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Conserved domains on  [gi|1896926521|ref|WP_186871214|]
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MULTISPECIES: redox-regulated ATPase YchF [Ornithinibacillus]

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] ...
 3-366 0e+00

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


:

Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 738.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   3 LTAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERLNKLTELVNPKKTVPTTFEFTDIAGIVKGASK 82
Cdd:COG0012     1 LKCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  83 GEGLGNQFLSHIRQVDAICQVVRCFVDENITHVSGKVDPIDDIEIINLELILADLETVNKRYQRVEKLAKQKDKDALVEF 162
Cdd:COG0012    81 GEGLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEKRLERLEKKAKSGDKEAKAEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 163 EVLSKLKTGLEEEKPARAIEFTEEQLKIVKGLHLLTSKPMLYVANVGEDEVAdpESNPNVQKVKEYASNEGAEVIVICAR 242
Cdd:COG0012   161 ELLEKLKEHLEEGKPARSLELSEEEKKLLKELQLLTAKPVLYVANVDEDDLA--EGNPYVEKVREYAAKEGAEVVVICAK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 243 IEEEISELDQEEKEMFLDELGITESGLDKLIKASYSLLGLATYFTAGEQEVRAWTFRKGMKAPQAAGIIHSDFERGFIRA 322
Cdd:COG0012   239 IEAELAELDEEERAEFLEELGLEESGLDRLIRAGYDLLGLITFFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFERGFIRA 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1896926521 323 ETVSYDDLVEAGSMTVAREKGKVRLEGKEYIVKDGDVIHFRFNV 366
Cdd:COG0012   319 EVISYDDLIAYGSEAAAKEAGKLRLEGKDYVVQDGDVIHFRFNV 362
 
Name Accession Description Interval E-value
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
 3-366 0e+00

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 738.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   3 LTAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERLNKLTELVNPKKTVPTTFEFTDIAGIVKGASK 82
Cdd:COG0012     1 LKCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  83 GEGLGNQFLSHIRQVDAICQVVRCFVDENITHVSGKVDPIDDIEIINLELILADLETVNKRYQRVEKLAKQKDKDALVEF 162
Cdd:COG0012    81 GEGLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEKRLERLEKKAKSGDKEAKAEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 163 EVLSKLKTGLEEEKPARAIEFTEEQLKIVKGLHLLTSKPMLYVANVGEDEVAdpESNPNVQKVKEYASNEGAEVIVICAR 242
Cdd:COG0012   161 ELLEKLKEHLEEGKPARSLELSEEEKKLLKELQLLTAKPVLYVANVDEDDLA--EGNPYVEKVREYAAKEGAEVVVICAK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 243 IEEEISELDQEEKEMFLDELGITESGLDKLIKASYSLLGLATYFTAGEQEVRAWTFRKGMKAPQAAGIIHSDFERGFIRA 322
Cdd:COG0012   239 IEAELAELDEEERAEFLEELGLEESGLDRLIRAGYDLLGLITFFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFERGFIRA 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1896926521 323 ETVSYDDLVEAGSMTVAREKGKVRLEGKEYIVKDGDVIHFRFNV 366
Cdd:COG0012   319 EVISYDDLIAYGSEAAAKEAGKLRLEGKDYVVQDGDVIHFRFNV 362
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
 5-280 3.88e-178

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: 495.06  E-value: 3.88e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   5 AGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERLNKLTELVNPKKTVPTTFEFTDIAGIVKGASKGE 84
Cdd:cd01900     1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASKGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  85 GLGNQFLSHIRQVDAICQVVRCFVDENITHVSGKVDPIDDIEIINLELILADLETVNKRYQRVEKLAKQKDKDALVEFEV 164
Cdd:cd01900    81 GLGNKFLSHIREVDAIAHVVRCFEDDDITHVEGSVDPVRDIEIINTELILADLETIEKRLERLEKKAKSGDKEAKEELEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 165 LSKLKTGLEEEKPARAIEFTEEQLKIVKGLHLLTSKPMLYVANVGEDEVADPesNPNVQKVKEYASNEGAEVIVICARIE 244
Cdd:cd01900   161 LEKIKEHLEEGKPARTLELTDEEIKILKSLQLLTAKPVIYVANVSEDDLIRG--NNKVLKVREIAAKEGAEVIPISAKLE 238

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1896926521 245 EEISELDQEEKEMFLDELGITESGLDKLIKASYSLL 280
Cdd:cd01900   239 AELAELDEEEAAEFLEELGLEESGLDKLIRAGYELL 274
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 3-366 5.40e-178

