKVDCLKqKSVLLELTAALTEgvvngkklKMrqa 269
Cdd:COG1159  82 DVDVILFVVDATEKIGEgdefilELL---------KKLKTPVILVINKIDLVK-KEELLPLLAEYSE--------LL--- 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 270 fhshpgthcpspavkdpntqsvgnpqrigwpHFKEIFMLSALSQEDVKTLKQYLLTQAQPGPWEYHSAVLTSQTPEEICA 349
Cdd:COG1159 141 -------------------------------DFAEIVPISALKGDNVDELLDEIAKLLPEGPPYYPEDQITDRPERFLAA 189

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 350 NIIREKLLEHLPQEVPYNVqqktAV----WEEGPGGeLVIQQKLLVPKESYVKLLIGPKGHVISQIAQEAGHDLMDIFLC 425
Cdd:COG1159 190 EIIREKILRLLRDELPYSV----AVeieeFEEREGL-LRIRATIYVERDSQKGIIIGKGGSMLKKIGTEARKDIEKLLGK 264


                ....*....
gi 24307899 426 DVDIRLSVK 434
Cdd:COG1159 265 KVFLELWVK 273
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 112-327 2.92e-45

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: 154.54  E-value: 2.92e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 112 RVLRVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGIISPgkqkRHHLELSLLEDPW 191
Cdd:cd04163   2 KSGFVAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIHKP----KKKLGERMVKAAW 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 192 KSMESADLVVVLVDVSDKWTRNqlSPQLLRCLtKYSQIPSVLVMNKVDCLKQKSVLLELTAALTEGVVngkklkmrqafh 271
Cdd:cd04163  78 SALKDVDLVLFVVDASEWIGEG--DEFILELL-KKSKTPVILVLNKIDLVKDKEDLLPLLEKLKELHP------------ 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24307899 272 shpgthcpspavkdpntqsvgnpqrigwphFKEIFMLSALSQEDVKTLKQYLLTQA 327
Cdd:cd04163 143 ------------------------------FAEIFPISALKGENVDELLEYIVEYL 168
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 114-434 1.23e-35

GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other]


Pssm-ID: 129528 [Multi-domain]  Cd Length: 270  Bit Score: 132.51  E-value: 1.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899   114 LRVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGIispgKQKRHHLELSLLEDPWKS 193
Cdd:TIGR00436   1 GFVAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGF----HEKKHSLNRLMMKEARSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899   194 MeSADLVVVLVDVSDKWtrNQLSPQLLRCLTKySQIPSVLVMNKVDcLKQKSVLLELTAALtEGVVNgkklkmrqafhsh 273
Cdd:TIGR00436  77 I-GGVDLILFVVDSDQW--NGDGEFVLTKLQN-LKRPVVLTRNKLD-NKFKDKLLPLIDKY-AILED------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899   274 pgthcpspavkdpntqsvgnpqrigwphFKEIFMLSALSQEDVKTLKQYLLTQAQPGPWEYHSAVLTSQTPEEICANIIR 353
Cdd:TIGR00436 138 ----------------------------FKDIVPISALTGDNTSFLAAFIEVHLPEGPFRYPEDYVTDQPDRFKISEIIR 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899   354 EKLLEHLPQEVPYNVQQKTAVWEEGPGGELVIQQKLLVPKESYVKLLIGPKGHVISQIAQEAGHDLMDIFLCDVDIRLSV 433
Cdd:TIGR00436 190 EKIIRYTKEEIPHSVRVEIERKSFNEKGLLKIHALISVERESQKKIIIGKNGSMIKAIGIAARKDILELFDCDVFLELFV 269


