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Conserved domains on  [gi|501220578|ref|WP_012263596|]
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redox-regulated ATPase YchF [Chlamydia trachomatis]

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] ...
 8-366 0e+00

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


:

Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 637.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   8 CGIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIVPVIDPRLETLARISQSQKIIYADMKFVDIAGLVKGAASGA 87
Cdd:COG0012    3 CGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASKGE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  88 GLGNRFLSHIRETHAIAHVVRCFDNDDITHVSGKIDPEEDIAVINLELVLADFSSATSVREKLGKQAK-GKKDIGQLLPL 166
Cdd:COG0012   83 GLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEKRLERLEKKAKsGDKEAKAELEL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 167 LDRVVDHLESGNPVRTFSLSLEEKVLLKPYPFLTGKPMLYIANIDEDSLTDlDNPYVQKVREIAKREEANVVPICVKLEE 246
Cdd:COG0012  163 LEKLKEHLEEGKPARSLELSEEEKKLLKELQLLTAKPVLYVANVDEDDLAE-GNPYVEKVREYAAKEGAEVVVICAKIEA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 247 EILSLPLEERQDFLHSLGLQESGLNRLVASAYHTLGLISYFTTGPQETRAWTISKGVTAAEAAGEIHSDIQRGFIRAEVV 326
Cdd:COG0012  242 ELAELDEEERAEFLEELGLEESGLDRLIRAGYDLLGLITFFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFERGFIRAEVI 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 501220578 327 TMEDIVAYDGRAGAREAGKLRAEGRDYIVQDGDIMLFLHN 366
Cdd:COG0012  322 SYDDLIAYGSEAAAKEAGKLRLEGKDYVVQDGDVIHFRFN 361
 
Name Accession Description Interval E-value
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
 8-366 0e+00

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 637.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   8 CGIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIVPVIDPRLETLARISQSQKIIYADMKFVDIAGLVKGAASGA 87
Cdd:COG0012    3 CGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASKGE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  88 GLGNRFLSHIRETHAIAHVVRCFDNDDITHVSGKIDPEEDIAVINLELVLADFSSATSVREKLGKQAK-GKKDIGQLLPL 166
Cdd:COG0012   83 GLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEKRLERLEKKAKsGDKEAKAELEL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 167 LDRVVDHLESGNPVRTFSLSLEEKVLLKPYPFLTGKPMLYIANIDEDSLTDlDNPYVQKVREIAKREEANVVPICVKLEE 246
Cdd:COG0012  163 LEKLKEHLEEGKPARSLELSEEEKKLLKELQLLTAKPVLYVANVDEDDLAE-GNPYVEKVREYAAKEGAEVVVICAKIEA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 247 EILSLPLEERQDFLHSLGLQESGLNRLVASAYHTLGLISYFTTGPQETRAWTISKGVTAAEAAGEIHSDIQRGFIRAEVV 326
Cdd:COG0012  242 ELAELDEEERAEFLEELGLEESGLDRLIRAGYDLLGLITFFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFERGFIRAEVI 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 501220578 327 TMEDIVAYDGRAGAREAGKLRAEGRDYIVQDGDIMLFLHN 366
Cdd:COG0012  322 SYDDLIAYGSEAAAKEAGKLRLEGKDYVVQDGDVIHFRFN 361
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
 8-281 1.34e-160

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: 450.76  E-value: 1.34e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   8 CGIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIVPVIDPRLETLARISQSQKIIYADMKFVDIAGLVKGAASGA 87
Cdd:cd01900    1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASKGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  88 GLGNRFLSHIRETHAIAHVVRCFDNDDITHVSGKIDPEEDIAVINLELVLADFSSATSVREKLGKQAK-GKKDIGQLLPL 166
Cdd:cd01900   81 GLGNKFLSHIREVDAIAHVVRCFEDDDITHVEGSVDPVRDIEIINTELILADLETIEKRLERLEKKAKsGDKEAKEELEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 167 LDRVVDHLESGNPVRTFSLSLEEKVLLKPYPFLTGKPMLYIANIDEDSLTDLDNpYVQKVREIAKREEANVVPICVKLEE 246
Cdd:cd01900  161 LEKIKEHLEEGKPARTLELTDEEIKILKSLQLLTAKPVIYVANVSEDDLIRGNN-KVLKVREIAAKEGAEVIPISAKLEA 239

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 501220578 247 EILSLPLEERQDFLHSLGLQESGLNRLVASAYHTL 281
Cdd:cd01900  240 ELAELDEEEAAEFLEELGLEESGLDKLIRAGYELL 274
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 8-366 7.61e-160

