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Conserved domains on  [gi|1101056089|gb|OIO18127|]
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redox-regulated ATPase YchF [Candidatus Kuenenbacteria bacterium CG1_02_38_13]

Protein Classification

redox-regulated ATPase YchF( domain architecture ID 17564584)

redox-regulated ATPase YchF belongs to the Obg (GTPase) family, but actually prefers ATP, associates with ribosomes, and appears to be regulated by the redox state of the cell

CATH:  3.40.50.300|3.10.20.30|1.10.150.300
EC:  3.6.-.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0046872|GO:0043022
PubMed:  16333325|11489118|21527254
SCOP:  4004039

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
 1-350 0e+00

Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 581.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   1 MKIGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERLEKLAKIYHSAKTIYSTIEFVDIAGLVKNAHK 80
Cdd:COG0012     1 LKCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  81 GEGLGNQFLSHIREVDAIAHVIRNFHDDNVIHVEGKIDPQNDLSTIETELAMADLATVEKVLAKLKDKAKTNNKEAGKAM 160
Cdd:COG0012    81 GEGLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEKRLERLEKKAKSGDKEAKAEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 161 EIINPILDKLAQGEKPDISKLSPDEYKLIKNLNLLSLKPELFIENIDEKNIQTFKPI------------IPCsIPICAQL 228
Cdd:COG0012   161 ELLEKLKEHLEEGKPARSLELSEEEKKLLKELQLLTAKPVLYVANVDEDDLAEGNPYvekvreyaakegAEV-VVICAKI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 229 EAEIGELGDDEIKKYLQELNIEKSGLDRLISAGYELLNLITFFTAGPKESHAWPIIAGTKAPQAAGEIHTDFEKGFIRAE 308
Cdd:COG0012   240 EAELAELDEEERAEFLEELGLEESGLDRLIRAGYDLLGLITFFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFERGFIRAE 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1101056089 309 IINWQNIVDCQSDVKAKEKGLMRLEGKEYIMRDGDVALFHFN 350
Cdd:COG0012   320 VISYDDLIAYGSEAAAKEAGKLRLEGKDYVVQDGDVIHFRFN 361
 
Name Accession Description Interval E-value
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
 1-350 0e+00

Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 581.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   1 MKIGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERLEKLAKIYHSAKTIYSTIEFVDIAGLVKNAHK 80
Cdd:COG0012     1 LKCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  81 GEGLGNQFLSHIREVDAIAHVIRNFHDDNVIHVEGKIDPQNDLSTIETELAMADLATVEKVLAKLKDKAKTNNKEAGKAM 160
Cdd:COG0012    81 GEGLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEKRLERLEKKAKSGDKEAKAEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 161 EIINPILDKLAQGEKPDISKLSPDEYKLIKNLNLLSLKPELFIENIDEKNIQTFKPI------------IPCsIPICAQL 228
Cdd:COG0012   161 ELLEKLKEHLEEGKPARSLELSEEEKKLLKELQLLTAKPVLYVANVDEDDLAEGNPYvekvreyaakegAEV-VVICAKI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 229 EAEIGELGDDEIKKYLQELNIEKSGLDRLISAGYELLNLITFFTAGPKESHAWPIIAGTKAPQAAGEIHTDFEKGFIRAE 308
Cdd:COG0012   240 EAELAELDEEERAEFLEELGLEESGLDRLIRAGYDLLGLITFFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFERGFIRAE 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1101056089 309 IINWQNIVDCQSDVKAKEKGLMRLEGKEYIMRDGDVALFHFN 350
Cdd:COG0012   320 VISYDDLIAYGSEAAAKEAGKLRLEGKDYVVQDGDVIHFRFN 361
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 2-350 8.04e-152

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 432.45  E-value: 8.04e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   2 KIGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERLEKLAKIYHSAKTIYSTIEFVDIAGLVKNAHKG 81
Cdd:PTZ00258   23 KMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDERFDWLCKHFKPKSIVPAQLDITDIAGLVKGASEG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  82 EGLGNQFLSHIREVDAIAHVIRNFHDDNVIHVEGKIDPQNDLSTIETELAMADLATVEKVLAKLKDKAKTN--NKEAGKA 159
Cdd:PTZ00258  103 EGLGNAFLSHIRAVDGIYHVVRAFEDEDITHVEGEIDPVRDLEIISSELILKDLEFVEKRLDELTKKRKKKkkKKEEKVE 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 160 MEIINPILDKLAQGEKPDISKLSPDEYKLIKNLNLLSLKPELFIENIDEKNIQ----TFKPII---------PCSIPICA 226
Cdd:PTZ00258  183 LDVLKKVLEWLEEGKPVRDGDWTDKEIEILNEYQLLTAKPMIYLVNMSEKDFIrqknKWLAKIkewvgekggGPIIPYSA 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 227 QLEAEIGELGDDEIKK-YLQELNIEKSGLDRLISAGYELLNLITFFTAGPKESHAWPIIAGTKAPQAAGEIHTDFEKGFI 305
Cdd:PTZ00258  263 EFEEELAELGSEEERKeYLEEYGIKQSMLDKIIKTGYKLLNLIHFFTAGPDEVRCWTIQKGTKAPQAAGVIHSDFEKGFI 342

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1101056089 306 RAEIINWQNIVDCQSDVKAKEKGLMRLEGKEYIMRDGDVALFHFN 350
Cdd:PTZ00258  343 CAEVMKYEDFLELGSEAAVKAEGKYRQEGKDYVVQDGDIIFFKFN 387
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
 3-265 6.88e-138

YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of GTPases: Obg, DRG, Ygr210, and NOG1. Obg is an essential gene that is involved in DNA replication in C. crescentus and Streptomyces griseus and is associated with the ribosome. Several members of the family, including YchF, possess the TGS domain related to the RNA-binding proteins. Experimental data and genomic analysis suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translational factor.