                  .
gi 24307899   434 K 434
Cdd:TIGR00436 270 K 270
KH-II_Era cd22534
type II K-homology (KH) RNA-binding domain found in GTPase Era and similar proteins; GTPase ...
 349-435 2.07e-32

type II K-homology (KH) RNA-binding domain found in GTPase Era and similar proteins; GTPase Era, also called ERA or GTP-binding protein Era, is an essential GTPase that binds both GDP and GTP, with nucleotide exchange occurring in the order of seconds whereas hydrolysis occurs in the order of minutes. It plays a role in numerous processes, including cell cycle regulation, energy metabolism, as a chaperone for 16S rRNA processing, and 30S ribosomal subunit biogenesis. Its presence in the 30S subunit may prevent translation initiation. GTPase Era may also be critical for maintaining cell growth and cell division rates. Members of this family contain only one canonical type II K-homology (KH) domain that has the signature motif GXXG (where X represents any amino acid).


Pssm-ID: 411791 [Multi-domain]  Cd Length: 87  Bit Score: 117.93  E-value: 2.07e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 349 ANIIREKLLEHLPQEVPYNVQQKTAVWEEGPGGELVIQQKLLVPKESYVKLLIGPKGHVISQIAQEAGHDLMDIFLCDVD 428
Cdd:cd22534   1 AEIIREKLLELLRQELPYSVAVEIEEWEEREDGSLRIEAEIIVEKESQKKIIIGKGGATIKKIGIEARKDLEKLFGRKVY 80


                ....*..
gi 24307899 429 IRLSVKL 435
Cdd:cd22534  81 LKLWVKV 87
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 115-237 9.91e-18

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: 78.43  E-value: 9.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899   115 RVVLLGAPNAGKSTLSNQLLGRKVfPVSRKVHTTRCQALGVITEKETQVILLDTPGIISPGKQKRHhlelslLEDPWKSM 194
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKA-IVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEG------LGRAFLAI 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 24307899   195 ESADLVVVLVDVSDKWTRNQLspQLLRCLTKySQIPSVLVMNK 237
Cdd:pfam01926  74 IEADLILFVVDSEEGITPLDE--ELLELLRE-NKKPIILVLNK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 117-244 3.68e-14

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: 69.97  E-value: 3.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 117 VLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKET-QVILLDTPGIISPGKQKRhhlelSLLEDPWKSME 195
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWELLPLgPVVLIDTPGLDEEGGLGR-----ERVEEARQVAD 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 24307899 196 SAdLVVVLVDVSDKW-TRNQLSPQLLRcltkYSQIPSVLVMNKVDCLKQK 244
Cdd:cd00880  76 RA-DLVLLVVDSDLTpVEEEAKLGLLR----ERGKPVLLVLNKIDLVPES 120
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 117-246 2.78e-12

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: 64.40  E-value: 2.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 117 VLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVIT--EKETQVILLDTPGIISPGKQKRHHLELSLLE------ 188
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKEldKGKVKLVLVDTPGLDEFGGLGREELARLLLRgadlil 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24307899 189 ---DpwksmesadlvvvlvdvSDKWTRNQLSPQLLRCLTKYSQIPSVLVMNKVDCLKQKSV 246
Cdd:cd00882  81 lvvD-----------------STDRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREV 124
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 115-247 3.54e-12

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: 64.32  E-value: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899   115 RVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITE--KETQVILLDTPGIISPGKQKRHHLE--LSLLED- 189
Cdd:TIGR00231   3 KIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEdgKTYKFNLLDTAGQEDYDAIRRLYYPqvERSLRVf 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24307899   190 ----PWKSMESADLvvvlvdvsdKWTrnqlsPQLLRCLTKysQIPSVLVMNKVDcLKQKSVL 247
Cdd:TIGR00231  83 diviLVLDVEEILE---------KQT-----KEIIHHADS--GVPIILVGNKID-LKDADLK 127
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
105-174 7.43e-10