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 453.25  E-value: 7.61e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   8 CGIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIVPVIDPRLETLARISQSQKIIYADMKFVDIAGLVKGAASGA 87
Cdd:PTZ00258  24 MGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDERFDWLCKHFKPKSIVPAQLDITDIAGLVKGASEGE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  88 GLGNRFLSHIRETHAIAHVVRCFDNDDITHVSGKIDPEEDIAVINLELVLADFSSATSVREKLGKQAKGKKDIGQL---L 164
Cdd:PTZ00258 104 GLGNAFLSHIRAVDGIYHVVRAFEDEDITHVEGEIDPVRDLEIISSELILKDLEFVEKRLDELTKKRKKKKKKKEEkveL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 165 PLLDRVVDHLESGNPVRTFSLSLEEKVLLKPYPFLTGKPMLYIANIDEDSLTDLDNPYVQKVRE-IAKREEANVVPICVK 243
Cdd:PTZ00258 184 DVLKKVLEWLEEGKPVRDGDWTDKEIEILNEYQLLTAKPMIYLVNMSEKDFIRQKNKWLAKIKEwVGEKGGGPIIPYSAE 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 244 LEEEILSLPL-EERQDFLHSLGLQESGLNRLVASAYHTLGLISYFTTGPQETRAWTISKGVTAAEAAGEIHSDIQRGFIR 322
Cdd:PTZ00258 264 FEEELAELGSeEERKEYLEEYGIKQSMLDKIIKTGYKLLNLIHFFTAGPDEVRCWTIQKGTKAPQAAGVIHSDFEKGFIC 343

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 501220578 323 AEVVTMEDIVAYDGRAGAREAGKLRAEGRDYIVQDGDIMLFLHN 366
Cdd:PTZ00258 344 AEVMKYEDFLELGSEAAVKAEGKYRQEGKDYVVQDGDIIFFKFN 387
TIGR00092 TIGR00092
GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in ...
 6-366 1.39e-127

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: 370.65  E-value: 1.39e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578    6 TECGIVGLPNVGKSGLFNALTGAQVA-SCNYPFCTIDPNVGIVPVIDPRLETLARISQSQKIIYADMKFVDIAGLVKGAA 84
Cdd:TIGR00092   3 LSGGIVGLPNVGKSTLFAATTNLLGNeAANPPFTTIEPNAGVVNPSDPRLDLLAIYIKPEKVPPTTTEFVDIAGLVGGAS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   85 SGAGLGNRFLSHIRETHAIAHVVRCFDNDDITHVSGKIDPEEDIAVINLELVLADFSSATSVREKLGKQAKGKKDIGQLL 164
Cdd:TIGR00092  83 KGEGLGNQFLANIREVDIIQHVVRCFEDDIIHHVGNVDDPRDDFEIIDEELLKADEFLVEKRIGRSKKSAEGGKDKKEEL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  165 PLLDRVVDHLESGNPVRTFSLSLEEKVLLKPYPFLTGKPMLYIANIDEDSLTDLDNPYVQKVREIAK--REEANVVPICV 242
Cdd:TIGR00092 163 LLLEIILPLLNGGQMARHVDLSKEELILIKSLNLLTKKPIILIANVSEDYLRNLNNNYLLIVEWIAAysKGDPKVVFVCA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  243 KLEEEILSLPLEERQDFLHSLGLQES-GLNRLVASAYHTLGLISYFTTGPQETRAWTISKGVTAAEAAGEIHSDIQRGFI 321
Cdd:TIGR00092 243 LEESELSELDDEERQEFLQKLGLTESaGLNIIIRARYKLLLLSFFFTGGKEEVRAWTRKGGWAAPQAAGIIHTDFETGFI 322

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 501220578  322 RAEVVTMEDIVAYDGRAGAREAGKLRAEGRDYIVQDGDIMLFLHN 366
Cdd:TIGR00092 323 AAEVISWDDFIYKKSSQGAKKGGLMRLEGKYYVVDDGDVLFFAFN 367
YchF-GTPase_C pfam06071
Protein of unknown function (DUF933); This domain is found at the C terminus of the YchF ...
 283-364 6.63e-50

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: 161.76  E-value: 6.63e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  283 LISYFTTGPQETRAWTISKGVTAAEAAGEIHSDIQRGFIRAEVVTMEDIVAYDGRAGAREAGKLRAEGRDYIVQDGDIML 362
Cdd:pfam06071   1 LITFFTAGPKEVRAWTIRKGTTAPQAAGVIHTDFEKGFIRAEVISYDDLIEYGSEAAAKEAGKLRLEGKDYVVQDGDIIH 80


                  ..
gi 501220578  363 FL 364
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] ...
 8-366 0e+00