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 499.47  E-value: 5.40e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   3 LTAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERLNKLTELVNPKKTVPTTFEFTDIAGIVKGASK 82
Cdd:PTZ00258   22 LKMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDERFDWLCKHFKPKSIVPAQLDITDIAGLVKGASE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  83 GEGLGNQFLSHIRQVDAICQVVRCFVDENITHVSGKVDPIDDIEIINLELILADLETVNKRYQRVEKLAK--QKDKDALV 160
Cdd:PTZ00258  102 GEGLGNAFLSHIRAVDGIYHVVRAFEDEDITHVEGEIDPVRDLEIISSELILKDLEFVEKRLDELTKKRKkkKKKKEEKV 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 161 EFEVLSKLKTGLEEEKPARAIEFTEEQLKIVKGLHLLTSKPMLYVANVGEDEVaDPESNPNVQKVKEY-ASNEGAEVIVI 239
Cdd:PTZ00258  182 ELDVLKKVLEWLEEGKPVRDGDWTDKEIEILNEYQLLTAKPMIYLVNMSEKDF-IRQKNKWLAKIKEWvGEKGGGPIIPY 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 240 CARIEEEISEL-DQEEKEMFLDELGITESGLDKLIKASYSLLGLATYFTAGEQEVRAWTFRKGMKAPQAAGIIHSDFERG 318
Cdd:PTZ00258  261 SAEFEEELAELgSEEERKEYLEEYGIKQSMLDKIIKTGYKLLNLIHFFTAGPDEVRCWTIQKGTKAPQAAGVIHSDFEKG 340

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1896926521 319 FIRAETVSYDDLVEAGSMTVAREKGKVRLEGKEYIVKDGDVIHFRFNV 366
Cdd:PTZ00258  341 FICAEVMKYEDFLELGSEAAVKAEGKYRQEGKDYVVQDGDIIFFKFNV 388
TIGR00092 TIGR00092
GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in ...
 1-366 2.85e-141

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: 405.31  E-value: 2.85e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   1 MALTAGIVGLPNVGKSTLFNAITQA-GAEAANYPFATIDPNVGMVEVPDERLNKLTELVNPKKTVPTTFEFTDIAGIVKG 79
Cdd:TIGR00092   1 MGLSGGIVGLPNVGKSTLFAATTNLlGNEAANPPFTTIEPNAGVVNPSDPRLDLLAIYIKPEKVPPTTTEFVDIAGLVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  80 ASKGEGLGNQFLSHIRQVDAICQVVRCFVDENITHVSGKVDPIDDIEIINLELILADLETVNKRYQRVEKLAKQKdKDAL 159
Cdd:TIGR00092  81 ASKGEGLGNQFLANIREVDIIQHVVRCFEDDIIHHVGNVDDPRDDFEIIDEELLKADEFLVEKRIGRSKKSAEGG-KDKK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 160 VEFEVLSKLKTGLEEEKPARAIEFTEEQLKIVKGLHLLTSKPMLYVANVGEDEVADpESNPNVQKVKEYA--SNEGAEVI 237
Cdd:TIGR00092 160 EELLLLEIILPLLNGGQMARHVDLSKEELILIKSLNLLTKKPIILIANVSEDYLRN-LNNNYLLIVEWIAaySKGDPKVV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 238 VICARIEEEISELDQEEKEMFLDELGITES-GLDKLIKASYSLLGLATYFTAGEQEVRAWTFRKGMKAPQAAGIIHSDFE 316
Cdd:TIGR00092 239 FVCALEESELSELDDEERQEFLQKLGLTESaGLNIIIRARYKLLLLSFFFTGGKEEVRAWTRKGGWAAPQAAGIIHTDFE 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1896926521 317 RGFIRAETVSYDDLVEAGSMTVAREKGKVRLEGKEYIVKDGDVIHFRFNV 366
Cdd:TIGR00092 319 TGFIAAEVISWDDFIYKKSSQGAKKGGLMRLEGKYYVVDDGDVLFFAFNV 368
YchF-GTPase_C pfam06071
Protein of unknown function (DUF933); This domain is found at the C terminus of the YchF ...
 282-363 3.03e-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: 183.33  E-value: 3.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 282 LATYFTAGEQEVRAWTFRKGMKAPQAAGIIHSDFERGFIRAETVSYDDLVEAGSMTVAREKGKVRLEGKEYIVKDGDVIH 361
Cdd:pfam06071   1 LITFFTAGPKEVRAWTIRKGTTAPQAAGVIHTDFEKGFIRAEVISYDDLIEYGSEAAAKEAGKLRLEGKDYVVQDGDIIH 80


                  ..
gi 1896926521 362 FR 363
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] ...
 3-366 0e+00

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 738.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   3 LTAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERLNKLTELVNPKKTVPTTFEFTDIAGIVKGASK 82
Cdd:COG0012     1 LKCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  83 GEGLGNQFLSHIRQVDAICQVVRCFVDENITHVSGKVDPIDDIEIINLELILADLETVNKRYQRVEKLAKQKDKDALVEF 162
Cdd:COG0012    81 GEGLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEKRLERLEKKAKSGDKEAKAEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 163 EVLSKLKTGLEEEKPARAIEFTEEQLKIVKGLHLLTSKPMLYVANVGEDEVAdpESNPNVQKVKEYASNEGAEVIVICAR 242
Cdd:COG0012   161 ELLEKLKEHLEEGKPARSLELSEEEKKLLKELQLLTAKPVLYVANVDEDDLA--EGNPYVEKVREYAAKEGAEVVVICAK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 243 IEEEISELDQEEKEMFLDELGITESGLDKLIKASYSLLGLATYFTAGEQEVRAWTFRKGMKAPQAAGIIHSDFERGFIRA 322
Cdd:COG0012   239 IEAELAELDEEERAEFLEELGLEESGLDRLIRAGYDLLGLITFFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFERGFIRA 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1896926521 323 ETVSYDDLVEAGSMTVAREKGKVRLEGKEYIVKDGDVIHFRFNV 366
Cdd:COG0012   319 EVISYDDLIAYGSEAAAKEAGKLRLEGKDYVVQDGDVIHFRFNV 362
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
 5-280 3.88e-178

