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Conserved domains on  [gi|76677911|ref|NP_001029099|]
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obg-like ATPase 1 [Rattus norvegicus]

Protein Classification

YchF/Obg family ATPase( domain architecture ID 11488321)

YchF/Obg family ATPase with similarity to bacterial ribosome-binding ATPase YchF and eukaryotic Obg-like ATPase 1

EC:  3.6.-.-
Gene Ontology:  GO:0016887|GO:0005524|GO:0005525|GO:0032555
PubMed:  21527254|11916378
SCOP:  4004039

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 1-390 0e+00

GTP-binding protein; Provisional


:

Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 615.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911    1 MPPKKGgDGLKPPPIIGRFGTSLKIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFLCQCHKP 80
Cdd:PTZ00258   1 MPPKKK-MEEEKKVLLGRPGNNLKMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDERFDWLCKHFKP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   81 ASKIPAFLNVVDIAGLVKGAHNGQGLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMI 160
Cdd:PTZ00258  80 KSIVPAQLDITDIAGLVKGASEGEGLGNAFLSHIRAVDGIYHVVRAFEDEDITHVEGEIDPVRDLEIISSELILKDLEFV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  161 GPIIDKLEKvaVRGGDKKLK---PEYDIMCKVKSWVIDqKKPVRFYhDWNDKEIEVLNKHLLLTSKPMVYLVNLSEKDYI 237
Cdd:PTZ00258 160 EKRLDELTK--KRKKKKKKKeekVELDVLKKVLEWLEE-GKPVRDG-DWTDKEIEILNEYQLLTAKPMIYLVNMSEKDFI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  238 RKKNKWLIKIKEWVDKSDPGALvIPFSGALELKLQEL-SAEERQKYL-EANMTQSALPKIIKAGFAALQLEYFFTAGPDE 315
Cdd:PTZ00258 236 RQKNKWLAKIKEWVGEKGGGPI-IPYSAEFEEELAELgSEEERKEYLeEYGIKQSMLDKIIKTGYKLLNLIHFFTAGPDE 314

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76677911  316 VRAWTIRKGTKAPQAAGKIHTDFEKGFIMAEVMKYDDFKDEGSENAVKAAGKYRQQGRNYIVEDGDIIFFKFNTP 390
Cdd:PTZ00258 315 VRCWTIQKGTKAPQAAGVIHSDFEKGFICAEVMKYEDFLELGSEAAVKAEGKYRQEGKDYVVQDGDIIFFKFNVS 389
 
Name Accession Description Interval E-value
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 1-390 0e+00

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 615.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911    1 MPPKKGgDGLKPPPIIGRFGTSLKIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFLCQCHKP 80
Cdd:PTZ00258   1 MPPKKK-MEEEKKVLLGRPGNNLKMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDERFDWLCKHFKP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   81 ASKIPAFLNVVDIAGLVKGAHNGQGLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMI 160
Cdd:PTZ00258  80 KSIVPAQLDITDIAGLVKGASEGEGLGNAFLSHIRAVDGIYHVVRAFEDEDITHVEGEIDPVRDLEIISSELILKDLEFV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  161 GPIIDKLEKvaVRGGDKKLK---PEYDIMCKVKSWVIDqKKPVRFYhDWNDKEIEVLNKHLLLTSKPMVYLVNLSEKDYI 237
Cdd:PTZ00258 160 EKRLDELTK--KRKKKKKKKeekVELDVLKKVLEWLEE-GKPVRDG-DWTDKEIEILNEYQLLTAKPMIYLVNMSEKDFI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  238 RKKNKWLIKIKEWVDKSDPGALvIPFSGALELKLQEL-SAEERQKYL-EANMTQSALPKIIKAGFAALQLEYFFTAGPDE 315
Cdd:PTZ00258 236 RQKNKWLAKIKEWVGEKGGGPI-IPYSAEFEEELAELgSEEERKEYLeEYGIKQSMLDKIIKTGYKLLNLIHFFTAGPDE 314

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76677911  316 VRAWTIRKGTKAPQAAGKIHTDFEKGFIMAEVMKYDDFKDEGSENAVKAAGKYRQQGRNYIVEDGDIIFFKFNTP 390
Cdd:PTZ00258 315 VRCWTIQKGTKAPQAAGVIHSDFEKGFICAEVMKYEDFLELGSEAAVKAEGKYRQEGKDYVVQDGDIIFFKFNVS 389
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
 23-388 0e+00

