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Conserved domains on  [gi|15833316|ref|NP_312089|]
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GTPase involved in cell partitioning and DNA repair [Escherichia coli O157:H7 str. Sakai]

Protein Classification

GTPase Obg( domain architecture ID 11485759)

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

EC:  3.6.5.-
Gene Ontology:  GO:0003924|GO:0005525|GO:0042254
PubMed:  35610748

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
obgE PRK12298
GTPase CgtA; Reviewed
1-390 0e+00

GTPase CgtA; Reviewed


:

Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 684.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316    1 MKFVDEASILVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTG 80
Cdd:PRK12298   1 MKFVDEAKIRVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVYLEADENLNTLIDYRFERHFRAERGQNGQGRDCTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   81 KRGKDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKRELLLELMLLA 160
Cdd:PRK12298  81 KRGKDITIKVPVGTRVIDADTGEVIGDLTEHGQRLLVAKGGWHGLGNTRFKSSVNRAPRQKTPGTPGEERELKLELKLLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  161 DVGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRV 240
Cdd:PRK12298 161 DVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDERSFVVADIPGLIEGASEGAGLGIRFLKHLERCRV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  241 LLHLIDIDPIDGTDPVENARIIISELEKYSQDLAAKPRWLVFNKIDLLDKVEAEEKAKAIAEALGWEDKYYLISAASGLG 320
Cdd:PRK12298 241 LLHLIDIAPIDGSDPVENARIIINELEKYSPKLAEKPRWLVFNKIDLLDEEEAEERAKAIVEALGWEGPVYLISAASGLG 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  321 VKDLCWDVMTFIIENPVVQAEEAKQPEKVEFMWDDYHRQQLEEIAEEDDEDWDDDWDEDDEEGVEFIYKR 390
Cdd:PRK12298 321 VKELCWDLMTFIEENPREEAEEAEAPEKVEFMWDDYHREQLEEVEEEDDDDWDDDWDEDDDEGVEVIYKR 390
 
Name Accession Description Interval E-value
obgE PRK12298
GTPase CgtA; Reviewed
1-390 0e+00

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 684.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316    1 MKFVDEASILVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTG 80
Cdd:PRK12298   1 MKFVDEAKIRVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVYLEADENLNTLIDYRFERHFRAERGQNGQGRDCTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   81 KRGKDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKRELLLELMLLA 160
Cdd:PRK12298  81 KRGKDITIKVPVGTRVIDADTGEVIGDLTEHGQRLLVAKGGWHGLGNTRFKSSVNRAPRQKTPGTPGEERELKLELKLLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  161 DVGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRV 240
Cdd:PRK12298 161 DVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDERSFVVADIPGLIEGASEGAGLGIRFLKHLERCRV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  241 LLHLIDIDPIDGTDPVENARIIISELEKYSQDLAAKPRWLVFNKIDLLDKVEAEEKAKAIAEALGWEDKYYLISAASGLG 320
Cdd:PRK12298 241 LLHLIDIAPIDGSDPVENARIIINELEKYSPKLAEKPRWLVFNKIDLLDEEEAEERAKAIVEALGWEGPVYLISAASGLG 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  321 VKDLCWDVMTFIIENPVVQAEEAKQPEKVEFMWDDYHRQQLEEIAEEDDEDWDDDWDEDDEEGVEFIYKR 390
Cdd:PRK12298 321 VKELCWDLMTFIEENPREEAEEAEAPEKVEFMWDDYHREQLEEVEEEDDDDWDDDWDEDDDEGVEVIYKR 390
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
3-348 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: 563.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   3 FVDEASILVVAGDGGNGCVSFRREKYIPKggpdggdggdggdVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTGKR 82
Cdd:COG0536   1 FVDEAKIYVKAGDGGNGCVSFRREKYVPKggpdggdggrggdVILVADENLNTLLDFRYKRHFKAENGENGMGKNRTGKN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  83 GKDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKRELLLELMLLADV 162
Cdd:COG0536  81 GEDLVIKVPVGTVVKDAETGEVLADLTEDGQRVVVAKGGRGGLGNAHFKSSTNRAPRFAEPGEPGEERWLRLELKLLADV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 163 GMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRVLL 242
Cdd:COG0536 161 GLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRSFVIADIPGLIEGASEGAGLGHRFLRHIERTRVLL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 243 HLIDIDPIDGTDPVENARIIISELEKYSQDLAAKPRWLVFNKIDLLDKVEAEEKAKAIaEALGWEdkYYLISAASGLGVK 322
Cdd:COG0536 241 HVVDAAPLDGRDPVEDYEIIRNELEAYSPELAEKPRIVVLNKIDLLDAEELEELKAEL-EKLGGP--VFPISAVTGEGLD 317
                       330       340
                ....*....|....*....|....*.
gi 15833316 323 DLCWDVMTFIIENPVVQAEEAKQPEK 348
Cdd:COG0536 318 ELLYALAELLEELRAEEAEEEEEVEE 343
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
3-332 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: 560.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316     3 FVDEASILVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTGKR 82
Cdd:TIGR02729   1 FVDEAKIFVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGSVILEADENLNTLLDFRYQRHFKAENGENGMGKNRTGKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316    83 GKDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKRELLLELMLLADV 162
Cdd:TIGR02729  81 GEDLVIKVPVGTVVYDADTGELLADLTEPGQRFLVAKGGRGGLGNAHFKSSTNRAPRFATPGEPGEERWLRLELKLLADV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   163 GMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRVLL 242
Cdd:TIGR02729 161 GLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   243 HLIDIDPIDGTDPVENARIIISELEKYSQDLAAKPRWLVFNKIDLLDKVEAEEKAKAIAEALGWedKYYLISAASGLGVK 322
Cdd:TIGR02729 241 HLIDISPEDGSDPVEDYEIIRNELKKYSPELAEKPRIVVLNKIDLLDEEELEELLKELKKELGK--PVFPISALTGEGLD 318
                         330
                  ....*....|
gi 15833316   323 DLCWDVMTFI 332
Cdd:TIGR02729 319 ELLDALAELL 328
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
160-332 2.91e-102

