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Conserved domains on  [gi|934118065|gb|KPL90683|]
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hypothetical protein SE18_06045 [Herpetosiphon geysericola]

Protein Classification

P-loop_NTPase and DLP_2 domain-containing protein( domain architecture ID 13591051)

P-loop_NTPase and DLP_2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 50-246 1.44e-72

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: 229.74  E-value: 1.44e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  50 FLLVVAGEFNAGKSSFINALLGDRVLPEGVTPTTDRINILRFGeqpdsqlledflllrthpapLLGDLNIVDTPGTNAII 129
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAVITVLRYG--------------------LLKGVVLVDTPGLNSTI 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 130 RRHEELTKRFVPRSDLVLFITSADRPFTESERTFLEHIREW-GKKIILVVNKIDILDEKGRNEVLEFVRSN--ATTLLGS 206
Cdd:cd09912   61 EHHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKWsGKKIFFVLNKIDLLSEEELEEVLEYSREElgVLELGGG 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 934118065 207 TPMIFAVSARSALRARENDDPKLWAESGFNAMEEYLLRTL 246
Cdd:cd09912  141 EPRIFPVSAKEALEARLQGDEELLEQSGFEELEEHLEEFL 180
RsgA_GTPase super family cl38114
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 11-75 4.66e-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.


The actual alignment was detected with superfamily member pfam03193:

Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 38.29  E-value: 4.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 934118065   11 ATEQSLFDRLHNALEQFGADVTAADAaRLREATEQLAELF---LLVVAGEFNAGKSSFINALLGDRVL 75
Cdd:pfam03193  66 LDEEEELEELLKIYRAIGYPVLFVSA-KTGEGIEALKELLkgkTTVLAGQSGVGKSTLLNALLPELDL 132
 
Name Accession Description Interval E-value
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 50-246 1.44e-72

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: 229.74  E-value: 1.44e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  50 FLLVVAGEFNAGKSSFINALLGDRVLPEGVTPTTDRINILRFGeqpdsqlledflllrthpapLLGDLNIVDTPGTNAII 129
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAVITVLRYG--------------------LLKGVVLVDTPGLNSTI 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 130 RRHEELTKRFVPRSDLVLFITSADRPFTESERTFLEHIREW-GKKIILVVNKIDILDEKGRNEVLEFVRSN--ATTLLGS 206
Cdd:cd09912   61 EHHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKWsGKKIFFVLNKIDLLSEEELEEVLEYSREElgVLELGGG 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 934118065 207 TPMIFAVSARSALRARENDDPKLWAESGFNAMEEYLLRTL 246
Cdd:cd09912  141 EPRIFPVSAKEALEARLQGDEELLEQSGFEELEEHLEEFL 180
Dynamin_N pfam00350
Dynamin family;
52-181 3.09e-31

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 119.26  E-value: 3.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065   52 LVVAGEFNAGKSSFINALLGDRVLPEGVTPTTDRINILRFGEQPDS-------------QLLEDFLLLRTH--------- 109
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGAsegavkveykdgeKKFEDFSELREEieketekia 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  110 ---------------PAPLLGDLNIVDTPGTNAIIRRHEELTKRFVPRSDLVLFITSADRPFTESERTFL-EHIREWGKK 173
Cdd:pfam00350  81 gtgkgissepivleiLSPLVPGLTLVDTPGLDSVAVGDQELTKEYIKPADIILAVTPANVDLSTSEALFLaREVDPNGKR 160


                  ....*...
gi 934118065  174 IILVVNKI 181
Cdd:pfam00350 161 TIGVLTKA 168
YeeP COG3596
Predicted GTPase [General function prediction only];
9-254 5.71e-20

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 90.98  E-value: 5.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065   9 LRATEQSLFDRLHnALEQFGADVTAADAARLREATEQLAElFLLVVAGEFNAGKSSFINALLGDRVLPEGVT-PTTDRIN 87
Cdd:COG3596    1 MSTEVSSLTERLE-ALKRLPQVLRELLAEALERLLVELPP-PVIALVGKTGAGKSSLINALFGAEVAEVGVGrPCTREIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  88 ILRFGEQPdsqlledflllrthpaplLGDLNIVDTPGTNAIIRRHEE--LTKRFVPRSDLVLFITSADRPFTESERTFLE 165
Cdd:COG3596   79 RYRLESDG------------------LPGLVLLDTPGLGEVNERDREyrELRELLPEADLILWVVKADDRALATDEEFLQ 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 166 HIREW--GKKIILVVNKIDILDEKGRNEVL-------------EFVRSNATTLLGSTPMIFAVSARSALRArenddpklw 230
Cdd:COG3596  141 ALRAQypDPPVLVVLTQVDRLEPEREWDPPynwpsppkeqnirRALEAIAEQLGVPIDRVIPVSAAEDRTG--------- 211

                        250       260
                 ....*....|....*....|....
gi 934118065 231 aeSGFNAMEEYLLRTLDEGERVRL 254
Cdd:COG3596  212 --YGLEELVDALAEALPEAKRSRL 233
era PRK00089
GTPase Era; Reviewed
 59-217 2.27e-15