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 513.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  23 LKIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFLCQCHKPASKIPAFLNVVDIAGLVKGAHN 102
Cdd:COG0012   1 LKCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 103 GQGLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMIGPIIDKLEKVAvRGGDKKLKPE 182
Cdd:COG0012  81 GEGLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEKRLERLEKKA-KSGDKEAKAE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 183 YDIMCKVKSwVIDQKKPVRfYHDWNDKEIEVLnKHL-LLTSKPMVYLVNLSEKDyIRKKNKWLIKIKEWVDKSdpGALVI 261
Cdd:COG0012 160 LELLEKLKE-HLEEGKPAR-SLELSEEEKKLL-KELqLLTAKPVLYVANVDEDD-LAEGNPYVEKVREYAAKE--GAEVV 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 262 PFSGALELKLQELSAEERQKYLEA-NMTQSALPKIIKAGFAALQLEYFFTAGPDEVRAWTIRKGTKAPQAAGKIHTDFEK 340
Cdd:COG0012 234 VICAKIEAELAELDEEERAEFLEElGLEESGLDRLIRAGYDLLGLITFFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFER 313

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 76677911 341 GFIMAEVMKYDDFKDEGSENAVKAAGKYRQQGRNYIVEDGDIIFFKFN 388
Cdd:COG0012 314 GFIRAEVISYDDLIAYGSEAAAKEAGKLRLEGKDYVVQDGDVIHFRFN 361
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
 25-303 7.04e-161

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: 452.68  E-value: 7.04e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  25 IGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFLCQCHKPASKIPAFLNVVDIAGLVKGAHNGQ 104
Cdd:cd01900   1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASKGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 105 GLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMIGPIIDKLEKVAvRGGDKKLKPEYD 184
Cdd:cd01900  81 GLGNKFLSHIREVDAIAHVVRCFEDDDITHVEGSVDPVRDIEIINTELILADLETIEKRLERLEKKA-KSGDKEAKEELE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 185 IMCKVKSWViDQKKPVRfYHDWNDKEIEVLNKHLLLTSKPMVYLVNLSEKDYIRKKNKWLikiKEWVDKSDPGALVIPFS 264
Cdd:cd01900 160 LLEKIKEHL-EEGKPAR-TLELTDEEIKILKSLQLLTAKPVIYVANVSEDDLIRGNNKVL---KVREIAAKEGAEVIPIS 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 76677911 265 GALELKLQELSAEERQKYLEA-NMTQSALPKIIKAGFAAL 303
Cdd:cd01900 235 AKLEAELAELDEEEAAEFLEElGLEESGLDKLIRAGYELL 274
TIGR00092 TIGR00092
GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in ...
 23-388 4.42e-113

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: 334.82  E-value: 4.42e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911    23 LKIGIVGLPNVGKSTFFNVLTNSQ-ASAENFPFCTIDPNESRVPVPDERFDFLCQCHKPASKIPAFLNVVDIAGLVKGAH 101
Cdd:TIGR00092   3 LSGGIVGLPNVGKSTLFAATTNLLgNEAANPPFTTIEPNAGVVNPSDPRLDLLAIYIKPEKVPPTTTEFVDIAGLVGGAS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   102 NGQGLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMIGPIIDKLEKVAvRGGdKKLKP 181
Cdd:TIGR00092  83 KGEGLGNQFLANIREVDIIQHVVRCFEDDIIHHVGNVDDPRDDFEIIDEELLKADEFLVEKRIGRSKKSA-EGG-KDKKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   182 EYDIMCKVKSwVIDQKKPVRfyHDWNDKEIEVLNKHLLLTSKPMVYLVNLSEKDYIRKKNKWLIKIKEWVDKSDPGALVI 261
Cdd:TIGR00092 161 ELLLLEIILP-LLNGGQMAR--HVDLSKEELILIKSLNLLTKKPIILIANVSEDYLRNLNNNYLLIVEWIAAYSKGDPKV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   262 PFSGALELK-LQELSAEERQKYL-EANMTQSALPK-IIKAGFAALQLEYFFTAGPDEVRAWTIRKGTKAPQAAGKIHTDF 338
Cdd:TIGR00092 238 VFVCALEESeLSELDDEERQEFLqKLGLTESAGLNiIIRARYKLLLLSFFFTGGKEEVRAWTRKGGWAAPQAAGIIHTDF 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 76677911   339 EKGFIMAEVMKYDDFKDEGSENAVKAAGKYRQQGRNYIVEDGDIIFFKFN 388
Cdd:TIGR00092 318 ETGFIAAEVISWDDFIYKKSSQGAKKGGLMRLEGKYYVVDDGDVLFFAFN 367
YchF-GTPase_C pfam06071
Protein of unknown function (DUF933); This domain is found at the C terminus of the YchF ...
 305-386 1.20e-59

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: 187.95  E-value: 1.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   305 LEYFFTAGPDEVRAWTIRKGTKAPQAAGKIHTDFEKGFIMAEVMKYDDFKDEGSENAVKAAGKYRQQGRNYIVEDGDIIF 384
Cdd:pfam06071   1 LITFFTAGPKEVRAWTIRKGTTAPQAAGVIHTDFEKGFIRAEVISYDDLIEYGSEAAAKEAGKLRLEGKDYVVQDGDIIH 80


