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Conserved domains on  [gi|795566923|ref|XP_011720934|]
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mitochondrial ribosome-associated GTPase 2 [Macaca nemestrina]

Protein Classification

GTPase Obg( domain architecture ID 11425313)

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
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
17-210 1.04e-88

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: 265.31  E-value: 1.04e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  17 NRFFLANDNRAPVTCTPGRPGQRRVLHLELKTVAHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGH 96
Cdd:COG0536  125 NAHFKSSTNRAPRFAEPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDG 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  97 QQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRFLLFVVDLSQPE---PWTQVDDLKYELEMYEEGLSERPHAIIANKID 173
Cdd:COG0536  205 RSFVIADIPGLIEGASEGAGLGHRFLRHIERTRVLLHVVDAAPLDgrdPVEDYEIIRNELEAYSPELAEKPRIVVLNKID 284
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 795566923 174 LPEA--RANLSQLRDHLGREVIALSALTGENLEQLLLHL 210
Cdd:COG0536  285 LLDAeeLEELKAELEKLGGPVFPISAVTGEGLDELLYAL 323
 
Name Accession Description Interval E-value
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
17-210 1.04e-88

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: 265.31  E-value: 1.04e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  17 NRFFLANDNRAPVTCTPGRPGQRRVLHLELKTVAHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGH 96
Cdd:COG0536  125 NAHFKSSTNRAPRFAEPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDG 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  97 QQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRFLLFVVDLSQPE---PWTQVDDLKYELEMYEEGLSERPHAIIANKID 173
Cdd:COG0536  205 RSFVIADIPGLIEGASEGAGLGHRFLRHIERTRVLLHVVDAAPLDgrdPVEDYEIIRNELEAYSPELAEKPRIVVLNKID 284
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 795566923 174 LPEA--RANLSQLRDHLGREVIALSALTGENLEQLLLHL 210
Cdd:COG0536  285 LLDAeeLEELKAELEKLGGPVFPISAVTGEGLDELLYAL 323
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
17-210 1.12e-88

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: 264.67  E-value: 1.12e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923   17 NRFFLANDNRAPVTCTPGRPGQRRVLHLELKTVAHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGH 96
Cdd:TIGR02729 125 NAHFKSSTNRAPRFATPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDG 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923   97 QQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRFLLFVVDLSQPEPWTQVDDLKY---ELEMYEEGLSERPHAIIANKID 173
Cdd:TIGR02729 205 RSFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLLHLIDISPEDGSDPVEDYEIirnELKKYSPELAEKPRIVVLNKID 284
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 795566923  174 LP---EARANLSQLRDHLGREVIALSALTGENLEQLLLHL 210
Cdd:TIGR02729 285 LLdeeELEELLKELKKELGKPVFPISALTGEGLDELLDAL 324
obgE PRK12299
GTPase CgtA; Reviewed
17-207 1.92e-87

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 261.93  E-value: 1.92e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  17 NRFFLANDNRAPVTCTPGRPGQRRVLHLELKTVAHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGH 96
Cdd:PRK12299 126 NAHFKSSTNRAPRYATPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDY 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  97 QQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRFLLFVVDLSQPEPWTQVDDLKYELEMYEEGLSERPHAIIANKIDLPE 176
Cdd:PRK12299 206 KSFVIADIPGLIEGASEGAGLGHRFLKHIERTRLLLHLVDIEAVDPVEDYKTIRNELEKYSPELADKPRILVLNKIDLLD 285
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 795566923 177 ARANLSQL----RDHLGREVIALSALTGENLEQLL 207
Cdd:PRK12299 286 EEEEREKRaaleLAALGGPVFLISAVTGEGLDELL 320
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
50-210 2.04e-86

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: 253.12  E-value: 2.04e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  50 AHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHQQIAVADIPGIIRGAHQNRGLGSAFLRHIERCR 129
Cdd:cd01898    1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 130 FLLFVVDLSQPE-PWTQVDDLKYELEMYEEGLSERPHAIIANKIDLPEARANLSQLRDHL----GREVIALSALTGENLE 204
Cdd:cd01898   81 VLLHVIDLSGEDdPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELLkelkGKKVFPISALTGEGLD 160