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: 495.06  E-value: 3.88e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   5 AGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERLNKLTELVNPKKTVPTTFEFTDIAGIVKGASKGE 84
Cdd:cd01900     1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASKGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  85 GLGNQFLSHIRQVDAICQVVRCFVDENITHVSGKVDPIDDIEIINLELILADLETVNKRYQRVEKLAKQKDKDALVEFEV 164
Cdd:cd01900    81 GLGNKFLSHIREVDAIAHVVRCFEDDDITHVEGSVDPVRDIEIINTELILADLETIEKRLERLEKKAKSGDKEAKEELEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 165 LSKLKTGLEEEKPARAIEFTEEQLKIVKGLHLLTSKPMLYVANVGEDEVADPesNPNVQKVKEYASNEGAEVIVICARIE 244
Cdd:cd01900   161 LEKIKEHLEEGKPARTLELTDEEIKILKSLQLLTAKPVIYVANVSEDDLIRG--NNKVLKVREIAAKEGAEVIPISAKLE 238

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1896926521 245 EEISELDQEEKEMFLDELGITESGLDKLIKASYSLL 280
Cdd:cd01900   239 AELAELDEEEAAEFLEELGLEESGLDKLIRAGYELL 274
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 3-366 5.40e-178

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 499.47  E-value: 5.40e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   3 LTAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERLNKLTELVNPKKTVPTTFEFTDIAGIVKGASK 82
Cdd:PTZ00258   22 LKMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDERFDWLCKHFKPKSIVPAQLDITDIAGLVKGASE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  83 GEGLGNQFLSHIRQVDAICQVVRCFVDENITHVSGKVDPIDDIEIINLELILADLETVNKRYQRVEKLAK--QKDKDALV 160
Cdd:PTZ00258  102 GEGLGNAFLSHIRAVDGIYHVVRAFEDEDITHVEGEIDPVRDLEIISSELILKDLEFVEKRLDELTKKRKkkKKKKEEKV 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 161 EFEVLSKLKTGLEEEKPARAIEFTEEQLKIVKGLHLLTSKPMLYVANVGEDEVaDPESNPNVQKVKEY-ASNEGAEVIVI 239
Cdd:PTZ00258  182 ELDVLKKVLEWLEEGKPVRDGDWTDKEIEILNEYQLLTAKPMIYLVNMSEKDF-IRQKNKWLAKIKEWvGEKGGGPIIPY 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 240 CARIEEEISEL-DQEEKEMFLDELGITESGLDKLIKASYSLLGLATYFTAGEQEVRAWTFRKGMKAPQAAGIIHSDFERG 318
Cdd:PTZ00258  261 SAEFEEELAELgSEEERKEYLEEYGIKQSMLDKIIKTGYKLLNLIHFFTAGPDEVRCWTIQKGTKAPQAAGVIHSDFEKG 340

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1896926521 319 FIRAETVSYDDLVEAGSMTVAREKGKVRLEGKEYIVKDGDVIHFRFNV 366
Cdd:PTZ00258  341 FICAEVMKYEDFLELGSEAAVKAEGKYRQEGKDYVVQDGDIIFFKFNV 388
TIGR00092 TIGR00092
GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in ...
 1-366 2.85e-141

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: 405.31  E-value: 2.85e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   1 MALTAGIVGLPNVGKSTLFNAITQA-GAEAANYPFATIDPNVGMVEVPDERLNKLTELVNPKKTVPTTFEFTDIAGIVKG 79
Cdd:TIGR00092   1 MGLSGGIVGLPNVGKSTLFAATTNLlGNEAANPPFTTIEPNAGVVNPSDPRLDLLAIYIKPEKVPPTTTEFVDIAGLVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  80 ASKGEGLGNQFLSHIRQVDAICQVVRCFVDENITHVSGKVDPIDDIEIINLELILADLETVNKRYQRVEKLAKQKdKDAL 159
Cdd:TIGR00092  81 ASKGEGLGNQFLANIREVDIIQHVVRCFEDDIIHHVGNVDDPRDDFEIIDEELLKADEFLVEKRIGRSKKSAEGG-KDKK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 160 VEFEVLSKLKTGLEEEKPARAIEFTEEQLKIVKGLHLLTSKPMLYVANVGEDEVADpESNPNVQKVKEYA--SNEGAEVI 237
Cdd:TIGR00092 160 EELLLLEIILPLLNGGQMARHVDLSKEELILIKSLNLLTKKPIILIANVSEDYLRN-LNNNYLLIVEWIAaySKGDPKVV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 238 VICARIEEEISELDQEEKEMFLDELGITES-GLDKLIKASYSLLGLATYFTAGEQEVRAWTFRKGMKAPQAAGIIHSDFE 316
Cdd:TIGR00092 239 FVCALEESELSELDDEERQEFLQKLGLTESaGLNIIIRARYKLLLLSFFFTGGKEEVRAWTRKGGWAAPQAAGIIHTDFE 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1896926521 317 RGFIRAETVSYDDLVEAGSMTVAREKGKVRLEGKEYIVKDGDVIHFRFNV 366
Cdd:TIGR00092 319 TGFIAAEVISWDDFIYKKSSQGAKKGGLMRLEGKYYVVDDGDVLFFAFNV 368
YchF-GTPase_C pfam06071
Protein of unknown function (DUF933); This domain is found at the C terminus of the YchF ...
 282-363 3.03e-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: 183.33  E-value: 3.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 282 LATYFTAGEQEVRAWTFRKGMKAPQAAGIIHSDFERGFIRAETVSYDDLVEAGSMTVAREKGKVRLEGKEYIVKDGDVIH 361
Cdd:pfam06071   1 LITFFTAGPKEVRAWTIRKGTTAPQAAGVIHTDFEKGFIRAEVISYDDLIEYGSEAAAKEAGKLRLEGKDYVVQDGDIIH 80