                  ..
gi 76677911   385 FK 386
Cdd:pfam06071  81 FR 82
 
Name Accession Description Interval E-value
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 1-390 0e+00

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 615.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911    1 MPPKKGgDGLKPPPIIGRFGTSLKIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFLCQCHKP 80
Cdd:PTZ00258   1 MPPKKK-MEEEKKVLLGRPGNNLKMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDERFDWLCKHFKP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   81 ASKIPAFLNVVDIAGLVKGAHNGQGLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMI 160
Cdd:PTZ00258  80 KSIVPAQLDITDIAGLVKGASEGEGLGNAFLSHIRAVDGIYHVVRAFEDEDITHVEGEIDPVRDLEIISSELILKDLEFV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  161 GPIIDKLEKvaVRGGDKKLK---PEYDIMCKVKSWVIDqKKPVRFYhDWNDKEIEVLNKHLLLTSKPMVYLVNLSEKDYI 237
Cdd:PTZ00258 160 EKRLDELTK--KRKKKKKKKeekVELDVLKKVLEWLEE-GKPVRDG-DWTDKEIEILNEYQLLTAKPMIYLVNMSEKDFI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  238 RKKNKWLIKIKEWVDKSDPGALvIPFSGALELKLQEL-SAEERQKYL-EANMTQSALPKIIKAGFAALQLEYFFTAGPDE 315
Cdd:PTZ00258 236 RQKNKWLAKIKEWVGEKGGGPI-IPYSAEFEEELAELgSEEERKEYLeEYGIKQSMLDKIIKTGYKLLNLIHFFTAGPDE 314

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76677911  316 VRAWTIRKGTKAPQAAGKIHTDFEKGFIMAEVMKYDDFKDEGSENAVKAAGKYRQQGRNYIVEDGDIIFFKFNTP 390
Cdd:PTZ00258 315 VRCWTIQKGTKAPQAAGVIHSDFEKGFICAEVMKYEDFLELGSEAAVKAEGKYRQEGKDYVVQDGDIIFFKFNVS 389
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
 23-388 0e+00

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 513.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  23 LKIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFLCQCHKPASKIPAFLNVVDIAGLVKGAHN 102
Cdd:COG0012   1 LKCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 103 GQGLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMIGPIIDKLEKVAvRGGDKKLKPE 182
Cdd:COG0012  81 GEGLGNQFLANIREVDAIVHVVRCFEDDNVTHVEGSVDPLRDIETINTELILADLETVEKRLERLEKKA-KSGDKEAKAE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 183 YDIMCKVKSwVIDQKKPVRfYHDWNDKEIEVLnKHL-LLTSKPMVYLVNLSEKDyIRKKNKWLIKIKEWVDKSdpGALVI 261
Cdd:COG0012 160 LELLEKLKE-HLEEGKPAR-SLELSEEEKKLL-KELqLLTAKPVLYVANVDEDD-LAEGNPYVEKVREYAAKE--GAEVV 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 262 PFSGALELKLQELSAEERQKYLEA-NMTQSALPKIIKAGFAALQLEYFFTAGPDEVRAWTIRKGTKAPQAAGKIHTDFEK 340
Cdd:COG0012 234 VICAKIEAELAELDEEERAEFLEElGLEESGLDRLIRAGYDLLGLITFFTAGPKEVRAWTIKKGTTAPQAAGVIHTDFER 313

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 76677911 341 GFIMAEVMKYDDFKDEGSENAVKAAGKYRQQGRNYIVEDGDIIFFKFN 388
Cdd:COG0012 314 GFIRAEVISYDDLIAYGSEAAAKEAGKLRLEGKDYVVQDGDVIHFRFN 361
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
 25-303 7.04e-161

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: 452.68  E-value: 7.04e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  25 IGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFLCQCHKPASKIPAFLNVVDIAGLVKGAHNGQ 104
Cdd:cd01900   1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERLDKLAEIVKPKKIVPATIEFVDIAGLVKGASKGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 105 GLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMIGPIIDKLEKVAvRGGDKKLKPEYD 184
Cdd:cd01900  81 GLGNKFLSHIREVDAIAHVVRCFEDDDITHVEGSVDPVRDIEIINTELILADLETIEKRLERLEKKA-KSGDKEAKEELE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 185 IMCKVKSWViDQKKPVRfYHDWNDKEIEVLNKHLLLTSKPMVYLVNLSEKDYIRKKNKWLikiKEWVDKSDPGALVIPFS 264
Cdd:cd01900 160 LLEKIKEHL-EEGKPAR-TLELTDEEIKILKSLQLLTAKPVIYVANVSEDDLIRGNNKVL---KVREIAAKEGAEVIPIS 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 76677911 265 GALELKLQELSAEERQKYLEA-NMTQSALPKIIKAGFAAL 303
Cdd:cd01900 235 AKLEAELAELDEEEAAEFLEElGLEESGLDKLIRAGYELL 274
TIGR00092 TIGR00092
GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in ...
 23-388 4.42e-113