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: 299.72  E-value: 2.91e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 160 ADVGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCR 239
Cdd:cd01898   1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 240 VLLHLIDIDPIDgtDPVENARIIISELEKYSQDLAAKPRWLVFNKIDLLDKVEAEEKAKAIAEALgWEDKYYLISAASGL 319
Cdd:cd01898  81 VLLHVIDLSGED--DPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELLKEL-KGKKVFPISALTGE 157
                       170
                ....*....|...
gi 15833316 320 GVKDLCWDVMTFI 332
Cdd:cd01898 158 GLDELLKKLAKLL 170
GTP1_OBG pfam01018
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ...
4-150 2.51e-69

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: 215.29  E-value: 2.51e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316     4 VDEASILVVAGDGGNGCVSFRREKYIPKggpdggdggdggdVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTGKRG 83
Cdd:pfam01018   1 VDRAKIKVKAGDGGNGCVSFRREKYVPKggpdggdggrggdVILVADENLNTLLDFRYKRHFKAENGENGGGKNCHGKNG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15833316    84 KDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKR 150
Cdd:pfam01018  81 EDLIIKVPVGTVVKDAETGEVLADLTEPGQRVLVAKGGRGGRGNAHFKTSTNQAPRFAEPGEPGEER 147
 
Name Accession Description Interval E-value
obgE PRK12298
GTPase CgtA; Reviewed
1-390 0e+00

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 684.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316    1 MKFVDEASILVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTG 80
Cdd:PRK12298   1 MKFVDEAKIRVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVYLEADENLNTLIDYRFERHFRAERGQNGQGRDCTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   81 KRGKDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKRELLLELMLLA 160
Cdd:PRK12298  81 KRGKDITIKVPVGTRVIDADTGEVIGDLTEHGQRLLVAKGGWHGLGNTRFKSSVNRAPRQKTPGTPGEERELKLELKLLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  161 DVGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRV 240
Cdd:PRK12298 161 DVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDERSFVVADIPGLIEGASEGAGLGIRFLKHLERCRV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  241 LLHLIDIDPIDGTDPVENARIIISELEKYSQDLAAKPRWLVFNKIDLLDKVEAEEKAKAIAEALGWEDKYYLISAASGLG 320
Cdd:PRK12298 241 LLHLIDIAPIDGSDPVENARIIINELEKYSPKLAEKPRWLVFNKIDLLDEEEAEERAKAIVEALGWEGPVYLISAASGLG 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  321 VKDLCWDVMTFIIENPVVQAEEAKQPEKVEFMWDDYHRQQLEEIAEEDDEDWDDDWDEDDEEGVEFIYKR 390
Cdd:PRK12298 321 VKELCWDLMTFIEENPREEAEEAEAPEKVEFMWDDYHREQLEEVEEEDDDDWDDDWDEDDDEGVEVIYKR 390
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
3-348 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: 563.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   3 FVDEASILVVAGDGGNGCVSFRREKYIPKggpdggdggdggdVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTGKR 82
Cdd:COG0536   1 FVDEAKIYVKAGDGGNGCVSFRREKYVPKggpdggdggrggdVILVADENLNTLLDFRYKRHFKAENGENGMGKNRTGKN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  83 GKDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKRELLLELMLLADV 162
Cdd:COG0536  81 GEDLVIKVPVGTVVKDAETGEVLADLTEDGQRVVVAKGGRGGLGNAHFKSSTNRAPRFAEPGEPGEERWLRLELKLLADV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 163 GMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRVLL 242
Cdd:COG0536 161 GLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRSFVIADIPGLIEGASEGAGLGHRFLRHIERTRVLL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 243 HLIDIDPIDGTDPVENARIIISELEKYSQDLAAKPRWLVFNKIDLLDKVEAEEKAKAIaEALGWEdkYYLISAASGLGVK 322
Cdd:COG0536 241 HVVDAAPLDGRDPVEDYEIIRNELEAYSPELAEKPRIVVLNKIDLLDAEELEELKAEL-EKLGGP--VFPISAVTGEGLD 317
                       330       340
                ....*....|....*....|....*.
gi 15833316 323 DLCWDVMTFIIENPVVQAEEAKQPEK 348
Cdd:COG0536 318 ELLYALAELLEELRAEEAEEEEEVEE 343
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
3-332 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: 560.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316     3 FVDEASILVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTGKR 82
Cdd:TIGR02729   1 FVDEAKIFVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGSVILEADENLNTLLDFRYQRHFKAENGENGMGKNRTGKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316    83 GKDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKRELLLELMLLADV 162
Cdd:TIGR02729  81 GEDLVIKVPVGTVVYDADTGELLADLTEPGQRFLVAKGGRGGLGNAHFKSSTNRAPRFATPGEPGEERWLRLELKLLADV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   163 GMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRVLL 242
Cdd:TIGR02729 161 GLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   243 HLIDIDPIDGTDPVENARIIISELEKYSQDLAAKPRWLVFNKIDLLDKVEAEEKAKAIAEALGWedKYYLISAASGLGVK 322
Cdd:TIGR02729 241 HLIDISPEDGSDPVEDYEIIRNELKKYSPELAEKPRIVVLNKIDLLDEEELEELLKELKKELGK--PVFPISALTGEGLD 318
                         330
                  ....*....|
gi 15833316   323 DLCWDVMTFI 332
Cdd:TIGR02729 319 ELLDALAELL 328
obgE PRK12299
GTPase CgtA; Reviewed
2-336 0e+00