                  ..
gi 1896926521 362 FR 363
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 ...
 280-364 1.52e-55

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: 176.57  E-value: 1.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 280 LGLATYFTAGEQEVRAWTFRKGMKAPQAAGIIHSDFERGFIRAETVSYDDLVEAGSMTVAREKGKVRLEGKEYIVKDGDV 359
Cdd:cd04867     1 LNLITFFTAGPDEVRAWTIRKGTKAPQAAGVIHTDFEKGFIRAEVIKYDDLKELGSEAAAKEAGKYRQEGKDYVVQDGDI 80


                  ....*
gi 1896926521 360 IHFRF 364
Cdd:cd04867    81 IHFKF 85
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 3-360 1.58e-45

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 160.36  E-value: 1.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   3 LTAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGM----VEVP----DERLNKLTEL-VNPKKTVPTtfEFTDI 73
Cdd:PRK09602    2 ITIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayvrVECPckelGVKCNPRNGKcIDGTRFIPV--ELIDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  74 AGIVKGASKGEGLGNQFLSHIRQVDAICQVvrcfVDenithVSGKV------------DPIDDIEIINLELILADLETVN 141
Cdd:PRK09602   80 AGLVPGAHEGRGLGNQFLDDLRQADALIHV----VD-----ASGSTdeegnpvepgshDPVEDIKFLEEELDMWIYGILE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 142 KRYQRVEKLAKQKDKDALVEF-EVLSKLKTG--------LEEEKPARAIEFTEEQL-KIVKGLhLLTSKPMLYVANvged 211
Cdd:PRK09602  151 KNWEKFSRKAQAEKFDIEEALaEQLSGLGINeehvkealRELGLPEDPSKWTDEDLlELAREL-RKISKPMVIAAN---- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 212 eVAD-PESNPNVQKVKEyasNEGAEVIVICARIE---------------------EEISELDQEEKEM------FLDELG 263
Cdd:PRK09602  226 -KADlPPAEENIERLKE---EKYYIVVPTSAEAElalrraakaglidyipgdsdfEILGELSEKQKKAleyireVLKKYG 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 264 ITesGLDKLI-KASYSLLGL-ATY-------FTAGEQEV--RAWTFRKGMKAPQAAGIIHSDFERGFIRAetvsyddlVE 332
Cdd:PRK09602  302 GT--GVQEAInTAVFDLLDMiVVYpvedenkLTDKKGNVlpDAFLLPKGSTARDLAYKIHTDIGEGFLYA--------ID 371

                         410       420
                  ....*....|....*....|....*...
gi 1896926521 333 AgsmtvareKGKVRLeGKEYIVKDGDVI 360
Cdd:PRK09602  372 A--------RTKRRI-GEDYELKDGDVI 390
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 6-252 4.64e-38

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: 138.51  E-value: 4.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   6 GIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGM----VEVPDERLN-----KLTELVNPKKTVPTtfEFTDIAGI 76
Cdd:cd01899     2 GLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVgyvrVECPCKELGvscnpRYGKCIDGKRYVPV--ELIDVAGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  77 VKGASKGEGLGNQFLSHIRQVDAICQVvrcfVD-------ENITHVSGKVDPIDDIEIINLELILADLETVNKRYQRVEK 149
Cdd:cd01899    80 VPGAHEGKGLGNQFLDDLRDADVLIHV----VDasggtdaEGNGVETGGYDPLEDIEFLENEIDMWIYGILERNWEKIVR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 150 LAKQKDKDALvefEVLSKLKTGL------------EEEKPARAIEFTEEQLKIVKGLHLLTSKPMLYVANvgedeVAD-P 216
Cdd:cd01899   156 KAKAEKTDIV---EALSEQLSGFgvnedvviealeELELPADLSKWDDEDLLRLARELRKRRKPMVIAAN-----KADiP 227

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1896926521 217 ESNPNVQKVKEYasNEGAEVIVICARIEEEISELDQ 252
Cdd:cd01899   228 DAEENISKLRLK--YPDEIVVPTSAEAELALRRAAK 261
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 6-142 3.30e-33