Pssm-ID: 206687 [Multi-domain]  Cd Length: 274  Bit Score: 392.59  E-value: 6.88e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   3 IGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERLEKLAKIYHSAKTIYSTIEFVDIAGLVKNAHKGE 82
Cdd:cd01900     1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASKGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  83 GLGNQFLSHIREVDAIAHVIRNFHDDNVIHVEGKIDPQNDLSTIETELAMADLATVEKVLAKLKDKAKTNNKEAGKAMEI 162
Cdd:cd01900    81 GLGNKFLSHIREVDAIAHVVRCFEDDDITHVEGSVDPVRDIEIINTELILADLETIEKRLERLEKKAKSGDKEAKEELEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 163 INPILDKLAQGEKPDISKLSPDEYKLIKNLNLLSLKPELFIENIDEKNIQTF------------KPIIPCsIPICAQLEA 230
Cdd:cd01900   161 LEKIKEHLEEGKPARTLELTDEEIKILKSLQLLTAKPVIYVANVSEDDLIRGnnkvlkvreiaaKEGAEV-IPISAKLEA 239

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1101056089 231 EIGELGDDEIKKYLQELNIEKSGLDRLISAGYELL 265
Cdd:cd01900   240 ELAELDEEEAAEFLEELGLEESGLDKLIRAGYELL 274
TIGR00092 TIGR00092
GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in ...
 4-351 1.42e-109

GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in every complete bacterial genome, and is found in Eukaryotes. A more distantly related protein, separated from this model, is found in the archaea. It is known to bind GTP and double-stranded nucleic acid. It is suggested to belong to a nucleoprotein complex and act as a translation factor. [Unknown function, General]


Pssm-ID: 129200 [Multi-domain]  Cd Length: 368  Bit Score: 324.42  E-value: 1.42e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   4 GIVGLPNIGKSTLFNALTKKQV-EASNYPFCTIDPNIGVVKVPDERLEKLAKIYHSAKTIYSTIEFVDIAGLVKNAHKGE 82
Cdd:TIGR00092   6 GIVGLPNVGKSTLFAATTNLLGnEAANPPFTTIEPNAGVVNPSDPRLDLLAIYIKPEKVPPTTTEFVDIAGLVGGASKGE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  83 GLGNQFLSHIREVDAIAHVIRNFHDDNVIHVEGKIDPQNDLSTIETELAMADLATVEKVLAKLKDKAKTNNKEagKAMEI 162
Cdd:TIGR00092  86 GLGNQFLANIREVDIIQHVVRCFEDDIIHHVGNVDDPRDDFEIIDEELLKADEFLVEKRIGRSKKSAEGGKDK--KEELL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 163 INPILDKLAQGEKPDISK-LSPDEYKLIKNLNLLSLKPELFIENIDE--------------KNIQTFKPIIPCSIPICAQ 227
Cdd:TIGR00092 164 LLEIILPLLNGGQMARHVdLSKEELILIKSLNLLTKKPIILIANVSEdylrnlnnnyllivEWIAAYSKGDPKVVFVCAL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 228 LEAEIGELGDDEIKKYLQELNIEKS-GLDRLISAGYELLNLITFFTAGPKESHAWPIIAGTKAPQAAGEIHTDFEKGFIR 306
Cdd:TIGR00092 244 EESELSELDDEERQEFLQKLGLTESaGLNIIIRARYKLLLLSFFFTGGKEEVRAWTRKGGWAAPQAAGIIHTDFETGFIA 323

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1101056089 307 AEIINWQNIVDCQSDVKAKEKGLMRLEGKEYIMRDGDVALFHFNK 351
Cdd:TIGR00092 324 AEVISWDDFIYKKSSQGAKKGGLMRLEGKYYVVDDGDVLFFAFNV 368
YchF-GTPase_C pfam06071
Protein of unknown function (DUF933); This domain is found at the C terminus of the YchF ...
 267-347 2.16e-48

Protein of unknown function (DUF933); This domain is found at the C terminus of the YchF GTP-binding protein and is possibly related to the ubiquitin-like and MoaD/ThiS superfamilies.


Pssm-ID: 461819 [Multi-domain]  Cd Length: 82  Bit Score: 157.52  E-value: 2.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 267 LITFFTAGPKESHAWPIIAGTKAPQAAGEIHTDFEKGFIRAEIINWQNIVDCQSDVKAKEKGLMRLEGKEYIMRDGDVAL 346
Cdd:pfam06071   1 LITFFTAGPKEVRAWTIRKGTTAPQAAGVIHTDFEKGFIRAEVISYDDLIEYGSEAAAKEAGKLRLEGKDYVVQDGDIIH 80


                  .
gi 1101056089 347 F 347
Cdd:pfam06071  81 F 81
 
Name Accession Description Interval E-value
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
 1-350 0e+00

Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 581.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   1 MKIGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERLEKLAKIYHSAKTIYSTIEFVDIAGLVKNAHK 80
Cdd:COG0012     1 LKCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  81 GEGLGNQFLSHIREVDAIAHVIRNFHDDNVIHVEGKIDPQNDLSTIETELAMADLATVEKVLAKLKDKAKTNNKEAGKAM 160
Cdd:COG0012    81 GEGLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEKRLERLEKKAKSGDKEAKAEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 161 EIINPILDKLAQGEKPDISKLSPDEYKLIKNLNLLSLKPELFIENIDEKNIQTFKPI------------IPCsIPICAQL 228
Cdd:COG0012   161 ELLEKLKEHLEEGKPARSLELSEEEKKLLKELQLLTAKPVLYVANVDEDDLAEGNPYvekvreyaakegAEV-VVICAKI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 229 EAEIGELGDDEIKKYLQELNIEKSGLDRLISAGYELLNLITFFTAGPKESHAWPIIAGTKAPQAAGEIHTDFEKGFIRAE 308
Cdd:COG0012   240 EAELAELDEEERAEFLEELGLEESGLDRLIRAGYDLLGLITFFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFERGFIRAE 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1101056089 309 IINWQNIVDCQSDVKAKEKGLMRLEGKEYIMRDGDVALFHFN 350
Cdd:COG0012   320 VISYDDLIAYGSEAAAKEAGKLRLEGKDYVVQDGDVIHFRFN 361
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 2-350 8.04e-152

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 432.45  E-value: 8.04e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   2 KIGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERLEKLAKIYHSAKTIYSTIEFVDIAGLVKNAHKG 81
Cdd:PTZ00258   23 KMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDERFDWLCKHFKPKSIVPAQLDITDIAGLVKGASEG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  82 EGLGNQFLSHIREVDAIAHVIRNFHDDNVIHVEGKIDPQNDLSTIETELAMADLATVEKVLAKLKDKAKTN--NKEAGKA 159
Cdd:PTZ00258  103 EGLGNAFLSHIRAVDGIYHVVRAFEDEDITHVEGEIDPVRDLEIISSELILKDLEFVEKRLDELTKKRKKKkkKKEEKVE 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 160 MEIINPILDKLAQGEKPDISKLSPDEYKLIKNLNLLSLKPELFIENIDEKNIQ----TFKPII---------PCSIPICA 226
Cdd:PTZ00258  183 LDVLKKVLEWLEEGKPVRDGDWTDKEIEILNEYQLLTAKPMIYLVNMSEKDFIrqknKWLAKIkewvgekggGPIIPYSA 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 227 QLEAEIGELGDDEIKK-YLQELNIEKSGLDRLISAGYELLNLITFFTAGPKESHAWPIIAGTKAPQAAGEIHTDFEKGFI 305
Cdd:PTZ00258  263 EFEEELAELGSEEERKeYLEEYGIKQSMLDKIIKTGYKLLNLIHFFTAGPDEVRCWTIQKGTKAPQAAGVIHSDFEKGFI 342

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1101056089 306 RAEIINWQNIVDCQSDVKAKEKGLMRLEGKEYIMRDGDVALFHFN 350
Cdd:PTZ00258  343 CAEVMKYEDFLELGSEAAVKAEGKYRQEGKDYVVQDGDIIFFKFN 387
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
 3-265 6.88e-138

YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of GTPases: Obg, DRG, Ygr210, and NOG1. Obg is an essential gene that is involved in DNA replication in C. crescentus and Streptomyces griseus and is associated with the ribosome. Several members of the family, including YchF, possess the TGS domain related to the RNA-binding proteins. Experimental data and genomic analysis suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translational factor.


Pssm-ID: 206687 [Multi-domain]  Cd Length: 274  Bit Score: 392.59  E-value: 6.88e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   3 IGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERLEKLAKIYHSAKTIYSTIEFVDIAGLVKNAHKGE 82
Cdd:cd01900     1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASKGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  83 GLGNQFLSHIREVDAIAHVIRNFHDDNVIHVEGKIDPQNDLSTIETELAMADLATVEKVLAKLKDKAKTNNKEAGKAMEI 162
Cdd:cd01900    81 GLGNKFLSHIREVDAIAHVVRCFEDDDITHVEGSVDPVRDIEIINTELILADLETIEKRLERLEKKAKSGDKEAKEELEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 163 INPILDKLAQGEKPDISKLSPDEYKLIKNLNLLSLKPELFIENIDEKNIQTF------------KPIIPCsIPICAQLEA 230
Cdd:cd01900   161 LEKIKEHLEEGKPARTLELTDEEIKILKSLQLLTAKPVIYVANVSEDDLIRGnnkvlkvreiaaKEGAEV-IPISAKLEA 239

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1101056089 231 EIGELGDDEIKKYLQELNIEKSGLDRLISAGYELL 265
Cdd:cd01900   240 ELAELDEEEAAEFLEELGLEESGLDKLIRAGYELL 274
TIGR00092 TIGR00092
GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in ...
 4-351 1.42e-109

GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in every complete bacterial genome, and is found in Eukaryotes. A more distantly related protein, separated from this model, is found in the archaea. It is known to bind GTP and double-stranded nucleic acid. It is suggested to belong to a nucleoprotein complex and act as a translation factor. [Unknown function, General]


Pssm-ID: 129200 [Multi-domain]  Cd Length: 368  Bit Score: 324.42  E-value: 1.42e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   4 GIVGLPNIGKSTLFNALTKKQV-EASNYPFCTIDPNIGVVKVPDERLEKLAKIYHSAKTIYSTIEFVDIAGLVKNAHKGE 82
Cdd:TIGR00092   6 GIVGLPNVGKSTLFAATTNLLGnEAANPPFTTIEPNAGVVNPSDPRLDLLAIYIKPEKVPPTTTEFVDIAGLVGGASKGE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  83 GLGNQFLSHIREVDAIAHVIRNFHDDNVIHVEGKIDPQNDLSTIETELAMADLATVEKVLAKLKDKAKTNNKEagKAMEI 162
Cdd:TIGR00092  86 GLGNQFLANIREVDIIQHVVRCFEDDIIHHVGNVDDPRDDFEIIDEELLKADEFLVEKRIGRSKKSAEGGKDK--KEELL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 163 INPILDKLAQGEKPDISK-LSPDEYKLIKNLNLLSLKPELFIENIDE--------------KNIQTFKPIIPCSIPICAQ 227
Cdd:TIGR00092 164 LLEIILPLLNGGQMARHVdLSKEELILIKSLNLLTKKPIILIANVSEdylrnlnnnyllivEWIAAYSKGDPKVVFVCAL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 228 LEAEIGELGDDEIKKYLQELNIEKS-GLDRLISAGYELLNLITFFTAGPKESHAWPIIAGTKAPQAAGEIHTDFEKGFIR 306
Cdd:TIGR00092 244 EESELSELDDEERQEFLQKLGLTESaGLNIIIRARYKLLLLSFFFTGGKEEVRAWTRKGGWAAPQAAGIIHTDFETGFIA 323

