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Conserved domains on  [gi|332007828|gb|AED95211|]
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Root hair defective 3 GTP-binding protein (RHD3) [Arabidopsis thaliana]

Protein Classification

GBP domain-containing protein( domain architecture ID 11160444)

GBP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sey1_3HB pfam20428
Sey1 three-helix bundle domain; This is the three-helix bundle (3HB) domain found at the ...
 322-762 0e+00

Sey1 three-helix bundle domain; This is the three-helix bundle (3HB) domain found at the C-terminal of Sey1 from yeast and RHD3 from Arabidopsis, GTP-binding proteins involved in homotypic membrane fusion of the endoplasmic reticulum. This is a stalk-like domain composed of four 3HBs that interacts with its own GTPase domain and that of a neighbouring molecule, to undergo major conformational changes during the GTP cycle to drive membrane fusion.


:

Pssm-ID: 466577  Cd Length: 419  Bit Score: 571.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  322 PGFGKKLSSILEKYFSEYDAEAIYFDEGVRKEKRLQLKLNALDFVYPSYATMLGHLRSNALESFKIRLEQSLNQGEGFAK 401
Cdd:pfam20428   1 GGLGAKLASIREKCLSEYDTEASRYNKGVYQEKRQELEEKLDSHLKPTFQAQLGALHKGLLESFKEAVSSALKAGEGFAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  402 AVRDSQQSCLMVFDKGCEDAAVKQATWDASKIREKLCRDIDAHTFFARSAKLSELTANYEKRLTQALSEPVESLFEAGGK 481
Cdd:pfam20428  81 SVKDLKTKCVEKFDEECESASIEGALWDTSKIRLKLEKDIDAHSARLRKEELKELTNRYEKKLSSALSEPVELLLNKLNK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  482 ETWPSIRKLLKRETETAVTDFLDVVTGFELDHAKIDAMVQNLKNYSQSLVEKKAREEAA--KILIRMKDRFSTVFSHDKD 559
Cdd:pfam20428 161 ETWDTVLKLFKREVEDAVSRFKDRVDFFDLSEEENDKMLKNLKRKSWGVLRTKIHEEASeeNLLMRLRDRFEDKFRYDSD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  560 SMPRVWTGKEDIRAITKDARAEALSLLSVMTAIRLDERPDNIESTLFSSLMDGTVSAASSHNRSVGTSTDPLASSSWEEV 639
Cdd:pfam20428 241 GMPRLWTGKEDIEGIYKVAREHALKLLPVLSRIRLSDGSDNIPPTLTRALGDTTSSATPSEDLPPIGGVDELASSTLEEV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  640 PPNNILLTPVQCKSLWRQFKSETEYTVTQAisaqeahKR---NNNWLPPAWAIVLMIVLGFNEFMMLLKNPLYllgFFVA 716
Cdd:pfam20428 321 PPSATILTEVQKKSLWVQFKKEADYTVTEA-------KRsiiNNNTQIPPYFYVLLLVLGWNEFMAVLRNPLY---FFLL 390

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 332007828  717 FLLSKALWVQLDiprefqhgavagvLSITSKflptVMNLLRKLAEE 762
Cdd:pfam20428 391 LLLGKTLYVQYD-------------LSLSGP----VMNVLQRAAEE 419
RHD3_GTPase super family cl46411
Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of ...
 46-281 4.61e-135

Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of several eukaryotic root hair defective 3 (RHD3) like GTP-binding proteins, including RHD3 from Arabidopsis and Sey1 from yeast, which are involved in homotypic membrane fusion of the endoplasmic reticulum. This domain binds GTP and forms dimers with other molecule for membrane tethering.


