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Conserved domains on  [gi|16765125|ref|NP_460740|]
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putative GTP-binding protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

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] ...
 3-363 0e+00

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


:

Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 763.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   3 FKCGIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRLDQLAEIVKPQRILPTTMEFVDIAGLVKGASK 82
Cdd:COG0012   1 LKCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  83 GEGLGNQFLTNIRETEAIGHVVRCFENDNIIHVAGKVNPAEDIDVINTELALADLDTCERAIHRVQKKAKGGDKDAKAEL 162
Cdd:COG0012  81 GEGLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEKRLERLEKKAKSGDKEAKAEL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 163 AALEKCLPHLAEAGMLRSLDLTDEDKAAIRYLSFLTLKPTMYIANVNEDGF-ENNPYLDQVREIAAKEGSVVVPVCAAVE 241
Cdd:COG0012 161 ELLEKLKEHLEEGKPARSLELSEEEKKLLKELQLLTAKPVLYVANVDEDDLaEGNPYVEKVREYAAKEGAEVVVICAKIE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 242 ADIAELDDDERDEFMAELGLEEPGLNRVIRAGYRLLNLQTYFTAGVKEVRAWTIPVGATAPQAAGKIHTDFEKGFIRAQT 321
Cdd:COG0012 241 AELAELDEEERAEFLEELGLEESGLDRLIRAGYDLLGLITFFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFERGFIRAEV 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 16765125 322 IAFDDFITYKGEQGAKEAGKMRAEGKDYIVKDGDIMNFLFNV 363
Cdd:COG0012 321 ISYDDLIAYGSEAAAKEAGKLRLEGKDYVVQDGDVIHFRFNV 362
 
Name Accession Description Interval E-value
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
 3-363 0e+00

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 763.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   3 FKCGIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRLDQLAEIVKPQRILPTTMEFVDIAGLVKGASK 82
Cdd:COG0012   1 LKCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  83 GEGLGNQFLTNIRETEAIGHVVRCFENDNIIHVAGKVNPAEDIDVINTELALADLDTCERAIHRVQKKAKGGDKDAKAEL 162
Cdd:COG0012  81 GEGLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEKRLERLEKKAKSGDKEAKAEL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 163 AALEKCLPHLAEAGMLRSLDLTDEDKAAIRYLSFLTLKPTMYIANVNEDGF-ENNPYLDQVREIAAKEGSVVVPVCAAVE 241
Cdd:COG0012 161 ELLEKLKEHLEEGKPARSLELSEEEKKLLKELQLLTAKPVLYVANVDEDDLaEGNPYVEKVREYAAKEGAEVVVICAKIE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 242 ADIAELDDDERDEFMAELGLEEPGLNRVIRAGYRLLNLQTYFTAGVKEVRAWTIPVGATAPQAAGKIHTDFEKGFIRAQT 321
Cdd:COG0012 241 AELAELDEEERAEFLEELGLEESGLDRLIRAGYDLLGLITFFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFERGFIRAEV 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 16765125 322 IAFDDFITYKGEQGAKEAGKMRAEGKDYIVKDGDIMNFLFNV 363
Cdd:COG0012 321 ISYDDLIAYGSEAAAKEAGKLRLEGKDYVVQDGDVIHFRFNV 362
TIGR00092 TIGR00092
GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in ...
 1-363 0e+00

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: 516.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125     1 MGFKCGIVGLPNVGKSTLFNALTKAGI-EAANFPFCTIEPNTGVVPMPDPRLDQLAEIVKPQRILPTTMEFVDIAGLVKG 79
Cdd:TIGR00092   1 MGLSGGIVGLPNVGKSTLFAATTNLLGnEAANPPFTTIEPNAGVVNPSDPRLDLLAIYIKPEKVPPTTTEFVDIAGLVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125    80 ASKGEGLGNQFLTNIRETEAIGHVVRCFENDNIIHVAGKVNPAEDIDVINTELALADLDTCERAIHRVQKKAKGGdKDAK 159
Cdd:TIGR00092  81 ASKGEGLGNQFLANIREVDIIQHVVRCFEDDIIHHVGNVDDPRDDFEIIDEELLKADEFLVEKRIGRSKKSAEGG-KDKK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   160 AELAALEKCLPHLAEAGMLRSLDLTDEDKAAIRYLSFLTLKPTMYIANVNEDGFEN--NPYLDQVREIAA--KEGSVVVP 235
Cdd:TIGR00092 160 EELLLLEIILPLLNGGQMARHVDLSKEELILIKSLNLLTKKPIILIANVSEDYLRNlnNNYLLIVEWIAAysKGDPKVVF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   236 VCAAVEADIAELDDDERDEFMAELGLEEP-GLNRVIRAGYRLLNLQTYFTAGVKEVRAWTIPVGATAPQAAGKIHTDFEK 314
Cdd:TIGR00092 240 VCALEESELSELDDEERQEFLQKLGLTESaGLNIIIRARYKLLLLSFFFTGGKEEVRAWTRKGGWAAPQAAGIIHTDFET 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 16765125   315 GFIRAQTIAFDDFITYKGEQGAKEAGKMRAEGKDYIVKDGDIMNFLFNV 363
Cdd:TIGR00092 320 GFIAAEVISWDDFIYKKSSQGAKKGGLMRLEGKYYVVDDGDVLFFAFNV 368
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 4-363 3.16e-179