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 59.35  E-value: 7.43e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24307899 105 PDMPENSRVLRVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQalgviteketQVI-------LLDTPGIISP 174
Cdd:COG1161 105 PEKGIKRRPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKGQ----------QWIklddgleLLDTPGILWP 171
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 111-171 2.84e-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: 52.92  E-value: 2.84e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24307899 111 SRVLRVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRcqALGVITEKEtQVILLDTPGI 171
Cdd:cd01856 113 PRPLRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTR--GQQWIRIGP-NIELLDTPGI 170
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 114-171 2.14e-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: 50.19  E-value: 2.14e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24307899 114 LRVVLLGAPNAGKSTLSNQLLGRKVFPVSrKVH-TTRcqalGVITEkETQ-----VILLDTPGI 171
Cdd:cd04164   4 IKVVIAGKPNVGKSSLLNALAGRDRAIVS-DIAgTTR----DVIEE-EIDlggipVRLIDTAGL 61
YeeP COG3596
Predicted GTPase [General function prediction only];
97-184 6.43e-07

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 50.92  E-value: 6.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899  97 QDVLLVHHPDMPENSRVLRVVLLGAPNAGKSTLSNQLLGRKVFPVS-RKVHTTRCQALGVITEKETQVILLDTPGIISPG 175
Cdd:COG3596  23 RELLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGvGRPCTREIQRYRLESDGLPGLVLLDTPGLGEVN 102


                ....*....
gi 24307899 176 KQKRHHLEL 184
Cdd:COG3596 103 ERDREYREL 111
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
 114-174 7.91e-07

AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).


Pssm-ID: 206651 [Multi-domain]  Cd Length: 201  Bit Score: 49.46  E-value: 7.91e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24307899 114 LRVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVH--TTRCQALGVITEkETQVILLDTPGIISP 174
Cdd:cd01852   1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASgvTKTCQKESAVWD-GRRVNVIDTPGLFDT 62
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
 114-173 8.96e-07

AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 49.14  E-value: 8.96e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24307899   114 LRVVLLGAPNAGKSTLSNQLLGRKVFpVSR---KVHTTRCQaLGVITEKETQVILLDTPGIIS 173
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAF-ESKlraQGVTKTCQ-LVSRTWDGRIINVIDTPGLFD 61
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 115-179 1.00e-06

Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding protein (DRG) subfamily is an uncharacterized member of the Obg family, an evolutionary branch of GTPase superfamily proteins. GTPases act as molecular switches regulating diverse cellular processes. DRG2 and DRG1 comprise the DRG subfamily in eukaryotes. In view of their widespread expression in various tissues and high conservation among distantly related species in eukaryotes and archaea, DRG proteins may regulate fundamental cellular processes. It is proposed that the DRG subfamily proteins play their physiological roles through RNA binding.


Pssm-ID: 206683 [Multi-domain]  Cd Length: 233  Bit Score: 49.47  E-value: 1.00e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24307899 115 RVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQAlGVITEKETQVILLDTPGIISPGKQKR 179
Cdd:cd01896   2 RVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVP-GVMEYKGAKIQLLDLPGIIEGASDGK 65
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 114-171 1.33e-06

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: 48.31  E-value: 1.33e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24307899 114 LRVVLLGAPNAGKSTLSNQLLGRKVFPVSrKVHTTrcqalGVIT----EKETQVILLDTPGI 171
Cdd:cd09912   1 FLLAVVGEFSAGKSTLLNALLGEEVLPTG-VTPTT-----AVITvlryGLLKGVVLVDTPGL 56
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 118-256 1.45e-06

Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 48.19  E-value: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 118 LLGAPNAGKSTLSNQLLGRKVfpvsrKV----HTTRCQALGVI-TEKETQVILLDTPGII---SPGKQKRH----HLE-- 183
Cdd:cd01898   5 LVGLPNAGKSTLLSAISNAKP-----KIadypFTTLVPNLGVVrVDDGRSFVIADIPGLIegaSEGKGLGHrflrHIErt 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 184 --------LSLLEDPWKSMEsadlvvvlvdvsdkwtrnqlspQLLRCLTKYSQI----PSVLVMNKVDCLKQKSVLLELT 251
Cdd:cd01898  80 rvllhvidLSGEDDPVEDYE----------------------TIRNELEAYNPGlaekPRIVVLNKIDLLDAEERFEKLK 137