                 ....*.
gi 795566923 205 QLLLHL 210
Cdd:cd01898  161 ELLKKL 166
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
51-171 1.21e-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: 114.64  E-value: 1.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923   51 HAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHqQIAVADIPGIIRGAHQNRGLGSAFLRHIErCRF 130
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGK-QIILVDTPGLIEGASEGEGLGRAFLAIIE-ADL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 795566923  131 LLFVVDLSqpEPWTQVDDlkyELEMYEEGlSERPHAIIANK 171
Cdd:pfam01926  79 ILFVVDSE--EGITPLDE---ELLELLRE-NKKPIILVLNK 113
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
51-189 2.21e-05

Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene required for transport of secretory proteins from the endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 197556 [Multi-domain]  Cd Length: 184  Bit Score: 43.77  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923    51 HAGMV--GFPNAGKSSLLRAISNARPAVASypfTTLKPhvgivhyeGHQQIAVADI--PGIIRGAHQN-RGLGSAFLRHI 125
Cdd:smart00178  17 HAKILflGLDNAGKTTLLHMLKNDRLAQHQ---PTQHP--------TSEELAIGNIkfTTFDLGGHQQaRRLWKDYFPEV 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795566923   126 ERcrfLLFVVDLSQPEpwtQVDDLKYELE--MYEEGLSERPHAIIANKIDLPEArANLSQLRDHLG 189
Cdd:smart00178  86 NG---IVYLVDAYDKE---RFAESKRELDalLSDEELATVPFLILGNKIDAPYA-ASEDELRYALG 144
 
Name Accession Description Interval E-value
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
17-210 1.04e-88

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: 265.31  E-value: 1.04e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  17 NRFFLANDNRAPVTCTPGRPGQRRVLHLELKTVAHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGH 96
Cdd:COG0536  125 NAHFKSSTNRAPRFAEPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDG 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  97 QQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRFLLFVVDLSQPE---PWTQVDDLKYELEMYEEGLSERPHAIIANKID 173
Cdd:COG0536  205 RSFVIADIPGLIEGASEGAGLGHRFLRHIERTRVLLHVVDAAPLDgrdPVEDYEIIRNELEAYSPELAEKPRIVVLNKID 284
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 795566923 174 LPEA--RANLSQLRDHLGREVIALSALTGENLEQLLLHL 210
Cdd:COG0536  285 LLDAeeLEELKAELEKLGGPVFPISAVTGEGLDELLYAL 323
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
17-210 1.12e-88

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: 264.67  E-value: 1.12e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923   17 NRFFLANDNRAPVTCTPGRPGQRRVLHLELKTVAHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGH 96
Cdd:TIGR02729 125 NAHFKSSTNRAPRFATPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDG 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923   97 QQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRFLLFVVDLSQPEPWTQVDDLKY---ELEMYEEGLSERPHAIIANKID 173
Cdd:TIGR02729 205 RSFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLLHLIDISPEDGSDPVEDYEIirnELKKYSPELAEKPRIVVLNKID 284
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 795566923  174 LP---EARANLSQLRDHLGREVIALSALTGENLEQLLLHL 210
Cdd:TIGR02729 285 LLdeeELEELLKELKKELGKPVFPISALTGEGLDELLDAL 324
obgE PRK12299
GTPase CgtA; Reviewed
17-207 1.92e-87

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 261.93  E-value: 1.92e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  17 NRFFLANDNRAPVTCTPGRPGQRRVLHLELKTVAHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGH 96
Cdd:PRK12299 126 NAHFKSSTNRAPRYATPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDY 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  97 QQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRFLLFVVDLSQPEPWTQVDDLKYELEMYEEGLSERPHAIIANKIDLPE 176
Cdd:PRK12299 206 KSFVIADIPGLIEGASEGAGLGHRFLKHIERTRLLLHLVDIEAVDPVEDYKTIRNELEKYSPELADKPRILVLNKIDLLD 285
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 795566923 177 ARANLSQL----RDHLGREVIALSALTGENLEQLL 207
Cdd:PRK12299 286 EEEEREKRaaleLAALGGPVFLISAVTGEGLDELL 320
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
50-210 2.04e-86