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 528.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316    2 KFVDEASILVVAGDGGNGCVSFRREKYIPKggpdggdggdggdVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTGK 81
Cdd:PRK12299   1 KFIDEAKIYVKAGDGGNGCVSFRREKFIPFggpdggdggrggsVILEADENLNTLIDFRYKRHFKAENGENGMGRNRTGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   82 RGKDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKRELLLELMLLAD 161
Cdd:PRK12299  81 SGKDLVLKVPVGTQIYDADTGELIADLTEHGQRFLVAKGGKGGLGNAHFKSSTNRAPRYATPGEPGEERWLRLELKLLAD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  162 VGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRVL 241
Cdd:PRK12299 161 VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKSFVIADIPGLIEGASEGAGLGHRFLKHIERTRLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  242 LHLIDidpIDGTDPVENARIIISELEKYSQDLAAKPRWLVFNKIDLLDKvEAEEKAKAIAEALGWEDKYYLISAASGLGV 321
Cdd:PRK12299 241 LHLVD---IEAVDPVEDYKTIRNELEKYSPELADKPRILVLNKIDLLDE-EEEREKRAALELAALGGPVFLISAVTGEGL 316
                        330
                 ....*....|....*
gi 15833316  322 KDLCWDVMTFIIENP 336
Cdd:PRK12299 317 DELLRALWELLEEAR 331
obgE PRK12297
GTPase CgtA; Reviewed
2-351 8.72e-154

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 440.31  E-value: 8.72e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316    2 KFVDEASILVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTGK 81
Cdd:PRK12297   1 MFIDQAKIYVKAGDGGDGMVSFRREKYVPKGGPDGGDGGKGGSVIFVADEGLRTLLDFRYKRHFKAENGENGMGKNMHGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   82 RGKDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKRELLLELMLLAD 161
Cdd:PRK12297  81 NGEDLIIKVPVGTVVKDAETGEVIADLVEPGQEVVVAKGGRGGRGNAHFATSTNQAPRIAENGEPGEERELRLELKLLAD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  162 VGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRVL 241
Cdd:PRK12297 161 VGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRSFVMADIPGLIEGASEGVGLGHQFLRHIERTRVI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  242 LHLIDIDPIDGTDPVENARIIISELEKYSQDLAAKPRWLVFNKIDLLdkvEAEEKAKAIAEALGweDKYYLISAASGLGV 321
Cdd:PRK12297 241 VHVIDMSGSEGRDPIEDYEKINKELKLYNPRLLERPQIVVANKMDLP---EAEENLEEFKEKLG--PKVFPISALTGQGL 315
                        330       340       350
                 ....*....|....*....|....*....|
gi 15833316  322 KDLCWDVMTFIIENPVVQAEEAKQPEKVEF 351
Cdd:PRK12297 316 DELLYAVAELLEETPEFPLEEEEVEEEVYY 345
obgE PRK12296
GTPase CgtA; Reviewed
1-347 7.95e-105

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 317.97  E-value: 7.95e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316    1 MKFVDEASILVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTG 80
Cdd:PRK12296   2 PRFVDRVVLHVKAGDGGNGCASVHREKFKPLGGPDGGNGGRGGSVVLVVDPQVTTLLDFHFRPHRKATNGKPGMGDNRDG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   81 KRGKDVTIKVPVGTrVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKRELLLELMLLA 160
Cdd:PRK12296  82 AAGEDLVLPVPDGT-VVLDEDGEVLADLVGAGTRFVAAAGGRGGLGNAALASKARKAPGFALLGEPGEERDLVLELKSVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  161 DVGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEkSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRV 240
Cdd:PRK12296 161 DVGLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQAGDT-RFTVADVPGLIPGASEGKGLGLDFLRHIERCAV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  241 LLHLID---IDPidGTDPVENARIIISELEKYSQ---------DLAAKPRWLVFNKIDLLDKVEAEEKAKAIAEALGWed 308
Cdd:PRK12296 240 LVHVVDcatLEP--GRDPLSDIDALEAELAAYAPaldgdlglgDLAERPRLVVLNKIDVPDARELAEFVRPELEARGW-- 315
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 15833316  309 KYYLISAASGLGVKDLCWDVMTfiienpVVQAEEAKQPE 347
Cdd:PRK12296 316 PVFEVSAASREGLRELSFALAE------LVEEARAAEPE 348
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
160-332 2.91e-102

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: 299.72  E-value: 2.91e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 160 ADVGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCR 239
Cdd:cd01898   1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 240 VLLHLIDIDPIDgtDPVENARIIISELEKYSQDLAAKPRWLVFNKIDLLDKVEAEEKAKAIAEALgWEDKYYLISAASGL 319
Cdd:cd01898  81 VLLHVIDLSGED--DPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELLKEL-KGKKVFPISALTGE 157
                       170
                ....*....|...
gi 15833316 320 GVKDLCWDVMTFI 332
Cdd:cd01898 158 GLDELLKKLAKLL 170
GTP1_OBG pfam01018
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ...
4-150 2.51e-69

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: 215.29  E-value: 2.51e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316     4 VDEASILVVAGDGGNGCVSFRREKYIPKggpdggdggdggdVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTGKRG 83
Cdd:pfam01018   1 VDRAKIKVKAGDGGNGCVSFRREKYVPKggpdggdggrggdVILVADENLNTLLDFRYKRHFKAENGENGGGKNCHGKNG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15833316    84 KDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKR 150
Cdd:pfam01018  81 EDLIIKVPVGTVVKDAETGEVLADLTEPGQRVLVAKGGRGGRGNAHFKTSTNQAPRFAEPGEPGEER 147
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
163-327 1.59e-38

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: 135.98  E-value: 1.59e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 163 GMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRVLL 242
Cdd:cd01881   1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 243 HLIDIDPIDGTDPVENARIIISELEKYSQDLAAKPRWLVFNKIdllDKVEAEEKAKAIAEALGWEDKYYLISAASGLG-- 320
Cdd:cd01881  81 HVIDASEDCVGDPLEDQKTLNEEVSGSFLFLKNKPEMIVANKI---DMASENNLKRLKLDKLKRGIPVVPTSALTRLGld 157

                ....*...
gi 15833316 321 -VKDLCWD 327
Cdd:cd01881 158 rVIRTIRK 165
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
161-284 9.96e-31