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: 334.82  E-value: 4.42e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911    23 LKIGIVGLPNVGKSTFFNVLTNSQ-ASAENFPFCTIDPNESRVPVPDERFDFLCQCHKPASKIPAFLNVVDIAGLVKGAH 101
Cdd:TIGR00092   3 LSGGIVGLPNVGKSTLFAATTNLLgNEAANPPFTTIEPNAGVVNPSDPRLDLLAIYIKPEKVPPTTTEFVDIAGLVGGAS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   102 NGQGLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMIGPIIDKLEKVAvRGGdKKLKP 181
Cdd:TIGR00092  83 KGEGLGNQFLANIREVDIIQHVVRCFEDDIIHHVGNVDDPRDDFEIIDEELLKADEFLVEKRIGRSKKSA-EGG-KDKKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   182 EYDIMCKVKSwVIDQKKPVRfyHDWNDKEIEVLNKHLLLTSKPMVYLVNLSEKDYIRKKNKWLIKIKEWVDKSDPGALVI 261
Cdd:TIGR00092 161 ELLLLEIILP-LLNGGQMAR--HVDLSKEELILIKSLNLLTKKPIILIANVSEDYLRNLNNNYLLIVEWIAAYSKGDPKV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   262 PFSGALELK-LQELSAEERQKYL-EANMTQSALPK-IIKAGFAALQLEYFFTAGPDEVRAWTIRKGTKAPQAAGKIHTDF 338
Cdd:TIGR00092 238 VFVCALEESeLSELDDEERQEFLqKLGLTESAGLNiIIRARYKLLLLSFFFTGGKEEVRAWTRKGGWAAPQAAGIIHTDF 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 76677911   339 EKGFIMAEVMKYDDFKDEGSENAVKAAGKYRQQGRNYIVEDGDIIFFKFN 388
Cdd:TIGR00092 318 ETGFIAAEVISWDDFIYKKSSQGAKKGGLMRLEGKYYVVDDGDVLFFAFN 367
TGS_YchF_OLA1 cd04867
TGS (ThrRS, GTPase and SpoT) domain found in the YchF/OLA1 family proteins; The YchF/Ola1 ...
 303-387 8.85e-62

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: 193.51  E-value: 8.85e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 303 LQLEYFFTAGPDEVRAWTIRKGTKAPQAAGKIHTDFEKGFIMAEVMKYDDFKDEGSENAVKAAGKYRQQGRNYIVEDGDI 382
Cdd:cd04867   1 LNLITFFTAGPDEVRAWTIRKGTKAPQAAGVIHTDFEKGFIRAEVIKYDDLKELGSEAAAKEAGKYRQEGKDYVVQDGDI 80


                ....*
gi 76677911 383 IFFKF 387
Cdd:cd04867  81 IHFKF 85
YchF-GTPase_C pfam06071
Protein of unknown function (DUF933); This domain is found at the C terminus of the YchF ...
 305-386 1.20e-59

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: 187.95  E-value: 1.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   305 LEYFFTAGPDEVRAWTIRKGTKAPQAAGKIHTDFEKGFIMAEVMKYDDFKDEGSENAVKAAGKYRQQGRNYIVEDGDIIF 384
Cdd:pfam06071   1 LITFFTAGPKEVRAWTIRKGTTAPQAAGVIHTDFEKGFIRAEVISYDDLIEYGSEAAAKEAGKLRLEGKDYVVQDGDIIH 80


                  ..
gi 76677911   385 FK 386
Cdd:pfam06071  81 FR 82
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 22-383 1.03e-37

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 140.33  E-value: 1.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   22 SLKIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNES----RVPVPDERFDFLCQ-----CHKPASKIPafLNVVD 92
Cdd:PRK09602   1 MITIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGvayvRVECPCKELGVKCNprngkCIDGTRFIP--VELID 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   93 IAGLVKGAHNGQGLGNAFLSHISACDGIFHLTRAFEDDDIT--HVE-GSVDPIRDIEIIHEELqlkDEEMIGpIIDK-LE 168
Cdd:PRK09602  79 VAGLVPGAHEGRGLGNQFLDDLRQADALIHVVDASGSTDEEgnPVEpGSHDPVEDIKFLEEEL---DMWIYG-ILEKnWE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  169 KVAVRGGDKKLKPEYDIMCK----------VKsWVIDQKKPVRFYHDWNDKEIEVLNKHLLLTSKPMVYLVNLSEKDYIR 238
Cdd:PRK09602 155 KFSRKAQAEKFDIEEALAEQlsglgineehVK-EALRELGLPEDPSKWTDEDLLELARELRKISKPMVIAANKADLPPAE 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  239 KKNKWLikikewvdKSDPGALVIPFSGALELKL---------------------QELSAEERQ------KYLEANMT--- 288
Cdd:PRK09602 234 ENIERL--------KEEKYYIVVPTSAEAELALrraakaglidyipgdsdfeilGELSEKQKKaleyirEVLKKYGGtgv 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  289 QSAlpkIIKAGFAALQL--------EYFFTAG-----PDevrAWTIRKGTKAPQAAGKIHTDFEKGFImaevmkyddfkd 355
Cdd:PRK09602 306 QEA---INTAVFDLLDMivvypvedENKLTDKkgnvlPD---AFLLPKGSTARDLAYKIHTDIGEGFL------------ 367