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 76.62  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  59 NAGKSSFINALLGDRVLPegVTP---TT-DRIN-ILrfgEQPDSQLLedflllrthpapllgdlnIVDTPGtnaIIRRHE 133
Cdd:PRK00089  15 NVGKSTLLNALVGQKISI--VSPkpqTTrHRIRgIV---TEDDAQII------------------FVDTPG---IHKPKR 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 134 ELTKRFVpRS--------DLVLFITSADRPFTESERTFLEHIREWGKKIILVVNKIDILDEKgrNEVLEFVRSnATTLLG 205
Cdd:PRK00089  69 ALNRAMN-KAawsslkdvDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKDK--EELLPLLEE-LSELMD 144

                        170
                 ....*....|..
gi 934118065 206 STPmIFAVSARS 217
Cdd:PRK00089 145 FAE-IVPISALK 155
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 52-198 1.35e-08

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 54.30  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065   52 LVVAGEFNAGKSSFINALLGDRVLPEGVTPTTDRiNILRFGEQPDSQLLEdflllrthpapllgdLNIVDTPGT---NAI 128
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTR-NYVTTVIEEDGKTYK---------------FNLLDTAGQedyDAI 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  129 IRRHEELTKRFVPRSDLVLFITSADRPFTESERTfLEHIREWGKKIILVVNKIDILDEKgrneVLEFVRS 198
Cdd:TIGR00231  68 RRLYYPQVERSLRVFDIVILVLDVEEILEKQTKE-IIHHADSGVPIILVGNKIDLKDAD----LKTHVAS 132
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 11-75 4.66e-03

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


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 38.29  E-value: 4.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 934118065   11 ATEQSLFDRLHNALEQFGADVTAADAaRLREATEQLAELF---LLVVAGEFNAGKSSFINALLGDRVL 75
Cdd:pfam03193  66 LDEEEELEELLKIYRAIGYPVLFVSA-KTGEGIEALKELLkgkTTVLAGQSGVGKSTLLNALLPELDL 132
 
Name Accession Description Interval E-value
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 50-246 1.44e-72

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: 229.74  E-value: 1.44e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  50 FLLVVAGEFNAGKSSFINALLGDRVLPEGVTPTTDRINILRFGeqpdsqlledflllrthpapLLGDLNIVDTPGTNAII 129
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAVITVLRYG--------------------LLKGVVLVDTPGLNSTI 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 130 RRHEELTKRFVPRSDLVLFITSADRPFTESERTFLEHIREW-GKKIILVVNKIDILDEKGRNEVLEFVRSN--ATTLLGS 206
Cdd:cd09912   61 EHHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKWsGKKIFFVLNKIDLLSEEELEEVLEYSREElgVLELGGG 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 934118065 207 TPMIFAVSARSALRARENDDPKLWAESGFNAMEEYLLRTL 246
Cdd:cd09912  141 EPRIFPVSAKEALEARLQGDEELLEQSGFEELEEHLEEFL 180
Dynamin_N pfam00350
Dynamin family;
52-181 3.09e-31

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 119.26  E-value: 3.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065   52 LVVAGEFNAGKSSFINALLGDRVLPEGVTPTTDRINILRFGEQPDS-------------QLLEDFLLLRTH--------- 109
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGAsegavkveykdgeKKFEDFSELREEieketekia 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  110 ---------------PAPLLGDLNIVDTPGTNAIIRRHEELTKRFVPRSDLVLFITSADRPFTESERTFL-EHIREWGKK 173
Cdd:pfam00350  81 gtgkgissepivleiLSPLVPGLTLVDTPGLDSVAVGDQELTKEYIKPADIILAVTPANVDLSTSEALFLaREVDPNGKR 160


                  ....*...
gi 934118065  174 IILVVNKI 181
Cdd:pfam00350 161 TIGVLTKA 168
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 53-217 1.03e-20

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: 89.05  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  53 VVAGEFNAGKSSFINALLGDRVLPEG-VTPTTDRINILRFGEQPDsqlledflllrthpaplLGDLNIVDTPG-TNAIIR 130
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSdVPGTTRDPDVYVKELDKG-----------------KVKLVLVDTPGlDEFGGL 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 131 RHEELTKRFVPRSDLVLFITSADRPFTESERTFLEHIREW--GKKIILVVNKIDILDEKGRNEVLEFVRSNattlLGSTP 208
Cdd:cd00882   64 GREELARLLLRGADLILLVVDSTDRESEEDAKLLILRRLRkeGIPIILVGNKIDLLEEREVEELLRLEELA----KILGV 139


                 ....*....
gi 934118065 209 MIFAVSARS 217
Cdd:cd00882  140 PVFEVSAKT 148
YeeP COG3596
Predicted GTPase [General function prediction only];
9-254 5.71e-20