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: 253.12  E-value: 2.04e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  50 AHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHQQIAVADIPGIIRGAHQNRGLGSAFLRHIERCR 129
Cdd:cd01898    1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 130 FLLFVVDLSQPE-PWTQVDDLKYELEMYEEGLSERPHAIIANKIDLPEARANLSQLRDHL----GREVIALSALTGENLE 204
Cdd:cd01898   81 VLLHVIDLSGEDdPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELLkelkGKKVFPISALTGEGLD 160

                 ....*.
gi 795566923 205 QLLLHL 210
Cdd:cd01898  161 ELLKKL 166
obgE PRK12297
GTPase CgtA; Reviewed
25-207 5.02e-83

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 253.48  E-value: 5.02e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  25 NRAPVTCTPGRPGQRRVLHLELKTVAHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHQQIAVADI 104
Cdd:PRK12297 134 NQAPRIAENGEPGEERELRLELKLLADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRSFVMADI 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 105 PGIIRGAHQNRGLGSAFLRHIERCRFLLFVVDLSQPE---PWTQVDDLKYELEMYEEGLSERPHAIIANKIDLPEARANL 181
Cdd:PRK12297 214 PGLIEGASEGVGLGHQFLRHIERTRVIVHVIDMSGSEgrdPIEDYEKINKELKLYNPRLLERPQIVVANKMDLPEAEENL 293
                        170       180
                 ....*....|....*....|....*.
gi 795566923 182 SQLRDHLGREVIALSALTGENLEQLL 207
Cdd:PRK12297 294 EEFKEKLGPKVFPISALTGQGLDELL 319
obgE PRK12298
GTPase CgtA; Reviewed
25-210 3.47e-70

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 219.35  E-value: 3.47e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  25 NRAPVTCTPGRPGQRRVLHLELKTVAHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHQQIAVADI 104
Cdd:PRK12298 135 NRAPRQKTPGTPGEERELKLELKLLADVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDERSFVVADI 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 105 PGIIRGAHQNRGLGSAFLRHIERCRFLLFVVDLS---QPEPWTQVDDLKYELEMYEEGLSERPHAIIANKIDL---PEAR 178
Cdd:PRK12298 215 PGLIEGASEGAGLGIRFLKHLERCRVLLHLIDIApidGSDPVENARIIINELEKYSPKLAEKPRWLVFNKIDLldeEEAE 294
                        170       180       190
                 ....*....|....*....|....*....|....
gi 795566923 179 ANLSQLRDHLG--REVIALSALTGENLEQLLLHL 210
Cdd:PRK12298 295 ERAKAIVEALGweGPVYLISAASGLGVKELCWDL 328
obgE PRK12296
GTPase CgtA; Reviewed
21-206 2.76e-56

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 186.61  E-value: 2.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  21 LANDNR-APVTCTPGRPGQRRVLHLELKTVAHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYeGHQQI 99
Cdd:PRK12296 130 LASKARkAPGFALLGEPGEERDLVLELKSVADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQA-GDTRF 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 100 AVADIPGIIRGAHQNRGLGSAFLRHIERCRFLLFVVDLSQPE----PWTQVDDLKYELEMYEE---------GLSERPHA 166
Cdd:PRK12296 209 TVADVPGLIPGASEGKGLGLDFLRHIERCAVLVHVVDCATLEpgrdPLSDIDALEAELAAYAPaldgdlglgDLAERPRL 288
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 795566923 167 IIANKIDLPEARANLSQLRDHL---GREVIALSALTGENLEQL 206
Cdd:PRK12296 289 VVLNKIDVPDARELAEFVRPELearGWPVFEVSAASREGLREL 331
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
53-207 3.52e-43