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 637.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   8 CGIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIVPVIDPRLETLARISQSQKIIYADMKFVDIAGLVKGAASGA 87
Cdd:COG0012    3 CGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASKGE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  88 GLGNRFLSHIRETHAIAHVVRCFDNDDITHVSGKIDPEEDIAVINLELVLADFSSATSVREKLGKQAK-GKKDIGQLLPL 166
Cdd:COG0012   83 GLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEKRLERLEKKAKsGDKEAKAELEL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 167 LDRVVDHLESGNPVRTFSLSLEEKVLLKPYPFLTGKPMLYIANIDEDSLTDlDNPYVQKVREIAKREEANVVPICVKLEE 246
Cdd:COG0012  163 LEKLKEHLEEGKPARSLELSEEEKKLLKELQLLTAKPVLYVANVDEDDLAE-GNPYVEKVREYAAKEGAEVVVICAKIEA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 247 EILSLPLEERQDFLHSLGLQESGLNRLVASAYHTLGLISYFTTGPQETRAWTISKGVTAAEAAGEIHSDIQRGFIRAEVV 326
Cdd:COG0012  242 ELAELDEEERAEFLEELGLEESGLDRLIRAGYDLLGLITFFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFERGFIRAEVI 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 501220578 327 TMEDIVAYDGRAGAREAGKLRAEGRDYIVQDGDIMLFLHN 366
Cdd:COG0012  322 SYDDLIAYGSEAAAKEAGKLRLEGKDYVVQDGDVIHFRFN 361
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
 8-281 1.34e-160

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: 450.76  E-value: 1.34e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   8 CGIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIVPVIDPRLETLARISQSQKIIYADMKFVDIAGLVKGAASGA 87
Cdd:cd01900    1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASKGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  88 GLGNRFLSHIRETHAIAHVVRCFDNDDITHVSGKIDPEEDIAVINLELVLADFSSATSVREKLGKQAK-GKKDIGQLLPL 166
Cdd:cd01900   81 GLGNKFLSHIREVDAIAHVVRCFEDDDITHVEGSVDPVRDIEIINTELILADLETIEKRLERLEKKAKsGDKEAKEELEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 167 LDRVVDHLESGNPVRTFSLSLEEKVLLKPYPFLTGKPMLYIANIDEDSLTDLDNpYVQKVREIAKREEANVVPICVKLEE 246
Cdd:cd01900  161 LEKIKEHLEEGKPARTLELTDEEIKILKSLQLLTAKPVIYVANVSEDDLIRGNN-KVLKVREIAAKEGAEVIPISAKLEA 239

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 501220578 247 EILSLPLEERQDFLHSLGLQESGLNRLVASAYHTL 281
Cdd:cd01900  240 ELAELDEEEAAEFLEELGLEESGLDKLIRAGYELL 274
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 8-366 7.61e-160

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 453.25  E-value: 7.61e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   8 CGIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIVPVIDPRLETLARISQSQKIIYADMKFVDIAGLVKGAASGA 87
Cdd:PTZ00258  24 MGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDERFDWLCKHFKPKSIVPAQLDITDIAGLVKGASEGE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  88 GLGNRFLSHIRETHAIAHVVRCFDNDDITHVSGKIDPEEDIAVINLELVLADFSSATSVREKLGKQAKGKKDIGQL---L 164
Cdd:PTZ00258 104 GLGNAFLSHIRAVDGIYHVVRAFEDEDITHVEGEIDPVRDLEIISSELILKDLEFVEKRLDELTKKRKKKKKKKEEkveL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 165 PLLDRVVDHLESGNPVRTFSLSLEEKVLLKPYPFLTGKPMLYIANIDEDSLTDLDNPYVQKVRE-IAKREEANVVPICVK 243
Cdd:PTZ00258 184 DVLKKVLEWLEEGKPVRDGDWTDKEIEILNEYQLLTAKPMIYLVNMSEKDFIRQKNKWLAKIKEwVGEKGGGPIIPYSAE 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 244 LEEEILSLPL-EERQDFLHSLGLQESGLNRLVASAYHTLGLISYFTTGPQETRAWTISKGVTAAEAAGEIHSDIQRGFIR 322
Cdd:PTZ00258 264 FEEELAELGSeEERKEYLEEYGIKQSMLDKIIKTGYKLLNLIHFFTAGPDEVRCWTIQKGTKAPQAAGVIHSDFEKGFIC 343

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 501220578 323 AEVVTMEDIVAYDGRAGAREAGKLRAEGRDYIVQDGDIMLFLHN 366
Cdd:PTZ00258 344 AEVMKYEDFLELGSEAAVKAEGKYRQEGKDYVVQDGDIIFFKFN 387
TIGR00092 TIGR00092
GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in ...
 6-366 1.39e-127

