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Conserved domains on  [gi|1900666673|emb|CAB5081119|]
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GTPase ObgE [Burkholderia cenocepacia]

Protein Classification

GTPase Obg( domain architecture ID 11485760)

GTPase Obg is a P-loop small G protein that is implicated in a variety of functions including bacterial ribosomal biogenesis, the cell cycle, and stress response

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
obgE PRK12299
GTPase CgtA; Reviewed
2-336 0e+00

GTPase CgtA; Reviewed


:

Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 547.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673   2 KFIDEARIEVIAGDGGDGSASMRREKFVPFggpdggdggrggSVYAIADRNINTLIDYRYAKKHLARNGENGRGSDCYGK 81
Cdd:PRK12299    1 KFIDEAKIYVKAGDGGNGCVSFRREKFIPFggpdggdggrggSVILEADENLNTLIDFRYKRHFKAENGENGMGRNRTGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673  82 GGDDVTLRMPVGTIISDMDTGELIADLTEHDQRVMLAQGGAGGLGNLHFKSSTNRAPRQKTDGKPGERRMLKLELKVLAD 161
Cdd:PRK12299   81 SGKDLVLKVPVGTQIYDADTGELIADLTEHGQRFLVAKGGKGGLGNAHFKSSTNRAPRYATPGEPGEERWLRLELKLLAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTGVL 241
Cdd:PRK12299  161 VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKSFVIADIPGLIEGASEGAGLGHRFLKHIERTRLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 242 LHLVDLApfdeSVDPVAEATAIVGELRKYDEALYEKPRWLVLNKLDMVPED-EREARVADFLDRFGwdGPVFEISALTGQ 320
Cdd:PRK12299  241 LHLVDIE----AVDPVEDYKTIRNELEKYSPELADKPRILVLNKIDLLDEEeEREKRAALELAALG--GPVFLISAVTGE 314
                         330
                  ....*....|....*.
gi 1900666673 321 GCEALCYAIYDYLSEH 336
Cdd:PRK12299  315 GLDELLRALWELLEEA 330
 
Name Accession Description Interval E-value
obgE PRK12299
GTPase CgtA; Reviewed
2-336 0e+00

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 547.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673   2 KFIDEARIEVIAGDGGDGSASMRREKFVPFggpdggdggrggSVYAIADRNINTLIDYRYAKKHLARNGENGRGSDCYGK 81
Cdd:PRK12299    1 KFIDEAKIYVKAGDGGNGCVSFRREKFIPFggpdggdggrggSVILEADENLNTLIDFRYKRHFKAENGENGMGRNRTGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673  82 GGDDVTLRMPVGTIISDMDTGELIADLTEHDQRVMLAQGGAGGLGNLHFKSSTNRAPRQKTDGKPGERRMLKLELKVLAD 161
Cdd:PRK12299   81 SGKDLVLKVPVGTQIYDADTGELIADLTEHGQRFLVAKGGKGGLGNAHFKSSTNRAPRYATPGEPGEERWLRLELKLLAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTGVL 241
Cdd:PRK12299  161 VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKSFVIADIPGLIEGASEGAGLGHRFLKHIERTRLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 242 LHLVDLApfdeSVDPVAEATAIVGELRKYDEALYEKPRWLVLNKLDMVPED-EREARVADFLDRFGwdGPVFEISALTGQ 320
Cdd:PRK12299  241 LHLVDIE----AVDPVEDYKTIRNELEKYSPELADKPRILVLNKIDLLDEEeEREKRAALELAALG--GPVFLISAVTGE 314
                         330
                  ....*....|....*.
gi 1900666673 321 GCEALCYAIYDYLSEH 336
Cdd:PRK12299  315 GLDELLRALWELLEEA 330
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
3-339 0e+00

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: 542.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673   3 FIDEARIEVIAGDGGDGSASMRREKFVPFggpdggdggrggSVYAIADRNINTLIDYRYAKKHLARNGENGRGSDCYGKG 82
Cdd:COG0536     1 FVDEAKIYVKAGDGGNGCVSFRREKYVPKggpdggdggrggDVILVADENLNTLLDFRYKRHFKAENGENGMGKNRTGKN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673  83 GDDVTLRMPVGTIISDMDTGELIADLTEHDQRVMlaqggagglgNLHFKSSTNRAPRQKTDGKPGERRMLKLELKVLADV 162
Cdd:COG0536    81 GEDLVIKVPVGTVVKDAETGEVLADLTEDGQRVVvakggrgglgNAHFKSSTNRAPRFAEPGEPGEERWLRLELKLLADV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 163 GLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTGVLL 242
Cdd:COG0536   161 GLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRSFVIADIPGLIEGASEGAGLGHRFLRHIERTRVLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 243 HLVDLAPFDESvDPVAEATAIVGELRKYDEALYEKPRWLVLNKLDMVPEDEREArVADFLDRFGwdGPVFEISALTGQGC 322
Cdd:COG0536   241 HVVDAAPLDGR-DPVEDYEIIRNELEAYSPELAEKPRIVVLNKIDLLDAEELEE-LKAELEKLG--GPVFPISAVTGEGL 316
                         330
                  ....*....|....*..
gi 1900666673 323 EALCYAIYDYLSEHSDA 339
Cdd:COG0536   317 DELLYALAELLEELRAE 333
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
3-333 0e+00

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: 537.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673   3 FIDEARIEVIAGDGGDGSASMRREKFVPFGGPDGGDGGRGGSVYAIADRNINTLIDYRYAKKHLARNGENGRGSDCYGKG 82
Cdd:TIGR02729   1 FVDEAKIFVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGSVILEADENLNTLLDFRYQRHFKAENGENGMGKNRTGKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673  83 GDDVTLRMPVGTIISDMDTGELIADLTEHDQRVMLAQGGAGGLGNLHFKSSTNRAPRQKTDGKPGERRMLKLELKVLADV 162
Cdd:TIGR02729  81 GEDLVIKVPVGTVVYDADTGELLADLTEPGQRFLVAKGGRGGLGNAHFKSSTNRAPRFATPGEPGEERWLRLELKLLADV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 163 GLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTGVLL 242
Cdd:TIGR02729 161 GLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 243 HLVDLAPFDESvDPVAEATAIVGELRKYDEALYEKPRWLVLNKLDMVPEDEREARVADFLDRFGWdgPVFEISALTGQGC 322
Cdd:TIGR02729 241 HLIDISPEDGS-DPVEDYEIIRNELKKYSPELAEKPRIVVLNKIDLLDEEELEELLKELKKELGK--PVFPISALTGEGL 317
                         330
                  ....*....|.
gi 1900666673 323 EALCYAIYDYL 333
Cdd:TIGR02729 318 DELLDALAELL 328
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
160-333 9.50e-100