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1101056089 307 AEIINWQNIVDCQSDVKAKEKGLMRLEGKEYIMRDGDVALFHFNK 351
Cdd:TIGR00092 324 AEVISWDDFIYKKSSQGAKKGGLMRLEGKYYVVDDGDVLFFAFNV 368
YchF-GTPase_C pfam06071
Protein of unknown function (DUF933); This domain is found at the C terminus of the YchF ...
 267-347 2.16e-48

Protein of unknown function (DUF933); This domain is found at the C terminus of the YchF GTP-binding protein and is possibly related to the ubiquitin-like and MoaD/ThiS superfamilies.


Pssm-ID: 461819 [Multi-domain]  Cd Length: 82  Bit Score: 157.52  E-value: 2.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 267 LITFFTAGPKESHAWPIIAGTKAPQAAGEIHTDFEKGFIRAEIINWQNIVDCQSDVKAKEKGLMRLEGKEYIMRDGDVAL 346
Cdd:pfam06071   1 LITFFTAGPKEVRAWTIRKGTTAPQAAGVIHTDFEKGFIRAEVISYDDLIEYGSEAAAKEAGKLRLEGKDYVVQDGDIIH 80


                  .
gi 1101056089 347 F 347
Cdd:pfam06071  81 F 81
TGS_YchF_OLA1 cd04867
TGS (ThrRS, GTPase and SpoT) domain found in the YchF/OLA1 family proteins; The YchF/Ola1 ...
 265-349 2.64e-46

TGS (ThrRS, GTPase and SpoT) domain found in the YchF/OLA1 family proteins; The YchF/Ola1 family includes bacterial ribosome-binding ATPase YchF as well as its human homolog Obg-like ATPase 1 (OLA1), both of which belong to the Obg family of GTPases, and are novel ATPases that bind and hydrolyze ATP more efficiently than GTP. They have been associated with various cellular processes and pathologies, including DNA repair, tumorigenesis, and apoptosis, in addition to the regulation of the oxidative stress response. OLA1 is also termed DNA damage-regulated overexpressed in cancer 45 (DOC45), or GTP-binding protein 9 (GTPBP9). It is over-expressed in several human malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus. It is linked to the cellular stress response and tumorigenesis, and may also serve as a valuable tumor marker. Members in this family contain a central Obg-type G (guanine nucleotide-binding) domain, flanked by a coiled-coil domain and this TGS (ThrRS, GTPase, SpoT) domain of unknown function.


Pssm-ID: 340516 [Multi-domain]  Cd Length: 85  Bit Score: 152.30  E-value: 2.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 265 LNLITFFTAGPKESHAWPIIAGTKAPQAAGEIHTDFEKGFIRAEIINWQNIVDCQSDVKAKEKGLMRLEGKEYIMRDGDV 344
Cdd:cd04867     1 LNLITFFTAGPDEVRAWTIRKGTKAPQAAGVIHTDFEKGFIRAEVIKYDDLKELGSEAAAKEAGKYRQEGKDYVVQDGDI 80


                  ....*
gi 1101056089 345 ALFHF 349
Cdd:cd04867    81 IHFKF 85
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 1-344 1.06e-40

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 147.26  E-value: 1.06e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   1 MKIGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGV--VKVP------DERLEKLAKIYHSaKTIYSTIEFVDIA 72
Cdd:PRK09602    2 ITIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayVRVEcpckelGVKCNPRNGKCID-GTRFIPVELIDVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  73 GLVKNAHKGEGLGNQFLSHIREVDAIAHVIrnfhD-----DnvihVEGKI------DPQNDLSTIETELAMADLATVEKV 141
Cdd:PRK09602   81 GLVPGAHEGRGLGNQFLDDLRQADALIHVV----DasgstD----EEGNPvepgshDPVEDIKFLEEELDMWIYGILEKN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 142 LAKLKDKAKTNNKEAGKAM-----------EIINPILDKLaqGEKPDISKLSPDE-YKLIKNLNLLSlKPELFIEN-ID- 207
Cdd:PRK09602  153 WEKFSRKAQAEKFDIEEALaeqlsglgineEHVKEALREL--GLPEDPSKWTDEDlLELARELRKIS-KPMVIAANkADl 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 208 ---EKNIQ-----TFKPIIPCSIpicaqlEAE-----------------------IGELGD------DEIKKYLQELNIe 250
Cdd:PRK09602  230 ppaEENIErlkeeKYYIVVPTSA------EAElalrraakaglidyipgdsdfeiLGELSEkqkkalEYIREVLKKYGG- 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 251 kSGLDRLI-SAGYELLNLITFFtagPKES-------------HAWPIIAGTKAPQAAGEIHTDFEKGFIRAeiinwqniv 316
Cdd:PRK09602  303 -TGVQEAInTAVFDLLDMIVVY---PVEDenkltdkkgnvlpDAFLLPKGSTARDLAYKIHTDIGEGFLYA--------- 369

                         410       420
                  ....*....|....*....|....*...
gi 1101056089 317 dcqsdVKAKEKglMRLeGKEYIMRDGDV 344
Cdd:PRK09602  370 -----IDARTK--RRI-GEDYELKDGDV 389
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 4-176 1.31e-33

Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified.