The actual alignment was detected with superfamily member pfam05879:

Pssm-ID: 461768  Cd Length: 243  Bit Score: 401.45  E-value: 4.61e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828   46 MGPQSSGKSTLLNHLFKTSFREMDAfAGRSQTTKGIWMARCVGI---EPFTIAMDLEGTDGRERGEDDTtFEKQSALFAI 122
Cdd:pfam05879   1 FGSQSTGKSTLLNHLFGTNFSVMDA-SGRQQTTKGIWLAKCKGIgnmEPNILVMDVEGTDGRERGEDQD-FERKSALFAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  123 AVADIVLINMWCHDIGREQAANKPLLKTVFQVMLRLF-----SPRKTTLLFVIRDKTK-TPIELLERALREDIQKIWDSV 196
Cdd:pfam05879  79 ATSEVLIVNMWEHQVGLYQGANMGLLKTVFEVNLQLFgkdkdNPHKTLLLFVIRDHVGvTPLENLEDTLREDLQKIWDSL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  197 RKPEAHKNTPLNEFFNVMIVALSSYEEKEKQFEQEVAELRQRFFHSISPGGLAGDRRGVVPASGFSFSSQQIWKVIKENR 276
Cdd:pfam05879 159 SKPAGLENSPLNDFFDVEFVALPHKELQEDQFKEEVKKLRQRFVHSISPGGFAPEYHGRIPADGFSFYAEQIWDQIENNK 238


                  ....*
gi 332007828  277 DLDLP 281
Cdd:pfam05879 239 DLDLP 243
 
Name Accession Description Interval E-value
Sey1_3HB pfam20428
Sey1 three-helix bundle domain; This is the three-helix bundle (3HB) domain found at the ...
 322-762 0e+00

Sey1 three-helix bundle domain; This is the three-helix bundle (3HB) domain found at the C-terminal of Sey1 from yeast and RHD3 from Arabidopsis, GTP-binding proteins involved in homotypic membrane fusion of the endoplasmic reticulum. This is a stalk-like domain composed of four 3HBs that interacts with its own GTPase domain and that of a neighbouring molecule, to undergo major conformational changes during the GTP cycle to drive membrane fusion.


Pssm-ID: 466577  Cd Length: 419  Bit Score: 571.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  322 PGFGKKLSSILEKYFSEYDAEAIYFDEGVRKEKRLQLKLNALDFVYPSYATMLGHLRSNALESFKIRLEQSLNQGEGFAK 401
Cdd:pfam20428   1 GGLGAKLASIREKCLSEYDTEASRYNKGVYQEKRQELEEKLDSHLKPTFQAQLGALHKGLLESFKEAVSSALKAGEGFAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  402 AVRDSQQSCLMVFDKGCEDAAVKQATWDASKIREKLCRDIDAHTFFARSAKLSELTANYEKRLTQALSEPVESLFEAGGK 481
Cdd:pfam20428  81 SVKDLKTKCVEKFDEECESASIEGALWDTSKIRLKLEKDIDAHSARLRKEELKELTNRYEKKLSSALSEPVELLLNKLNK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  482 ETWPSIRKLLKRETETAVTDFLDVVTGFELDHAKIDAMVQNLKNYSQSLVEKKAREEAA--KILIRMKDRFSTVFSHDKD 559
Cdd:pfam20428 161 ETWDTVLKLFKREVEDAVSRFKDRVDFFDLSEEENDKMLKNLKRKSWGVLRTKIHEEASeeNLLMRLRDRFEDKFRYDSD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  560 SMPRVWTGKEDIRAITKDARAEALSLLSVMTAIRLDERPDNIESTLFSSLMDGTVSAASSHNRSVGTSTDPLASSSWEEV 639
Cdd:pfam20428 241 GMPRLWTGKEDIEGIYKVAREHALKLLPVLSRIRLSDGSDNIPPTLTRALGDTTSSATPSEDLPPIGGVDELASSTLEEV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  640 PPNNILLTPVQCKSLWRQFKSETEYTVTQAisaqeahKR---NNNWLPPAWAIVLMIVLGFNEFMMLLKNPLYllgFFVA 716
Cdd:pfam20428 321 PPSATILTEVQKKSLWVQFKKEADYTVTEA-------KRsiiNNNTQIPPYFYVLLLVLGWNEFMAVLRNPLY---FFLL 390

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 332007828  717 FLLSKALWVQLDiprefqhgavagvLSITSKflptVMNLLRKLAEE 762
Cdd:pfam20428 391 LLLGKTLYVQYD-------------LSLSGP----VMNVLQRAAEE 419
RHD3_GTPase pfam05879
Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of ...
 46-281 4.61e-135

Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of several eukaryotic root hair defective 3 (RHD3) like GTP-binding proteins, including RHD3 from Arabidopsis and Sey1 from yeast, which are involved in homotypic membrane fusion of the endoplasmic reticulum. This domain binds GTP and forms dimers with other molecule for membrane tethering.