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: 292.41  E-value: 9.50e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 160 ADVGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTG 239
Cdd:cd01898     1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 240 VLLHLVDLAPFDesvDPVAEATAIVGELRKYDEALYEKPRWLVLNKLDMVPEDEREARVADFLDRFgWDGPVFEISALTG 319
Cdd:cd01898    81 VLLHVIDLSGED---DPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELLKEL-KGKKVFPISALTG 156
                         170
                  ....*....|....
gi 1900666673 320 QGCEALCYAIYDYL 333
Cdd:cd01898   157 EGLDELLKKLAKLL 170
GTP1_OBG pfam01018
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ...
4-158 1.76e-61

GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three glycine-rich regions inserted into a small 8-stranded beta-sandwich these regions form six left-handed collagen-like helices packed and H-bonded together.


Pssm-ID: 460027 [Multi-domain]  Cd Length: 155  Bit Score: 194.49  E-value: 1.76e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673   4 IDEARIEVIAGDGGDGSASMRREKFVPFGGPDGGDGGRGGSVYAIADRNINTLIDYRYAKKHLARNGENGRGSDCYGKGG 83
Cdd:pfam01018   1 VDRAKIKVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGDVILVADENLNTLLDFRYKRHFKAENGENGGGKNCHGKNG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1900666673  84 DDVTLRMPVGTIISDMDTGELIADLTEHDQRVMLAQGGAGGLGNLHFKSSTNRAPRQKTDGKPGERRMLKLELKV 158
Cdd:pfam01018  81 EDLIIKVPVGTVVKDAETGEVLADLTEPGQRVLVAKGGRGGRGNAHFKTSTNQAPRFAEPGEPGEERWLELELKL 155
 
Name Accession Description Interval E-value
obgE PRK12299
GTPase CgtA; Reviewed
2-336 0e+00

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 547.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673   2 KFIDEARIEVIAGDGGDGSASMRREKFVPFggpdggdggrggSVYAIADRNINTLIDYRYAKKHLARNGENGRGSDCYGK 81
Cdd:PRK12299    1 KFIDEAKIYVKAGDGGNGCVSFRREKFIPFggpdggdggrggSVILEADENLNTLIDFRYKRHFKAENGENGMGRNRTGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673  82 GGDDVTLRMPVGTIISDMDTGELIADLTEHDQRVMLAQGGAGGLGNLHFKSSTNRAPRQKTDGKPGERRMLKLELKVLAD 161
Cdd:PRK12299   81 SGKDLVLKVPVGTQIYDADTGELIADLTEHGQRFLVAKGGKGGLGNAHFKSSTNRAPRYATPGEPGEERWLRLELKLLAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTGVL 241
Cdd:PRK12299  161 VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKSFVIADIPGLIEGASEGAGLGHRFLKHIERTRLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 242 LHLVDLApfdeSVDPVAEATAIVGELRKYDEALYEKPRWLVLNKLDMVPED-EREARVADFLDRFGwdGPVFEISALTGQ 320
Cdd:PRK12299  241 LHLVDIE----AVDPVEDYKTIRNELEKYSPELADKPRILVLNKIDLLDEEeEREKRAALELAALG--GPVFLISAVTGE 314
                         330
                  ....*....|....*.
gi 1900666673 321 GCEALCYAIYDYLSEH 336
Cdd:PRK12299  315 GLDELLRALWELLEEA 330
obgE PRK12298
GTPase CgtA; Reviewed
1-336 0e+00

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 546.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673   1 MKFIDEARIEVIAGDGGDGSASMRREKFVPFGGPDGGDGGRGGSVYAIADRNINTLIDYRYAKKHLARNGENGRGSDCYG 80
Cdd:PRK12298    1 MKFVDEAKIRVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVYLEADENLNTLIDYRFERHFRAERGQNGQGRDCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673  81 KGGDDVTLRMPVGTIISDMDTGELIADLTEHDQRVMLAQGGAGGLGNLHFKSSTNRAPRQKTDGKPGERRMLKLELKVLA 160
Cdd:PRK12298   81 KRGKDITIKVPVGTRVIDADTGEVIGDLTEHGQRLLVAKGGWHGLGNTRFKSSVNRAPRQKTPGTPGEERELKLELKLLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 161 DVGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTGV 240
Cdd:PRK12298  161 DVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDERSFVVADIPGLIEGASEGAGLGIRFLKHLERCRV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 241 LLHLVDLAPFDESvDPVAEATAIVGELRKYDEALYEKPRWLVLNKLDMVPEDEREARVADFLDRFGWDGPVFEISALTGQ 320
Cdd:PRK12298  241 LLHLIDIAPIDGS-DPVENARIIINELEKYSPKLAEKPRWLVFNKIDLLDEEEAEERAKAIVEALGWEGPVYLISAASGL 319
                         330
                  ....*....|....*.
gi 1900666673 321 GCEALCYAIYDYLSEH 336
Cdd:PRK12298  320 GVKELCWDLMTFIEEN 335
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
3-339 0e+00