Pssm-ID: 206668 [Multi-domain]  Cd Length: 167  Bit Score: 122.12  E-value: 1.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   4 GIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDerleklakiyhsaktiYSTIEFVDIAGLVKNAHKGEG 83
Cdd:cd01881     1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGD----------------GVDIQIIDLPGLLDGASEGRG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  84 LGNQFLSHIREVDAIAHVIRNFHDDnvihvegKIDPQNDLSTIETELAMADLATVEK---VLAKLKDKAKTNNkeagkam 160
Cdd:cd01881    65 LGEQILAHLYRSDLILHVIDASEDC-------VGDPLEDQKTLNEEVSGSFLFLKNKpemIVANKIDMASENN------- 130

                         170
                  ....*....|....*.
gi 1101056089 161 eIINPILDKLAQGEKP 176
Cdd:cd01881   131 -LKRLKLDKLKRGIPV 145
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 3-132 1.58e-31

Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They are characterized by a distinct glycine-rich motif immediately following the Walker B motif. The Ygr210 and YyaF/YchF subfamilies appear to form one major branch of the Obg-like family. Among eukaryotes, the Ygr210 subfamily is represented only in fungi. These fungal proteins form a tight cluster with their archaeal orthologs, which suggests the possibility of horizontal transfer from archaea to fungi.


Pssm-ID: 206686 [Multi-domain]  Cd Length: 318  Bit Score: 120.80  E-value: 1.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   3 IGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGV----VKVPDERLEKLAKIYHS---AKTIYSTIEFVDIAGLV 75
Cdd:cd01899     1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVgyvrVECPCKELGVSCNPRYGkciDGKRYVPVELIDVAGLV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  76 KNAHKGEGLGNQFLSHIREVDAIAHVIR---NFHDDNVIHVEGKIDPQNDLSTIETELAM 132
Cdd:cd01899    81 PGAHEGKGLGNQFLDDLRDADVLIHVVDasgGTDAEGNGVETGGYDPLEDIEFLENEIDM 140
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 2-107 2.84e-26

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: 100.77  E-value: 2.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   2 KIGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERleklakiyhsaktiystIEFVDIAGLVKNAHKG 81
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQ-----------------IILVDTPGLIEGASEG 63

                          90       100
                  ....*....|....*....|....*.
gi 1101056089  82 EGLGNQFLSHIrEVDAIAHVIRNFHD 107
Cdd:pfam01926  64 EGLGRAFLAII-EADLILFVVDSEEG 88
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 3-140 9.32e-26

Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome GTP-binding protein that associates with ribosomal subunits and appears to play a role in ribosomal RNA maturation. This GTPase, related to the nucleolar protein Obg, is designated CgtA in bacteria. Mutations in this gene are pleiotropic, but it appears that effects on cellular functions such as chromosome partition may be secondary to the effect on ribosome structure. Recent work done in Vibrio cholerae shows an essential role in the stringent response, in which RelA-dependent ability to synthesize the alarmone ppGpp is required for deletion of this GTPase to be lethal. [Protein synthesis, Other]


Pssm-ID: 274271 [Multi-domain]  Cd Length: 328  Bit Score: 105.20  E-value: 9.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   3 IGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERleklakiyhsaktiystiEFV--DIAGLVKNAHK 80
Cdd:TIGR02729 160 VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGR------------------SFViaDIPGLIEGASE 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  81 GEGLGNQFLSHIREVDAIAHVIrnfhddNVIHVEGKiDPQNDLSTIETELAMADLATVEK 140
Cdd:TIGR02729 222 GAGLGHRFLKHIERTRVLLHLI------DISPEDGS-DPVEDYEIIRNELKKYSPELAEK 274
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 3-130 7.19e-25

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


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 99.04  E-value: 7.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   3 IGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERleklakiyhsaktiysTIEFVDIAGLVKNAHKGE 82
Cdd:cd01898     3 VGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGR----------------SFVIADIPGLIEGASEGK 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1101056089  83 GLGNQFLSHIREVDAIAHVIrnfhDdnvihVEGKIDPQNDLSTIETEL 130
Cdd:cd01898    67 GLGHRFLRHIERTRVLLHVI----D-----LSGEDDPVEDYETIRNEL 105
obgE PRK12297
GTPase CgtA; Reviewed
 3-150 7.56e-25

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 104.03  E-value: 7.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   3 IGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERleklakiyhsaktiystiEFV--DIAGLVKNAHK 80
Cdd:PRK12297  161 VGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGR------------------SFVmaDIPGLIEGASE 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  81 GEGLGNQFLSHIREVDAIAHVIrnfhddNVIHVEGKiDPQNDLSTIETELAM----------------ADLATVEKVLAK 144
Cdd:PRK12297  223 GVGLGHQFLRHIERTRVIVHVI------DMSGSEGR-DPIEDYEKINKELKLynprllerpqivvankMDLPEAEENLEE 295


                  ....*.
gi 1101056089 145 LKDKAK 150
Cdd:PRK12297  296 FKEKLG 301
obgE PRK12299
GTPase CgtA; Reviewed
 3-172 2.73e-23

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 98.60  E-value: 2.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   3 IGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERleklakiyhsaktiystiEFV--DIAGLVKNAHK 80
Cdd:PRK12299  161 VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYK------------------SFViaDIPGLIEGASE 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089  81 GEGLGNQFLSHIREVDAIAHVIRNFHDdnvihvegkiDPQNDLSTIETELAM----------------ADLATVEKVLAK 144
Cdd:PRK12299  223 GAGLGHRFLKHIERTRLLLHLVDIEAV----------DPVEDYKTIRNELEKyspeladkprilvlnkIDLLDEEEEREK 292