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 90.98  E-value: 5.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065   9 LRATEQSLFDRLHnALEQFGADVTAADAARLREATEQLAElFLLVVAGEFNAGKSSFINALLGDRVLPEGVT-PTTDRIN 87
Cdd:COG3596    1 MSTEVSSLTERLE-ALKRLPQVLRELLAEALERLLVELPP-PVIALVGKTGAGKSSLINALFGAEVAEVGVGrPCTREIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  88 ILRFGEQPdsqlledflllrthpaplLGDLNIVDTPGTNAIIRRHEE--LTKRFVPRSDLVLFITSADRPFTESERTFLE 165
Cdd:COG3596   79 RYRLESDG------------------LPGLVLLDTPGLGEVNERDREyrELRELLPEADLILWVVKADDRALATDEEFLQ 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 166 HIREW--GKKIILVVNKIDILDEKGRNEVL-------------EFVRSNATTLLGSTPMIFAVSARSALRArenddpklw 230
Cdd:COG3596  141 ALRAQypDPPVLVVLTQVDRLEPEREWDPPynwpsppkeqnirRALEAIAEQLGVPIDRVIPVSAAEDRTG--------- 211

                        250       260
                 ....*....|....*....|....
gi 934118065 231 aeSGFNAMEEYLLRTLDEGERVRL 254
Cdd:COG3596  212 --YGLEELVDALAEALPEAKRSRL 233
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 53-215 7.05e-19

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: 83.83  E-value: 7.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  53 VVAGEFNAGKSSFINALLGDRVLPEGVTP-TTDRINILRFGEQPdsqlledflllrthpaplLGDLNIVDTPG---TNAI 128
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPgTTRDPVRKEWELLP------------------LGPVVLIDTPGldeEGGL 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 129 IRRHEELTKRFVPRSDLVLFITSADRPFTESERTFLEhIREWGKKIILVVNKIDILDEKGRNEVLEFVRSNattLLGSTP 208
Cdd:cd00880   63 GRERVEEARQVADRADLVLLVVDSDLTPVEEEAKLGL-LRERGKPVLLVLNKIDLVPESEEEELLRERKLE---LLPDLP 138


                 ....*..
gi 934118065 209 MIfAVSA 215
Cdd:cd00880  139 VI-AVSA 144
CrfC COG0699
Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, ...
 18-379 1.47e-18

Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, recombination and repair];


Pssm-ID: 440463 [Multi-domain]  Cd Length: 582  Bit Score: 89.31  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  18 DRLHNALEQFGADVTAADAARLREATEQlaelFLLVVAGEFNAGKSSFINALLGDRVLPEGVTPTTDRINILRFGEQPDS 97
Cdd:COG0699    5 GVLDETIEDRADLRRRLDQARLDLADPS----LRIVMAGTTSQGKSQLVNALLGRRLLPSGAGETTGVPTEIKHAEGSSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  98 QLLE------DFLLLRTH-----------------------------------PAPLLGD-LNIVDTPGTNAIIRRHEEL 135
Cdd:COG0699   81 RLLPtagsvaDTKRWPGLdteeiynpihqvsqtkkrrargsngpevlralvglPHPLLRQgLVIVDTPGLGALVGSEAEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 136 TKRFVPRSDLVLFITSADRPFTESERTFLEHIREWGK---KIILVVNKIdilDEKGRNEVLEFVRSNATTL-LGSTPMIF 211
Cdd:COG0699  161 TLAKLPDADAVLVVLDADAEVTASEMELLRRVIQNLRicpSVFVVLNKI---DRRWRDLQPRQRTADQLHLqRADVSRVL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 212 AVSARSALRARENDDPKLWAESGFNAMEEYLLRTLdegERVRLKLLNPLGVGQKLATTYRTAS--DERLQTLSDDIKAIN 289
Cdd:COG0699  238 PLSALLGLLAKVAGDKELNEESRFPGLEAILSEQI---LARAGELERPQVLGEFNSAVAQSGKllSSELERAEREADELR 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 290 NIEGQIQVYKADMQRDFTPRIA---QLENLIHEFEQRGHTFFDEQIRLGRARDLLKKDLLEqrFRDQVVGDLdadTDRIT 366
Cdd:COG0699  315 QNYARWQAELGDELNDLTADVHhdlRTRFRTLRTAQRLLDSQDPTLRAPISQYLLEEHWDE--LFRNLANSL---TTAGG 389

                        410
                 ....*....|...
gi 934118065 367 QQIIdWLIERNLK 379
Cdd:COG0699  390 DNFI-WAFFRSVA 401
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 59-215 9.92e-16

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 75.19  E-value: 9.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  59 NAGKSSFINALLGDRVLPegVTP---TT-DRIN-ILrfgEQPDSQLLedflllrthpapllgdlnIVDTPGtnaIIRRHE 133
Cdd:cd04163   13 NVGKSTLLNALVGQKISI--VSPkpqTTrNRIRgIY---TDDDAQII------------------FVDTPG---IHKPKK 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 134 ELTKRFV--PRS-----DLVLFITSADRPFTESERTFLEHIREWGKKIILVVNKIDILDEKgrNEVLEFVrsNATTLLGS 206
Cdd:cd04163   67 KLGERMVkaAWSalkdvDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVKDK--EDLLPLL--EKLKELHP 142