                ....*
gi 24307899 252 AALTE 256
Cdd:cd01898 138 ELLKE 142
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
98-171 4.78e-06

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: 4.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899  98 DVLLVHHPDMPEN---SRVLRVVLLGAPNAGKSTLSNQLLGRK---VFPVSrkvHTTRcQALGV-ITEKETQVILLDTPG 170
Cdd:COG1160 157 DAVLELLPEEEEEeeeDDPIKIAIVGRPNVGKSSLINALLGEErviVSDIA---GTTR-DSIDTpFERDGKKYTLIDTAG 232


                .
gi 24307899 171 I 171
Cdd:COG1160 233 I 233
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
111-173 6.80e-06

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 48.58  E-value: 6.80e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 111 SRVLRVVLLGAPNAGKSTLSNQLLGRKV----FP---VSRKVhttrcqalGVITEKETQVILLDTPGIIS 173
Cdd:COG0370   1 MKMITIALVGNPNVGKTTLFNALTGSRQkvgnWPgvtVEKKE--------GKFKLKGKEIELVDLPGTYS 62
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 114-138 1.51e-05

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: 46.98  E-value: 1.51e-05
                        10        20
                ....*....|....*....|....*
gi 24307899 114 LRVVLLGAPNAGKSTLSNQLLGRKV 138
Cdd:COG0486 214 IKVVIVGRPNVGKSSLLNALLGEER 238
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 114-171 2.07e-05

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 44.73  E-value: 2.07e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24307899 114 LRVVLLGAPNAGKSTLSNQLLGRK---VFPVSrkvHTTRCQALGVITEKETQVILLDTPGI 171
Cdd:cd01895   3 IKIAIIGRPNVGKSSLLNALLGEErviVSDIA---GTTRDSIDVPFEYDGQKYTLIDTAGI 60
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 109-136 3.05e-05

MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 45.55  E-value: 3.05e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 24307899   109 ENSRVLR----VVLLGAPNAGKSTLSNQLLGR 136
Cdd:pfam12631  86 DRGRILRegikVVIVGKPNVGKSSLLNALLGE 117
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
114-136 4.24e-05

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 45.49  E-value: 4.24e-05
                         10        20
                 ....*....|....*....|...
gi 24307899  114 LRVVLLGAPNAGKSTLSNQLLGR 136
Cdd:PRK05291 216 LKVVIAGRPNVGKSSLLNALLGE 238
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 105-171 4.66e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 45.43  E-value: 4.66e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24307899  105 PDMPENSRVLRVVLLGAPNAGKSTLSNQLLGRK---VFPVSrkvHTTRcQALGVITEKETQVILL-DTPGI 171
Cdd:PRK00093 165 EEEDEEDEPIKIAIIGRPNVGKSSLINALLGEErviVSDIA---GTTR-DSIDTPFERDGQKYTLiDTAGI 231
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 118-173 5.95e-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: 43.21  E-value: 5.95e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24307899 118 LLGAPNAGKSTLSNQLLGRKV----FP---VSRKVhttrcqalGVITEKETQVILLDTPGIIS 173
Cdd:cd01879   2 LVGNPNVGKTTLFNALTGARQkvgnWPgvtVEKKE--------GEFKLGGKEIEIVDLPGTYS 56
PRK01889 PRK01889
GTPase RsgA; Reviewed
 116-171 6.31e-05