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1101056089 145 LKDKAKtnNKEAGKAMEI-------INPILDKLAQ 172
Cdd:PRK12299  293 RAALEL--AALGGPVFLIsavtgegLDELLRALWE 325
obgE PRK12296
GTPase CgtA; Reviewed
 3-131 1.08e-16

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 81.07  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   3 IGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERLeklakiyhsaktiysTIefVDIAGLVKNAHKGE 82
Cdd:PRK12296  162 VGLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQAGDTRF---------------TV--ADVPGLIPGASEGK 224

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1101056089  83 GLGNQFLSHIREVDAIAHVIrnfhdDNVIHVEGKiDPQNDLSTIETELA 131
Cdd:PRK12296  225 GLGLDFLRHIERCAVLVHVV-----DCATLEPGR-DPLSDIDALEAELA 267
obgE PRK12298
GTPase CgtA; Reviewed
 3-102 2.18e-16

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 79.53  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   3 IGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERleklakiyhsaktiystiEFV--DIAGLVKNAHK 80
Cdd:PRK12298  162 VGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDER------------------SFVvaDIPGLIEGASE 223

                          90       100
                  ....*....|....*....|..
gi 1101056089  81 GEGLGNQFLSHIREVDAIAHVI 102
Cdd:PRK12298  224 GAGLGIRFLKHLERCRVLLHLI 245
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
6-110 7.28e-15

Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 74.83  E-value: 7.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   6 VGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKvpderleklakiYHSAKtiystIEFVDIAGLVKNAHKGEGLG 85
Cdd:COG1163    69 VGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLE------------YKGAK-----IQILDVPGLIEGAASGKGRG 131

                          90       100
                  ....*....|....*....|....*
gi 1101056089  86 NQFLSHIREVDAIAHVIRNFHDDNV 110
Cdd:COG1163   132 KEVLSVVRNADLILIVLDVFELEQY 156
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 3-102 1.92e-14

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


Pssm-ID: 206683 [Multi-domain]  Cd Length: 233  Bit Score: 71.81  E-value: 1.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   3 IGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKvpderleklakiYHSAKtiystIEFVDIAGLVKNAHKGE 82
Cdd:cd01896     3 VALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVME------------YKGAK-----IQLLDLPGIIEGASDGK 65

                          90       100
                  ....*....|....*....|
gi 1101056089  83 GLGNQFLSHIREVDAIAHVI 102
Cdd:cd01896    66 GRGRQVIAVARTADLILIVL 85
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 4-102 1.26e-12

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: 64.96  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   4 GIVGLPNIGKSTLFNALTKKQV-EASNYPFCTIDPNIGVVKVPDERleklakiyhsaktiysTIEFVDIAGLVKNAHKGE 82
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVgIVSPIPGTTRDPVRKEWELLPLG----------------PVVLIDTPGLDEEGGLGR 64

                          90       100
                  ....*....|....*....|
gi 1101056089  83 GLGNQFLSHIREVDAIAHVI 102
Cdd:cd00880    65 ERVEEARQVADRADLVLLVV 84
TGS cd01616
TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; ...
 269-347 1.41e-08

TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; This family includes eukaryotic and some bacterial threonyl-tRNA synthetases (ThrRSs), a distinct Obg family GTPases, and guanosine polyphosphate hydrolase (SpoT) and synthetase (RelA), which are involved in stringent response in bacteria, as well as uridine kinase (UDK) from Thermotogales. All family members contain a TGS domain named after the ThrRS, GTPase, and SpoT/RelA proteins where it occurs. It is a small domain with a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. The functions of the TGS domain remains unclear, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, with a regulatory role.


Pssm-ID: 340455 [Multi-domain]  Cd Length: 61  Bit Score: 50.68  E-value: 1.41e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1101056089 269 TFFTAGPKESHAWPIIAGTKAPQAAGEIHTDFEKGFIRAEIINwqnivdcqsdvkakekglmRLEGKEYIMRDGDVALF 347
Cdd:cd01616     1 EVFTVGKTPGTVFVMNKGATAYSCAMHLHEDYCRKSILALVDG-------------------QLWDMYYPLTKGDEIKF 60
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 1-102 2.31e-07

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: 50.12  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   1 MKIGIVGLPNIGKSTLFNALTKKQ-VEASNYPFCTIDPnigvVKVPDERLEKlakiyhsaktiysTIEFVDIAGLVKNAH 79
Cdd:cd01895     3 IKIAIIGRPNVGKSSLLNALLGEErVIVSDIAGTTRDS----IDVPFEYDGQ-------------KYTLIDTAGIRKKGK 65

                          90       100
                  ....*....|....*....|....*
gi 1101056089  80 KGEGLgnQFLSHIREVDAI--AHVI 102
Cdd:cd01895    66 VTEGI--EKYSVLRTLKAIerADVV 88
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-50 3.04e-07

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 52.04  E-value: 3.04e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1101056089   1 MKIGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERLE 50
Cdd:COG0370     4 ITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIE 53
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 5-50 3.97e-07

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: 48.99  E-value: 3.97e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1101056089   5 IVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERLE 50
Cdd:cd01879     2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIE 47
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 4-102 4.96e-07

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: 48.99  E-value: 4.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   4 GIVGLPNIGKSTLFNALTKKQV-EASNYPFCTIDPNIGVVKVPDERLeklakiyhsaktiysTIEFVDIAGLVKNAhkGE 82
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVgEVSDVPGTTRDPDVYVKELDKGKV---------------KLVLVDTPGLDEFG--GL 63