                        410       420
                 ....*....|....*....|....*...
gi 76677911  356 egseNAVKAAGKyRQQGRNYIVEDGDII 383
Cdd:PRK09602 368 ----YAIDARTK-RRIGEDYELKDGDVI 390
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 25-283 1.15e-30

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


Pssm-ID: 206686 [Multi-domain]  Cd Length: 318  Bit Score: 119.64  E-value: 1.15e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  25 IGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNES----RVPVPDERFDFLCQ-----CHKPASKIPafLNVVDIAG 95
Cdd:cd01899   1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGvgyvRVECPCKELGVSCNprygkCIDGKRYVP--VELIDVAG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  96 LVKGAHNGQGLGNAFLSHISACDGIFHLTRA--FEDDDITHVE-GSVDPIRDIEIIHEELqlkDEEMIGPIIDKLEKVAV 172
Cdd:cd01899  79 LVPGAHEGKGLGNQFLDDLRDADVLIHVVDAsgGTDAEGNGVEtGGYDPLEDIEFLENEI---DMWIYGILERNWEKIVR 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 173 RGGDKKLKPEYDIM----------CKVKSWVIDQKKPVRFYhDWNDKEIEVLNKHLLLTSKPMVYLVNlseKDYIRKKNK 242
Cdd:cd01899 156 KAKAEKTDIVEALSeqlsgfgvneDVVIEALEELELPADLS-KWDDEDLLRLARELRKRRKPMVIAAN---KADIPDAEE 231

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 76677911 243 WLIKIKewvdKSDPGALVIPFSGALELKLQELSAEERQKYL 283
Cdd:cd01899 232 NISKLR----LKYPDEIVVPTSAEAELALRRAAKQGLIKYV 268
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 24-164 2.90e-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: 2.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911    24 KIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFlcqchkpaskipaflnvVDIAGLVKGAHNG 103
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIIL-----------------VDTPGLIEGASEG 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76677911   104 QGLGNAFLSHISAcDGIFHLtrafedddithvegsVDPIRDIEIIHEELQLKDEEMIGPII 164
Cdd:pfam01926  64 EGLGRAFLAIIEA-DLILFV---------------VDSEEGITPLDEELLELLRENKKPII 108
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 26-157 1.58e-24

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: 98.62  E-value: 1.58e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  26 GIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDerfdflcqchkpaskiPAFLNVVDIAGLVKGAHNGQG 105
Cdd:cd01881   1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGD----------------GVDIQIIDLPGLLDGASEGRG 64

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 76677911 106 LGNAFLSHISACDGIFHLTRAFEDDDIthvegsvDPIRDIEIIHEELQLKDE 157
Cdd:cd01881  65 LGEQILAHLYRSDLILHVIDASEDCVG-------DPLEDQKTLNEEVSGSFL 109
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 25-159 1.38e-22

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: 93.26  E-value: 1.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  25 IGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERfDFLcqchkpaskipaflnVVDIAGLVKGAHNGQ 104
Cdd:cd01898   3 VGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGR-SFV---------------IADIPGLIEGASEGK 66

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 76677911 105 GLGNAFLSHISACDGIFHLTrafeddDITHVEgsvDPIRDIEIIHEELQLKDEEM 159
Cdd:cd01898  67 GLGHRFLRHIERTRVLLHVI------DLSGED---DPVEDYETIRNELEAYNPGL 112
obgE PRK12297
GTPase CgtA; Reviewed
 23-158 5.58e-22

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 96.71  E-value: 5.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   23 LKI----GIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERfDFlcqchkpaskipaflnVV-DIAGLV 97
Cdd:PRK12297 155 LKLladvGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGR-SF----------------VMaDIPGLI 217

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76677911   98 KGAHNGQGLGNAFLSHISACDGIFHLTrafeddDITHVEGSvDPIRDIEIIHEELQLKDEE 158
Cdd:PRK12297 218 EGASEGVGLGHQFLRHIERTRVIVHVI------DMSGSEGR-DPIEDYEKINKELKLYNPR 271
obgE PRK12299
GTPase CgtA; Reviewed
 25-159 2.89e-21