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: 113.48  E-value: 9.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   161 DVGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNeKSFVVADIPGLIEGAAEGAGLGIRFLKHlERCRV 240
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKG-KQIILVDTPGLIEGASEGEGLGRAFLAI-IEADL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15833316   241 LLHLIDIDpidgtdpvENARIIISELEKYSQDlAAKPRWLVFNK 284
Cdd:pfam01926  79 ILFVVDSE--------EGITPLDEELLELLRE-NKKPIILVLNK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
163-324 3.09e-21

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: 89.23  E-value: 3.09e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 163 GMLGMPNAGKSTFIRAVSAAKP-KVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRVL 241
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNVgIVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 242 LHLIDIDpIDGTDPVENariiISELEKYSqdlaaKPRWLVFNKIDLLDKVEAEEKAKAIAEALGWEDKYYLISAASGLGV 321
Cdd:cd00880  81 LLVVDSD-LTPVEEEAK----LGLLRERG-----KPVLLVLNKIDLVPESEEEELLRERKLELLPDLPVIAVSALPGEGI 150

                ...
gi 15833316 322 KDL 324
Cdd:cd00880 151 DEL 153
PRK09602 PRK09602
translation-associated GTPase; Reviewed
162-361 1.57e-19

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 89.48  E-value: 1.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  162 VGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGV--VRMD------------------NEKSFV---VADIPGLI 218
Cdd:PRK09602   4 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayVRVEcpckelgvkcnprngkciDGTRFIpveLIDVAGLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  219 EGAAEGAGLGIRFLKHLERCRVLLHLID----------IDPIDGTDPVENARIIISELEKysqdlaakprWLvFNKID-- 286
Cdd:PRK09602  84 PGAHEGRGLGNQFLDDLRQADALIHVVDasgstdeegnPVEPGSHDPVEDIKFLEEELDM----------WI-YGILEkn 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  287 ---LLDKVEAEEK--AKAIAEALgwedkyylisaaSGLGVKDlcWDVMTFIIEnpvvqAEEAKQPEKvefmWDDYHRQQL 361
Cdd:PRK09602 153 wekFSRKAQAEKFdiEEALAEQL------------SGLGINE--EHVKEALRE-----LGLPEDPSK----WTDEDLLEL 209
PTZ00258 PTZ00258
GTP-binding protein; Provisional
162-266 3.39e-19

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 88.08  E-value: 3.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  162 VGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVV-----RMD------NEKSFV-----VADIPGLIEGAAEGA 225
Cdd:PTZ00258  24 MGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVnvpdeRFDwlckhfKPKSIVpaqldITDIAGLVKGASEGE 103
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15833316  226 GLGIRFLKHLERCRVLLHLI------DIDPIDGT-DPVENARIIISEL 266
Cdd:PTZ00258 104 GLGNAFLSHIRAVDGIYHVVrafedeDITHVEGEiDPVRDLEIISSEL 151
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
166-334 5.53e-19

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 86.81  E-value: 5.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 166 GMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKsFVVADIPGL----------IEGAAEGAglgirfLKHL 235
Cdd:COG1084 167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGR-YQVIDTPGLldrplserneIERQAILA------LKHL 239
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 236 ErcRVLLHLIDIDPIDGTDPVENARI---IISELEkysqdlaaKPRWLVFNKIDLLDKVEAEEKAkaiaealgwEDKYYL 312
Cdd:COG1084 240 A--DVILFLFDPSETCGYSLEEQLNLleeIRSLFD--------VPVIVVINKIDLSDEEELKEAE---------EEADIK 300
                       170       180
                ....*....|....*....|..
gi 15833316 313 ISAASGLGVKDLcwdvMTFIIE 334
Cdd:COG1084 301 ISALTGEGVDEL----LDELIE 318
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
160-332 1.54e-18

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 86.01  E-value: 1.54e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 160 ADVGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKsFVVADIPGLIEGAAEGAGLGIRFL------- 232
Cdd:COG1163  64 ATVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLEYKGAK-IQILDVPGLIEGAASGKGRGKEVLsvvrnad 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 233 -----------KHLERCRVLLH----LIDIDP--------------IDGTDPVE----------------NARIIISE-- 265
Cdd:COG1163 143 lilivldvfelEQYDVLKEELYdagiRLNKPPpdvtiekkgkggirVNSTGKLDldeedikkilreygivNADVLIREdv 222
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833316 266 ----LEKY-SQDLAAKPRWLVFNKIDLLDkveaEEKAKAIAEALGWEDKYYLISAASGLG---VKDLCWDVMTFI 332
Cdd:COG1163 223 tlddLIDAlMGNRVYKPAIVVVNKIDLAD----EEYVEELKSKLPDGVPVIFISAEKGIGleeLKEEIFEELGLI 293
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
162-268 2.61e-18

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: 84.59  E-value: 2.61e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 162 VGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGV--VRMD------------------NEKSFV---VADIPGLI 218
Cdd:cd01899   1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVgyVRVEcpckelgvscnprygkciDGKRYVpveLIDVAGLV 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 219 EGAAEGAGLGIRFLKHLERCRVLLHLIDI----------DPIDGTDPVENARIIISELEK 268
Cdd:cd01899  81 PGAHEGKGLGNQFLDDLRDADVLIHVVDAsggtdaegngVETGGYDPLEDIEFLENEIDM 140
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
165-324 3.65e-17

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: 78.27  E-value: 3.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 165 LGMPNAGKSTFIRAVSAAK-PKVADYPFTTLVPSLGVVRMDNEK-SFVVADIPGLIEGaaEGAGLGIRFLKHLERCRVLL 242
Cdd:cd00882   3 VGRGGVGKSSLLNALLGGEvGEVSDVPGTTRDPDVYVKELDKGKvKLVLVDTPGLDEF--GGLGREELARLLLRGADLIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 243 HLIDIDpiDGTDPVENARIIISELEKYSqdlaaKPRWLVFNKIDLLDKVEAEEKAKAIAEALGWEDKYYLISAASGLGVK 322
Cdd:cd00882  81 LVVDST--DRESEEDAKLLILRRLRKEG-----IPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFEVSAKTGEGVD 153