Pssm-ID: 461768  Cd Length: 243  Bit Score: 401.45  E-value: 4.61e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828   46 MGPQSSGKSTLLNHLFKTSFREMDAfAGRSQTTKGIWMARCVGI---EPFTIAMDLEGTDGRERGEDDTtFEKQSALFAI 122
Cdd:pfam05879   1 FGSQSTGKSTLLNHLFGTNFSVMDA-SGRQQTTKGIWLAKCKGIgnmEPNILVMDVEGTDGRERGEDQD-FERKSALFAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  123 AVADIVLINMWCHDIGREQAANKPLLKTVFQVMLRLF-----SPRKTTLLFVIRDKTK-TPIELLERALREDIQKIWDSV 196
Cdd:pfam05879  79 ATSEVLIVNMWEHQVGLYQGANMGLLKTVFEVNLQLFgkdkdNPHKTLLLFVIRDHVGvTPLENLEDTLREDLQKIWDSL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  197 RKPEAHKNTPLNEFFNVMIVALSSYEEKEKQFEQEVAELRQRFFHSISPGGLAGDRRGVVPASGFSFSSQQIWKVIKENR 276
Cdd:pfam05879 159 SKPAGLENSPLNDFFDVEFVALPHKELQEDQFKEEVKKLRQRFVHSISPGGFAPEYHGRIPADGFSFYAEQIWDQIENNK 238


                  ....*
gi 332007828  277 DLDLP 281
Cdd:pfam05879 239 DLDLP 243
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 34-242 2.17e-54

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 187.53  E-value: 2.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  34 SDCGLSYAVVAIMGPQSSGKSTLLNHLFKTS--FREMDAFagrSQTTKGIWMARCV-----GIEPFTIAMDLEGTDGRER 106
Cdd:cd01851    1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSdgFDVMDTS---QQTTKGIWMWSDPfkdtdGKKHAVLLLDTEGTDGRER 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828 107 GEddttFEKQSALFAIAVA--DIVLINMWCHDIGREQAANKPLLKTVF----QVMLRLFSPRKTTLLFVIRDKT-KTPIE 179
Cdd:cd01851   78 GE----FENDARLFALATLlsSVLIYNMWQTILGDDLDKLMGLLKTALetlgLAGLHNFSKPKPLLLFVVRDFTgPTPLE 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332007828 180 LLE-----RALREDIQKIWDSVRKPEahknTPLNEFFNVMIVALSSYEEKEKQFEQ-------EVAELRQRFFHS 242
Cdd:cd01851  154 GLDvteksETLIEELNKIWSSIRKPF----TPITCFVLPHPGLLHKLLQNDGRLKDlppefrkALKALRQRFFSS 224
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 40-130 6.35e-03

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: 38.12  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828   40 YAVVAIMGPQSSGKSTLLNHLFKTSFREMDAFAGrsqTTKGIWMaRCVGIEPFTIAMDLEGTDGRERGEDDTTFEKQSAL 119
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPG---TTRNYVT-TVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVE 76

                          90
                  ....*....|.
gi 332007828  120 FAIAVADIVLI 130
Cdd:TIGR00231  77 RSLRVFDIVIL 87
 
Name Accession Description Interval E-value
Sey1_3HB pfam20428
Sey1 three-helix bundle domain; This is the three-helix bundle (3HB) domain found at the ...
 322-762 0e+00

Sey1 three-helix bundle domain; This is the three-helix bundle (3HB) domain found at the C-terminal of Sey1 from yeast and RHD3 from Arabidopsis, GTP-binding proteins involved in homotypic membrane fusion of the endoplasmic reticulum. This is a stalk-like domain composed of four 3HBs that interacts with its own GTPase domain and that of a neighbouring molecule, to undergo major conformational changes during the GTP cycle to drive membrane fusion.