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 93.60  E-value: 2.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   25 IGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERfDFLcqchkpaskipaflnVVDIAGLVKGAHNGQ 104
Cdd:PRK12299 161 VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYK-SFV---------------IADIPGLIEGASEGA 224

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 76677911  105 GLGNAFLSHISACDGIFHLTrafeddDIThvegSVDPIRDIEIIHEELQLKDEEM 159
Cdd:PRK12299 225 GLGHRFLKHIERTRLLLHLV------DIE----AVDPVEDYKTIRNELEKYSPEL 269
obgE PRK12298
GTPase CgtA; Reviewed
 25-159 7.07e-18

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 84.53  E-value: 7.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   25 IGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERfDFLcqchkpaskipaflnVVDIAGLVKGAHNGQ 104
Cdd:PRK12298 162 VGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDER-SFV---------------VADIPGLIEGASEGA 225

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 76677911  105 GLGNAFLSHISACDGIFHLTrafeddDITHVEGSvDPIRDIEIIHEELQLKDEEM 159
Cdd:PRK12298 226 GLGIRFLKHLERCRVLLHLI------DIAPIDGS-DPVENARIIINELEKYSPKL 273
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
28-383 3.61e-11

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 64.05  E-value: 3.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  28 VGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPvpderfdflcqcHKPAsKIpaflNVVDIAGLVKGAHNGQGLG 107
Cdd:COG1163  69 VGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLE------------YKGA-KI----QILDVPGLIEGAASGKGRG 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 108 NAFLSHISACDGIFHLTRAFEDDdithvegsvdpirDIEIIHEELqlkdeEMIGPIIDKLE-----KVAVRGG------- 175
Cdd:COG1163 132 KEVLSVVRNADLILIVLDVFELE-------------QYDVLKEEL-----YDAGIRLNKPPpdvtiEKKGKGGirvnstg 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 176 ----D----KKLKPEYDIMCKVkswvidqkkpVRFYHDWN-DKEIEVL--NKhlllTSKPMVYLVN---LSEKDYIRKKN 241
Cdd:COG1163 194 kldlDeediKKILREYGIVNAD----------VLIREDVTlDDLIDALmgNR----VYKPAIVVVNkidLADEEYVEELK 259

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 242 KwliKIKEWVDksdpgalVIPFSGALELKLQELsAEERQKYLEanmtqsalpkIIKagfaalqleyFFT----AGPDEVR 317
Cdd:COG1163 260 S---KLPDGVP-------VIFISAEKGIGLEEL-KEEIFEELG----------LIR----------VYLkppgGKADMEE 308

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 318 AWTIRKGTKAPQAAGKIHTDFEKGFIMAEV----MKYDDfkdegsenavkaagkyRQQGRNYIVEDGDII 383
Cdd:COG1163 309 PLILRKGSTVGDVCEKIHRDFVERFRYARVwgksAKHPG----------------QRVGLDHVLEDGDIV 362
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 25-152 8.98e-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: 58.33  E-value: 8.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  25 IGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPnesrvpvpderfdflcqchkpaskIPAFLN-------VVDIAGLV 97
Cdd:cd01896   3 VALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTC------------------------VPGVMEykgakiqLLDLPGII 58

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 76677911  98 KGAHNGQGLGNAFLSHISACDGIFHLTRAFEDDDithvegsvdpirDIEIIHEEL 152
Cdd:cd01896  59 EGASDGKGRGRQVIAVARTADLILIVLDATKPEG------------QREILEREL 101
TGS_Obg cd04938
TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases ...
 310-386 1.06e-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: 54.37  E-value: 1.06e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 76677911 310 TAGPDEVRAWTIRKGTKAPQAAGKIHTDFEKGFIMAEVmkyddfkdegsenavkaAGKYRQQGRNYIVEDGDIIFFK 386
Cdd:cd04938  18 SGNSVFRDCVLVKKGTTVKDFANKIHTDLEKGFINAEG-----------------IGGRRLEGEDYILQDNDVVKFT 77
TGS cd01616
TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; ...
 308-385 3.88e-08

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


Pssm-ID: 340455 [Multi-domain]  Cd Length: 61  Bit Score: 49.53  E-value: 3.88e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76677911 308 FFTAGPDEVRAWTIRKGTKAPQAAGKIHTDFEKGFIMAEVMkyddfkdegsenavkaagkYRQQGRNYIVEDGDIIFF 385
Cdd:cd01616   2 VFTVGKTPGTVFVMNKGATAYSCAMHLHEDYCRKSILALVD-------------------GQLWDMYYPLTKGDEIKF 60
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 26-155 5.69e-07