                 ....*....
gi 934118065 207 TPMIFAVSA 215
Cdd:cd04163  143 FAEIFPISA 151
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 53-180 1.54e-15

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: 72.65  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065   53 VVAGEFNAGKSSFINALLGDRVLPEGVTPTTdRINILRFGEQPDSQLLedflllrthpapllgdlnIVDTPGTNAIIRRH 132
Cdd:pfam01926   3 ALVGRPNVGKSTLINALTGAKAIVSDYPGTT-RDPNEGRLELKGKQII------------------LVDTPGLIEGASEG 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 934118065  133 EELTKRFVP--RSDLVLFITSADRPFTESERTFLEHIREWGKKIILVVNK 180
Cdd:pfam01926  64 EGLGRAFLAiiEADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
era PRK00089
GTPase Era; Reviewed
 59-217 2.27e-15

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 76.62  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  59 NAGKSSFINALLGDRVLPegVTP---TT-DRIN-ILrfgEQPDSQLLedflllrthpapllgdlnIVDTPGtnaIIRRHE 133
Cdd:PRK00089  15 NVGKSTLLNALVGQKISI--VSPkpqTTrHRIRgIV---TEDDAQII------------------FVDTPG---IHKPKR 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 134 ELTKRFVpRS--------DLVLFITSADRPFTESERTFLEHIREWGKKIILVVNKIDILDEKgrNEVLEFVRSnATTLLG 205
Cdd:PRK00089  69 ALNRAMN-KAawsslkdvDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKDK--EELLPLLEE-LSELMD 144

                        170
                 ....*....|..
gi 934118065 206 STPmIFAVSARS 217
Cdd:PRK00089 145 FAE-IVPISALK 155
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
52-217 2.72e-15

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 73.86  E-value: 2.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  52 LVVAGEFNAGKSSFINALLGDRVLPEGVTPTTdRINILRFGEQPDSQLLedflllrthpapllgDLNIVDTPGTNAIIRR 131
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTN-GVTIDKKELKLDGLDV---------------DLVIWDTPGQDEFRET 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 132 HEELtKRFVPRSDLVLFITSADRPFT-ESERTFLEHIREWGKK--IILVVNKIDILDEKGRNEvLEFVRSNATTLLGSTp 208
Cdd:COG1100   70 RQFY-ARQLTGASLYLFVVDGTREETlQSLYELLESLRRLGKKspIILVLNKIDLYDEEEIED-EERLKEALSEDNIVE- 146


                 ....*....
gi 934118065 209 mIFAVSARS 217
Cdd:COG1100  147 -VVATSAKT 154
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
59-196 2.09e-14

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 73.87  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  59 NAGKSSFINALLGDRVLPegVTP---TT-DRIN-ILrfgEQPDSQLLedflllrthpapllgdlnIVDTPGtnaIIRRHE 133
Cdd:COG1159   13 NVGKSTLLNALVGQKVSI--VSPkpqTTrHRIRgIV---TREDAQIV------------------FVDTPG---IHKPKR 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 934118065 134 ELTKRFVpRS--------DLVLFITSADRPFTESERTFLEHIREWGKKIILVVNKIDILDekgRNEVLEFV 196
Cdd:COG1159   67 KLGRRMN-KAawsaledvDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVK---KEELLPLL 133
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
 54-185 8.50e-14

Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling.


Pssm-ID: 206740  Cd Length: 241  Bit Score: 71.15  E-value: 8.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  54 VAGEFNAGKSSFINALLGDRV--LPEGVTPTTDRINILRFGE------------QPDSQL--LEDF-------LLLRTHP 110
Cdd:cd09913    4 FLGQYSTGKSTFINYLLGQDYpgLRTGPEPTTDRFTVVMHGEddgtipgnalvvDPDKPFrgLSKFgngflnkFEGSTLP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 111 APLLGDLNIVDTPG-----TNAIIRRH--EELTKRFVPRSDLVLFITSADRPFTESE-RTFLEHIREWGKKIILVVNKID 182
Cdd:cd09913   84 HPLLESVTIVDTPGilsgeKQRQSRGYdfNAVCRWFAERADLIFLLFDPHKLDISDEfRRVIEQLKGHESKIRIVLNKAD 163


                 ...
gi 934118065 183 ILD 185
Cdd:cd09913  164 MVD 166
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 59-215 3.45e-12

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 68.54  E-value: 3.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  59 NAGKSSFINALLG-DRVLpegVTP----TTDRINIL--RFGEQpdsqlledflllrthpapllgdLNIVDTPGtnaiIRR 131
Cdd:PRK00093 183 NVGKSSLINALLGeERVI---VSDiagtTRDSIDTPfeRDGQK----------------------YTLIDTAG----IRR 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 132 ----HEEL-------TKRFVPRSDLVLFITSADRPFTESERTFLEHIREWGKKIILVVNKIDILDEKGRNEVLEFVRSNA 200
Cdd:PRK00093 234 kgkvTEGVekysvirTLKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWDLVDEKTMEEFKKELRRRL 313