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 502.55  E-value: 3.16e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125    4 KCGIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRLDQLAEIVKPQRILPTTMEFVDIAGLVKGASKG 83
Cdd:PTZ00258  23 KMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDERFDWLCKHFKPKSIVPAQLDITDIAGLVKGASEG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   84 EGLGNQFLTNIRETEAIGHVVRCFENDNIIHVAGKVNPAEDIDVINTELALADLDTCERAIHRVQKKAKGG--DKDAKAE 161
Cdd:PTZ00258 103 EGLGNAFLSHIRAVDGIYHVVRAFEDEDITHVEGEIDPVRDLEIISSELILKDLEFVEKRLDELTKKRKKKkkKKEEKVE 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  162 LAALEKCLPHLAEAGMLRSLDLTDEDKAAIRYLSFLTLKPTMYIANVNEDGF--ENNPYLDQVRE-IAAKEGSVVVPVCA 238
Cdd:PTZ00258 183 LDVLKKVLEWLEEGKPVRDGDWTDKEIEILNEYQLLTAKPMIYLVNMSEKDFirQKNKWLAKIKEwVGEKGGGPIIPYSA 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  239 AVEADIAEL-DDDERDEFMAELGLEEPGLNRVIRAGYRLLNLQTYFTAGVKEVRAWTIPVGATAPQAAGKIHTDFEKGFI 317
Cdd:PTZ00258 263 EFEEELAELgSEEERKEYLEEYGIKQSMLDKIIKTGYKLLNLIHFFTAGPDEVRCWTIQKGTKAPQAAGVIHSDFEKGFI 342

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 16765125  318 RAQTIAFDDFITYKGEQGAKEAGKMRAEGKDYIVKDGDIMNFLFNV 363
Cdd:PTZ00258 343 CAEVMKYEDFLELGSEAAVKAEGKYRQEGKDYVVQDGDIIFFKFNV 388
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
 5-277 7.54e-179

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: 496.98  E-value: 7.54e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   5 CGIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRLDQLAEIVKPQRILPTTMEFVDIAGLVKGASKGE 84
Cdd:cd01900   1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASKGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  85 GLGNQFLTNIRETEAIGHVVRCFENDNIIHVAGKVNPAEDIDVINTELALADLDTCERAIHRVQKKAKGGDKDAKAELAA 164
Cdd:cd01900  81 GLGNKFLSHIREVDAIAHVVRCFEDDDITHVEGSVDPVRDIEIINTELILADLETIEKRLERLEKKAKSGDKEAKEELEL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 165 LEKCLPHLAEAGMLRSLDLTDEDKAAIRYLSFLTLKPTMYIANVNEDGFENNPYLD-QVREIAAKEGSVVVPVCAAVEAD 243
Cdd:cd01900 161 LEKIKEHLEEGKPARTLELTDEEIKILKSLQLLTAKPVIYVANVSEDDLIRGNNKVlKVREIAAKEGAEVIPISAKLEAE 240

                       250       260       270
                ....*....|....*....|....*....|....
gi 16765125 244 IAELDDDERDEFMAELGLEEPGLNRVIRAGYRLL 277
Cdd:cd01900 241 LAELDEEEAAEFLEELGLEESGLDKLIRAGYELL 274
YchF-GTPase_C pfam06071
Protein of unknown function (DUF933); This domain is found at the C terminus of the YchF ...
 279-360 3.81e-58

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: 182.94  E-value: 3.81e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   279 LQTYFTAGVKEVRAWTIPVGATAPQAAGKIHTDFEKGFIRAQTIAFDDFITYKGEQGAKEAGKMRAEGKDYIVKDGDIMN 358
Cdd:pfam06071   1 LITFFTAGPKEVRAWTIRKGTTAPQAAGVIHTDFEKGFIRAEVISYDDLIEYGSEAAAKEAGKLRLEGKDYVVQDGDIIH 80


                  ..
gi 16765125   359 FL 360
Cdd:pfam06071  81 FR 82
 
Name Accession Description Interval E-value
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
 3-363 0e+00