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 48.78  E-value: 5.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  26 GIVGLPNVGKSTFFNVLTNSQASA-ENFPFCTIDPNESRVPVPDER-FDFlcqchkpaskipaflnvVDIAGLVKGAHNG 103
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNVGIvSPIPGTTRDPVRKEWELLPLGpVVL-----------------IDTPGLDEEGGLG 63

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 76677911 104 QGLGNAFLSHISACDGIFHLtrafedddithVEGSVDPIRDIEIIHEELQLK 155
Cdd:cd00880  64 RERVEEARQVADRADLVLLV-----------VDSDLTPVEEEAKLGLLRERG 104
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 25-70 8.75e-07

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


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 48.99  E-value: 8.75e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 76677911  25 IGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDER 70
Cdd:cd01878  44 VALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTTRRIKLPGGR 89
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 27-74 9.40e-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: 45.52  E-value: 9.40e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 76677911  27 IVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFL 74
Cdd:cd01879   2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIV 49
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 25-70 1.18e-05

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 47.00  E-value: 1.18e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 76677911  25 IGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDER 70
Cdd:COG2262 202 VALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRRLELPDGR 247
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
 29-73 1.34e-05

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


Pssm-ID: 273077 [Multi-domain]  Cd Length: 591  Bit Score: 47.04  E-value: 1.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 76677911    29 GLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDF 73
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIEI 45
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 26-164 1.76e-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: 44.75  E-value: 1.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911  26 GIVGLPNVGKSTFFNVLTNSQ-ASAENFPFCTIDPNESRVPVPDERFDflcqchkpaskipafLNVVDIAGLVKGahNGQ 104
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEvGEVSDVPGTTRDPDVYVKELDKGKVK---------------LVLVDTPGLDEF--GGL 63

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911 105 GLGNAFLSHISACDGIFHLTrafeddDIThvegsvDPIRDIEIIHEELQLKDEEMIgPII 164
Cdd:cd00882  64 GREELARLLLRGADLILLVV------DST------DRESEEDAKLLILRRLRKEGI-PII 110
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 27-64 3.16e-05

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


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 43.96  E-value: 3.16e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 76677911  27 IVGLPNVGKSTFFNVLTNS-QASAENFPFCTIDPNESRV 64
Cdd:cd01894   2 IVGRPNVGKSTLFNRLTGRrDAIVSDTPGVTRDRKYGEA 40
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 23-58 4.29e-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: 43.21  E-value: 4.29e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 76677911    23 LKIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTID 58
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVE 36
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
22-53 4.95e-05

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 45.50  E-value: 4.95e-05
                        10        20        30
                ....*....|....*....|....*....|..
gi 76677911  22 SLKIGIVGLPNVGKSTFFNVLTNSQASAENFP 53
Cdd:COG0370   3 MITIALVGNPNVGKTTLFNALTGSRQKVGNWP 34
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
24-48 5.95e-05

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 45.01  E-value: 5.95e-05
                        10        20
                ....*....|....*....|....*
gi 76677911  24 KIGIVGLPNVGKSTFFNVLTNSQAS 48
Cdd:COG1160   4 VVAIVGRPNVGKSTLFNRLTGRRDA 28
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 24-48 9.11e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 44.27  E-value: 9.11e-05
                         10        20
                 ....*....|....*....|....*
gi 76677911   24 KIGIVGLPNVGKSTFFNVLTNSQAS 48
Cdd:PRK00093   3 VVAIVGRPNVGKSTLFNRLTGKRDA 27
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 17-44 1.10e-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: 42.52  E-value: 1.10e-04
                        10        20
                ....*....|....*....|....*...
gi 76677911  17 GRFGTSLKIGIVGLPNVGKSTFFNVLTN 44
Cdd:cd01856 110 GLLPRPLRAMVVGIPNVGKSTLINRLRG 137
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 27-56 1.61e-04

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: 41.78  E-value: 1.61e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 76677911  27 IVGLPNVGKSTFFNVLTNSQASAENFPFCT 56
Cdd:cd01897   5 IAGYPNVGKSSLVNKLTRAKPEVAPYPFTT 34
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 23-48 2.10e-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: 41.33  E-value: 2.10e-04
                        10        20
                ....*....|....*....|....*.
gi 76677911  23 LKIGIVGLPNVGKSTFFNVLTNSQAS 48
Cdd:cd04164   4 IKVVIAGKPNVGKSSLLNALAGRDRA 29
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 20-47 4.17e-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: 4.17e-04
                        10        20
                ....*....|....*....|....*...
gi 76677911  20 GTSLKIGIVGLPNVGKSTFFNVLTNSQA 47
Cdd:cd04178 114 KTSITVGVVGYPNVGKSSVINSLKRSRA 141
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 24-126 5.73e-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: 40.05  E-value: 5.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911    24 KIGIVGLPNVGKSTFFNVLT-NSQASAENFPFCTidpnesrvpvpderFDFLCQCHKPASKiPAFLNVVDIAGLVKGAHN 102
Cdd:TIGR00231   3 KIVIVGHPNVGKSTLLNSLLgNKGSITEYYPGTT--------------RNYVTTVIEEDGK-TYKFNLLDTAGQEDYDAI 67