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: 542.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673   3 FIDEARIEVIAGDGGDGSASMRREKFVPFggpdggdggrggSVYAIADRNINTLIDYRYAKKHLARNGENGRGSDCYGKG 82
Cdd:COG0536     1 FVDEAKIYVKAGDGGNGCVSFRREKYVPKggpdggdggrggDVILVADENLNTLLDFRYKRHFKAENGENGMGKNRTGKN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673  83 GDDVTLRMPVGTIISDMDTGELIADLTEHDQRVMlaqggagglgNLHFKSSTNRAPRQKTDGKPGERRMLKLELKVLADV 162
Cdd:COG0536    81 GEDLVIKVPVGTVVKDAETGEVLADLTEDGQRVVvakggrgglgNAHFKSSTNRAPRFAEPGEPGEERWLRLELKLLADV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 163 GLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTGVLL 242
Cdd:COG0536   161 GLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRSFVIADIPGLIEGASEGAGLGHRFLRHIERTRVLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 243 HLVDLAPFDESvDPVAEATAIVGELRKYDEALYEKPRWLVLNKLDMVPEDEREArVADFLDRFGwdGPVFEISALTGQGC 322
Cdd:COG0536   241 HVVDAAPLDGR-DPVEDYEIIRNELEAYSPELAEKPRIVVLNKIDLLDAEELEE-LKAELEKLG--GPVFPISAVTGEGL 316
                         330
                  ....*....|....*..
gi 1900666673 323 EALCYAIYDYLSEHSDA 339
Cdd:COG0536   317 DELLYALAELLEELRAE 333
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
3-333 0e+00

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: 537.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673   3 FIDEARIEVIAGDGGDGSASMRREKFVPFGGPDGGDGGRGGSVYAIADRNINTLIDYRYAKKHLARNGENGRGSDCYGKG 82
Cdd:TIGR02729   1 FVDEAKIFVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGSVILEADENLNTLLDFRYQRHFKAENGENGMGKNRTGKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673  83 GDDVTLRMPVGTIISDMDTGELIADLTEHDQRVMLAQGGAGGLGNLHFKSSTNRAPRQKTDGKPGERRMLKLELKVLADV 162
Cdd:TIGR02729  81 GEDLVIKVPVGTVVYDADTGELLADLTEPGQRFLVAKGGRGGLGNAHFKSSTNRAPRFATPGEPGEERWLRLELKLLADV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 163 GLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTGVLL 242
Cdd:TIGR02729 161 GLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 243 HLVDLAPFDESvDPVAEATAIVGELRKYDEALYEKPRWLVLNKLDMVPEDEREARVADFLDRFGWdgPVFEISALTGQGC 322
Cdd:TIGR02729 241 HLIDISPEDGS-DPVEDYEIIRNELKKYSPELAEKPRIVVLNKIDLLDEEELEELLKELKKELGK--PVFPISALTGEGL 317
                         330
                  ....*....|.
gi 1900666673 323 EALCYAIYDYL 333
Cdd:TIGR02729 318 DELLDALAELL 328
obgE PRK12297
GTPase CgtA; Reviewed
2-335 2.32e-153

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 438.38  E-value: 2.32e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673   2 KFIDEARIEVIAGDGGDGSASMRREKFVPFGGPDGGDGGRGGSVYAIADRNINTLIDYRYAKKHLARNGENGRGSDCYGK 81
Cdd:PRK12297    1 MFIDQAKIYVKAGDGGDGMVSFRREKYVPKGGPDGGDGGKGGSVIFVADEGLRTLLDFRYKRHFKAENGENGMGKNMHGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673  82 GGDDVTLRMPVGTIISDMDTGELIADLTEHDQRVMLAQGGAGGLGNLHFKSSTNRAPRQKTDGKPGERRMLKLELKVLAD 161
Cdd:PRK12297   81 NGEDLIIKVPVGTVVKDAETGEVIADLVEPGQEVVVAKGGRGGRGNAHFATSTNQAPRIAENGEPGEERELRLELKLLAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTGVL 241
Cdd:PRK12297  161 VGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRSFVMADIPGLIEGASEGVGLGHQFLRHIERTRVI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 242 LHLVDLAPFdESVDPVAEATAIVGELRKYDEALYEKPRWLVLNKLDMvpeDEREARVADFLDRFGWdgPVFEISALTGQG 321
Cdd:PRK12297  241 VHVIDMSGS-EGRDPIEDYEKINKELKLYNPRLLERPQIVVANKMDL---PEAEENLEEFKEKLGP--KVFPISALTGQG 314
                         330
                  ....*....|....
gi 1900666673 322 CEALCYAIYDYLSE 335
Cdd:PRK12297  315 LDELLYAVAELLEE 328
obgE PRK12296
GTPase CgtA; Reviewed
1-340 2.06e-110

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 331.83  E-value: 2.06e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673   1 MKFIDEARIEVIAGDGGDGSASMRREKFVPFGGPDGGDGGRGGSVYAIADRNINTLIDYRYAKKHLARNGENGRGSDCYG 80
Cdd:PRK12296    2 PRFVDRVVLHVKAGDGGNGCASVHREKFKPLGGPDGGNGGRGGSVVLVVDPQVTTLLDFHFRPHRKATNGKPGMGDNRDG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673  81 KGGDDVTLRMPVGTIISDMDtGELIADLTEHDQRVMLAQGGAGGLGNLHFKSSTNRAPRQKTDGKPGERRMLKLELKVLA 160
Cdd:PRK12296   82 AAGEDLVLPVPDGTVVLDED-GEVLADLVGAGTRFVAAAGGRGGLGNAALASKARKAPGFALLGEPGEERDLVLELKSVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 161 DVGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGpSKSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTGV 240
Cdd:PRK12296  161 DVGLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQAG-DTRFTVADVPGLIPGASEGKGLGLDFLRHIERCAV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 241 LLHLVDLAPFDESVDPVAEATAIVGELRKYDEALY---------EKPRWLVLNKLDmVPE-DEREARVADFLDRFGWdgP 310
Cdd:PRK12296  240 LVHVVDCATLEPGRDPLSDIDALEAELAAYAPALDgdlglgdlaERPRLVVLNKID-VPDaRELAEFVRPELEARGW--P 316
                         330       340       350
                  ....*....|....*....|....*....|
gi 1900666673 311 VFEISALTGQGCEALCYAIYDYLSEHSDAH 340
Cdd:PRK12296  317 VFEVSAASREGLRELSFALAELVEEARAAE 346
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
160-333 9.50e-100

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: 292.41  E-value: 9.50e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 160 ADVGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTG 239
Cdd:cd01898     1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 240 VLLHLVDLAPFDesvDPVAEATAIVGELRKYDEALYEKPRWLVLNKLDMVPEDEREARVADFLDRFgWDGPVFEISALTG 319
Cdd:cd01898    81 VLLHVIDLSGED---DPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELLKEL-KGKKVFPISALTG 156
                         170
                  ....*....|....
gi 1900666673 320 QGCEALCYAIYDYL 333
Cdd:cd01898   157 EGLDELLKKLAKLL 170
GTP1_OBG pfam01018
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ...
4-158 1.76e-61

GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three glycine-rich regions inserted into a small 8-stranded beta-sandwich these regions form six left-handed collagen-like helices packed and H-bonded together.