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 763.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   3 FKCGIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRLDQLAEIVKPQRILPTTMEFVDIAGLVKGASK 82
Cdd:COG0012   1 LKCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  83 GEGLGNQFLTNIRETEAIGHVVRCFENDNIIHVAGKVNPAEDIDVINTELALADLDTCERAIHRVQKKAKGGDKDAKAEL 162
Cdd:COG0012  81 GEGLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEKRLERLEKKAKSGDKEAKAEL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 163 AALEKCLPHLAEAGMLRSLDLTDEDKAAIRYLSFLTLKPTMYIANVNEDGF-ENNPYLDQVREIAAKEGSVVVPVCAAVE 241
Cdd:COG0012 161 ELLEKLKEHLEEGKPARSLELSEEEKKLLKELQLLTAKPVLYVANVDEDDLaEGNPYVEKVREYAAKEGAEVVVICAKIE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 242 ADIAELDDDERDEFMAELGLEEPGLNRVIRAGYRLLNLQTYFTAGVKEVRAWTIPVGATAPQAAGKIHTDFEKGFIRAQT 321
Cdd:COG0012 241 AELAELDEEERAEFLEELGLEESGLDRLIRAGYDLLGLITFFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFERGFIRAEV 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 16765125 322 IAFDDFITYKGEQGAKEAGKMRAEGKDYIVKDGDIMNFLFNV 363
Cdd:COG0012 321 ISYDDLIAYGSEAAAKEAGKLRLEGKDYVVQDGDVIHFRFNV 362
TIGR00092 TIGR00092
GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in ...
 1-363 0e+00

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: 516.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125     1 MGFKCGIVGLPNVGKSTLFNALTKAGI-EAANFPFCTIEPNTGVVPMPDPRLDQLAEIVKPQRILPTTMEFVDIAGLVKG 79
Cdd:TIGR00092   1 MGLSGGIVGLPNVGKSTLFAATTNLLGnEAANPPFTTIEPNAGVVNPSDPRLDLLAIYIKPEKVPPTTTEFVDIAGLVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125    80 ASKGEGLGNQFLTNIRETEAIGHVVRCFENDNIIHVAGKVNPAEDIDVINTELALADLDTCERAIHRVQKKAKGGdKDAK 159
Cdd:TIGR00092  81 ASKGEGLGNQFLANIREVDIIQHVVRCFEDDIIHHVGNVDDPRDDFEIIDEELLKADEFLVEKRIGRSKKSAEGG-KDKK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   160 AELAALEKCLPHLAEAGMLRSLDLTDEDKAAIRYLSFLTLKPTMYIANVNEDGFEN--NPYLDQVREIAA--KEGSVVVP 235
Cdd:TIGR00092 160 EELLLLEIILPLLNGGQMARHVDLSKEELILIKSLNLLTKKPIILIANVSEDYLRNlnNNYLLIVEWIAAysKGDPKVVF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   236 VCAAVEADIAELDDDERDEFMAELGLEEP-GLNRVIRAGYRLLNLQTYFTAGVKEVRAWTIPVGATAPQAAGKIHTDFEK 314
Cdd:TIGR00092 240 VCALEESELSELDDEERQEFLQKLGLTESaGLNIIIRARYKLLLLSFFFTGGKEEVRAWTRKGGWAAPQAAGIIHTDFET 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 16765125   315 GFIRAQTIAFDDFITYKGEQGAKEAGKMRAEGKDYIVKDGDIMNFLFNV 363
Cdd:TIGR00092 320 GFIAAEVISWDDFIYKKSSQGAKKGGLMRLEGKYYVVDDGDVLFFAFNV 368
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 4-363 3.16e-179

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 502.55  E-value: 3.16e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125    4 KCGIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRLDQLAEIVKPQRILPTTMEFVDIAGLVKGASKG 83
Cdd:PTZ00258  23 KMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDERFDWLCKHFKPKSIVPAQLDITDIAGLVKGASEG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   84 EGLGNQFLTNIRETEAIGHVVRCFENDNIIHVAGKVNPAEDIDVINTELALADLDTCERAIHRVQKKAKGG--DKDAKAE 161
Cdd:PTZ00258 103 EGLGNAFLSHIRAVDGIYHVVRAFEDEDITHVEGEIDPVRDLEIISSELILKDLEFVEKRLDELTKKRKKKkkKKEEKVE 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  162 LAALEKCLPHLAEAGMLRSLDLTDEDKAAIRYLSFLTLKPTMYIANVNEDGF--ENNPYLDQVRE-IAAKEGSVVVPVCA 238
Cdd:PTZ00258 183 LDVLKKVLEWLEEGKPVRDGDWTDKEIEILNEYQLLTAKPMIYLVNMSEKDFirQKNKWLAKIKEwVGEKGGGPIIPYSA 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  239 AVEADIAEL-DDDERDEFMAELGLEEPGLNRVIRAGYRLLNLQTYFTAGVKEVRAWTIPVGATAPQAAGKIHTDFEKGFI 317
Cdd:PTZ00258 263 EFEEELAELgSEEERKEYLEEYGIKQSMLDKIIKTGYKLLNLIHFFTAGPDEVRCWTIQKGTKAPQAAGVIHSDFEKGFI 342

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 16765125  318 RAQTIAFDDFITYKGEQGAKEAGKMRAEGKDYIVKDGDIMNFLFNV 363
Cdd:PTZ00258 343 CAEVMKYEDFLELGSEAAVKAEGKYRQEGKDYVVQDGDIIFFKFNV 388
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
 5-277 7.54e-179