                        170
                 ....*....|....*
gi 934118065 201 TTLLGStPMIFaVSA 215
Cdd:PRK00093 314 PFLDYA-PIVF-ISA 326
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 36-187 3.46e-12

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: 68.55  E-value: 3.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  36 AARLREATEQLAEL-------------FLLVVAGEFNAGKSSFINALLG-DRVLpegVTP----TTDrinilrfgeqpds 97
Cdd:COG0486  187 LERLEELREELEALlasarqgellregIKVVIVGRPNVGKSSLLNALLGeERAI---VTDiagtTRD------------- 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  98 qLLEDFLLLRTHPapllgdLNIVDTPG----TNAI----IRRheelTKRFVPRSDLVLFITSADRPFTESERTFLEHIRe 169
Cdd:COG0486  251 -VIEERINIGGIP------VRLIDTAGlretEDEVekigIER----AREAIEEADLVLLLLDASEPLTEEDEEILEKLK- 318

                        170
                 ....*....|....*...
gi 934118065 170 wGKKIILVVNKIDILDEK 187
Cdd:COG0486  319 -DKPVIVVLNKIDLPSEA 335
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 52-194 3.95e-12

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: 64.44  E-value: 3.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  52 LVVAGEFNAGKSSFINALLG-DRVLpegVTP---TT-DrinilrfgeqpdsqLLEDFLLLRTHPapllgdLNIVDTPG-- 124
Cdd:cd04164    6 VVIAGKPNVGKSSLLNALAGrDRAI---VSDiagTTrD--------------VIEEEIDLGGIP------VRLIDTAGlr 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 934118065 125 --TNAI----IRRheelTKRFVPRSDLVLFITSADRPFTESERTFLEHIRewGKKIILVVNKIDILDEKGRNEVLE 194
Cdd:cd04164   63 etEDEIekigIER----AREAIEEADLVLLVVDASEGLDEEDLEILELPA--KKPVIVVLNKSDLLSDAEGISELN 132
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 12-195 5.98e-12

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: 67.12  E-value: 5.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065   12 TEQSLFDRLHNALEQFGADVTAADAARLreateqLAELFLLVVAGEFNAGKSSFINALLG-DRVLpegVTP---TT-Dri 86
Cdd:pfam12631  63 TEEELLERLEELLAELEKLLATADRGRI------LREGIKVVIVGKPNVGKSSLLNALLGeERAI---VTDipgTTrD-- 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065   87 nilrfgeqpdsqLLEDFLLLRTHPapllgdLNIVDTPGtnaiIRRHE--------ELTKRFVPRSDLVLFITSADRPFTE 158
Cdd:pfam12631 132 ------------VIEETINIGGIP------LRLIDTAG----IRETDdevekigiERAREAIEEADLVLLVLDASRPLDE 189

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 934118065  159 SERTFLEHIREwGKKIILVVNKIDILDEKGRNEVLEF 195
Cdd:pfam12631 190 EDLEILELLKD-KKPIIVVLNKSDLLGEIDELEELKG 225
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 53-217 9.66e-12

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 63.68  E-value: 9.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  53 VVAGEFNAGKSSFINALLGDRVLPE-GVTP-TTDRINILRFGEQpdsqlledflllrthpapllgdLNIVDTPG------ 124
Cdd:cd01876    3 AFAGRSNVGKSSLINALTNRKKLARtSKTPgRTQLINFFNVGDK----------------------FRLVDLPGygyakv 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 125 TNAIIRRHEELTKRFVPRSD---LVLFITSADRPFTESERTFLEHIREWGKKIILVVNKIDILDEKGRNEVLEFVRsNAT 201
Cdd:cd01876   61 SKEVREKWGKLIEEYLENREnlkGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIK-EEL 139

                        170
                 ....*....|....*.
gi 934118065 202 TLLGSTPMIFAVSARS 217
Cdd:cd01876  140 NLFNILPPVILFSSKK 155
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
59-197 3.66e-11

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 65.43  E-value: 3.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  59 NAGKSSFINALLG-DRVLpegVTP---TT-DRINIL--RFGEqpdsqlleDFLLlrthpapllgdlniVDTPGtnaiIRR 131
Cdd:COG1160  185 NVGKSSLINALLGeERVI---VSDiagTTrDSIDTPfeRDGK--------KYTL--------------IDTAG----IRR 235

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 934118065 132 ----HEEL-------TKRFVPRSDLVLFITSADRPFTESERTFLEHIREWGKKIILVVNKIDIL--DEKGRNEVLEFVR 197
Cdd:COG1160  236 kgkvDEGIekysvlrTLRAIERADVVLLVIDATEGITEQDLKIAGLALEAGKALVIVVNKWDLVekDRKTREELEKEIR 314
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 59-220 8.02e-11