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


Pssm-ID: 206668 [Multi-domain]  Cd Length: 167  Bit Score: 121.35  E-value: 3.30e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   6 GIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDerlnkltelvnpkktvPTTFEFTDIAGIVKGASKGEG 85
Cdd:cd01881     1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGD----------------GVDIQIIDLPGLLDGASEGRG 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1896926521  86 LGNQFLSHIRQVDAICQVVRCFVDENIthvsgkvDPIDDIEIINLELILADLETVNK 142
Cdd:cd01881    65 LGEQILAHLYRSDLILHVIDASEDCVG-------DPLEDQKTLNEEVSGSFLFLKNK 114
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 5-174 1.09e-31

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: 117.53  E-value: 1.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   5 AGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERlnkltelvnpkktvptTFEFTDIAGIVKGASKGE 84
Cdd:cd01898     3 VGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGR----------------SFVIADIPGLIEGASEGK 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  85 GLGNQFLSHI-RqvdaiCQVVRCFVDenithVSGKVDPIDDIEIINLELIL----------------ADLETVNKRYQRV 147
Cdd:cd01898    67 GLGHRFLRHIeR-----TRVLLHVID-----LSGEDDPVEDYETIRNELEAynpglaekprivvlnkIDLLDAEERFEKL 136

                         170       180
                  ....*....|....*....|....*..
gi 1896926521 148 EKLAKQKDKDALveFEVLSKLKTGLEE 174
Cdd:cd01898   137 KELLKELKGKKV--FPISALTGEGLDE 161
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 6-174 2.17e-29

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: 115.60  E-value: 2.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   6 GIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERlnkltelvnpkktvptTFEFTDIAGIVKGASKGEG 85
Cdd:TIGR02729 161 GLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGR----------------SFVIADIPGLIEGASEGAG 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  86 LGNQFLSHI-RqvdaiCQVVRCFVDenITHVSGKvDPIDDIEIINLEL------------ILA----DLETVNKRYQRVE 148
Cdd:TIGR02729 225 LGHRFLKHIeR-----TRVLLHLID--ISPEDGS-DPVEDYEIIRNELkkyspelaekprIVVlnkiDLLDEEELEELLK 296

                         170       180
                  ....*....|....*....|....*.
gi 1896926521 149 KLAKQKDKDAlveFEVLSKLKTGLEE 174
Cdd:TIGR02729 297 ELKKELGKPV---FPISALTGEGLDE 319
obgE PRK12297
GTPase CgtA; Reviewed
 5-142 2.82e-29

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 117.12  E-value: 2.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   5 AGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERlnkltelvnpkktvptTFEFTDIAGIVKGASKGE 84
Cdd:PRK12297  161 VGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGR----------------SFVMADIPGLIEGASEGV 224

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896926521  85 GLGNQFLSHIRqvdaicqvvRCFVdenITHV---SGKV--DPIDDIEIINLELILADLETVNK 142
Cdd:PRK12297  225 GLGHQFLRHIE---------RTRV---IVHVidmSGSEgrDPIEDYEKINKELKLYNPRLLER 275
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
 5-217 7.68e-28

GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, chromosome partitioning, Replication, recombination, and repair];


Pssm-ID: 440302 [Multi-domain]  Cd Length: 343  Bit Score: 111.61  E-value: 7.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   5 AGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERlnkltelvnpkktvptTFEFTDIAGIVKGASKGE 84
Cdd:COG0536   160 VGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGR----------------SFVIADIPGLIEGASEGA 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  85 GLGNQFLSHIRqvdaicqvvRC-----FVDenITHVSGKvDPIDDIEIINLELiladletvnKRYQrvEKLAkqkDKDAL 159
Cdd:COG0536   224 GLGHRFLRHIE---------RTrvllhVVD--AAPLDGR-DPVEDYEIIRNEL---------EAYS--PELA---EKPRI 277

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896926521 160 VefeVLSKLKTGLEEEKPARAIEFTEEQLKIV-------KGLHLLTSKPMLYVANVGEDEVADPE 217
Cdd:COG0536   278 V---VLNKIDLLDAEELEELKAELEKLGGPVFpisavtgEGLDELLYALAELLEELRAEEAEEEE 339
obgE PRK12299
GTPase CgtA; Reviewed
 5-132 7.21e-26

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 105.92  E-value: 7.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   5 AGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERlnkltelvnpkktvptTFEFTDIAGIVKGASKGE 84
Cdd:PRK12299  161 VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYK----------------SFVIADIPGLIEGASEGA 224

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1896926521  85 GLGNQFLSHI-RqvdaiCQVVRCFVDenITHvsgkVDPIDDIEIINLEL 132
Cdd:PRK12299  225 GLGHRFLKHIeR-----TRLLLHLVD--IEA----VDPVEDYKTIRNEL 262
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 4-142 2.06e-25

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: 98.85  E-value: 2.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   4 TAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERlnkltelvnpkktvpttFEFTDIAGIVKGASKG 83
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQ-----------------IILVDTPGLIEGASEG 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  84 EGLGNQFLSHIRqVDAICQVVRcfvdenithVSGKVDPID-DIEIINLELILADLETVNK 142
Cdd:pfam01926  64 EGLGRAFLAIIE-ADLILFVVD---------SEEGITPLDeELLELLRENKKPIILVLNK 113
obgE PRK12298
GTPase CgtA; Reviewed
 6-186 1.63e-21