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: 496.98  E-value: 7.54e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   5 CGIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRLDQLAEIVKPQRILPTTMEFVDIAGLVKGASKGE 84
Cdd:cd01900   1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASKGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  85 GLGNQFLTNIRETEAIGHVVRCFENDNIIHVAGKVNPAEDIDVINTELALADLDTCERAIHRVQKKAKGGDKDAKAELAA 164
Cdd:cd01900  81 GLGNKFLSHIREVDAIAHVVRCFEDDDITHVEGSVDPVRDIEIINTELILADLETIEKRLERLEKKAKSGDKEAKEELEL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 165 LEKCLPHLAEAGMLRSLDLTDEDKAAIRYLSFLTLKPTMYIANVNEDGFENNPYLD-QVREIAAKEGSVVVPVCAAVEAD 243
Cdd:cd01900 161 LEKIKEHLEEGKPARTLELTDEEIKILKSLQLLTAKPVIYVANVSEDDLIRGNNKVlKVREIAAKEGAEVIPISAKLEAE 240

                       250       260       270
                ....*....|....*....|....*....|....
gi 16765125 244 IAELDDDERDEFMAELGLEEPGLNRVIRAGYRLL 277
Cdd:cd01900 241 LAELDEEEAAEFLEELGLEESGLDKLIRAGYELL 274
YchF-GTPase_C pfam06071
Protein of unknown function (DUF933); This domain is found at the C terminus of the YchF ...
 279-360 3.81e-58

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: 182.94  E-value: 3.81e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   279 LQTYFTAGVKEVRAWTIPVGATAPQAAGKIHTDFEKGFIRAQTIAFDDFITYKGEQGAKEAGKMRAEGKDYIVKDGDIMN 358
Cdd:pfam06071   1 LITFFTAGPKEVRAWTIRKGTTAPQAAGVIHTDFEKGFIRAEVISYDDLIEYGSEAAAKEAGKLRLEGKDYVVQDGDIIH 80


                  ..
gi 16765125   359 FL 360
Cdd:pfam06071  81 FR 82
TGS_YchF_OLA1 cd04867
TGS (ThrRS, GTPase and SpoT) domain found in the YchF/OLA1 family proteins; The YchF/Ola1 ...
 277-361 2.11e-54

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: 173.48  E-value: 2.11e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 277 LNLQTYFTAGVKEVRAWTIPVGATAPQAAGKIHTDFEKGFIRAQTIAFDDFITYKGEQGAKEAGKMRAEGKDYIVKDGDI 356
Cdd:cd04867   1 LNLITFFTAGPDEVRAWTIRKGTKAPQAAGVIHTDFEKGFIRAEVIKYDDLKELGSEAAAKEAGKYRQEGKDYVVQDGDI 80


                ....*
gi 16765125 357 MNFLF 361
Cdd:cd04867  81 IHFKF 85
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 6-277 9.59e-48

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: 159.10  E-value: 9.59e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   6 GIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRldqlaeivkpqrilptTMEFVDIAGLVKGASKGEG 85
Cdd:cd01881   1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGV----------------DIQIIDLPGLLDGASEGRG 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  86 LGNQFLTNIRETEAIGHVVRCFENDNIihvagkvNPAEDIDVINTELALADLdtceraihrvqkkakggdkdakaelaal 165
Cdd:cd01881  65 LGEQILAHLYRSDLILHVIDASEDCVG-------DPLEDQKTLNEEVSGSFL---------------------------- 109

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 166 ekclphlaeagmlrsldltdedkaairylsFLTLKPTMYIANVNEDGFENNPYLDqvREIAAKEGSVVVPVCAAVEAdia 245
Cdd:cd01881 110 ------------------------------FLKNKPEMIVANKIDMASENNLKRL--KLDKLKRGIPVVPTSALTRL--- 154

                       250       260       270
                ....*....|....*....|....*....|..
gi 16765125 246 elddderdefmaelgleepGLNRVIRAGYRLL 277
Cdd:cd01881 155 -------------------GLDRVIRTIRKLL 167
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 6-356 5.69e-45

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 158.82  E-value: 5.69e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125    6 GIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGV----VPMPDPRLD-----QLAEIVKPQRILPTtmEFVDIAGL 76
Cdd:PRK09602   5 GLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayvrVECPCKELGvkcnpRNGKCIDGTRFIPV--ELIDVAGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   77 VKGASKGEGLGNQFLTNIRETEAIGHVV----RCFENDNIIHVaGKVNPAEDIDVINTELALADLDTCERAIHRVQKKAK 152
Cdd:PRK09602  83 VPGAHEGRGLGNQFLDDLRQADALIHVVdasgSTDEEGNPVEP-GSHDPVEDIKFLEEELDMWIYGILEKNWEKFSRKAQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  153 GGDKDAKAELA----ALEKCLPHLAEAgmLRSLDL-------TDEDKAA----IRYLSfltlKPTMYIAN-VNEDGFENN 216
Cdd:PRK09602 162 AEKFDIEEALAeqlsGLGINEEHVKEA--LRELGLpedpskwTDEDLLElareLRKIS----KPMVIAANkADLPPAEEN 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  217 pyldqVREIAAKEGSVVVPVCAAVE-----AD----------------IAELDDDERD--EFMAELgLEEPGLNRV---- 269
Cdd:PRK09602 236 -----IERLKEEKYYIVVPTSAEAElalrrAAkaglidyipgdsdfeiLGELSEKQKKalEYIREV-LKKYGGTGVqeai 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  270 IRAGYRLLNL--------QTYFTAGVKEV--RAWTIPVGATAPQAAGKIHTDFEKGFIRaqtiAFDdfitykgeqgAKEa 339
Cdd:PRK09602 310 NTAVFDLLDMivvypvedENKLTDKKGNVlpDAFLLPKGSTARDLAYKIHTDIGEGFLY----AID----------ART- 374