Pssm-ID: 466577  Cd Length: 419  Bit Score: 571.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  322 PGFGKKLSSILEKYFSEYDAEAIYFDEGVRKEKRLQLKLNALDFVYPSYATMLGHLRSNALESFKIRLEQSLNQGEGFAK 401
Cdd:pfam20428   1 GGLGAKLASIREKCLSEYDTEASRYNKGVYQEKRQELEEKLDSHLKPTFQAQLGALHKGLLESFKEAVSSALKAGEGFAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  402 AVRDSQQSCLMVFDKGCEDAAVKQATWDASKIREKLCRDIDAHTFFARSAKLSELTANYEKRLTQALSEPVESLFEAGGK 481
Cdd:pfam20428  81 SVKDLKTKCVEKFDEECESASIEGALWDTSKIRLKLEKDIDAHSARLRKEELKELTNRYEKKLSSALSEPVELLLNKLNK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  482 ETWPSIRKLLKRETETAVTDFLDVVTGFELDHAKIDAMVQNLKNYSQSLVEKKAREEAA--KILIRMKDRFSTVFSHDKD 559
Cdd:pfam20428 161 ETWDTVLKLFKREVEDAVSRFKDRVDFFDLSEEENDKMLKNLKRKSWGVLRTKIHEEASeeNLLMRLRDRFEDKFRYDSD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  560 SMPRVWTGKEDIRAITKDARAEALSLLSVMTAIRLDERPDNIESTLFSSLMDGTVSAASSHNRSVGTSTDPLASSSWEEV 639
Cdd:pfam20428 241 GMPRLWTGKEDIEGIYKVAREHALKLLPVLSRIRLSDGSDNIPPTLTRALGDTTSSATPSEDLPPIGGVDELASSTLEEV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  640 PPNNILLTPVQCKSLWRQFKSETEYTVTQAisaqeahKR---NNNWLPPAWAIVLMIVLGFNEFMMLLKNPLYllgFFVA 716
Cdd:pfam20428 321 PPSATILTEVQKKSLWVQFKKEADYTVTEA-------KRsiiNNNTQIPPYFYVLLLVLGWNEFMAVLRNPLY---FFLL 390

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 332007828  717 FLLSKALWVQLDiprefqhgavagvLSITSKflptVMNLLRKLAEE 762
Cdd:pfam20428 391 LLLGKTLYVQYD-------------LSLSGP----VMNVLQRAAEE 419
RHD3_GTPase pfam05879
Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of ...
 46-281 4.61e-135

Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of several eukaryotic root hair defective 3 (RHD3) like GTP-binding proteins, including RHD3 from Arabidopsis and Sey1 from yeast, which are involved in homotypic membrane fusion of the endoplasmic reticulum. This domain binds GTP and forms dimers with other molecule for membrane tethering.


Pssm-ID: 461768  Cd Length: 243  Bit Score: 401.45  E-value: 4.61e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828   46 MGPQSSGKSTLLNHLFKTSFREMDAfAGRSQTTKGIWMARCVGI---EPFTIAMDLEGTDGRERGEDDTtFEKQSALFAI 122
Cdd:pfam05879   1 FGSQSTGKSTLLNHLFGTNFSVMDA-SGRQQTTKGIWLAKCKGIgnmEPNILVMDVEGTDGRERGEDQD-FERKSALFAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  123 AVADIVLINMWCHDIGREQAANKPLLKTVFQVMLRLF-----SPRKTTLLFVIRDKTK-TPIELLERALREDIQKIWDSV 196
Cdd:pfam05879  79 ATSEVLIVNMWEHQVGLYQGANMGLLKTVFEVNLQLFgkdkdNPHKTLLLFVIRDHVGvTPLENLEDTLREDLQKIWDSL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  197 RKPEAHKNTPLNEFFNVMIVALSSYEEKEKQFEQEVAELRQRFFHSISPGGLAGDRRGVVPASGFSFSSQQIWKVIKENR 276
Cdd:pfam05879 159 SKPAGLENSPLNDFFDVEFVALPHKELQEDQFKEEVKKLRQRFVHSISPGGFAPEYHGRIPADGFSFYAEQIWDQIENNK 238