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 94.55  E-value: 1.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   6 GIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERlnkltelvnpkktvptTFEFTDIAGIVKGASKGEG 85
Cdd:PRK12298  163 GLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDER----------------SFVVADIPGLIEGASEGAG 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  86 LGNQFLSHIrqvdAICQVVRCFVDenithvsgkVDPIDDIEII-NLELILADLETVNkryqrvEKLAkqkDKDALVefeV 164
Cdd:PRK12298  227 LGIRFLKHL----ERCRVLLHLID---------IAPIDGSDPVeNARIIINELEKYS------PKLA---EKPRWL---V 281

                         170       180
                  ....*....|....*....|..
gi 1896926521 165 LSKLKTGLEEEKPARAIEFTEE 186
Cdd:PRK12298  282 FNKIDLLDEEEAEERAKAIVEA 303
obgE PRK12296
GTPase CgtA; Reviewed
 6-132 1.27e-19

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 89.93  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   6 GIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDerlnkltelvnpkktvpTTFEFTDIAGIVKGASKGEG 85
Cdd:PRK12296  163 GLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQAGD-----------------TRFTVADVPGLIPGASEGKG 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1896926521  86 LGNQFLSHIRQVDAICQVVRCFVDEnithvSGKvDPIDDIEIINLEL 132
Cdd:PRK12296  226 LGLDFLRHIERCAVLVHVVDCATLE-----PGR-DPLSDIDALEAEL 266
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
4-363 4.75e-17

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 81.38  E-value: 4.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   4 TAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDerlnkltelvnpkktvpTTFEFTDIAGIVKGASKG 83
Cdd:COG1163    65 TVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLEYKG-----------------AKIQILDVPGLIEGAASG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521  84 EGLGNQFLSHIRQVDAICQVVRCFvdenithvsgkvdpiddiEIINLELILADLE----TVNKRYQRVEklAKQKDKDAL 159
Cdd:COG1163   128 KGRGKEVLSVVRNADLILIVLDVF------------------ELEQYDVLKEELYdagiRLNKPPPDVT--IEKKGKGGI 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 160 vefEVLSKLKTGLEEEKpARAI---------------EFTEEQLkiVKGL-HLLTSKPMLYVANVGedEVADPESnpnVQ 223
Cdd:COG1163   188 ---RVNSTGKLDLDEED-IKKIlreygivnadvlireDVTLDDL--IDALmGNRVYKPAIVVVNKI--DLADEEY---VE 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 224 KVKEYASnEGAEVIVICARIEEEISELdqeeKEMFLDELGItesgldklikasysllglatyftageqeVRAWTFRKGMK 303
Cdd:COG1163   257 ELKSKLP-DGVPVIFISAEKGIGLEEL----KEEIFEELGL----------------------------IRVYLKPPGGK 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 304 APQ--------------AAGIIHSDFERGF----IRAETVSYDDlveagsMTVarekgkvrleGKEYIVKDGDV--IHFR 363
Cdd:COG1163   304 ADMeeplilrkgstvgdVCEKIHRDFVERFryarVWGKSAKHPG------QRV----------GLDHVLEDGDIveIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 4-110 1.57e-16

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: 77.97  E-value: 1.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   4 TAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERLNKLtelvnpkktvpttfeftDIAGIVKGASKG 83
Cdd:cd01896     2 RVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLL-----------------DLPGIIEGASDG 64

                          90       100
                  ....*....|....*....|....*..
gi 1896926521  84 EGLGNQFLSHIRQVDAICQVVRCFVDE 110
Cdd:cd01896    65 KGRGRQVIAVARTADLILIVLDATKPE 91
TGS cd01616
TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; ...
 284-363 5.58e-13

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: 63.01  E-value: 5.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 284 TYFTAGEQEVRAWTFRKGMKAPQAAGIIHSDFERGFIRAETVSyddlveagsmtvarekgkvRLEGKEYIVKDGDVIHFR 363
Cdd:cd01616     1 EVFTVGKTPGTVFVMNKGATAYSCAMHLHEDYCRKSILALVDG-------------------QLWDMYYPLTKGDEIKFL 61
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 4-50 5.10e-09

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 57.40  E-value: 5.10e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1896926521   4 TAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDER 50
Cdd:COG2262   201 TVALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRRLELPDGR 247
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 6-106 7.17e-09

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: 54.17  E-value: 7.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   6 GIVGLPNVGKSTLFNAIT-QAGAEAANYPFATIDPNVGMVEVPDERlnkltelvnpkktvptTFEFTDIAGIVKGASKGE 84
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLgQNVGIVSPIPGTTRDPVRKEWELLPLG----------------PVVLIDTPGLDEEGGLGR 64

                          90       100
                  ....*....|....*....|..
gi 1896926521  85 GLGNQFLSHIRQVDAICQVVRC 106
Cdd:cd00880    65 ERVEEARQVADRADLVLLVVDS 86
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
 4-50 1.74e-08