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: 60.91  E-value: 8.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  59 NAGKSSFINALLG-DRVLpegVTP----TTDRINIL-RFGEQPdsqlledFLLlrthpapllgdlniVDTPGtnaiIRR- 131
Cdd:cd01895   12 NVGKSSLLNALLGeERVI---VSDiagtTRDSIDVPfEYDGQK-------YTL--------------IDTAG----IRKk 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 132 ---HEEL-------TKRFVPRSDLVLFITSADRPFTESERTFLEHIREWGKKIILVVNKIDILDEKG--RNEVLEFVRSN 199
Cdd:cd01895   64 gkvTEGIekysvlrTLKAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEKDEktMKEFEKELRRK 143

                        170       180
                 ....*....|....*....|.
gi 934118065 200 ATTLLGStPMIFaVSARSALR 220
Cdd:cd01895  144 LPFLDYA-PIVF-ISALTGQG 162
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
32-186 2.12e-09

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 59.74  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  32 TAADAARLREAteqlaelFLLVVAGEFNAGKSSFINALLG-DRVLpegVTP---TT-DRInilrfgeqpdsqllEDFLLL 106
Cdd:PRK05291 205 SARQGEILREG-------LKVVIAGRPNVGKSSLLNALLGeERAI---VTDiagTTrDVI--------------EEHINL 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 107 RTHPapllgdLNIVDTPG----TNAI----IRRheelTKRFVPRSDLVLFITSADRPFTESERTFLEHIRewGKKIILVV 178
Cdd:PRK05291 261 DGIP------LRLIDTAGiretDDEVekigIER----SREAIEEADLVLLVLDASEPLTEEDDEILEELK--DKPVIVVL 328


                 ....*...
gi 934118065 179 NKIDILDE 186
Cdd:PRK05291 329 NKADLTGE 336
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 53-182 6.58e-09

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: 54.65  E-value: 6.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  53 VVAGEFNAGKSSFINALLGDRVLPEGVT-PTTDRINILRFGEQPDSqlledflllrthpapllgdLNIVDTPGTNAIIRR 131
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEVAAVGDRrPTTRAAQAYVWQTGGDG-------------------LVLLDLPGVGERGRR 61

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 934118065 132 H---EELTKRFVPRSDLVLFITSADRPFTESERTFLEHI-REWGKKIILVVNKID 182
Cdd:cd11383   62 DreyEELYRRLLPEADLVLWLLDADDRALAADHDFYLLPlAGHDAPLLFVLNQVD 116
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 52-198 1.35e-08

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 54.30  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065   52 LVVAGEFNAGKSSFINALLGDRVLPEGVTPTTDRiNILRFGEQPDSQLLEdflllrthpapllgdLNIVDTPGT---NAI 128
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTR-NYVTTVIEEDGKTYK---------------FNLLDTAGQedyDAI 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  129 IRRHEELTKRFVPRSDLVLFITSADRPFTESERTfLEHIREWGKKIILVVNKIDILDEKgrneVLEFVRS 198
Cdd:TIGR00231  68 RRLYYPQVERSLRVFDIVILVLDVEEILEKQTKE-IIHHADSGVPIILVGNKIDLKDAD----LKTHVAS 132
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 59-195 4.37e-07

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: 4.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  59 NAGKSSFINALLGDRV-----LPeGVTptTDRInilrfgeqpdsqlledflllrTHPAPLLG-DLNIVDTPG----TNAI 128
Cdd:cd01894    7 NVGKSTLFNRLTGRRDaivsdTP-GVT--RDRK---------------------YGEAEWGGrEFILIDTGGiepdDEGI 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 934118065 129 IRRHEELTKRFVPRSDLVLFITSADRPFTESERTFLEHIREWGKKIILVVNKIDilDEKGRNEVLEF 195
Cdd:cd01894   63 SKEIREQAEIAIEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKID--NIKEEEEAAEF 127
Miro1 cd01893
Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) ...
 53-198 4.91e-07

Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the N-terminal GTPase domain of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature.


Pssm-ID: 206680 [Multi-domain]  Cd Length: 168  Bit Score: 50.03  E-value: 4.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  53 VVAGEFNAGKSSFINALLGDRvLPEGVTPTTDRINIlrfgeqpdsqlledflllrthPAPLLGD---LNIVDTPGTNaii 129
Cdd:cd01893    6 VLIGDEGVGKSSLIMSLVSEE-FPENVPRVLPEITI---------------------PADVTPErvpTTIVDTSSRP--- 60

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 934118065 130 rRHEELTKRFVPRSDLVLFITSADRPFT-ESERTF-LEHIREWGKK--IILVVNKIDILDEKGRN---EVLEFVRS 198
Cdd:cd01893   61 -QDRANLAAEIRKANVICLVYSVDRPSTlERIRTKwLPLIRRLGVKvpIILVGNKSDLRDGSSQAgleEEMLPIMN 135
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
59-195 5.17e-07