                          90       100
                  ....*....|....*....|
gi 1101056089  83 GLGNQFLSHIREVDAIAHVI 102
Cdd:cd00882    64 GREELARLLLRGADLILLVV 83
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 2-50 5.77e-07

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


Pssm-ID: 460552 [Multi-domain]  Cd Length: 156  Bit Score: 48.60  E-value: 5.77e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1101056089   2 KIGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERLE 50
Cdd:pfam02421   2 TIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKGYEIE 50
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 3-48 9.01e-07

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 50.09  E-value: 9.01e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1101056089   3 IGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDER 48
Cdd:COG2262   202 VALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRRLELPDGR 247
TGS_Obg cd04938
TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases ...
 266-347 2.22e-06

TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases function has been implicated in cellular processes as diverse as sporulation, stress response, control of DNA replication, and ribosome assembly. It consists of several subfamilies such as DRG and YchF with TGS domain. The TGS domain is named after the various RNA-binding multidomain ThrRS, GTPase, and SpoT/RelA proteins in which this domain occurs. The TGS domain of Obg-like GTPases such as those present in DRG (developmentally regulated GTP-binding protein), and GTP-binding proteins Ygr210 and YchF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340517 [Multi-domain]  Cd Length: 77  Bit Score: 45.13  E-value: 2.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089 266 NLITFFTA-----------GPKESHAWPIIAGTKAPQAAGEIHTDFEKGFIRAEIInwqnivdcqsdvkakekGLMRLEG 334
Cdd:cd04938     1 GLIPVYPVkniqtftngsgNSVFRDCVLVKKGTTVKDFANKIHTDLEKGFINAEGI-----------------GGRRLEG 63

                          90
                  ....*....|...
gi 1101056089 335 KEYIMRDGDVALF 347
Cdd:cd04938    64 EDYILQDNDVVKF 76
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 3-37 2.23e-06

HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 47.84  E-value: 2.23e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1101056089   3 IGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDP 37
Cdd:cd01878    44 VALVGYTNAGKSTLFNALTGADVLAEDQLFATLDP 78
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
 7-50 1.19e-05

ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane protein required for iron(II) update, is encoded in an operon with FeoA (75 amino acids), which is also required, and is regulated by Fur. There appear to be two copies in Archaeoglobus fulgidus and Clostridium acetobutylicum. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273077 [Multi-domain]  Cd Length: 591  Bit Score: 47.04  E-value: 1.19e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1101056089   7 GLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDERLE 50
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIE 44
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 1-103 1.27e-05

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 44.67  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   1 MKIGIVGLPNIGKSTLFNALTK-KQVEASNYPFCTIDPNIGVVKVpderleklakiyhsaKTIYSTIEFVDIAGLVKNAH 79
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGnKGSITEYYPGTTRNYVTTVIEE---------------DGKTYKFNLLDTAGQEDYDA 66

                          90       100
                  ....*....|....*....|....
gi 1101056089  80 KGEGLGNQFLSHIREVDAIAHVIR 103
Cdd:TIGR00231  67 IRRLYYPQVERSLRVFDIVILVLD 90
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 5-40 2.72e-05

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: 44.09  E-value: 2.72e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1101056089   5 IVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIG 40
Cdd:cd01897     5 IAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVG 40
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 5-44 3.05e-05

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: 43.58  E-value: 3.05e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1101056089   5 IVGLPNIGKSTLFNALTKKQvEA--SNYPFCTIDPNIGVVKV 44
Cdd:cd01894     2 IVGRPNVGKSTLFNRLTGRR-DAivSDTPGVTRDRKYGEAEW 42
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
1-102 3.65e-05

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 45.40  E-value: 3.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   1 MKIGIVGLPNIGKSTLFNALTKKQ-VEASNYPFCTIDPnigvVKVPDERLEKlakiyhsaktiysTIEFVDIAGLVKNAH 79
Cdd:COG1160   176 IKIAIVGRPNVGKSSLINALLGEErVIVSDIAGTTRDS----IDTPFERDGK-------------KYTLIDTAGIRRKGK 238

                          90       100
                  ....*....|....*....|....*
gi 1101056089  80 KGEGLgnQFLSHIREVDAI--AHVI 102
Cdd:COG1160   239 VDEGI--EKYSVLRTLRAIerADVV 261
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
2-23 4.97e-05

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 45.01  E-value: 4.97e-05
                          10        20
                  ....*....|....*....|..
gi 1101056089   2 KIGIVGLPNIGKSTLFNALTKK 23
Cdd:COG1160     4 VVAIVGRPNVGKSTLFNRLTGR 25
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 2-24 6.02e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 44.66  E-value: 6.02e-05
                          10        20
                  ....*....|....*....|...
gi 1101056089   2 KIGIVGLPNIGKSTLFNALTKKQ 24
Cdd:PRK00093    3 VVAIVGRPNVGKSTLFNRLTGKR 25
PRK11058 PRK11058
GTPase HflX; Provisional
 3-46 1.15e-04

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 43.55  E-value: 1.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1101056089   3 IGIVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPD 46
Cdd:PRK11058  200 VSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVAD 243
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 2-102 1.25e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 43.50  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   2 KIGIVGLPNIGKSTLFNALTKKQ-VEASNYPFCTIDPnigvVKVPDERLEKlakiyhsaktiysTIEFVDIAGLVKNAHK 80
Cdd:PRK00093  175 KIAIIGRPNVGKSSLINALLGEErVIVSDIAGTTRDS----IDTPFERDGQ-------------KYTLIDTAGIRRKGKV 237

                          90       100
                  ....*....|....*....|....
gi 1101056089  81 GEGLgnQFLSHIREVDAI--AHVI 102
Cdd:PRK00093  238 TEGV--EKYSVIRTLKAIerADVV 259
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
5-48 1.78e-04

GTP-binding protein, GTP1/Obg family [General function prediction only];


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 42.90  E-value: 1.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1101056089   5 IVGLPNIGKSTLFNALTKKQVEASNYPFCTIDPNIGVVKVPDER 48
Cdd:COG1084   165 VAGYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGR 208
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
 1-44 2.04e-04

A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; Autoantigen NGP-1 (Nucleolar G-protein gene 1) has been shown to localize in the nucleolus and nucleolar organizers in all cell types analyzed, which is indicative of a function in ribosomal assembly. NGP-1 and its homologs show a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with NKXD motif) are relocated to the N terminus.