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: 370.65  E-value: 1.39e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578    6 TECGIVGLPNVGKSGLFNALTGAQVA-SCNYPFCTIDPNVGIVPVIDPRLETLARISQSQKIIYADMKFVDIAGLVKGAA 84
Cdd:TIGR00092   3 LSGGIVGLPNVGKSTLFAATTNLLGNeAANPPFTTIEPNAGVVNPSDPRLDLLAIYIKPEKVPPTTTEFVDIAGLVGGAS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   85 SGAGLGNRFLSHIRETHAIAHVVRCFDNDDITHVSGKIDPEEDIAVINLELVLADFSSATSVREKLGKQAKGKKDIGQLL 164
Cdd:TIGR00092  83 KGEGLGNQFLANIREVDIIQHVVRCFEDDIIHHVGNVDDPRDDFEIIDEELLKADEFLVEKRIGRSKKSAEGGKDKKEEL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  165 PLLDRVVDHLESGNPVRTFSLSLEEKVLLKPYPFLTGKPMLYIANIDEDSLTDLDNPYVQKVREIAK--REEANVVPICV 242
Cdd:TIGR00092 163 LLLEIILPLLNGGQMARHVDLSKEELILIKSLNLLTKKPIILIANVSEDYLRNLNNNYLLIVEWIAAysKGDPKVVFVCA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  243 KLEEEILSLPLEERQDFLHSLGLQES-GLNRLVASAYHTLGLISYFTTGPQETRAWTISKGVTAAEAAGEIHSDIQRGFI 321
Cdd:TIGR00092 243 LEESELSELDDEERQEFLQKLGLTESaGLNIIIRARYKLLLLSFFFTGGKEEVRAWTRKGGWAAPQAAGIIHTDFETGFI 322

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 501220578  322 RAEVVTMEDIVAYDGRAGAREAGKLRAEGRDYIVQDGDIMLFLHN 366
Cdd:TIGR00092 323 AAEVISWDDFIYKKSSQGAKKGGLMRLEGKYYVVDDGDVLFFAFN 367
YchF-GTPase_C pfam06071
Protein of unknown function (DUF933); This domain is found at the C terminus of the YchF ...
 283-364 6.63e-50

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: 161.76  E-value: 6.63e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  283 LISYFTTGPQETRAWTISKGVTAAEAAGEIHSDIQRGFIRAEVVTMEDIVAYDGRAGAREAGKLRAEGRDYIVQDGDIML 362
Cdd:pfam06071   1 LITFFTAGPKEVRAWTIRKGTTAPQAAGVIHTDFEKGFIRAEVISYDDLIEYGSEAAAKEAGKLRLEGKDYVVQDGDIIH 80


                  ..
gi 501220578  363 FL 364
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 ...
 281-365 2.29e-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: 152.68  E-value: 2.29e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 281 LGLISYFTTGPQETRAWTISKGVTAAEAAGEIHSDIQRGFIRAEVVTMEDIVAYDGRAGAREAGKLRAEGRDYIVQDGDI 360
Cdd:cd04867    1 LNLITFFTAGPDEVRAWTIRKGTKAPQAAGVIHTDFEKGFIRAEVIKYDDLKELGSEAAAKEAGKYRQEGKDYVVQDGDI 80


                 ....*
gi 501220578 361 MLFLH 365
Cdd:cd04867   81 IHFKF 85
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 9-360 3.80e-33

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 127.23  E-value: 3.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   9 GIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGI--VPVIDPRLETLARIS-QSQKII----YADMKFVDIAGLVK 81
Cdd:PRK09602   5 GLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayVRVECPCKELGVKCNpRNGKCIdgtrFIPVELIDVAGLVP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  82 GAASGAGLGNRFLSHIRETHAIAHVVRCFDNDDITHVSGKI---DPEEDIAVINLELVLADFSSATSVREKLGKQAKGKK 158
Cdd:PRK09602  85 GAHEGRGLGNQFLDDLRQADALIHVVDASGSTDEEGNPVEPgshDPVEDIKFLEEELDMWIYGILEKNWEKFSRKAQAEK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 159 -------------------DIGQLLPLLDRVVDHLE-SGNPVRTFSLSLEEKvllkpypfltGKPMLYIAN-IDEDsltd 217
Cdd:PRK09602 165 fdieealaeqlsglgineeHVKEALRELGLPEDPSKwTDEDLLELARELRKI----------SKPMVIAANkADLP---- 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 218 ldnPYVQKVREIAKREEANVVPIC-------VKLEE-------------EILSlPLEERQ--------DFLH---SLGLQ 266
Cdd:PRK09602 231 ---PAEENIERLKEEKYYIVVPTSaeaelalRRAAKaglidyipgdsdfEILG-ELSEKQkkaleyirEVLKkygGTGVQ 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 267 ESgLNRLVasaYHTLGLISYFTTGpQETRaWT------------ISKGVTAAEAAGEIHSDIQRGFIRaevvtmedivAY 334
Cdd:PRK09602 307 EA-INTAV---FDLLDMIVVYPVE-DENK-LTdkkgnvlpdaflLPKGSTARDLAYKIHTDIGEGFLY----------AI 370