                          90       100
                  ....*....|....*....|....
gi 76677911   103 GQGLGNAFLSHISACDGIFHLTRA 126
Cdd:TIGR00231  68 RRLYYPQVERSLRVFDIVILVLDV 91
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 22-46 8.46e-04

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: 39.72  E-value: 8.46e-04
                        10        20
                ....*....|....*....|....*
gi 76677911  22 SLKIGIVGLPNVGKSTFFNVLTNSQ 46
Cdd:cd01895   2 PIKIAIIGRPNVGKSSLLNALLGEE 26
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 24-105 1.28e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 40.93  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   24 KIGIVGLPNVGKSTFFNVLTNSQAS-AENFPFCTIDPNESRVPVPDERFDFlcqchkpaskipaflnvVDIAGLVKGAHN 102
Cdd:PRK09518 452 RVALVGRPNVGKSSLLNQLTHEERAvVNDLAGTTRDPVDEIVEIDGEDWLF-----------------IDTAGIKRRQHK 514


                 ...
gi 76677911  103 GQG 105
Cdd:PRK09518 515 LTG 517
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 22-42 1.30e-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: 39.37  E-value: 1.30e-03
                        10        20
                ....*....|....*....|.
gi 76677911  22 SLKIGIVGLPNVGKSTFFNVL 42
Cdd:cd04163   3 SGFVAIIGRPNVGKSTLLNAL 23
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
23-46 2.23e-03

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 40.01  E-value: 2.23e-03
                        10        20
                ....*....|....*....|....
gi 76677911  23 LKIGIVGLPNVGKSTFFNVLTNSQ 46
Cdd:COG1160 176 IKIAIVGRPNVGKSSLINALLGEE 199
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 23-48 2.47e-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: 39.39  E-value: 2.47e-03
                          10        20
                  ....*....|....*....|....*.
gi 76677911    23 LKIGIVGLPNVGKSTFFNVLTNSQAS 48
Cdd:pfam12631  95 IKVVIVGKPNVGKSSLLNALLGEERA 120
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 9-44 2.70e-03

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


Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 39.41  E-value: 2.70e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 76677911     9 GLKPPPIigrfgtslKIGIVGLPNVGKSTFFNVLTN 44
Cdd:TIGR03596 113 GLKNRPI--------RAMIVGIPNVGKSTLINRLAG 140
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 23-44 3.13e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 39.65  E-value: 3.13e-03
                         10        20
                 ....*....|....*....|..
gi 76677911   23 LKIGIVGLPNVGKSTFFNVLTN 44
Cdd:PRK00093 174 IKIAIIGRPNVGKSSLINALLG 195
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 23-48 4.05e-03

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


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 39.27  E-value: 4.05e-03
                        10        20
                ....*....|....*....|....*.
gi 76677911  23 LKIGIVGLPNVGKSTFFNVLTNSQAS 48
Cdd:COG0486 214 IKVVIVGRPNVGKSSLLNALLGEERA 239
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 24-105 5.46e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 38.80  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677911   24 KIGIVGLPNVGKSTFFNVLTNSQAS-AENFPFCTIDPNESRVPVPDERFDFlcqchkpaskipaflnvVDIAGLVKGAHN 102
Cdd:PRK03003 213 RVALVGKPNVGKSSLLNKLAGEERSvVDDVAGTTVDPVDSLIELGGKTWRF-----------------VDTAGLRRRVKQ 275


                 ...
gi 76677911  103 GQG 105
Cdd:PRK03003 276 ASG 278
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 23-45 6.04e-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: 36.98  E-value: 6.04e-03
                        10        20
                ....*....|....*....|...
gi 76677911  23 LKIGIVGLPNVGKSTFFNVLTNS 45
Cdd:cd01849  92 IRVGVVGLPNVGKSSFINALLNK 114
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
23-47 7.29e-03

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 38.17  E-value: 7.29e-03
                         10        20
                 ....*....|....*....|....*
gi 76677911   23 LKIGIVGLPNVGKSTFFNVLTNSQA 47
Cdd:PRK05291 216 LKVVIAGRPNVGKSSLLNALLGEER 240
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
27-53 9.70e-03

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 37.39  E-value: 9.70e-03
                        10        20
                ....*....|....*....|....*...
gi 76677911  27 IVGLPNVGKSTFFNVLTNSQ-ASAENFP 53
Cdd:COG1161 118 IVGIPNVGKSTLINRLAGKKvAKTGNKP 145
 
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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