GTP-binding protein HflX; This protein family is one of a number of homologous small, well-conserved GTP-binding proteins with pleiotropic effects. Bacterial members are designated HflX, following the naming convention in Escherichia coli where HflX is encoded immediately downstream of the RNA chaperone Hfq, and immediately upstream of HflKC, a membrane-associated protease pair with an important housekeeping function. Over large numbers of other bacterial genomes, the pairing with hfq is more significant than with hflK and hlfC. The gene from Homo sapiens in this family has been named PGPL (pseudoautosomal GTP-binding protein-like). [Unknown function, General]


Pssm-ID: 274455 [Multi-domain]  Cd Length: 351  Bit Score: 55.56  E-value: 1.74e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1896926521   4 TAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDER 50
Cdd:TIGR03156 191 TVALVGYTNAGKSTLFNALTGADVYAADQLFATLDPTTRRLDLPDGG 237
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 4-50 2.50e-08

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: 53.62  E-value: 2.50e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1896926521   4 TAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDER 50
Cdd:cd01878    43 TVALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTTRRIKLPGGR 89
TGS_Obg cd04938
TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases ...
 284-363 2.73e-08

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: 50.52  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521 284 TYFTAGEQEVRAWTFRKGMKAPQAAGIIHSDFERGFIRAETVSYddlveagsmtvarekgkVRLEGKEYIVKDGDVIHFR 363
Cdd:cd04938    15 TNGSGNSVFRDCVLVKKGTTVKDFANKIHTDLEKGFINAEGIGG-----------------RRLEGEDYILQDNDVVKFT 77
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 7-50 1.43e-07

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: 50.64  E-value: 1.43e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1896926521   7 IVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDER 50
Cdd:cd01897     5 IAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLR 48
PRK11058 PRK11058
GTPase HflX; Provisional
 4-48 1.52e-07

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 52.80  E-value: 1.52e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1896926521   4 TAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPD 48
Cdd:PRK11058  199 TVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVAD 243
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
7-50 3.63e-07

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 51.37  E-value: 3.63e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1896926521   7 IVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDER 50
Cdd:COG1084   165 VAGYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGR 208
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-52 4.96e-07

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 51.66  E-value: 4.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1896926521   1 MALTAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERLN 52
Cdd:COG0370     2 KMITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIE 53
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 7-51 6.27e-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: 6.27e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1896926521   7 IVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERL 51
Cdd:cd01879     2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEI 46
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 3-42 4.21e-06

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: 46.29  E-value: 4.21e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1896926521   3 LTAGIVGLPNVGKSTLFNAITQAGAEAANYPFATIDPNVG 42
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEG 40
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
1-24 2.28e-05

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 46.17  E-value: 2.28e-05
                          10        20
                  ....*....|....*....|....
gi 1896926521   1 MALTAGIVGLPNVGKSTLFNAITQ 24
Cdd:COG1160     1 MSPVVAIVGRPNVGKSTLFNRLTG 24
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
 9-75 2.83e-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: 45.89  E-value: 2.83e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896926521   9 GLPNVGKSTLFNAITQAGAEAANYPFATIDPNVGMVEVPDERLnKLTELvnpkktvPTTFEFTDIAG 75
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDI-EIVDL-------PGIYSLTTFSL 59
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 6-104 3.70e-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: 43.60  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   6 GIVGLPNVGKSTLFNAIT-QAGAEAANYPFATIDPNVGMVEVPDERLNkltelvnpkktvpttFEFTDIAGIVKGAskGE 84
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLgGEVGEVSDVPGTTRDPDVYVKELDKGKVK---------------LVLVDTPGLDEFG--GL 63

                          90       100
                  ....*....|....*....|
gi 1896926521  85 GLGNQFLSHIRQVDAICQVV 104
Cdd:cd00882    64 GREELARLLLRGADLILLVV 83
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 7-23 5.60e-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: 42.81  E-value: 5.60e-05
                          10
                  ....*....|....*..
gi 1896926521   7 IVGLPNVGKSTLFNAIT 23
Cdd:cd01894     2 IVGRPNVGKSTLFNRLT 18
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 2-33 7.97e-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: 7.97e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1896926521   2 ALTAGIVGLPNVGKSTLFNAITQAG-AEAANYP 33
Cdd:cd01856   115 PLRAMVVGIPNVGKSTLINRLRGKKvAKVGNKP 147
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 7-114 9.36e-05

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: 42.42  E-value: 9.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   7 IVGLPNVGKSTLFNAITqaGAEAA---NYPFATIDPnvgmVEVPDERLNKltelvnpkktvptTFEFTDIAGIVKGASKG 83
Cdd:cd01895     7 IIGRPNVGKSSLLNALL--GEERVivsDIAGTTRDS----IDVPFEYDGQ-------------KYTLIDTAGIRKKGKVT 67

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1896926521  84 EGLgnQFLSHIRQVDAI--CQVVRCFVD--ENITH 114
Cdd:cd01895    68 EGI--EKYSVLRTLKAIerADVVLLVLDasEGITE 100
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 7-24 1.09e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 43.89  E-value: 1.09e-04
                          10
                  ....*....|....*...
gi 1896926521   7 IVGLPNVGKSTLFNAITQ 24
Cdd:PRK00093    6 IVGRPNVGKSTLFNRLTG 23
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 7-30 1.87e-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: 43.13  E-value: 1.87e-04
                          10        20
                  ....*....|....*....|....
gi 1896926521   7 IVGLPNVGKSTLFNAItqAGAEAA 30
Cdd:COG0486   218 IVGRPNVGKSSLLNAL--LGEERA 239
GTPase_EngA TIGR03594
ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase ...
 7-23 2.54e-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: 42.82  E-value: 2.54e-04
                          10
                  ....*....|....*..
gi 1896926521   7 IVGLPNVGKSTLFNAIT 23
Cdd:TIGR03594   3 IVGRPNVGKSTLFNRLT 19
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
2-47 4.14e-04