                        410       420
                 ....*....|....*....|....*.
gi 501220578 335 DGRAGAReagklraEGRDYIVQDGDI 360
Cdd:PRK09602 371 DARTKRR-------IGEDYELKDGDV 389
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 9-191 1.48e-30

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: 114.41  E-value: 1.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   9 GIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIVPVIDPRletlarisqsqkiiyaDMKFVDIAGLVKGAASGAG 88
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGV----------------DIQIIDLPGLLDGASEGRG 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  89 LGNRFLSHIRETHAIAHVVRCFDNDdithvsgKIDPEEDIAVINLELVLADfssaTSVREKLGKQAKGKKDIGQLLPLLD 168
Cdd:cd01881   65 LGEQILAHLYRSDLILHVIDASEDC-------VGDPLEDQKTLNEEVSGSF----LFLKNKPEMIVANKIDMASENNLKR 133

                        170       180
                 ....*....|....*....|...
gi 501220578 169 RVVDHLESGNPVRTFSLSLEEKV 191
Cdd:cd01881  134 LKLDKLKRGIPVVPTSALTRLGL 156
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 9-137 1.13e-26

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: 104.04  E-value: 1.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   9 GIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIVPVIDprletlarisqsqkiiYADMKFVDIAGLVKGAASGAG 88
Cdd:cd01898    4 GLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDD----------------GRSFVIADIPGLIEGASEGKG 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 501220578  89 LGNRFLSHIRETHAIAHVVrcfdndDIthvSGKIDPEEDIAVINLELVL 137
Cdd:cd01898   68 LGHRFLRHIERTRVLLHVI------DL---SGEDDPVEDYETIRNELEA 107
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 9-135 8.79e-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: 105.58  E-value: 8.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578    9 GIVGLPNVGKSGLFNALTGAQ--VAscNYPFCTIDPNVGIVPVIDPRletlarisqsqkiiyaDMKFVDIAGLVKGAASG 86
Cdd:TIGR02729 161 GLVGLPNAGKSTLISAVSAAKpkIA--DYPFTTLVPNLGVVRVDDGR----------------SFVIADIPGLIEGASEG 222

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 501220578   87 AGLGNRFLSHIRETHAIAHVVrcfdndDITHVSGKiDPEEDIAVINLEL 135
Cdd:TIGR02729 223 AGLGHRFLKHIERTRVLLHLI------DISPEDGS-DPVEDYEIIRNEL 264
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 9-135 8.09e-25

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: 102.69  E-value: 8.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   9 GIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGI--VPVIDPRLEtLARISQSQ------KIIYADMKFVDIAGLV 80
Cdd:cd01899    2 GLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVgyVRVECPCKE-LGVSCNPRygkcidGKRYVPVELIDVAGLV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 501220578  81 KGAASGAGLGNRFLSHIRETHAIAHVVRC---FDNDDITHVSGKIDPEEDIAVINLEL 135
Cdd:cd01899   81 PGAHEGKGLGNQFLDDLRDADVLIHVVDAsggTDAEGNGVETGGYDPLEDIEFLENEI 138
obgE PRK12299
GTPase CgtA; Reviewed
 9-135 5.93e-24

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 100.53  E-value: 5.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   9 GIVGLPNVGKSGLFNALTGAQ--VAscNYPFCTIDPNVGIVPVIDprletlarisqsqkiiYADMKFVDIAGLVKGAASG 86
Cdd:PRK12299 162 GLVGLPNAGKSTLISAVSAAKpkIA--DYPFTTLHPNLGVVRVDD----------------YKSFVIADIPGLIEGASEG 223

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 501220578  87 AGLGNRFLSHIRETHAIAHVVrcfdndDITHVsgkiDPEEDIAVINLEL 135
Cdd:PRK12299 224 AGLGHRFLKHIERTRLLLHLV------DIEAV----DPVEDYKTIRNEL 262
obgE PRK12297
GTPase CgtA; Reviewed
 9-135 5.04e-23

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 99.41  E-value: 5.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   9 GIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIVPVIDPRLETLArisqsqkiiyadmkfvDIAGLVKGAASGAG 88
Cdd:PRK12297 162 GLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRSFVMA----------------DIPGLIEGASEGVG 225

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501220578  89 LGNRFLSHIRETHAIAHVVrcfdndDITHVSGKiDPEEDIAVINLEL 135
Cdd:PRK12297 226 LGHQFLRHIERTRVIVHVI------DMSGSEGR-DPIEDYEKINKEL 265
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 7-131 7.37e-22