                        410
                 ....*....|....*..
gi 16765125  340 gKMRAeGKDYIVKDGDI 356
Cdd:PRK09602 375 -KRRI-GEDYELKDGDV 389
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 6-241 4.95e-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: 119.64  E-value: 4.95e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   6 GIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGV----VPMPDPRLD-----QLAEIVKPQRILPTtmEFVDIAGL 76
Cdd:cd01899   2 GLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVgyvrVECPCKELGvscnpRYGKCIDGKRYVPV--ELIDVAGL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  77 VKGASKGEGLGNQFLTNIRETEAIGHVVRCFENDNIIHVA---GKVNPAEDIDVINTELALADLDTCERAIHRVQKKAKG 153
Cdd:cd01899  80 VPGAHEGKGLGNQFLDDLRDADVLIHVVDASGGTDAEGNGvetGGYDPLEDIEFLENEIDMWIYGILERNWEKIVRKAKA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 154 GDKDAKAELAalekclPHLAEAGMLRSL------------DLTDEDKAAIRYL--SFLTL-KPTMYIAN----VNEDGFE 214
Cdd:cd01899 160 EKTDIVEALS------EQLSGFGVNEDVviealeelelpaDLSKWDDEDLLRLarELRKRrKPMVIAANkadiPDAEENI 233

                       250       260
                ....*....|....*....|....*..
gi 16765125 215 NnpyldqvREIAAKEGSVVVPVCAAVE 241
Cdd:cd01899 234 S-------KLRLKYPDEIVVPTSAEAE 253
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 6-134 5.60e-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: 99.42  E-value: 5.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   6 GIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVpmpdpRLDQLAEIVkpqrilpttmeFVDIAGLVKGASKGEG 85
Cdd:cd01898   4 GLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVV-----RVDDGRSFV-----------IADIPGLIEGASEGKG 67

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 16765125  86 LGNQFLtnireteaiGHVVRCfenDNIIHV---AGKVNPAEDIDVINTELAL 134
Cdd:cd01898  68 LGHRFL---------RHIERT---RVLLHVidlSGEDDPVEDYETIRNELEA 107
obgE PRK12297
GTPase CgtA; Reviewed
 6-142 5.04e-24

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 102.10  E-value: 5.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125    6 GIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRldqlaeivkpqrilpttmEFV--DIAGLVKGASKG 83
Cdd:PRK12297 162 GLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGR------------------SFVmaDIPGLIEGASEG 223

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16765125   84 EGLGNQFLTNIRETEAIGHVVRCFENDniihvaGKvNPAEDIDVINTELALADLDTCER 142
Cdd:PRK12297 224 VGLGHQFLRHIERTRVIVHVIDMSGSE------GR-DPIEDYEKINKELKLYNPRLLER 275
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 4-128 1.72e-23

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: 93.84  E-value: 1.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125     4 KCGIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRLdqlaeivkpqrilpttmEFVDIAGLVKGASKG 83
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQI-----------------ILVDTPGLIEGASEG 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 16765125    84 EGLGNQFLTnIRETEAIGHVVRCFEN-DNIIHVAGKVNPAEDIDVI 128
Cdd:pfam01926  64 EGLGRAFLA-IIEADLILFVVDSEEGiTPLDEELLELLRENKKPII 108
obgE PRK12299
GTPase CgtA; Reviewed
 6-134 5.90e-22

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 95.14  E-value: 5.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125    6 GIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRldqlaeivkpqrilpttmEFV--DIAGLVKGASKG 83
Cdd:PRK12299 162 GLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYK------------------SFViaDIPGLIEGASEG 223

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16765125   84 EGLGNQFLtnireteaiGHVVRCfendNI-IHV--AGKVNPAEDIDVINTELAL 134
Cdd:PRK12299 224 AGLGHRFL---------KHIERT----RLlLHLvdIEAVDPVEDYKTIRNELEK 264
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
8-356 1.45e-17