Pssm-ID: 460027 [Multi-domain]  Cd Length: 155  Bit Score: 194.49  E-value: 1.76e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673   4 IDEARIEVIAGDGGDGSASMRREKFVPFGGPDGGDGGRGGSVYAIADRNINTLIDYRYAKKHLARNGENGRGSDCYGKGG 83
Cdd:pfam01018   1 VDRAKIKVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGDVILVADENLNTLLDFRYKRHFKAENGENGGGKNCHGKNG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1900666673  84 DDVTLRMPVGTIISDMDTGELIADLTEHDQRVMLAQGGAGGLGNLHFKSSTNRAPRQKTDGKPGERRMLKLELKV 158
Cdd:pfam01018  81 EDLIIKVPVGTVVKDAETGEVLADLTEPGQRVLVAKGGRGGRGNAHFKTSTNQAPRFAEPGEPGEERWLELELKL 155
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
163-333 5.85e-42

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: 144.46  E-value: 5.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 163 GLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTGVLL 242
Cdd:cd01881     1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 243 HLVDLAPfDESVDPVAEATAIVGELRKYDEALYEKPRWLVLNKLDMVPEDEREarvADFLDRFGWDGPVFEISALTGQGC 322
Cdd:cd01881    81 HVIDASE-DCVGDPLEDQKTLNEEVSGSFLFLKNKPEMIVANKIDMASENNLK---RLKLDKLKRGIPVVPTSALTRLGL 156
                         170
                  ....*....|.
gi 1900666673 323 EALCYAIYDYL 333
Cdd:cd01881   157 DRVIRTIRKLL 167
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
161-285 1.32e-32

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: 118.11  E-value: 1.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 161 DVGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPsKSFVIADIPGLIEGAAEGAGLGHQFLRHlQRTGV 240
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKG-KQIILVDTPGLIEGASEGEGLGRAFLAI-IEADL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1900666673 241 LLHLVDlapFDESVDPVAEataivgELRKYDEAlYEKPRWLVLNK 285
Cdd:pfam01926  79 ILFVVD---SEEGITPLDE------ELLELLRE-NKKPIILVLNK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
163-333 4.83e-27

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: 105.02  E-value: 4.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 163 GLLGMPNAGKSTFISSVSNAKPKI-ADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTGVL 241
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVGIvSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 242 LHLVdlapfDESVDPVaEATAIVGELRKydealYEKPRWLVLNKLDMVPEDEREARVADFLDRFGWDGPVFEISALTGQG 321
Cdd:cd00880    81 LLVV-----DSDLTPV-EEEAKLGLLRE-----RGKPVLLVLNKIDLVPESEEEELLRERKLELLPDLPVIAVSALPGEG 149
                         170
                  ....*....|..
gi 1900666673 322 CEALCYAIYDYL 333
Cdd:cd00880   150 IDELRKKIAELL 161
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
166-341 3.12e-24

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 101.45  E-value: 3.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 166 GMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKsFVIADIPGL----------IEGAAEGAglghqfLRHL 235
Cdd:COG1084   167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGR-YQVIDTPGLldrplserneIERQAILA------LKHL 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 236 qrTGVLLHLVDlaPFDESVDPVAEataivgELRKYDE--ALYEKPRWLVLNKLDMVPEDEREARVADfldrfgwdgPVFE 313
Cdd:COG1084   240 --ADVILFLFD--PSETCGYSLEE------QLNLLEEirSLFDVPVIVVINKIDLSDEEELKEAEEE---------ADIK 300
                         170       180
                  ....*....|....*....|....*...
gi 1900666673 314 ISALTGQGCEALCYAIYDYLSEHSDAHR 341
Cdd:COG1084   301 ISALTGEGVDELLDELIEALEEEPELPP 328
PTZ00258 PTZ00258
GTP-binding protein; Provisional
162-304 1.59e-23

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 100.41  E-value: 1.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRV------------GPsKSFV-----IADIPGLIEGAAEG 224
Cdd:PTZ00258   24 MGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVpderfdwlckhfKP-KSIVpaqldITDIAGLVKGASEG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 225 AGLGHQFLRHLQRTGVLLHLV------DLAPFDESVDPVAEATAIVGELRKYDEALYEKPRWLVLNKLDMVPEDEREARV 298
Cdd:PTZ00258  103 EGLGNAFLSHIRAVDGIYHVVrafedeDITHVEGEIDPVRDLEIISSELILKDLEFVEKRLDELTKKRKKKKKKKEEKVE 182

                  ....*.
gi 1900666673 299 ADFLDR 304
Cdd:PTZ00258  183 LDVLKK 188
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
162-246 1.79e-22

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: 96.53  E-value: 1.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGV--VRV-----------GPSKSFVIA----------DIPGLI 218
Cdd:cd01899     1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVgyVRVecpckelgvscNPRYGKCIDgkryvpveliDVAGLV 80
                          90       100
                  ....*....|....*....|....*...
gi 1900666673 219 EGAAEGAGLGHQFLRHLQRTGVLLHLVD 246
Cdd:cd01899    81 PGAHEGKGLGNQFLDDLRDADVLIHVVD 108
PRK09602 PRK09602
translation-associated GTPase; Reviewed
162-246 2.87e-22

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 96.80  E-value: 2.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGV--VRV-----------GPSKSFVI----------ADIPGLI 218
Cdd:PRK09602    4 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayVRVecpckelgvkcNPRNGKCIdgtrfipvelIDVAGLV 83
                          90       100
                  ....*....|....*....|....*...
gi 1900666673 219 EGAAEGAGLGHQFLRHLQRTGVLLHLVD 246
Cdd:PRK09602   84 PGAHEGRGLGNQFLDDLRQADALIHVVD 111
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
162-300 7.39e-22