                ..
gi 15833316 323 DL 324
Cdd:cd00882 154 EL 155
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
160-284 3.72e-17

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: 79.90  E-value: 3.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 160 ADVGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVaDIPGLIEGAAEGAGLGIRFLKHLERCR 239
Cdd:cd01896   1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLL-DLPGIIEGASDGKGRGRQVIAVARTAD 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15833316 240 VLLHLIDIdpidgTDPVENARIIISELEKYSQDLAAKPRWLVFNK 284
Cdd:cd01896  80 LILIVLDA-----TKPEGQREILERELEGVGIRLNKKPPNVTIKK 119
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
162-315 3.48e-16

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: 77.88  E-value: 3.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 162 VGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVV-----RMDN-------EK------SFVvaDIPGLIEGAAE 223
Cdd:cd01900   1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVpvpdeRLDKlaeivkpKKivpatiEFV--DIAGLVKGASK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 224 GAGLGIRFLKHLERCRVLLHLI------DIDPIDGT-DPVENARIIISEL--------EKY---------SQDLAAKPrw 279
Cdd:cd01900  79 GEGLGNKFLSHIREVDAIAHVVrcfeddDITHVEGSvDPVRDIEIINTELiladletiEKRlerlekkakSGDKEAKE-- 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15833316 280 lvfnKIDLLDKVEA--EEKAKAIAEALGWEDK-----YYLISA 315
Cdd:cd01900 157 ----ELELLEKIKEhlEEGKPARTLELTDEEIkilksLQLLTA 195
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
166-324 4.15e-16

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: 75.29  E-value: 4.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 166 GMPNAGKSTFIRAVSAAKPKVADYPFTTlvPSLGVVRMD-NEKSFVVADIPGL----------IEGAAegaglgIRFLKH 234
Cdd:cd01897   7 GYPNVGKSSLVNKLTRAKPEVAPYPFTT--KSLFVGHFDyKYLRWQVIDTPGIldrpleerntIEMQA------ITALAH 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 235 LERCrvLLHLIDIDPIDGTdPVENARIIISELEKysqdLAAKPRWLVFNKIDLLDkveaEEKAKAIAEALGWE-DKYYLI 313
Cdd:cd01897  79 LRAA--VLFFIDPSETCGY-SIEEQLSLFKEIKP----LFNKPVIVVLNKIDLLT----EEDLSEIEKELEKEgEEVIKI 147
                       170
                ....*....|.
gi 15833316 314 SAASGLGVKDL 324
Cdd:cd01897 148 STLTEEGVDEL 158
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
162-266 1.11e-15

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 77.75  E-value: 1.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 162 VGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVV-----RMDN-------EK------SFVvaDIPGLIEGAAE 223
Cdd:COG0012   3 CGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVpvpdeRLDKlaeivkpKKivpatiEFV--DIAGLVKGASK 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15833316 224 GAGLGIRFLKHLERCRVLLHLI------DIDPIDGT-DPVENARIIISEL 266
Cdd:COG0012  81 GEGLGNQFLANIREVDAIVHVVrcfeddNVTHVEGSvDPLRDIETINTEL 130
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
162-324 6.37e-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: 67.10  E-value: 6.37e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 162 VGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIegaaegaglgiRFLKH------- 234
Cdd:cd01878  44 VALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTTRRIKLPGGREVLLTDTVGFI-----------RDLPHqlveafr 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 235 --LERCR---VLLHLIDIdpidgTDPVENARI-----IISELekysqDLAAKPRWLVFNKIDLLDKVEAEEKAKAIaeal 304
Cdd:cd01878 113 stLEEVAeadLLLHVVDA-----SDPDREEQIetveeVLKEL-----GADDIPIILVLNKIDLLDDEELEERLRAG---- 178
                       170       180
                ....*....|....*....|
gi 15833316 305 gwEDKYYLISAASGLGVKDL 324
Cdd:cd01878 179 --RPDAVFISAKTGEGLDLL 196
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
162-324 3.03e-12

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: 64.40  E-value: 3.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 162 VGMLGMPNAGKSTFIRA-----VSAAKPKvadyPFTTLVPSLGVVrMDNEKSFVVADIPGLIEgaaEGAGLGIRFLKH-- 234
Cdd:cd04163   6 VAIIGRPNVGKSTLLNAlvgqkISIVSPK----PQTTRNRIRGIY-TDDDAQIIFVDTPGIHK---PKKKLGERMVKAaw 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 235 --LERCRVLLHLIDIDpidgTDPVENARIIISELEKYSqdlaaKPRWLVFNKIDLLDKVEAEEKAKAIAEALGWEDKYYL 312
Cdd:cd04163  78 saLKDVDLVLFVVDAS----EWIGEGDEFILELLKKSK-----TPVILVLNKIDLVKDKEDLLPLLEKLKELHPFAEIFP 148
                       170
                ....*....|..
gi 15833316 313 ISAASGLGVKDL 324
Cdd:cd04163 149 ISALKGENVDEL 160
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
169-324 3.22e-12

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 67.42  E-value: 3.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 169 NAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIegaaegaglgiRFLKH---------LERCR 239
Cdd:COG2262 209 NAGKSTLFNRLTGADVLAEDKLFATLDPTTRRLELPDGRPVLLTDTVGFI-----------RKLPHqlveafrstLEEVR 277
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 240 ---VLLHLIDI-DPidgtDPVENARI---IISELekysqDLAAKPRWLVFNKIDLLDKVEAEEKAKAIAEALgwedkyyL 312
Cdd:COG2262 278 eadLLLHVVDAsDP----DFEEQIETvneVLEEL-----GADDKPIILVFNKIDLLDDEELERLRAGYPDAV-------F 341
                       170
                ....*....|..
gi 15833316 313 ISAASGLGVKDL 324
Cdd:COG2262 342 ISAKTGEGIDEL 353
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
162-324 2.40e-11