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: 89.22  E-value: 7.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578    7 ECGIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIVPVIDPRLEtlarisqsqkiiyadmkFVDIAGLVKGAASG 86
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQII-----------------LVDTPGLIEGASEG 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 501220578   87 AGLGNRFLSHIrETHAIAHVVRCFDN-DDITHVSGKIDPEEDIAVI 131
Cdd:pfam01926  64 EGLGRAFLAII-EADLILFVVDSEEGiTPLDEELLELLRENKKPII 108
obgE PRK12298
GTPase CgtA; Reviewed
 9-135 1.39e-18

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 86.07  E-value: 1.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   9 GIVGLPNVGKSGLFNALTGA--QVAscNYPFCTIDPNVGIVPVidprletlaRISQSqkiiyadmkFV--DIAGLVKGAA 84
Cdd:PRK12298 163 GLLGLPNAGKSTFIRAVSAAkpKVA--DYPFTTLVPNLGVVRV---------DDERS---------FVvaDIPGLIEGAS 222

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501220578  85 SGAGLGNRFLSHIRETHAIAHVVrcfdndDITHVSGKiDPEEDIAVINLEL 135
Cdd:PRK12298 223 EGAGLGIRFLKHLERCRVLLHLI------DIAPIDGS-DPVENARIIINEL 266
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
11-360 2.88e-18

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 84.85  E-value: 2.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  11 VGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIvpvidprLEtlarisqsqkiiYADMKF--VDIAGLVKGAASGAG 88
Cdd:COG1163   69 VGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGM-------LE------------YKGAKIqiLDVPGLIEGAASGKG 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  89 LGNRFLSHIRETHAIAHVVRCFDND---------------------DIT-----------HVSGKID-PEEDIAVInlel 135
Cdd:COG1163  130 RGKEVLSVVRNADLILIVLDVFELEqydvlkeelydagirlnkpppDVTiekkgkggirvNSTGKLDlDEEDIKKI---- 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 136 vLADF---SSATSVREKLGkqakgkkdigqllplLDRVVDHLeSGNPVrtfslsleekvllkpYpfltgKPMLYIANide 212
Cdd:COG1163  206 -LREYgivNADVLIREDVT---------------LDDLIDAL-MGNRV---------------Y-----KPAIVVVN--- 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 213 dsLTDL-DNPYVQKVREiAKREEANVVPIcvKLEEEIlslpleerqdflhslglqesGLNRLVASAYHTLGLISYFTTGP 291
Cdd:COG1163  246 --KIDLaDEEYVEELKS-KLPDGVPVIFI--SAEKGI--------------------GLEELKEEIFEELGLIRVYLKPP 300

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501220578 292 -QET---RAWTISKGVTAAEAAGEIHSDIQRGFiRAEVVTMEDiVAYDGRagareagklRAeGRDYIVQDGDI 360
Cdd:COG1163  301 gGKAdmeEPLILRKGSTVGDVCEKIHRDFVERF-RYARVWGKS-AKHPGQ---------RV-GLDHVLEDGDI 361
obgE PRK12296
GTPase CgtA; Reviewed
 9-135 4.74e-16

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 79.14  E-value: 4.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   9 GIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIVPVIDPRLeTLArisqsqkiiyadmkfvDIAGLVKGAASGAG 88
Cdd:PRK12296 163 GLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQAGDTRF-TVA----------------DVPGLIPGASEGKG 225

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501220578  89 LGNRFLSHIRETHAIAHVVRCfdnddITHVSGKiDPEEDIAVINLEL 135
Cdd:PRK12296 226 LGLDFLRHIERCAVLVHVVDC-----ATLEPGR-DPLSDIDALEAEL 266
TGS cd01616
TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; ...
 286-364 1.33e-10

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: 56.46  E-value: 1.33e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501220578 286 YFTTGPQETRAWTISKGVTAAEAAGEIHSDIQRGFIRAEVVTmedivaydgragareagklRAEGRDYIVQDGDIMLFL 364
Cdd:cd01616    2 VFTVGKTPGTVFVMNKGATAYSCAMHLHEDYCRKSILALVDG-------------------QLWDMYYPLTKGDEIKFL 61
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 8-110 2.81e-10

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: 59.87  E-value: 2.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   8 CGIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIvpvidprletlarisqsqkIIYADMK--FVDIAGLVKGAAS 85
Cdd:cd01896    3 VALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGV-------------------MEYKGAKiqLLDLPGIIEGASD 63

                         90       100
                 ....*....|....*....|....*
gi 501220578  86 GAGLGNRFLSHIRETHAIAHVVRCF 110
Cdd:cd01896   64 GKGRGRQVIAVARTADLILIVLDAT 88
TGS_Obg cd04938
TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases ...
 282-364 3.29e-09