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: 93.68  E-value: 7.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRV------------GPSK------SFViaDIPGLIEGAAE 223
Cdd:cd01900     1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVpderldklaeivKPKKivpatiEFV--DIAGLVKGASK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 224 GAGLGHQFLRHLQRTGVLLHLVDLapFDE--------SVDPVAEATAIVGELRKYDEALYEKprwlVLNKLdmvpedERE 295
Cdd:cd01900    79 GEGLGNKFLSHIREVDAIAHVVRC--FEDddithvegSVDPVRDIEIINTELILADLETIEK----RLERL------EKK 146

                  ....*
gi 1900666673 296 ARVAD 300
Cdd:cd01900   147 AKSGD 151
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
163-329 1.15e-19

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: 84.82  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 163 GLLGMPNAGKSTFISSVSNAKPKI-ADYPFTTLAPNLGVVRV-GPSKSFVIADIPGLIEGaaEGAGLGHQFLRHLQRTGV 240
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEvSDVPGTTRDPDVYVKELdKGKVKLVLVDTPGLDEF--GGLGREELARLLLRGADL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 241 LLHLVDlapfdeSVDPVAEATAIVGELRKYDEalYEKPRWLVLNKLDMVPEDEREARVADFLDRFGWDGPVFEISALTGQ 320
Cdd:cd00882    79 ILLVVD------STDRESEEDAKLLILRRLRK--EGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFEVSAKTGE 150

                  ....*....
gi 1900666673 321 GCEALCYAI 329
Cdd:cd00882   151 GVDELFEKL 159
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
162-267 1.97e-19

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 88.15  E-value: 1.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRV------------GPSK------SFViaDIPGLIEGAAE 223
Cdd:COG0012     3 CGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVpderldklaeivKPKKivpatiEFV--DIAGLVKGASK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1900666673 224 GAGLGHQFLRHLQRTGVLLHLV------DLAPFDESVDPVAEATAIVGEL 267
Cdd:COG0012    81 GEGLGNQFLANIREVDAIVHVVrcfeddNVTHVEGSVDPLRDIETINTEL 130
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
160-333 5.54e-19

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 87.16  E-value: 5.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 160 ADVGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKsFVIADIPGLIEGAAEGAGLGHQFLRhLQRTG 239
Cdd:COG1163    64 ATVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLEYKGAK-IQILDVPGLIEGAASGKGRGKEVLS-VVRNA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 240 VLLHLVdLAPFDE--------------------------------------SVDPVAEATAIVGELRKY----------- 270
Cdd:COG1163   142 DLILIV-LDVFELeqydvlkeelydagirlnkpppdvtiekkgkggirvnsTGKLDLDEEDIKKILREYgivnadvlire 220
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1900666673 271 ----DE---ALYE----KPRWLVLNKLDMVPEDEREarvaDFLDRFGWDGPVFEISALTGQGCEALCYAIYDYL 333
Cdd:COG1163   221 dvtlDDlidALMGnrvyKPAIVVVNKIDLADEEYVE----ELKSKLPDGVPVIFISAEKGIGLEELKEEIFEEL 290
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
166-325 6.95e-19

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: 82.99  E-value: 6.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 166 GMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIaDIPGL----------IEGAAEGAglghqfLRHL 235
Cdd:cd01897     7 GYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVI-DTPGIldrpleerntIEMQAITA------LAHL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 236 QrtGVLLHLVDLApfDESVDPVAEATAIVGELRKydeaLYEKPRWLVLNKLDMVPEDEREARVADFLDRfgwDGPVFEIS 315
Cdd:cd01897    80 R--AAVLFFIDPS--ETCGYSIEEQLSLFKEIKP----LFNKPVIVVLNKIDLLTEEDLSEIEKELEKE---GEEVIKIS 148
                         170
                  ....*....|
gi 1900666673 316 ALTGQGCEAL 325
Cdd:cd01897   149 TLTEEGVDEL 158
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
160-232 4.63e-18

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: 82.21  E-value: 4.63e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1900666673 160 ADVGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKsFVIADIPGLIEGAAEGAGLGHQFL 232
Cdd:cd01896     1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAK-IQLLDLPGIIEGASDGKGRGRQVI 72
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
162-336 3.64e-14

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 71.94  E-value: 3.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTF--------ISSVSNaKPKiadypfTTLAPNLGVVRVGPSKsFVIADIPGLIEGaaegaglGHQFLR 233
Cdd:COG1159     6 VAIVGRPNVGKSTLlnalvgqkVSIVSP-KPQ------TTRHRIRGIVTREDAQ-IVFVDTPGIHKP-------KRKLGR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 234 HLQRT--------GVLLHLVDLapfDESVDPvaEATAIVGELRKYDealyeKPRWLVLNKLDMVPEDEREARVADFLDRF 305
Cdd:COG1159    71 RMNKAawsaledvDVILFVVDA---TEKIGE--GDEFILELLKKLK-----TPVILVINKIDLVKKEELLPLLAEYSELL 140
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1900666673 306 GWDgPVFEISALTGQGCEALCYAIYDYLSEH 336
Cdd:COG1159   141 DFA-EIVPISALKGDNVDELLDEIAKLLPEG 170
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
162-333 8.72e-14

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: 68.64  E-value: 8.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTF--------ISSVSNaKPKiadypfTTLAPNLGVVrvgpSKS---FVIADIPGLIEgaaEGAGLGHQ 230
Cdd:cd04163     6 VAIIGRPNVGKSTLlnalvgqkISIVSP-KPQ------TTRNRIRGIY----TDDdaqIIFVDTPGIHK---PKKKLGER 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 231 FLRH----LQRTGVLLHLVDLapfdeSVDPVAEATAIVGELRKYdealyEKPRWLVLNKLDMVPEDEREARVADFLDRFG 306
Cdd:cd04163    72 MVKAawsaLKDVDLVLFVVDA-----SEWIGEGDEFILELLKKS-----KTPVILVLNKIDLVKDKEDLLPLLEKLKELH 141
                         170       180
                  ....*....|....*....|....*..
gi 1900666673 307 WDGPVFEISALTGQGCEALCYAIYDYL 333
Cdd:cd04163   142 PFAEIFPISALKGENVDELLEYIVEYL 168
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
162-333 4.00e-13