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 82.92  E-value: 1.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   8 VGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDprldqlAEIvkpqrilpttmEFVDIAGLVKGASKGEGLG 87
Cdd:COG1163  69 VGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLEYKG------AKI-----------QILDVPGLIEGAASGKGRG 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125  88 NQFLTNIRETEAIGHVVRCFEndniihvagkvnpAEDIDVINTELALAD--LDTcERAIHRVQKKAKGGdkdakaelaal 165
Cdd:COG1163 132 KEVLSVVRNADLILIVLDVFE-------------LEQYDVLKEELYDAGirLNK-PPPDVTIEKKGKGG----------- 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 166 ekclphLAEAGMLRsLDLTDEDKAAIrylsfltlkptmyianVNEDGFEN-------NPYLDQVreIAAKEGSVV-VPVC 237
Cdd:COG1163 187 ------IRVNSTGK-LDLDEEDIKKI----------------LREYGIVNadvlireDVTLDDL--IDALMGNRVyKPAI 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 238 AAV-EADIAelDDDERDEFMAELGLEEP----------GLNRVIRAGYRLLNLQTYFT----AGVKEVRAWTIPVGATAP 302
Cdd:COG1163 242 VVVnKIDLA--DEEYVEELKSKLPDGVPvifisaekgiGLEELKEEIFEELGLIRVYLkppgGKADMEEPLILRKGSTVG 319

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 16765125 303 QAAGKIHTDFEKGFIRAQtiafddfITYKgeqGAKEAGkMRAeGKDYIVKDGDI 356
Cdd:COG1163 320 DVCEKIHRDFVERFRYAR-------VWGK---SAKHPG-QRV-GLDHVLEDGDI 361
obgE PRK12296
GTPase CgtA; Reviewed
 6-133 1.14e-16

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 81.07  E-value: 1.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125    6 GIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRLdqlaeivkpqrilptTMefVDIAGLVKGASKGEG 85
Cdd:PRK12296 163 GLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQAGDTRF---------------TV--ADVPGLIPGASEGKG 225

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 16765125   86 LGNQFLTNIRETEAIGHVVRC--FENDNiihvagkvNPAEDIDVINTELA 133
Cdd:PRK12296 226 LGLDFLRHIERCAVLVHVVDCatLEPGR--------DPLSDIDALEAELA 267
obgE PRK12298
GTPase CgtA; Reviewed
 6-133 1.52e-16

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 79.91  E-value: 1.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125    6 GIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRldqlaeivkpqrilpttmEFV--DIAGLVKGASKG 83
Cdd:PRK12298 163 GLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDER------------------SFVvaDIPGLIEGASEG 224

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 16765125   84 EGLGNQFLTNIRETEAIGHVVRCFENDNiihvagkVNPAEDIDVINTELA 133
Cdd:PRK12298 225 AGLGIRFLKHLERCRVLLHLIDIAPIDG-------SDPVENARIIINELE 267
TGS cd01616
TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; ...
 281-360 7.37e-16

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: 71.10  E-value: 7.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 281 TYFTAGVKEVRAWTIPVGATAPQAAGKIHTDFEKGFIRAQTIAfddfitykgeqgakeagkmRAEGKDYIVKDGDIMNFL 360
Cdd:cd01616   1 EVFTVGKTPGTVFVMNKGATAYSCAMHLHEDYCRKSILALVDG-------------------QLWDMYYPLTKGDEIKFL 61
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 5-132 2.60e-13

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: 68.73  E-value: 2.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   5 CGIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDprldqlAEIvkpqrilpttmEFVDIAGLVKGASKGE 84
Cdd:cd01896   3 VALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKG------AKI-----------QLLDLPGIIEGASDGK 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 16765125  85 GLGNQFLTNIRETEAIGHVVRCFEndniihvagkvnPAEDIDVINTEL 132
Cdd:cd01896  66 GRGRQVIAVARTADLILIVLDATK------------PEGQREILEREL 101
TGS_Obg cd04938
TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases ...
 278-360 2.46e-12

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: 61.69  E-value: 2.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125 278 NLQTYFTAGVK-----------EVRAWTIPVGATAPQAAGKIHTDFEKGFIRAQTIafddfitykgeqgakeaGKMRAEG 346
Cdd:cd04938   1 GLIPVYPVKNIqtftngsgnsvFRDCVLVKKGTTVKDFANKIHTDLEKGFINAEGI-----------------GGRRLEG 63

                        90
                ....*....|....
gi 16765125 347 KDYIVKDGDIMNFL 360
Cdd:cd04938  64 EDYILQDNDVVKFT 77
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 3-44 2.32e-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: 49.76  E-value: 2.32e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 16765125     3 FKCGIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVV 44
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKF 42
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 7-58 6.76e-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: 48.61  E-value: 6.76e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 16765125   7 IVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPdprlDQLAEIV 58
Cdd:cd01879   2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLG----GKEIEIV 49
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 6-106 7.78e-07

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: 48.40  E-value: 7.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   6 GIVGLPNVGKSTLFNALTKAGI-EAANFPFCTIEPNTGVVPMPDPRldqlaeivkpqrilptTMEFVDIAGLVKGASKGE 84
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNVgIVSPIPGTTRDPVRKEWELLPLG----------------PVVLIDTPGLDEEGGLGR 64

                        90       100
                ....*....|....*....|..
gi 16765125  85 GLGNQFLTNIRETEAIGHVVRC 106
Cdd:cd00880  65 ERVEEARQVADRADLVLLVVDS 86
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 6-50 1.10e-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: 48.61  E-value: 1.10e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 16765125   6 GIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPR 50
Cdd:cd01878  45 ALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTTRRIKLPGGR 89
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 7-48 2.54e-06