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: 52.83  E-value: 3.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578 282 GLISYFTT-----------GPQETRAWTISKGVTAAEAAGEIHSDIQRGFIRAEVVtmedivaydgragareaGKLRAEG 350
Cdd:cd04938    1 GLIPVYPVkniqtftngsgNSVFRDCVLVKKGTTVKDFANKIHTDLEKGFINAEGI-----------------GGRRLEG 63

                         90
                 ....*....|....
gi 501220578 351 RDYIVQDGDIMLFL 364
Cdd:cd04938   64 EDYILQDNDVVKFT 77
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 9-133 1.26e-08

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: 53.79  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   9 GIVGLPNVGKSGLFNALTGAQVASC-NYPFCTIDPNVGIVPvidprletlarisqsqKIIYADMKFVDIAGLVKGAASGA 87
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIVsPIPGTTRDPVRKEWE----------------LLPLGPVVLIDTPGLDEEGGLGR 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 501220578  88 GLGNRFLSHIRETHAIAHVvrcfdnddithVSGKIDPEEDIAVINL 133
Cdd:cd00880   65 ERVEEARQVADRADLVLLV-----------VDSDLTPVEEEAKLGL 99
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 10-45 1.17e-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: 47.94  E-value: 1.17e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 501220578  10 IVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVG 45
Cdd:cd01897    5 IAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVG 40
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 10-45 1.50e-06

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: 47.45  E-value: 1.50e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 501220578  10 IVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVG 45
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEG 37
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 11-47 1.44e-05

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: 44.75  E-value: 1.44e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 501220578   11 VGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIV 47
Cdd:pfam02421   6 VGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKF 42
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
 12-55 6.51e-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: 44.73  E-value: 6.51e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 501220578   12 GLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIVPVIDPRLE 55
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIE 44
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 9-165 7.75e-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: 42.44  E-value: 7.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578   9 GIVGLPNVGKSGLFNALTGAQVASC-NYPFCTIDPNVGIVPVIDPRLetlarisqsqkiiyaDMKFVDIAGLVKGAASga 87
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVsDVPGTTRDPDVYVKELDKGKV---------------KLVLVDTPGLDEFGGL-- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  88 GLGNRFLSHIRETHAIAHVVRCFDNDDITHVSGKIDPEEDIAVINLELVL--ADFSSATSVREKLGKQAKGKKDIGQLLP 165
Cdd:cd00882   64 GREELARLLLRGADLILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVGnkIDLLEEREVEELLRLEELAKILGVPVFE 143
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
10-36 1.02e-04

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 44.34  E-value: 1.02e-04
                         10        20
                 ....*....|....*....|....*....
gi 501220578  10 IVGLPNVGKSGLFNALTGA--QVAscNYP 36
Cdd:COG0370    8 LVGNPNVGKTTLFNALTGSrqKVG--NWP 34
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 10-31 1.77e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 43.11  E-value: 1.77e-04
                         10        20
                 ....*....|....*....|..
gi 501220578  10 IVGLPNVGKSGLFNALTGAQVA 31
Cdd:PRK00093   6 IVGRPNVGKSTLFNRLTGKRDA 27
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
10-31 1.89e-04

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 43.09  E-value: 1.89e-04
                         10        20
                 ....*....|....*....|..
gi 501220578  10 IVGLPNVGKSGLFNALTGAQVA 31
Cdd:COG1160    7 IVGRPNVGKSTLFNRLTGRRDA 28
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 9-42 2.86e-04

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: 41.68  E-value: 2.86e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 501220578   9 GIVGLPNVGKSGLFNALTGAQVASCNYPFCTIDP 42
Cdd:cd01878   45 ALVGYTNAGKSTLFNALTGADVLAEDQLFATLDP 78
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 10-27 3.63e-04

EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 40.50  E-value: 3.63e-04
                         10
                 ....*....|....*...
gi 501220578  10 IVGLPNVGKSGLFNALTG 27
Cdd:cd01894    2 IVGRPNVGKSTLFNRLTG 19
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
10-45 3.85e-04

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 41.74  E-value: 3.85e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 501220578  10 IVGLPNVGKSGLFNALTGA--QVAScnYPFCTIDPNVG 45
Cdd:COG1084  165 VAGYPNVGKSSLVSKVTSAkpEIAS--YPFTTKGIIVG 200
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 10-31 3.99e-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: 3.99e-04
                         10        20
                 ....*....|....*....|..
gi 501220578  10 IVGLPNVGKSGLFNALTGAQVA 31
Cdd:cd01856  120 VVGIPNVGKSTLINRLRGKKVA 141
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 10-31 4.96e-04