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: 67.48  E-value: 4.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEgaaegaGLGHQ----FLRHLQR 237
Cdd:cd01878    44 VALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTTRRIKLPGGREVLLTDTVGFIR------DLPHQlveaFRSTLEE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 238 TG---VLLHLVDLApfdesvDPVAEAT-----AIVGELrkydeALYEKPRWLVLNKLDMVPEDEREARvadflDRFGWDG 309
Cdd:cd01878   118 VAeadLLLHVVDAS------DPDREEQietveEVLKEL-----GADDIPIILVLNKIDLLDDEELEER-----LRAGRPD 181
                         170       180
                  ....*....|....*....|....
gi 1900666673 310 PVFeISALTGQGCEALCYAIYDYL 333
Cdd:cd01878   182 AVF-ISAKTGEGLDLLKEAIEELL 204
era PRK00089
GTPase Era; Reviewed
162-336 9.51e-12

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 65.07  E-value: 9.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAK-----PKiadyPFTTLAPNLGVVRVGPSKsFVIADIPGLIEGaaegaglGHQFLRHLQ 236
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVGQKisivsPK----PQTTRHRIRGIVTEDDAQ-IIFVDTPGIHKP-------KRALNRAMN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 237 RTgVL--LHLVDLAPFdesvdpVAEATAIVGElrkYDEALYEK------PRWLVLNKLDMV-PEDEREARVADFLDRFGW 307
Cdd:PRK00089   76 KA-AWssLKDVDLVLF------VVDADEKIGP---GDEFILEKlkkvktPVILVLNKIDLVkDKEELLPLLEELSELMDF 145
                         170       180
                  ....*....|....*....|....*....
gi 1900666673 308 DgPVFEISALTGQGCEALCYAIYDYLSEH 336
Cdd:PRK00089  146 A-EIVPISALKGDNVDELLDVIAKYLPEG 173
PRK11058 PRK11058
GTPase HflX; Provisional
162-334 6.40e-11

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 63.20  E-value: 6.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGPSKSFVIADIPGLIEgaaegaGLGHQ----FLRHLQR 237
Cdd:PRK11058  200 VSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIR------HLPHDlvaaFKATLQE 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 238 T---GVLLHLVDLApfDESVDPVAEATAIVGELRKYDEAlyekPRWLVLNKLDMVpeDEREARVadflDRFGWDGPV-FE 313
Cdd:PRK11058  274 TrqaTLLLHVVDAA--DVRVQENIEAVNTVLEEIDAHEI----PTLLVMNKIDML--DDFEPRI----DRDEENKPIrVW 341
                         170       180
                  ....*....|....*....|.
gi 1900666673 314 ISALTGQGCEALCYAIYDYLS 334
Cdd:PRK11058  342 LSAQTGAGIPLLFQALTERLS 362
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
162-335 9.49e-11

GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other]


Pssm-ID: 129528 [Multi-domain]  Cd Length: 270  Bit Score: 61.64  E-value: 9.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKI-ADYPFTTLAPNLGVVRVGPSKSFVIaDIPGLIEgaaEGAGLGHQFLRHLQRTgv 240
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISItSPKAQTTRNRISGIHTTGASQIIFI-DTPGFHE---KKHSLNRLMMKEARSA-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 241 lLHLVDLAPFdesvdpVAEATAIVGELRKYDEALYE--KPRWLVLNKLDMVPEDEREARVADFLDRFGWDgPVFEISALT 318
Cdd:TIGR00436  77 -IGGVDLILF------VVDSDQWNGDGEFVLTKLQNlkRPVVLTRNKLDNKFKDKLLPLIDKYAILEDFK-DIVPISALT 148
                         170
                  ....*....|....*..
gi 1900666673 319 GQGCEALCYAIYDYLSE 335
Cdd:TIGR00436 149 GDNTSFLAAFIEVHLPE 165
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
162-325 3.08e-10

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: 58.15  E-value: 3.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKI-ADYPFTTLAPNLGVVRV-GPSKSFVIADIPGLIEGAAEGAGlghqflrHLQRTG 239
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSItEYYPGTTRNYVTTVIEEdGKTYKFNLLDTAGQEDYDAIRRL-------YYPQVE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 240 VLLHLVDLAPFDESV-DPVAEATAIVGELRKYDealyeKPRWLVLNKLDMVPEDEREARVADFLDRFGwdGPVFEISALT 318
Cdd:TIGR00231  77 RSLRVFDIVILVLDVeEILEKQTKEIIHHADSG-----VPIILVGNKIDLKDADLKTHVASEFAKLNG--EPIIPLSAET 149

                  ....*..
gi 1900666673 319 GQGCEAL 325
Cdd:TIGR00231 150 GKNIDSA 156
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
139-333 6.31e-10

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: 59.79  E-value: 6.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 139 RQK----TDGkPGE------RRM-------LKLELKVLAD----------------VGLLGMPNAGKSTFISSVSNAKPK 185
Cdd:TIGR03156 137 RQGggigTRG-PGEtqletdRRLireriaqLKKELEKVEKqrerqrrrrkradvptVALVGYTNAGKSTLFNALTGADVY 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 186 IADYPFTTLAPNLGVVRVGPSKSFVIADIPGliegaaegaglghqFLRHLQRTGV---------------LLHLVDLA-P 249
Cdd:TIGR03156 216 AADQLFATLDPTTRRLDLPDGGEVLLTDTVG--------------FIRDLPHELVaafratleevreadlLLHVVDASdP 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 250 -FDESVDPVAEataIVGELrkydEALyEKPRWLVLNKLDMVPEDEREARVADFLDRfgwdgpVFeISALTGQGCEALCYA 328
Cdd:TIGR03156 282 dREEQIEAVEK---VLEEL----GAE-DIPQLLVYNKIDLLDEPRIERLEEGYPEA------VF-VSAKTGEGLDLLLEA 346

                  ....*
gi 1900666673 329 IYDYL 333
Cdd:TIGR03156 347 IAERL 351
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
162-333 4.75e-08