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 44.92  E-value: 6.31e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24307899  116 VVLLGAPNAGKSTLSNQLLGRKVFPV-------SRKVHTTRCQALGVITEKetqVILLDTPGI 171
Cdd:PRK01889 198 VALLGSSGVGKSTLVNALLGEEVQKTgavreddSKGRHTTTHRELHPLPSG---GLLIDTPGM 257
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 118-174 1.23e-04

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: 41.83  E-value: 1.23e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24307899 118 LLGAPNAGKSTLSNQLLGRKVFPVSRKV-HTTRCQALGVitekETQVILLDTPGIISP 174
Cdd:cd01857  87 LVGYPNVGKSSLINALVGSKKVSVSSTPgKTKHFQTIFL----EPGITLCDCPGLVFP 140
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 117-250 1.90e-04

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: 41.65  E-value: 1.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 117 VLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGII--SPG--KQKRHHLELSLLE---- 188
Cdd:cd01894   1 AIVGRPNVGKSTLFNRLTGRRDAIVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEpdDEGisKEIREQAEIAIEEadvi 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24307899 189 ----DpwksmesadlvvvlvdvsdkwTRNQLSP------QLLRCLTKysqiPSVLVMNKVDCLKQKSVLLEL 250
Cdd:cd01894  81 lfvvD---------------------GREGLTPadeeiaKYLRKSKK----PVILVVNKIDNIKEEEEAAEF 127
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 109-171 2.06e-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: 41.53  E-value: 2.06e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24307899 109 ENSRVLRVVLLGAPNAGKSTLSNQLLGRKVFPVSRKV----HTTRCQALGvITEKetqVILLDTPGI 171
Cdd:cd01859  95 IDGKPVIVGVVGYPKVGKSSIINALKGRHSASTSPIPgspgYTKGIQLVR-IDSK---IYLIDTPGV 157
Dynamin_N pfam00350
Dynamin family;
116-150 2.42e-04

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 41.45  E-value: 2.42e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 24307899   116 VVLLGAPNAGKSTLSNQLLGRKVFPVSrKVHTTRC 150
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRG-PGPTTRR 34
mnmE_trmE_thdF TIGR00450
tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF ...
 114-239 4.02e-04

tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF (thiophene and furan oxidation protein), is a GTPase involved in tRNA modification to create 5-methylaminomethyl-2-thiouridine in the wobble position of some tRNAs. This protein and GidA form an alpha2/beta2 heterotetramer. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273083 [Multi-domain]  Cd Length: 442  Bit Score: 42.47  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899   114 LRVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGIispgKQKRHHLELSLLEDPWKS 193
Cdd:TIGR00450 204 FKLAIVGSPNVGKSSLLNALLKQDRAIVSDIKGTTRDVVEGDFELNGILIKLLDTAGI----REHADFVERLGIEKSFKA 279

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 24307899   194 MESADLVVVLVDVSDKWTRNqlsPQLLRCLTKySQIPSVLVMNKVD 239
Cdd:TIGR00450 280 IKQADLVIYVLDASQPLTKD---DFLIIDLNK-SKKPFILVLNKID 321
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
114-173 7.78e-04

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 42.01  E-value: 7.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24307899  114 LRVVLLGAPNAGKSTLSNQLLG--RKV-----FPVSRKVhttrcqalGVITEKETQVILLDTPGIIS 173
Cdd:PRK09554   4 LTIGLIGNPNSGKTTLFNQLTGarQRVgnwagVTVERKE--------GQFSTTDHQVTLVDLPGTYS 62
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 95-182 1.15e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 41.32  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899   95 DEQDVLLVHHPDMPENSRVL------RVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDT 168
Cdd:PRK09518 426 DLLDEALDSLKVAEKTSGFLtpsglrRVALVGRPNVGKSSLLNQLTHEERAVVNDLAGTTRDPVDEIVEIDGEDWLFIDT 505