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 63.85  E-value: 2.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 162 VGMLGMPNAGKSTFIRA-----VSAAKPKvadyPFTTLVPSLGVVrMDNEKSFVVADIPGLIEG----------AAEGAg 226
Cdd:COG1159   6 VAIVGRPNVGKSTLLNAlvgqkVSIVSPK----PQTTRHRIRGIV-TREDAQIVFVDTPGIHKPkrklgrrmnkAAWSA- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 227 lgirflkhLERCRVLLHLIDID-PIDGTDpvenaRIIISELEKYSqdlaaKPRWLVFNKIDLLDKVEAEEKAKAIAEALG 305
Cdd:COG1159  80 --------LEDVDVILFVVDATeKIGEGD-----EFILELLKKLK-----TPVILVINKIDLVKKEELLPLLAEYSELLD 141
                       170
                ....*....|....*....
gi 15833316 306 WEDkYYLISAASGLGVKDL 324
Cdd:COG1159 142 FAE-IVPISALKGDNVDEL 159
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
162-324 3.00e-11

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: 64.03  E-value: 3.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   162 VGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLiegaaegaglgIRFLKH------- 234
Cdd:TIGR03156 192 VALVGYTNAGKSTLFNALTGADVYAADQLFATLDPTTRRLDLPDGGEVLLTDTVGF-----------IRDLPHelvaafr 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   235 --LERCR---VLLHLIDIdpidgTDPVENARI-----IISELekysqDLAAKPRWLVFNKIDLLDKVEAEEKAKAIAEAL 304
Cdd:TIGR03156 261 atLEEVReadLLLHVVDA-----SDPDREEQIeavekVLEEL-----GAEDIPQLLVYNKIDLLDEPRIERLEEGYPEAV 330
                         170       180
                  ....*....|....*....|
gi 15833316   305 gwedkyyLISAASGLGVKDL 324
Cdd:TIGR03156 331 -------FVSAKTGEGLDLL 343
era PRK00089
GTPase Era; Reviewed
162-324 5.80e-10

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 59.68  E-value: 5.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  162 VGMLGMPNAGKSTFIRA-----VSAAKPKvadyPFTTLVPSLGVVrMDNEKSFVVADIPGLIEgaAEGAgLGIRFLKH-- 234
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNAlvgqkISIVSPK----PQTTRHRIRGIV-TEDDAQIIFVDTPGIHK--PKRA-LNRAMNKAaw 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  235 --LERCRVLLHLIDID-PIDGTDpvenaRIIISELEKysqdlAAKPRWLVFNKIDLL-DKVEAEEKAKAIAEALGWEDkY 310
Cdd:PRK00089  80 ssLKDVDLVLFVVDADeKIGPGD-----EFILEKLKK-----VKTPVILVLNKIDLVkDKEELLPLLEELSELMDFAE-I 148
                        170
                 ....*....|....
gi 15833316  311 YLISAASGLGVKDL 324
Cdd:PRK00089 149 VPISALKGDNVDEL 162
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
162-324 1.29e-09

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 56.91  E-value: 1.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 162 VGMLGMPNAGKSTFIRAVSAAKPKVADYpfttlVPSLGV------VRMDNEK-SFVVADIPGLIEGAAEGAglgiRFLKH 234
Cdd:COG1100   6 IVVVGTGGVGKTSLVNRLVGDIFSLEKY-----LSTNGVtidkkeLKLDGLDvDLVIWDTPGQDEFRETRQ----FYARQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 235 LERCRVLLHLIDIDPIDGTDPVENARIIISELEKYSqdlaakPRWLVFNKIDLLDK---VEAEEKAKAIAEALGWEdkYY 311
Cdd:COG1100  77 LTGASLYLFVVDGTREETLQSLYELLESLRRLGKKS------PIILVLNKIDLYDEeeiEDEERLKEALSEDNIVE--VV 148
                       170
                ....*....|...
gi 15833316 312 LISAASGLGVKDL 324
Cdd:COG1100 149 ATSAKTGEGVEEL 161
PRK11058 PRK11058
GTPase HflX; Provisional
162-330 1.24e-07

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 53.18  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  162 VGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEG------AAEGAGlgirfLKHL 235
Cdd:PRK11058 200 VSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIRHlphdlvAAFKAT-----LQET 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  236 ERCRVLLHLIDIDPIDGTDPVENARIIISELEkySQDLaakPRWLVFNKIDLLD----KVEAEEKAKAIAEalgWedkyy 311
Cdd:PRK11058 275 RQATLLLHVVDAADVRVQENIEAVNTVLEEID--AHEI---PTLLVMNKIDMLDdfepRIDRDEENKPIRV---W----- 341
                        170
                 ....*....|....*....
gi 15833316  312 lISAASGLGVkDLCWDVMT 330
Cdd:PRK11058 342 -LSAQTGAGI-PLLFQALT 358
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
162-298 6.53e-07

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: 48.91  E-value: 6.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   162 VGMLGMPNAGKSTFIRAVSAAKP-KVADYPFTTLVPSLGVVRMDNEK-SFVVADIPGLIEGAAEGAGLGIRFLKHLERCR 239
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGsITEYYPGTTRNYVTTVIEEDGKTyKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFD 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833316   240 VLLHLIDIDPIdgtdPVENARIIISELEKysqdlaAKPRWLVFNKIDL----LDKVEAEEKAK 298
Cdd:TIGR00231  84 IVILVLDVEEI----LEKQTKEIIHHADS------GVPIILVGNKIDLkdadLKTHVASEFAK 136
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
165-324 2.63e-06