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 48.93  E-value: 2.54e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 16765125   7 IVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPD 48
Cdd:COG2262 204 LVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRRLELPD 245
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-44 4.36e-06

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 48.58  E-value: 4.36e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 16765125   1 MGFKCGIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVV 44
Cdd:COG0370   2 KMITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKF 45
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 7-36 4.78e-06

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: 46.40  E-value: 4.78e-06
                        10        20        30
                ....*....|....*....|....*....|
gi 16765125   7 IVGLPNVGKSTLFNALTKAGIEAANFPFCT 36
Cdd:cd01897   5 IAGYPNVGKSSLVNKLTRAKPEVAPYPFTT 34
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
1-24 9.20e-06

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 47.33  E-value: 9.20e-06
                        10        20
                ....*....|....*....|....
gi 16765125   1 MGFKCGIVGLPNVGKSTLFNALTK 24
Cdd:COG1160   1 MSPVVAIVGRPNVGKSTLFNRLTG 24
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
 9-75 1.02e-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: 47.43  E-value: 1.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16765125     9 GLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRLdqlaEIVKpqriLPTTMEFVDIAG 75
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDI----EIVD----LPGIYSLTTFSL 59
era PRK00089
GTPase Era; Reviewed
 1-22 1.10e-05

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 46.58  E-value: 1.10e-05
                         10        20
                 ....*....|....*....|....*
gi 16765125    1 MGFKCG---IVGLPNVGKSTLFNAL 22
Cdd:PRK00089   1 MGFKSGfvaIVGRPNVGKSTLLNAL 25
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 7-24 1.16e-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: 44.73  E-value: 1.16e-05
                        10
                ....*....|....*...
gi 16765125   7 IVGLPNVGKSTLFNALTK 24
Cdd:cd01894   2 IVGRPNVGKSTLFNRLTG 19
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 2-30 1.73e-05

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 44.41  E-value: 1.73e-05
                        10        20
                ....*....|....*....|....*....
gi 16765125   2 GFKCGIVGLPNVGKSTLFNALtkAGIEAA 30
Cdd:cd04164   3 GIKVVIAGKPNVGKSSLLNAL--AGRDRA 29
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 7-24 2.18e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 46.20  E-value: 2.18e-05
                         10
                 ....*....|....*...
gi 16765125    7 IVGLPNVGKSTLFNALTK 24
Cdd:PRK00093   6 IVGRPNVGKSTLFNRLTG 23
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 3-22 2.63e-05

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: 43.99  E-value: 2.63e-05
                        10        20
                ....*....|....*....|...
gi 16765125   3 FKCG---IVGLPNVGKSTLFNAL 22
Cdd:cd04163   1 FKSGfvaIIGRPNVGKSTLLNAL 23
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 2-30 4.04e-05

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


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 45.05  E-value: 4.04e-05
                        10        20
                ....*....|....*....|....*....
gi 16765125   2 GFKCGIVGLPNVGKSTLFNALtkAGIEAA 30
Cdd:COG0486 213 GIKVVIVGRPNVGKSSLLNAL--LGEERA 239
GTPase_EngA TIGR03594
ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase ...
 7-24 4.21e-05

ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase with a duplication of its GTP-binding domain. It is broadly to universally distributed among bacteria. It appears to function in ribosome biogenesis or stability. [Protein synthesis, Other]


Pssm-ID: 274667 [Multi-domain]  Cd Length: 428  Bit Score: 45.13  E-value: 4.21e-05
                          10
                  ....*....|....*...
gi 16765125     7 IVGLPNVGKSTLFNALTK 24
Cdd:TIGR03594   3 IVGRPNVGKSTLFNRLTG 20
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 6-104 4.43e-05

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: 43.21  E-value: 4.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16765125   6 GIVGLPNVGKSTLFNALTKAGI-EAANFPFCTIEPNTGVVPMPDPRLDqlaeivkpqrilpttMEFVDIAGLVkgasKGE 84
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVgEVSDVPGTTRDPDVYVKELDKGKVK---------------LVLVDTPGLD----EFG 61

                        90       100
                ....*....|....*....|..
gi 16765125  85 GLGNQFLTN--IRETEAIGHVV 104
Cdd:cd00882  62 GLGREELARllLRGADLILLVV 83
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
3-22 5.03e-05

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 44.59  E-value: 5.03e-05
                        10        20
                ....*....|....*....|...
gi 16765125   3 FKCG---IVGLPNVGKSTLFNAL 22
Cdd:COG1159   1 FRSGfvaIVGRPNVGKSTLLNAL 23
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 2-27 6.29e-05

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: 42.90  E-value: 6.29e-05
                        10        20
                ....*....|....*....|....*.
gi 16765125   2 GFKCGIVGLPNVGKSTLFNALTKAGI 27
Cdd:cd01856 115 PLRAMVVGIPNVGKSTLINRLRGKKV 140
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
7-36 8.81e-05