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 52.33  E-value: 5.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  59 NAGKSSFINALLGDRV-----LPeGVTptTDRInilrfgeqpdsqlledflllrTHPAPLLG-DLNIVDTPG-----TNA 127
Cdd:COG1160   12 NVGKSTLFNRLTGRRDaivddTP-GVT--RDRI---------------------YGEAEWGGrEFTLIDTGGiepddDDG 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 934118065 128 IIRRHEELTKRFVPRSDLVLFITSADRPFTESERTFLEHIREWGKKIILVVNKIDilDEKGRNEVLEF 195
Cdd:COG1160   68 LEAEIREQAELAIEEADVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVD--GPKREADAAEF 133
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 59-195 7.62e-07

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 51.59  E-value: 7.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  59 NAGKSSFINALLGDRV-----LPeGVTptTDRInilrFGEqpdsqlledflllrthpAPLLG-DLNIVDTPG----TNAI 128
Cdd:PRK00093  11 NVGKSTLFNRLTGKRDaivadTP-GVT--RDRI----YGE-----------------AEWLGrEFILIDTGGiepdDDGF 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 934118065 129 IRRHEELTKRFVPRSDLVLFITSADRPFTESERTFLEHIREWGKKIILVVNKIDilDEKGRNEVLEF 195
Cdd:PRK00093  67 EKQIREQAELAIEEADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVD--GPDEEADAYEF 131
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 54-215 1.02e-06

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 49.22  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  54 VAGEFNAGKSSFINALLGdrvlpegVTPTTDRINIlRFGEQPDSQLLEDFLLLRTHPAPLLGDL-----NIVDTPGtnai 128
Cdd:cd00881    4 VIGHVDHGKTTLTGSLLY-------QTGAIDRRGT-RKETFLDTLKEERERGITIKTGVVEFEWpkrriNFIDTPG---- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 129 irrHEELTKRFV---PRSDLVLFITSADRPFTESERTFLEHIREWGKKIILVVNKIDILDEKGRNEVLEFVRS-----NA 200
Cdd:cd00881   72 ---HEDFSKETVrglAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFDEVLREIKEllkliGF 148

                        170
                 ....*....|....*
gi 934118065 201 TTLLGSTPMIFAVSA 215
Cdd:cd00881  149 TFLKGKDVPIIPISA 163
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 117-219 6.24e-06

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 47.13  E-value: 6.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  117 LNIVDTPGtnaiirrHEELTKRfVPRS----DLVLFITSADRPFTESERTFLEHIREWGKKIILVVNKIDILDEKGRNEV 192
Cdd:pfam00009  71 INLIDTPG-------HVDFVKE-VIRGlaqaDGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDGAELEEV 142

                          90       100       110
                  ....*....|....*....|....*....|.
gi 934118065  193 LEFVRSNATTLLG----STPMIFaVSARSAL 219
Cdd:pfam00009 143 VEEVSRELLEKYGedgeFVPVVP-GSALKGE 172
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 51-217 6.09e-05

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 43.75  E-value: 6.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  51 LLVVAGEFNAGKSSFINALLG---DRvLPE----GVTpttdrINI-LRFGEQPDSQLLEdflllrthpapllgdlnIVDT 122
Cdd:cd04171    1 IIGTAGHIDHGKTTLIKALTGietDR-LPEekkrGIT-----IDLgFAYLDLPDGKRLG-----------------FIDV 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 123 PGtnaiirrHEELTKRFVPRS---DLVLFITSADRPFTESERTFLEHIREWG-KKIILVVNKIDILDEkgrnEVLEFVRS 198
Cdd:cd04171   58 PG-------HEKFVKNMLAGAggiDAVLLVVAADEGIMPQTREHLEILELLGiKKGLVVLTKADLVDE----DRLELVEE 126

                        170       180
                 ....*....|....*....|...
gi 934118065 199 NATTLLGSTPM----IFAVSARS 217
Cdd:cd04171  127 EILELLAGTFLadapIFPVSSVT 149
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 59-188 7.00e-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: 7.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  59 NAGKSSFINALLGDRV----LPeGVTptTDRI-NILRFGEQpdsqlledflllrthpapllgDLNIVDTPGTNAIIRRH- 132
Cdd:cd01879    7 NVGKTTLFNALTGARQkvgnWP-GVT--VEKKeGEFKLGGK---------------------EIEIVDLPGTYSLTPYSe 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 934118065 133 -EELTKRFV--PRSDLVLFITSAdrpfTESERT--FLEHIREWGKKIILVVNKIDILDEKG 188
Cdd:cd01879   63 dEKVARDFLlgEEPDLIVNVVDA----TNLERNlyLTLQLLELGLPVVVALNMIDEAEKRG 119
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 56-189 2.07e-04

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 44.40  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  56 GEFNAGKSSFINALLG-DRVLPEGVTPTT-DRIN-ILRFGEqpdsqllEDFLLlrthpapllgdlniVDTPGtnaIIRRH 132
Cdd:PRK09518 457 GRPNVGKSSLLNQLTHeERAVVNDLAGTTrDPVDeIVEIDG-------EDWLF--------------IDTAG---IKRRQ 512