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: 47.10  E-value: 2.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 165 LGMPNAGKSTFIRAVsAAKPK--VADYPFTT--LVpslgvvrmdnEKSFVVADIP-------GL------IEGaaegagL 227
Cdd:cd04164   9 AGKPNVGKSSLLNAL-AGRDRaiVSDIAGTTrdVI----------EEEIDLGGIPvrlidtaGLretedeIEK------I 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 228 GI-RFLKHLERCRVLLHLIDIDpidGTDPVENARIIIselekysqDLAAKPRWLVFNKIDLLDKVEAEEKAKaiaealgw 306
Cdd:cd04164  72 GIeRAREAIEEADLVLLVVDAS---EGLDEEDLEILE--------LPAKKPVIVVLNKSDLLSDAEGISELN-------- 132
                       170
                ....*....|....*...
gi 15833316 307 EDKYYLISAASGLGVKDL 324
Cdd:cd04164 133 GKPIIAISAKTGEGIDEL 150
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
166-324 4.95e-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: 48.13  E-value: 4.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 166 GMPNAGKSTFIRAVSaakpkvadypfttlvpslgvvrmdNEKSFVVADIPG----LIEGAA--EG--------AGL---- 227
Cdd:COG0486 220 GRPNVGKSSLLNALL------------------------GEERAIVTDIAGttrdVIEERIniGGipvrlidtAGLrete 275
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 228 ------GIRF-LKHLERCRVLLHLIDidpiDGTDPVENARIIISELEKysqdlaaKPRWLVFNKIDLLDKVEAEEKAKAI 300
Cdd:COG0486 276 devekiGIERaREAIEEADLVLLLLD----ASEPLTEEDEEILEKLKD-------KPVIVVLNKIDLPSEADGELKSLPG 344
                       170       180
                ....*....|....*....|....
gi 15833316 301 AEALGwedkyylISAASGLGVKDL 324
Cdd:COG0486 345 EPVIA-------ISAKTGEGIDEL 361
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
165-324 5.28e-06

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: 46.35  E-value: 5.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 165 LGMPNAGKSTFIRAVSAAK--PKVADYPFTTLvpSLGVVRMDNEKSFVvaDIPGLI------EGAAEGAGLGIRFLKHLE 236
Cdd:cd01876   5 AGRSNVGKSSLINALTNRKklARTSKTPGRTQ--LINFFNVGDKFRLV--DLPGYGyakvskEVREKWGKLIEEYLENRE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 237 RCRVLLHLIDID----PIDgtdpvenaRIIISELEKYSQDLAakprwLVFNKIDLLDKVEAEEKAKAIAEALG---WEDK 309
Cdd:cd01876  81 NLKGVVLLIDARhgptPID--------LEMLEFLEELGIPFL-----IVLTKADKLKKSELAKVLKKIKEELNlfnILPP 147
                       170
                ....*....|....*
gi 15833316 310 YYLISAASGLGVKDL 324
Cdd:cd01876 148 VILFSSKKGTGIDEL 162
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
166-324 3.93e-05

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 45.49  E-value: 3.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  166 GMPNAGKSTFI-------RAVsaakpkVADYPFTT--LVpslgvvrmdnEKSFVVADIP-------GLIEGAAEGAGLGI 229
Cdd:PRK05291 222 GRPNVGKSSLLnallgeeRAI------VTDIAGTTrdVI----------EEHINLDGIPlrlidtaGIRETDDEVEKIGI 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  230 -RFLKHLERCRVLLHLIDIDPIDGTDPVEnariIISELEKysqdlaaKPRWLVFNKIDLLDKVEAEEKAKaiaealgweD 308
Cdd:PRK05291 286 eRSREAIEEADLVLLVLDASEPLTEEDDE----ILEELKD-------KPVIVVLNKADLTGEIDLEEENG---------K 345
                        170
                 ....*....|....*.
gi 15833316  309 KYYLISAASGLGVKDL 324
Cdd:PRK05291 346 PVIRISAKTGEGIDEL 361
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
162-324 4.53e-05

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


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 43.58  E-value: 4.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 162 VGMLGMPNAGKSTFI-------RAVsaakpkVADYPFTTLvPSLGVVRMDNEKSFVVADIPGL-----IEGAAEGAGLgI 229
Cdd:cd01895   5 IAIIGRPNVGKSSLLnallgeeRVI------VSDIAGTTR-DSIDVPFEYDGQKYTLIDTAGIrkkgkVTEGIEKYSV-L 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 230 RFLKHLERCRVLLHLIDidpidgtdpvenARIIISElekysQDL--------AAKPRWLVFNKIDLLDKVEAEEKA--KA 299
Cdd:cd01895  77 RTLKAIERADVVLLVLD------------ASEGITE-----QDLriaglileEGKALIIVVNKWDLVEKDEKTMKEfeKE 139
                       170       180
                ....*....|....*....|....*..
gi 15833316 300 IAEALGWED--KYYLISAASGLGVKDL 324
Cdd:cd01895 140 LRRKLPFLDyaPIVFISALTGQGVDKL 166
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
166-342 4.59e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 45.04  E-value: 4.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  166 GMPNAGKST-FIRAVSAAKPKVADYPfttlvpslGVVRmD--------NEKSFVVADIPGlIEGAAEGAGLGIR--FLKH 234
Cdd:PRK00093   8 GRPNVGKSTlFNRLTGKRDAIVADTP--------GVTR-DriygeaewLGREFILIDTGG-IEPDDDGFEKQIReqAELA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  235 LERCRVLLHLID----IDPIDgtdpvenaRIIISELEKYSqdlaaKPRWLVFNKIDlldkveAEEKAKAIAE--ALGWED 308
Cdd:PRK00093  78 IEEADVILFVVDgragLTPAD--------EEIAKILRKSN-----KPVILVVNKVD------GPDEEADAYEfySLGLGE 138
                        170       180       190
                 ....*....|....*....|....*....|....
gi 15833316  309 kYYLISAASGLGVKDLCWDVMTFIIENPVVQAEE 342
Cdd:PRK00093 139 -PYPISAEHGRGIGDLLDAILEELPEEEEEDEED 171
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
162-324 1.79e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 43.50  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  162 VGMLGMPNAGKSTFI-------RAVsaakpkVADYPFTTL----VPslgVVRmdNEKSFVVADIPGL-----IEGAAEGA 225
Cdd:PRK00093 176 IAIIGRPNVGKSSLInallgeeRVI------VSDIAGTTRdsidTP---FER--DGQKYTLIDTAGIrrkgkVTEGVEKY 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316  226 GLgIRFLKHLERCRVLLHLIDidpidgtdpvenARIIISElekysQDL--------AAKPRWLVFNKIDLLDKVEAEEKA 297
Cdd:PRK00093 245 SV-IRTLKAIERADVVLLVID------------ATEGITE-----QDLriaglaleAGRALVIVVNKWDLVDEKTMEEFK 306
                        170       180       190
                 ....*....|....*....|....*....|....
gi 15833316  298 KAIAEALgwedkYYL-------ISAASGLGVKDL 324
Cdd:PRK00093 307 KELRRRL-----PFLdyapivfISALTGQGVDKL 335
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
164-216 3.31e-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: 3.31e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15833316 164 MLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRmDNEKSFVVADIPG 216
Cdd:cd01879   2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFK-LGGKEIEIVDLPG 53
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
232-335 4.91e-04