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 52.13  E-value: 4.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKpKIADY---PFTTLAPNLgvVRVGPSKSFViaDIPG----------------LIEgaa 222
Cdd:cd01876     2 VAFAGRSNVGKSSLINALTNRK-KLARTsktPGRTQLINF--FNVGDKFRLV--DLPGygyakvskevrekwgkLIE--- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 223 egaglghQFL---RHLQRtgvLLHLVDlapfdesvdpvaeataIVGELRKYDEALYEkprWL---------VLNKLDMVP 290
Cdd:cd01876    74 -------EYLenrENLKG---VVLLID----------------ARHGPTPIDLEMLE---FLeelgipfliVLTKADKLK 124
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1900666673 291 EDEREAR---VADFLDRFGWDGPVFEISALTGQGCEALCYAIYDYL 333
Cdd:cd01876   125 KSELAKVlkkIKEELNLFNILPPVILFSSKKGTGIDELRALIAEWL 170
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
164-333 5.42e-07

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: 49.03  E-value: 5.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 164 LLGMPNAGKSTFIssvsNAkpkiadypfttLApnlgvvrvGPSKSFViADIPG----LIEGaaegaglghqflrHLQRTG 239
Cdd:cd04164     8 IAGKPNVGKSSLL----NA-----------LA--------GRDRAIV-SDIAGttrdVIEE-------------EIDLGG 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 240 VLLHLVDLAPFDESVDPV------------AEA----------TAIVGELRKYDEALYEKPRWLVLNKLDMVPEDEREAR 297
Cdd:cd04164    51 IPVRLIDTAGLRETEDEIekigierareaiEEAdlvllvvdasEGLDEEDLEILELPAKKPVIVVLNKSDLLSDAEGISE 130
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1900666673 298 VADfldrfgwdGPVFEISALTGQGCEALCYAIYDYL 333
Cdd:cd04164   131 LNG--------KPIIAISAKTGEGIDELKEALLELA 158
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
164-337 2.35e-06

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: 49.29  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 164 LLGMPNAGKSTFIssvsNAkpkiadypfttLApnlgvvrvGPSKSFViADIPG----LIEGaaegaglghqflrHLQRTG 239
Cdd:COG0486   218 IVGRPNVGKSSLL----NA-----------LL--------GEERAIV-TDIAGttrdVIEE-------------RINIGG 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 240 VLLHLVDLAPFDESVDPV------------AEATAIV------GELRKYDEALYE----KPRWLVLNKLDMVPEDEREAR 297
Cdd:COG0486   261 IPVRLIDTAGLRETEDEVekigierareaiEEADLVLllldasEPLTEEDEEILEklkdKPVIVVLNKIDLPSEADGELK 340
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1900666673 298 VADfldrfgwDGPVFEISALTGQGCEALCYAIYDYLSEHS 337
Cdd:COG0486   341 SLP-------GEPVIAISAKTGEGIDELKEAILELVGEGA 373
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
282-325 6.84e-05

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 44.90  E-value: 6.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1900666673 282 VLNKLDMVPED---EREARVADFLDRFGWDG-PVFEISALTGQGCEAL 325
Cdd:COG3276   110 VLTKADLVDEEwleLVEEEIRELLAGTFLEDaPIVPVSAVTGEGIDEL 157
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
281-325 1.09e-04

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ 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. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 42.77  E-value: 1.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1900666673 281 LVLNKLDMVPEDEREARVADFLDrfgWDGPVFEISALTGQGCEAL 325
Cdd:cd01854    38 IVLNKADLVDDEELEELLEIYEK---LGYPVLAVSAKTGEGLDEL 79
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
164-335 1.22e-04

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 43.95  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 164 LLGMPNAGKSTFIssvsNAkpkiadypfttLApnlgvvrvGPSKSFViADIPG----LIEGaaegaglghqflrHLQRTG 239
Cdd:PRK05291  220 IAGRPNVGKSSLL----NA-----------LL--------GEERAIV-TDIAGttrdVIEE-------------HINLDG 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 240 VLLHLVDLAPFDESVDPV------------AEATAIV------GELRKYDEALYE----KPRWLVLNKLDMVPEDEREAr 297
Cdd:PRK05291  263 IPLRLIDTAGIRETDDEVekigiersreaiEEADLVLlvldasEPLTEEDDEILEelkdKPVIVVLNKADLTGEIDLEE- 341
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1900666673 298 vadfldrfGWDGPVFEISALTGQGCEALCYAIYDYLSE 335
Cdd:PRK05291  342 --------ENGKPVIRISAKTGEGIDELREAIKELAFG 371
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
281-325 1.51e-04

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 42.14  E-value: 1.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1900666673 281 LVLNKLDMVPEDEREARVADFLDRFGWdgPVFEISALTGQGCEAL 325
Cdd:pfam03193  58 IVLNKIDLLDEEEELEELLKIYRAIGY--PVLFVSAKTGEGIEAL 100
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
162-329 2.28e-04

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 43.24  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKIA-DYPFTTLAPNLGVVRVGpSKSFVIADIPGL------IEGAAEGAGLGHQFLrh 234
Cdd:PRK09518  453 VALVGRPNVGKSSLLNQLTHEERAVVnDLAGTTRDPVDEIVEID-GEDWLFIDTAGIkrrqhkLTGAEYYSSLRTQAA-- 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 235 LQRTGVLLHLVDlapfdeSVDPVAEAtaivgELRKYDEALyEKPRWLVL--NKLDMVPEDERE--ARVADF-LDRFGWdG 309
Cdd:PRK09518  530 IERSELALFLFD------ASQPISEQ-----DLKVMSMAV-DAGRALVLvfNKWDLMDEFRRQrlERLWKTeFDRVTW-A 596
                         170       180
                  ....*....|....*....|
gi 1900666673 310 PVFEISALTGQGCEALCYAI 329
Cdd:PRK09518  597 RRVNLSAKTGWHTNRLAPAM 616
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
164-216 3.21e-04