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 42.40  E-value: 4.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1896926521   2 ALTAGIVGLPNVGKSTLFNAITQAGAEAANYP----------FATIDPNVGMVEVP 47
Cdd:PRK09554    3 KLTIGLIGNPNSGKTTLFNQLTGARQRVGNWAgvtverkegqFSTTDHQVTLVDLP 58
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 2-27 4.21e-04

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: 40.64  E-value: 4.21e-04
                          10        20
                  ....*....|....*....|....*.
gi 1896926521   2 ALTAGIVGLPNVGKSTLFNAITQAGA 27
Cdd:cd04178   116 SITVGVVGYPNVGKSSVINSLKRSRA 141
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 7-30 5.18e-04

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


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 40.17  E-value: 5.18e-04
                          10        20
                  ....*....|....*....|....
gi 1896926521   7 IVGLPNVGKSTLFNAItqAGAEAA 30
Cdd:cd04164     8 IAGKPNVGKSSLLNAL--AGRDRA 29
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
7-104 8.53e-04

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 41.16  E-value: 8.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   7 IVGLPNVGKSTLFNAItqAGAE---AANYPFATIDPnvgmVEVPDERLNKltelvnpkktvptTFEFTDIAGIVKGASKG 83
Cdd:COG1160   180 IVGRPNVGKSSLINAL--LGEErviVSDIAGTTRDS----IDTPFERDGK-------------KYTLIDTAGIRRKGKVD 240

                          90       100
                  ....*....|....*....|...
gi 1896926521  84 EGLgnQFLSHIRQVDAI--CQVV 104
Cdd:COG1160   241 EGI--EKYSVLRTLRAIerADVV 261
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 6-98 9.38e-04

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: 39.28  E-value: 9.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   6 GIVGLPNVGKSTLFNAITQ-AGAEAANYPFATIDPNVGMVEVpderlnkltelvnpkKTVPTTFEFTDIAGIVKGASKGE 84
Cdd:TIGR00231   5 VIVGHPNVGKSTLLNSLLGnKGSITEYYPGTTRNYVTTVIEE---------------DGKTYKFNLLDTAGQEDYDAIRR 69

                          90
                  ....*....|....
gi 1896926521  85 GLGNQFLSHIRQVD 98
Cdd:TIGR00231  70 LYYPQVERSLRVFD 83
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
7-30 1.20e-03

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 40.48  E-value: 1.20e-03
                          10        20
                  ....*....|....*....|....
gi 1896926521   7 IVGLPNVGKSTLFNAItqAGAEAA 30
Cdd:PRK05291  220 IAGRPNVGKSSLLNAL--LGEERA 241
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 7-30 1.66e-03

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


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 39.77  E-value: 1.66e-03
                          10        20
                  ....*....|....*....|....
gi 1896926521   7 IVGLPNVGKSTLFNAItqAGAEAA 30
Cdd:pfam12631  99 IVGKPNVGKSSLLNAL--LGEERA 120
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 7-22 1.74e-03

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


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 38.60  E-value: 1.74e-03
                          10
                  ....*....|....*.
gi 1896926521   7 IVGLPNVGKSTLFNAI 22
Cdd:cd04163     8 IIGRPNVGKSTLLNAL 23
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 7-104 4.80e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 38.88  E-value: 4.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896926521   7 IVGLPNVGKSTLFNAITqaGAE---AANYPFATIDPnvgmVEVPDERLNKltelvnpkktvptTFEFTDIAGIVKGASKG 83
Cdd:PRK00093  178 IIGRPNVGKSSLINALL--GEErviVSDIAGTTRDS----IDTPFERDGQ-------------KYTLIDTAGIRRKGKVT 238

                          90       100
                  ....*....|....*....|...
gi 1896926521  84 EGLgnQFLSHIRQVDAI--CQVV 104
Cdd:PRK00093  239 EGV--EKYSVIRTLKAIerADVV 259
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
7-22 6.15e-03

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 38.05  E-value: 6.15e-03
                          10
                  ....*....|....*.
gi 1896926521   7 IVGLPNVGKSTLFNAI 22
Cdd:COG1159     8 IVGRPNVGKSTLLNAL 23
era PRK00089
GTPase Era; Reviewed
 7-22 7.23e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 37.72  E-value: 7.23e-03
                          10
                  ....*....|....*.
gi 1896926521   7 IVGLPNVGKSTLFNAI 22
Cdd:PRK00089   10 IVGRPNVGKSTLLNAL 25
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 3-22 8.98e-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: 36.21  E-value: 8.98e-03
                          10        20
                  ....*....|....*....|
gi 1896926521   3 LTAGIVGLPNVGKSTLFNAI 22
Cdd:cd01849    92 IRVGVVGLPNVGKSSFINAL 111
 
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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