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 44.05  E-value: 8.81e-05
                        10        20        30
                ....*....|....*....|....*....|
gi 16765125   7 IVGLPNVGKSTLFNALTKAGIEAANFPFCT 36
Cdd:COG1084 165 VAGYPNVGKSSLVSKVTSAKPEIASYPFTT 194
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
2-30 1.00e-04

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 43.95  E-value: 1.00e-04
                         10        20
                 ....*....|....*....|....*....
gi 16765125    2 GFKCGIVGLPNVGKSTLFNALtkAGIEAA 30
Cdd:PRK05291 215 GLKVVIAGRPNVGKSSLLNAL--LGEERA 241
PRK11058 PRK11058
GTPase HflX; Provisional
 7-65 2.80e-04

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 42.40  E-value: 2.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16765125    7 IVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRLDQLAEIVKPQRILP 65
Cdd:PRK11058 202 LVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIRHLP 260
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 2-24 3.88e-04

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


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 41.70  E-value: 3.88e-04
                          10        20
                  ....*....|....*....|...
gi 16765125     2 GFKCGIVGLPNVGKSTLFNALTK 24
Cdd:pfam12631  94 GIKVVIVGKPNVGKSSLLNALLG 116
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
7-33 1.35e-03

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 40.09  E-value: 1.35e-03
                        10        20
                ....*....|....*....|....*...
gi 16765125   7 IVGLPNVGKSTLFNALT-KAGIEAANFP 33
Cdd:COG1161 118 IVGIPNVGKSTLINRLAgKKVAKTGNKP 145
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 2-24 1.61e-03

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: 38.95  E-value: 1.61e-03
                        10        20
                ....*....|....*....|...
gi 16765125   2 GFKCGIVGLPNVGKSTLFNALTK 24
Cdd:cd01895   2 PIKIAIIGRPNVGKSSLLNALLG 24
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
7-22 2.29e-03

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 39.62  E-value: 2.29e-03
                        10
                ....*....|....*.
gi 16765125   7 IVGLPNVGKSTLFNAL 22
Cdd:COG1160 180 IVGRPNVGKSSLINAL 195
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 2-25 2.42e-03

Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 38.13  E-value: 2.42e-03
                        10        20
                ....*....|....*....|....
gi 16765125   2 GFKCGIVGLPNVGKSTLFNALTKA 25
Cdd:cd01849  91 GIRVGVVGLPNVGKSSFINALLNK 114
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 3-24 2.59e-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: 2.59e-03
                          10        20
                  ....*....|....*....|..
gi 16765125     3 FKCGIVGLPNVGKSTLFNALTK 24
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLG 23
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 2-24 2.92e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 39.26  E-value: 2.92e-03
                         10        20
                 ....*....|....*....|...
gi 16765125    2 GFKCGIVGLPNVGKSTLFNALTK 24
Cdd:PRK00093 173 PIKIAIIGRPNVGKSSLINALLG 195
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 3-24 3.15e-03

ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members. [Protein synthesis, Other]


Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 39.03  E-value: 3.15e-03
                          10        20
                  ....*....|....*....|..
gi 16765125     3 FKCGIVGLPNVGKSTLFNALTK 24
Cdd:TIGR03596 119 IRAMIVGIPNVGKSTLINRLAG 140
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 6-22 3.74e-03

A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein that functions as a regulator of cell growth and proliferation in stem cells and in several types of cancer cells, but is not expressed in the differentiated cells of most mammalian adult tissues. NS shuttles between the nucleolus and nucleoplasm bidirectionally at a rate that is fast and independent of cell type. Lowering GTP levels decreases the nucleolar retention of NS, and expression of NS is abruptly down-regulated during differentiation prior to terminal cell division. Found only in eukaryotes, NS consists of an N-terminal basic domain, a coiled-coil domain, a GTP-binding domain, an intermediate domain, and a C-terminal acidic domain. Experimental evidence indicates that NS uses its GTP-binding property as a molecular switch to control the transition between the nucleolus and nucleoplasm, and this process involves interaction between the basic, GTP-binding, and intermediate domains of the protein.


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 37.94  E-value: 3.74e-03
                        10
                ....*....|....*..
gi 16765125   6 GIVGLPNVGKSTLFNAL 22
Cdd:cd04178 120 GVVGYPNVGKSSVINSL 136
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 7-24 5.71e-03

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 37.63  E-value: 5.71e-03
                        10
                ....*....|....*...
gi 16765125   7 IVGLPNVGKSTLFNALTK 24
Cdd:cd01855 130 VVGATNVGKSTLINALLK 147
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
6-42 6.97e-03

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 38.54  E-value: 6.97e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 16765125    6 GIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTG 42
Cdd:PRK09554   7 GLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEG 43
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 3-24 8.98e-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: 8.98e-03
                        10        20
                ....*....|....*....|..
gi 16765125   3 FKCGIVGLPNVGKSTLFNALTK 24
Cdd:cd01859 100 VIVGVVGYPKVGKSSIINALKG 121
 
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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