                  ....*
gi 332007828  277 DLDLP 281
Cdd:pfam05879 239 DLDLP 243
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 34-242 2.17e-54

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 187.53  E-value: 2.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  34 SDCGLSYAVVAIMGPQSSGKSTLLNHLFKTS--FREMDAFagrSQTTKGIWMARCV-----GIEPFTIAMDLEGTDGRER 106
Cdd:cd01851    1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSdgFDVMDTS---QQTTKGIWMWSDPfkdtdGKKHAVLLLDTEGTDGRER 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828 107 GEddttFEKQSALFAIAVA--DIVLINMWCHDIGREQAANKPLLKTVF----QVMLRLFSPRKTTLLFVIRDKT-KTPIE 179
Cdd:cd01851   78 GE----FENDARLFALATLlsSVLIYNMWQTILGDDLDKLMGLLKTALetlgLAGLHNFSKPKPLLLFVVRDFTgPTPLE 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332007828 180 LLE-----RALREDIQKIWDSVRKPEahknTPLNEFFNVMIVALSSYEEKEKQFEQ-------EVAELRQRFFHS 242
Cdd:cd01851  154 GLDvteksETLIEELNKIWSSIRKPF----TPITCFVLPHPGLLHKLLQNDGRLKDlppefrkALKALRQRFFSS 224
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 44-189 5.40e-06

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: 47.45  E-value: 5.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  44 AIMGPQSSGKSTLLNHLFKTSFREMDAFAGrsqTTKGIWmARCVGIEPFTIAMDLEGTDGRERGEDDTTFEKqsALFAIA 123
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPG---TTRDPD-VYVKELDKGKVKLVLVDTPGLDEFGGLGREEL--ARLLLR 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332007828 124 VADIVLINMwchdigreQAANKPLLKTVFQVMLRLFSPRKTTLLFVIrdkTKtpIELLERALREDI 189
Cdd:cd00882   75 GADLILLVV--------DSTDRESEEDAKLLILRRLRKEGIPIILVG---NK--IDLLEEREVEEL 127
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 44-148 3.58e-04

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: 41.85  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  44 AIMGPQSSGKSTLLNHLFKTSFREMDAFAGrsqTTKGiWMARCVGIEPFTIAM--DLEGTDgreRGEDDTTFEKQSALFA 121
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPG---TTRD-PVRKEWELLPLGPVVliDTPGLD---EEGGLGRERVEEARQV 73

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 332007828 122 IAVADIVLI----NMWCHD----IGREQAANKPLL 148
Cdd:cd00880   74 ADRADLVLLvvdsDLTPVEeeakLGLLRERGKPVL 108
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 44-136 3.66e-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: 38.48  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828  44 AIMGPQSSGKSTLLNHLFKTSFREMDafaGRSQTTKGIWMARCVGIEPFTIAMDLEGTDGRERgeDDTTFEKQsALFAIA 123
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEVAAVG---DRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGR--RDREYEEL-YRRLLP 74

                         90
                 ....*....|...
gi 332007828 124 VADIVLinmWCHD 136
Cdd:cd11383   75 EADLVL---WLLD 84
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 40-130 6.35e-03

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: 38.12  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007828   40 YAVVAIMGPQSSGKSTLLNHLFKTSFREMDAFAGrsqTTKGIWMaRCVGIEPFTIAMDLEGTDGRERGEDDTTFEKQSAL 119
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPG---TTRNYVT-TVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVE 76

                          90
                  ....*....|.
gi 332007828  120 FAIAVADIVLI 130
Cdd:TIGR00231  77 RSLRVFDIVIL 87
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 42-60 8.66e-03

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 38.62  E-value: 8.66e-03
                         10
                 ....*....|....*....
gi 332007828  42 VVAIMGPQSSGKSTLLNHL 60
Cdd:cd03255   32 FVAIVGPSGSGKSTLLNIL 50
 
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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