Pssm-ID: 206751 [Multi-domain]  Cd Length: 157  Bit Score: 41.13  E-value: 2.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1101056089   1 MKIGIVGLPNIGKSTLFNALTKKQVeasnypfCTIDPNIGVVKV 44
Cdd:cd01858   103 ISVGFIGYPNVGKSSVINTLRSKKV-------CKVAPIPGETKV 139
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 2-25 4.56e-04

Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 40.59  E-value: 4.56e-04
                          10        20
                  ....*....|....*....|....
gi 1101056089   2 KIGIVGLPNIGKSTLFNALTKKQV 25
Cdd:cd01856   117 RAMVVGIPNVGKSTLINRLRGKKV 140
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 1-25 8.18e-04

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: 39.40  E-value: 8.18e-04
                          10        20
                  ....*....|....*....|....*
gi 1101056089   1 MKIGIVGLPNIGKSTLFNALTKKQV 25
Cdd:cd04164     4 IKVVIAGKPNVGKSSLLNALAGRDR 28
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 1-23 1.41e-03

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 40.43  E-value: 1.41e-03
                          10        20
                  ....*....|....*....|...
gi 1101056089   1 MKIGIVGLPNIGKSTLFNALTKK 23
Cdd:COG0486   214 IKVVIVGRPNVGKSSLLNALLGE 236
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
1-23 1.50e-03

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 40.09  E-value: 1.50e-03
                          10        20
                  ....*....|....*....|...
gi 1101056089   1 MKIGIVGLPNIGKSTLFNALTKK 23
Cdd:PRK05291  216 LKVVIAGRPNVGKSSLLNALLGE 238
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 2-98 1.51e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 40.55  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   2 KIGIVGLPNIGKSTLFNALTKKQVE-ASNYPFCTIDPNIGVVKVPDErleklakiyhsaktiysTIEFVDIAGLVKNAHK 80
Cdd:PRK09518  452 RVALVGRPNVGKSSLLNQLTHEERAvVNDLAGTTRDPVDEIVEIDGE-----------------DWLFIDTAGIKRRQHK 514

                          90
                  ....*....|....*...
gi 1101056089  81 GEglGNQFLSHIREVDAI 98
Cdd:PRK09518  515 LT--GAEYYSSLRTQAAI 530
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 2-102 1.89e-03

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: 38.60  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   2 KIGIVGLPNIGKSTLFNALtkkqveasnypfctidpnIGvvkvpderlEKLAKIYHSAKT-------IYST----IEFVD 70
Cdd:cd04163     5 FVAIIGRPNVGKSTLLNAL------------------VG---------QKISIVSPKPQTtrnrirgIYTDddaqIIFVD 57

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1101056089  71 IAGLVKNAHK-GEGLGNQFLSHIREVDAIAHVI 102
Cdd:cd04163    58 TPGIHKPKKKlGERMVKAAWSALKDVDLVLFVV 90
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 3-31 2.81e-03

A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC class I region and is highly homologous to a putative GTP-binding protein, MMR1 from mouse. These proteins represent a new subfamily of GTP-binding proteins that has only eukaryote members. This subfamily shows a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with sequence NKXD) are relocated to the N-terminus.


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 37.60  E-value: 2.81e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1101056089   3 IGIVGLPNIGKSTLFNAL-TKKQVEASNYP 31
Cdd:cd01857    85 IGLVGYPNVGKSSLINALvGSKKVSVSSTP 114
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
5-31 3.35e-03

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 38.55  E-value: 3.35e-03
                          10        20
                  ....*....|....*....|....*...
gi 1101056089   5 IVGLPNIGKSTLFNALTKKQV-EASNYP 31
Cdd:COG1161   118 IVGIPNVGKSTLINRLAGKKVaKTGNKP 145
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 1-25 3.74e-03

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: 38.62  E-value: 3.74e-03
                          10        20
                  ....*....|....*....|....*
gi 1101056089   1 MKIGIVGLPNIGKSTLFNALTKKQV 25
Cdd:pfam12631  95 IKVVIVGKPNVGKSSLLNALLGEER 119
era PRK00089
GTPase Era; Reviewed
 3-102 7.35e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 37.72  E-value: 7.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101056089   3 IGIVGLPNIGKSTLFNALtkkqveasnypfctidpnIGvvkvpderlEKLAKIYHSAKT-------IYST----IEFVDI 71
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNAL------------------VG---------QKISIVSPKPQTtrhrirgIVTEddaqIIFVDT 60

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1101056089  72 AGLvknaHKGEGLGNQFL-----SHIREVDAIAHVI 102
Cdd:PRK00089   61 PGI----HKPKRALNRAMnkaawSSLKDVDLVLFVV 92
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 2-25 8.20e-03

An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 36.53  E-value: 8.20e-03
                          10        20
                  ....*....|....*....|....
gi 1101056089   2 KIGIVGLPNIGKSTLFNALTKKQV 25
Cdd:cd01859   101 IVGVVGYPKVGKSSIINALKGRHS 124
 
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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