                         90
                 ....*....|....
gi 24307899  169 PGIispgKQKRHHL 182
Cdd:PRK09518 506 AGI----KRRQHKL 515
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 109-259 1.30e-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: 39.75  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 109 ENSRVLRVVLLGAPNAGKSTLSNQLLGRKVF----------PVSRKVHttrcqalgviTEKETQVILLDTPGIIS--Pgk 176
Cdd:cd01878  37 KRSGVPTVALVGYTNAGKSTLFNALTGADVLaedqlfatldPTTRRIK----------LPGGREVLLTDTVGFIRdlP-- 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307899 177 qkrHHL-E--LSLLEDpwkSMES--------AdlvvvlvdvSDKWTRNQLSP--QLLRCLtKYSQIPSVLVMNKVDCLKQ 243
Cdd:cd01878 105 ---HQLvEafRSTLEE---VAEAdlllhvvdA---------SDPDREEQIETveEVLKEL-GADDIPIILVLNKIDLLDD 168

                       170
                ....*....|....*.
gi 24307899 244 KSVLLELTAALTEGVV 259
Cdd:cd01878 169 EELEERLRAGRPDAVF 184
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 115-171 1.77e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 40.42  E-value: 1.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24307899  115 RVVLLGAPNAGKSTLSNQLLGRKV-----FP-VSRKVHTTRCQALGViteketQVILLDTPGI 171
Cdd:PRK00093   3 VVAIVGRPNVGKSTLFNRLTGKRDaivadTPgVTRDRIYGEAEWLGR------EFILIDTGGI 59
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 116-171 1.91e-03

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: 39.30  E-value: 1.91e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24307899 116 VVLLGAPNAGKSTLSNQLLGRKVF---PVSRKV----HTTRCQALgVITEKETQVIllDTPGI 171
Cdd:cd01854  88 SVLVGQSGVGKSTLLNALLPELVLatgEISEKLgrgrHTTTHREL-FPLPGGGLII--DTPGF 147
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 115-171 2.19e-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: 39.17  E-value: 2.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24307899 115 RVVLLGAPNAGKSTLSNQLL--GRKVFPVSRKVH---------TTrcqaLGVITEK-ETQVILLDTPGI 171
Cdd:cd01855 127 DVYVVGATNVGKSTLINALLksNGGKVQAQALVQrltvspipgTT----LGLIKIPlGEGKKLYDTPGI 191
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 111-133 2.99e-03

Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 442405 [Multi-domain]  Cd Length: 178  Bit Score: 38.65  E-value: 2.99e-03
                        10        20
                ....*....|....*....|...
gi 24307899 111 SRVLRVVLLGAPNAGKSTLSNQL 133
Cdd:COG3172   6 SFVKKIVLLGAESTGKTTLARAL 28
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 116-175 5.67e-03

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 37.52  E-value: 5.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24307899   116 VVLLGAPNAGKSTLSNQLLGR---KVFPVS----RKVHTTRCQALgVITEKETQVIllDTPGIISPG 175
Cdd:pfam03193 109 TVLAGQSGVGKSTLLNALLPEldlRTGEISeklgRGRHTTTHVEL-FPLPGGGLLI--DTPGFRELG 172
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 117-186 6.34e-03

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: 36.93  E-value: 6.34e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24307899 117 VLLGAPNAGKSTLSNQLLGRKVFPVS-RKVHTTRCQALGVITEKETQViLLDTPGIISPGKQKRHHLELSL 186
Cdd:cd11383   1 GLMGKTGAGKSSLCNALFGTEVAAVGdRRPTTRAAQAYVWQTGGDGLV-LLDLPGVGERGRRDREYEELYR 70
AAA_28 pfam13521
AAA domain;
115-140 7.19e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 37.24  E-value: 7.19e-03
                          10        20
                  ....*....|....*....|....*....
gi 24307899   115 RVVLLGAPNAGKSTLSNQL---LGRKVFP 140
Cdd:pfam13521   1 RIVITGGPSTGKTTLAEALaarFGYPVVP 29
 
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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