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


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 40.71  E-value: 4.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 232 LKHLERCRVL-LHLIDIDPIDGTdpvenariIISELEKYsqdLAAKPRWLVFNKIDLL--DKVEAEEKA---KAIAEALG 305
Cdd:cd01855  27 LSTLLNDNALvVHVVDIFDFPGS--------LIPGLAEL---IGAKPVILVGNKIDLLpkDVKPNRLKQwvkKRLKIGGL 95
                        90       100       110
                ....*....|....*....|....*....|
gi 15833316 306 WEDKYYLISAASGLGVKDLcwdvMTFIIEN 335
Cdd:cd01855  96 KIKDVILVSAKKGWGVEEL----IEEIKKL 121
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
259-324 1.07e-03

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 40.48  E-value: 1.07e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15833316 259 ARIIIS----ELEKYSQDlaaKPRWLVFNKIDLLDKVEAEEkakaiaealgWEDKY-------YLISAASGLGVKDL 324
Cdd:COG1161  33 ARIPLSsrnpMLDELVGN---KPRLLVLNKADLADPSVTKQ----------WLKYFekqgvdaLAISAKKGKGIKEL 96
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
280-324 2.13e-03

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: 38.68  E-value: 2.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15833316   280 LVFNKIDLLDKVEAEEKAKAIAEALGWEdkYYLISAASGLGVKDL 324
Cdd:pfam03193  58 IVLNKIDLLDEEEELEELLKIYRAIGYP--VLFVSAKTGEGIEAL 100
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
166-324 2.34e-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: 38.19  E-value: 2.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 166 GMPNAGKST-FIR------AVsaakpkVADYPfttlvpslGVVRmD--------NEKSFVVADIPGlIEGAAEGaglgir 230
Cdd:cd01894   4 GRPNVGKSTlFNRltgrrdAI------VSDTP--------GVTR-DrkygeaewGGREFILIDTGG-IEPDDEG------ 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 231 FLKH--------LERCRVLLHLID----IDPIDgtdpvenaRIIISELEKYsqdlaAKPRWLVFNKIDLLDKVEaeekak 298
Cdd:cd01894  62 ISKEireqaeiaIEEADVILFVVDgregLTPAD--------EEIAKYLRKS-----KKPVILVVNKIDNIKEEE------ 122
                       170       180
                ....*....|....*....|....*...
gi 15833316 299 AIAE--ALGWEDkYYLISAASGLGVKDL 324
Cdd:cd01894 123 EAAEfySLGFGE-PIPISAEHGRGIGDL 149
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
280-324 2.43e-03

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: 38.92  E-value: 2.43e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 15833316 280 LVFNKIDLLDKVEAEEKAKAIaEALGwedkY--YLISAASGLGVKDL 324
Cdd:cd01854  38 IVLNKADLVDDEELEELLEIY-EKLG----YpvLAVSAKTGEGLDEL 79
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
165-324 3.14e-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: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   165 LGMPNAGKSTFIRAVSaakpkvadypfttlvpslgvvrmdNEKSFVVADIPG----LIEGAA--EG--------AGL--- 227
Cdd:pfam12631 100 VGKPNVGKSSLLNALL------------------------GEERAIVTDIPGttrdVIEETIniGGiplrlidtAGIret 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316   228 -------GIRF-LKHLERCRVLLHLIDIDpidgTDPVENARIIISELEKysqdlaAKPRWLVFNKIDLLDKVEAEEKAKA 299
Cdd:pfam12631 156 ddevekiGIERaREAIEEADLVLLVLDAS----RPLDEEDLEILELLKD------KKPIIVVLNKSDLLGEIDELEELKG 225
                         170       180
                  ....*....|....*....|....*
gi 15833316   300 IAEalgwedkyYLISAASGLGVKDL 324
Cdd:pfam12631 226 KPV--------LAISAKTGEGLDEL 242
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
169-315 3.67e-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: 37.91  E-value: 3.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 169 NAGKSTFIRAV-------SAAKPkvadypfTTLVPSLGVVRMDNEKSFVvaDIPGL---IEGAAEGAglgirfLKHLERC 238
Cdd:cd09912  10 SAGKSTLLNALlgeevlpTGVTP-------TTAVITVLRYGLLKGVVLV--DTPGLnstIEHHTEIT------ESFLPRA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833316 239 RVLLHLIDIDPidgtdPV-ENARIIISELEKYSqdlaAKPRWLVFNKIDLLDK------VEAEEKAKAIAEALGWEDKYY 311
Cdd:cd09912  75 DAVIFVLSADQ-----PLtESEREFLKEILKWS----GKKIFFVLNKIDLLSEeeleevLEYSREELGVLELGGGEPRIF 145

                ....
gi 15833316 312 LISA 315
Cdd:cd09912 146 PVSA 149
PRK00098 PRK00098
GTPase RsgA; Reviewed
280-324 3.88e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 38.65  E-value: 3.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 15833316  280 LVFNKIDLLDKVEAEEKAKAIAEALGWEdkYYLISAASGLGVKDL 324
Cdd:PRK00098 116 IVLNKIDLLDDLEEARELLALYRAIGYD--VLELSAKEGEGLDEL 158
 
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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