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 934118065 133 EEL----------TKRFVPRSDLVLFITSADRPFTESERTFLEHIREWGKKIILVVNKIDILDEKGR 189
Cdd:PRK09518 513 HKLtgaeyysslrTQAAIERSELALFLFDASQPISEQDLKVMSMAVDAGRALVLVFNKWDLMDEFRR 579
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 52-186 2.89e-04

Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. 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 interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206738  Cd Length: 278  Bit Score: 43.00  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  52 LVVAGEFNAGKSSFINALLGDRVLPEGVTPTTDRINILRFGEQPDSQL------LEDFLLLR----THPAPL-------- 113
Cdd:cd08771    6 IVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSPSESDedekeeWGEFLHLKskefTDFEELreeieket 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 114 -----------------------LGDLNIVDTPG---------TNAIIRRHEELTKRFV--PRSdLVLFITSADRPFTES 159
Cdd:cd08771   86 drvagenkgispepirleiespdVPNLTLVDLPGlikvpvgdqPEDIEEQIRSMVKSYIsnPRS-IILAVVPANVDLANS 164

                        170       180
                 ....*....|....*....|....*...
gi 934118065 160 E-RTFLEHIREWGKKIILVVNKIDILDE 186
Cdd:cd08771  165 EaLKLAREVDPEGERTIGVLTKLDLMDP 192
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 2-182 1.74e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 41.32  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065   2 LGEREAELRATEQSLFDRLHNALEQFGADVTAADAARLREATEQLAELFLLVVAGEFNAGKSSFINALLGDRVLPEGVTP 81
Cdd:PRK09518 228 LVEDAIEEQEYDQYAANLEGYELDEGDEDLLEGSGFVAGDEKAGPKAVGVVAIVGRPNVGKSTLVNRILGRREAVVEDTP 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  82 --TTDRInilrfgeqpdsqlledflllrTHPAPLLG-DLNIVDT-------PGTNAIIRRHEELTkrfVPRSDLVLFITS 151
Cdd:PRK09518 308 gvTRDRV---------------------SYDAEWAGtDFKLVDTggweadvEGIDSAIASQAQIA---VSLADAVVFVVD 363

                        170       180       190
                 ....*....|....*....|....*....|.
gi 934118065 152 ADRPFTESERTFLEHIREWGKKIILVVNKID 182
Cdd:PRK09518 364 GQVGLTSTDERIVRMLRRAGKPVVLAVNKID 394
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 144-222 1.83e-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: 40.07  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 144 DLVLFITSADRPFTESERT--FLEHIREWGKKIILVVNKIDILDEKGRNEVLEFVRSnattlLGSTpmIFAVSARS---- 217
Cdd:cd01854    4 DQVLIVFSLKEPFFNLRLLdrYLVAAEASGIEPVIVLNKADLVDDEELEELLEIYEK-----LGYP--VLAVSAKTgegl 76


                 ....*.
gi 934118065 218 -ALRAR 222
Cdd:cd01854   77 dELREL 82
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 52-197 2.02e-03

Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins.


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 39.08  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  52 LVVAGEFNAGKSSFINALlgDRVLPEgVTP---TTDRINILRFgeqpdsqlleDFLLLRthpapllgdLNIVDTPGtnaI 128
Cdd:cd01897    3 LVIAGYPNVGKSSLVNKL--TRAKPE-VAPypfTTKSLFVGHF----------DYKYLR---------WQVIDTPG---I 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065 129 IRRHEE----------LTKRFVPrsDLVLFI----TSADRPFTESERTFLEhIRE-WGKKIILVVNKIDILDEKGRNEVL 193
Cdd:cd01897   58 LDRPLEerntiemqaiTALAHLR--AAVLFFidpsETCGYSIEEQLSLFKE-IKPlFNKPVIVVLNKIDLLTEEDLSEIE 134


                 ....
gi 934118065 194 EFVR 197
Cdd:cd01897  135 KELE 138
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 11-75 4.66e-03

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


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 38.29  E-value: 4.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 934118065   11 ATEQSLFDRLHNALEQFGADVTAADAaRLREATEQLAELF---LLVVAGEFNAGKSSFINALLGDRVL 75
Cdd:pfam03193  66 LDEEEELEELLKIYRAIGYPVLFVSA-KTGEGIEALKELLkgkTTVLAGQSGVGKSTLLNALLPELDL 132
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 52-182 5.20e-03

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 39.11  E-value: 5.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 934118065  52 LVVAGEFNAGKSSFINALLGdrvlpegvtpTTDRINilRFGEQPDSQLLEDF--------LLLRTHPAPLLGD---LNIV 120
Cdd:cd04170    2 IALVGHSGSGKTTLAEALLY----------ATGAID--RLGRVEDGNTVSDYdpeekkrkMSIETSVAPLEWNghkINLI 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 934118065 121 DTPGTNAIIRRheelTKRFVPRSDLVLFITSADRPFTESERTFLEHIREWGKKIILVVNKID 182
Cdd:cd04170   70 DTPGYADFVGE----TLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMD 127
 
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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