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: 40.90  E-value: 3.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1900666673 164 LLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGpSKSFVIADIPG 216
Cdd:cd01879     2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLG-GKEIEIVDLPG 53
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
162-339 6.71e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 41.57  E-value: 6.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKST-FissvsN--AKPKIA---DYPFTTLAPNLGVVRVGpSKSFVIADIPGlIEGAAEG--AGLGHQFLR 233
Cdd:PRK00093    4 VAIVGRPNVGKSTlF-----NrlTGKRDAivaDTPGVTRDRIYGEAEWL-GREFILIDTGG-IEPDDDGfeKQIREQAEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 234 HLQRTGVLLHLVD----LAPFDESvdpVAEataivgELRKYDealyeKPRWLVLNKLDmvpEDEREARVADFLdRFGWDG 309
Cdd:PRK00093   77 AIEEADVILFVVDgragLTPADEE---IAK------ILRKSN-----KPVILVVNKVD---GPDEEADAYEFY-SLGLGE 138
                         170       180       190
                  ....*....|....*....|....*....|
gi 1900666673 310 PVFeISALTGQGCEALCYAIYDYLSEHSDA 339
Cdd:PRK00093  139 PYP-ISAEHGRGIGDLLDAILEELPEEEEE 167
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
273-334 8.02e-04

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 39.97  E-value: 8.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1900666673 273 ALYEKPRWLVLNKLDMVPE---DEREARVADFLDRFGW------DGPVFEISALTGQGCEALCYAIYDYLS 334
Cdd:cd00881   111 LAGGLPIIVAVNKIDRVGEedfDEVLREIKELLKLIGFtflkgkDVPIIPISALTGEGIEELLDAIVEHLP 181
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
164-321 1.02e-03

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: 39.34  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 164 LLGMPNAGKST-FissvsN--AKPKIA---DYPFTTLAPNLGVVRVGpSKSFVIADIPGlIEGAAEG--AGLGHQFLRHL 235
Cdd:cd01894     2 IVGRPNVGKSTlF-----NrlTGRRDAivsDTPGVTRDRKYGEAEWG-GREFILIDTGG-IEPDDEGisKEIREQAEIAI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 236 QRTGVLLHLVD----LAPFDESvdpvaeataIVGELRKYDealyeKPRWLVLNKLDmvpEDEREARVADFLdRFGWDGPV 311
Cdd:cd01894    75 EEADVILFVVDgregLTPADEE---------IAKYLRKSK-----KPVILVVNKID---NIKEEEEAAEFY-SLGFGEPI 136
                         170
                  ....*....|
gi 1900666673 312 FeISALTGQG 321
Cdd:cd01894   137 P-ISAEHGRG 145
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
162-329 1.41e-03

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 38.95  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKIA-DYPFTTLAPNLGVVRVGpSKSFVIADIPGL-----IEGAAEGAGLgHQFLRHL 235
Cdd:cd01895     5 IAIIGRPNVGKSSLLNALLGEERVIVsDIAGTTRDSIDVPFEYD-GQKYTLIDTAGIrkkgkVTEGIEKYSV-LRTLKAI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 236 QRTGVLLHLVDlapfdeSVDPVAEA-TAIVGELRKYDEALYekprwLVLNKLDMVPEDE--REARVADFLDRFGW--DGP 310
Cdd:cd01895    83 ERADVVLLVLD------ASEGITEQdLRIAGLILEEGKALI-----IVVNKWDLVEKDEktMKEFEKELRRKLPFldYAP 151
                         170
                  ....*....|....*....
gi 1900666673 311 VFEISALTGQGCEALCYAI 329
Cdd:cd01895   152 IVFISALTGQGVDKLFDAI 170
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
275-333 3.11e-03

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 38.27  E-value: 3.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1900666673 275 YEKPRWLVLNKLDMVPEDEREARVADFLDRF-------GWDGPVFEISALTGQGCEALCYAIYDYL 333
Cdd:pfam00009 120 LGVPIIVFINKMDRVDGAELEEVVEEVSRELlekygedGEFVPVVPGSALKGEGVQTLLDALDEYL 185
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
276-329 3.14e-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: 37.75  E-value: 3.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1900666673 276 EKPRWLVLNKLDMVPEDEREARVADFLDRFGWdgPVFEISALTGQGCEALCYAI 329
Cdd:cd01849    28 NKKLIMVLNKADLVPKEVLRKWVAELSELYGT--KTFFISATNGQGILKLKAEI 79
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
148-216 5.66e-03

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: 37.12  E-value: 5.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 148 ERRMLKLELKVLadvgLLGMPNAGKSTFISSVSNAK-PKIADYPFTTLapNLGVVRVGPskSFVIADIPG 216
Cdd:cd01856   108 AKGLLPRPLRAM----VVGIPNVGKSTLINRLRGKKvAKVGNKPGVTR--GQQWIRIGP--NIELLDTPG 169
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
169-316 8.14e-03

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 36.76  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 169 NAGKSTFISSVSNAK-------PkiadypfTTLAPNlgVVRVGPSKSFVIADIPgliegaaegaGLGHQFLRHLQRTGVL 241
Cdd:cd09912    10 SAGKSTLLNALLGEEvlptgvtP-------TTAVIT--VLRYGLLKGVVLVDTP----------GLNSTIEHHTEITESF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 242 LHLVDLAPFDESVDPVAEATAiVGELRKYdeALYEKPR-WLVLNKLDMVPEDEREARVADF------LDRFGWDGPVFEI 314
Cdd:cd09912    71 LPRADAVIFVLSADQPLTESE-REFLKEI--LKWSGKKiFFVLNKIDLLSEEELEEVLEYSreelgvLELGGGEPRIFPV 147

                  ..
gi 1900666673 315 SA 316
Cdd:cd09912   148 SA 149
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
162-341 9.68e-03

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 37.79  E-value: 9.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 162 VGLLGMPNAGKSTFISSVSNAKPKIADYPFTTLAPNLGVVRVGpSKSFVIADIPGLIegaaegaglghqflrhlqrtgvl 241
Cdd:COG0370     6 IALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLK-GKEIELVDLPGTY----------------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900666673 242 lhlvDLAPF--DESV--------DP-----VAEATAI------VGELRKYDealyeKPRWLVLNKLDMVpedERE----- 295
Cdd:COG0370    62 ----SLSAYspDEKVardflleeKPdvvvnVVDATNLernlylTLQLLELG-----IPVVLALNMMDEA---EKKgikid 129
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1900666673 296 -ARVADFLdrfgwdG-PVFEISALTGQGCEALCYAIYDYLSEHSDAHR 341
Cdd:COG0370   130 vEKLSKLL------GvPVVPTSARKGKGIDELKEAIIEAAEGKKPRPL 171
 
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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