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: 41.97  E-value: 4.96e-04
                         10        20
                 ....*....|....*....|..
gi 501220578  10 IVGLPNVGKSGLFNALTGAQVA 31
Cdd:COG0486  218 IVGRPNVGKSSLLNALLGEERA 239
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 10-31 7.22e-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: 39.79  E-value: 7.22e-04
                         10        20
                 ....*....|....*....|..
gi 501220578  10 IVGLPNVGKSGLFNALTGAQVA 31
Cdd:cd04164    8 IAGKPNVGKSSLLNALAGRDRA 29
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 10-42 7.32e-04

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 41.23  E-value: 7.32e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 501220578  10 IVGLPNVGKSGLFNALTGAQVASCNYPFCTIDP 42
Cdd:COG2262  204 LVGYTNAGKSTLFNRLTGADVLAEDKLFATLDP 236
GTPase_EngA TIGR03594
ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase ...
 10-31 7.44e-04

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: 41.28  E-value: 7.44e-04
                          10        20
                  ....*....|....*....|..
gi 501220578   10 IVGLPNVGKSGLFNALTGAQVA 31
Cdd:TIGR03594   3 IVGRPNVGKSTLFNRLTGKRDA 24
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 9-32 8.65e-04

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


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 39.14  E-value: 8.65e-04
                         10        20
                 ....*....|....*....|....
gi 501220578   9 GIVGLPNVGKSGLFNALTGAQVAS 32
Cdd:cd01857   86 GLVGYPNVGKSSLINALVGSKKVS 109
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 10-31 8.75e-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: 40.93  E-value: 8.75e-04
                          10        20
                  ....*....|....*....|..
gi 501220578   10 IVGLPNVGKSGLFNALTGAQVA 31
Cdd:pfam12631  99 IVGKPNVGKSSLLNALLGEERA 120
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
10-31 1.04e-03

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 40.86  E-value: 1.04e-03
                         10        20
                 ....*....|....*....|..
gi 501220578  10 IVGLPNVGKSGLFNALTGAQVA 31
Cdd:PRK05291 220 IAGRPNVGKSSLLNALLGEERA 241
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 9-48 2.06e-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: 38.71  E-value: 2.06e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 501220578   9 GIVGLPNVGKSGLFNALTGAQVAscnypfctidpNVGIVP 48
Cdd:cd04178  120 GVVGYPNVGKSSVINSLKRSRAC-----------NVGATP 148
era PRK00089
GTPase Era; Reviewed
 8-31 2.17e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 39.26  E-value: 2.17e-03
                         10        20
                 ....*....|....*....|....*..
gi 501220578   8 CG---IVGLPNVGKSGLFNALTGAQVA 31
Cdd:PRK00089   5 SGfvaIVGRPNVGKSTLLNALVGQKIS 31
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 9-32 2.51e-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: 38.07  E-value: 2.51e-03
                         10        20
                 ....*....|....*....|....
gi 501220578   9 GIVGLPNVGKSGLFNALTGAQVAS 32
Cdd:cd01859  103 GVVGYPKVGKSSIINALKGRHSAS 126
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
8-31 3.32e-03

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 38.82  E-value: 3.32e-03
                         10        20
                 ....*....|....*....|....*..
gi 501220578   8 CG---IVGLPNVGKSGLFNALTGAQVA 31
Cdd:COG1159    3 SGfvaIVGRPNVGKSTLLNALVGQKVS 29
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 8-31 3.64e-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: 37.83  E-value: 3.64e-03
                         10        20
                 ....*....|....*....|....*..
gi 501220578   8 CG---IVGLPNVGKSGLFNALTGAQVA 31
Cdd:cd04163    3 SGfvaIIGRPNVGKSTLLNALVGQKIS 29
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 10-103 6.63e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 38.62  E-value: 6.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501220578  10 IVGLPNVGKSGLFNALTGAQVASCN-YPFCTIDPnvgivpvidprLETLARISQSqkiiyaDMKFVDIAGLVK--GAASG 86
Cdd:PRK09518 455 LVGRPNVGKSSLLNQLTHEERAVVNdLAGTTRDP-----------VDEIVEIDGE------DWLFIDTAGIKRrqHKLTG 517

                         90
                 ....*....|....*..
gi 501220578  87 AglgnRFLSHIRETHAI 103
Cdd:PRK09518 518 A----EYYSSLRTQAAI 530
PRK11058 PRK11058
GTPase HflX; Provisional
 10-51 7.02e-03

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 38.16  E-value: 7.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 501220578  10 IVGLPNVGKSGLFNALTGAQVASCNYPFCTIDPNVGIVPVID 51
Cdd:PRK11058 202 LVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVAD 243
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
10-31 7.43e-03

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 37.78  E-value: 7.43e-03
                         10        20
                 ....*....|....*....|..
gi 501220578  10 IVGLPNVGKSGLFNALTGAQVA 31
Cdd:COG1161  118 IVGIPNVGKSTLINRLAGKKVA 139
 
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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