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: 143.30  E-value: 3.52e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  53 GMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHQQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRFLL 132
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 133 FVVDLSQPEPWTQVDDLK---YELEMYEEGLSERPHAIIANKIDLPEARANLSQLRDHLGRE--VIALSALTGENLEQLL 207
Cdd:cd01881   81 HVIDASEDCVGDPLEDQKtlnEEVSGSFLFLKNKPEMIVANKIDMASENNLKRLKLDKLKRGipVVPTSALTRLGLDRVI 160
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
51-171 1.21e-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: 114.64  E-value: 1.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923   51 HAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHqQIAVADIPGIIRGAHQNRGLGSAFLRHIErCRF 130
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGK-QIILVDTPGLIEGASEGEGLGRAFLAIIE-ADL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 795566923  131 LLFVVDLSqpEPWTQVDDlkyELEMYEEGlSERPHAIIANK 171
Cdd:pfam01926  79 ILFVVDSE--EGITPLDE---ELLELLRE-NKKPIILVLNK 113
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
48-206 1.85e-29

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 112.97  E-value: 1.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  48 TVAhagMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGhQQIAVADIPGIIRGAHQNRGLGSAFLRHIER 127
Cdd:COG1163   65 TVV---LVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLEYKG-AKIQILDVPGLIEGAASGKGRGKEVLSVVRN 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 128 CRFLLFVVDLSQPEpwtQVDDLKYELE----------------------------------------------MY----- 156
Cdd:COG1163  141 ADLILIVLDVFELE---QYDVLKEELYdagirlnkpppdvtiekkgkggirvnstgkldldeedikkilreygIVnadvl 217
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795566923 157 ----------EEGLSER----PHAIIANKIDLPEaRANLSQLRDHL--GREVIALSALTGENLEQL 206
Cdd:COG1163  218 iredvtlddlIDALMGNrvykPAIVVVNKIDLAD-EEYVEELKSKLpdGVPVIFISAEKGIGLEEL 282
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
50-154 2.47e-29

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: 109.56  E-value: 2.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  50 AHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGhQQIAVADIPGIIRGAHQNRGLGSAFLRHIERCR 129
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKG-AKIQLLDLPGIIEGASDGKGRGRQVIAVARTAD 79
                         90       100
                 ....*....|....*....|....*
gi 795566923 130 FLLFVVDLSQPEpwTQVDDLKYELE 154
Cdd:cd01896   80 LILIVLDATKPE--GQREILERELE 102
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
53-207 5.09e-25

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: 96.16  E-value: 5.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  53 GMVGFPNAGKSSLLRAISNARPA-VASYPFTTLKPHVGIVHYEGHQQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRFL 131
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGiVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 132 LFVVDLSQPEpwtqvddlkYELEMYEEGLSER--PHAIIANKIDLPEARANLSQLRD-----HLGREVIALSALTGENLE 204
Cdd:cd00880   81 LLVVDSDLTP---------VEEEAKLGLLRERgkPVLLVLNKIDLVPESEEEELLRErklelLPDLPVIAVSALPGEGID 151

                 ...
gi 795566923 205 QLL 207
Cdd:cd00880  152 ELR 154
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
45-207 5.16e-25

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 100.29  E-value: 5.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  45 ELKTVAHAGMvgfPNAGKSSLLRAISNARPAVASYPFTTLKPHVGivHYE-GHQQIAVADIPGII------RGAHQNRGL 117
Cdd:COG1084  159 DLPTIVVAGY---PNVGKSSLVSKVTSAKPEIASYPFTTKGIIVG--HFErGHGRYQVIDTPGLLdrplseRNEIERQAI 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 118 gSAfLRHIERCrfLLFVVDLSQpepwTQVDDLKYELEMYEE--GLSERPHAIIANKIDLPEARanlsQLRDHLGREVIAL 195
Cdd:COG1084  234 -LA-LKHLADV--ILFLFDPSE----TCGYSLEEQLNLLEEirSLFDVPVIVVINKIDLSDEE----ELKEAEEEADIKI 301
                        170
                 ....*....|..
gi 795566923 196 SALTGENLEQLL 207
Cdd:COG1084  302 SALTGEGVDELL 313
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
56-206 2.31e-24

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: 94.55  E-value: 2.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  56 GFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGivHYE-GHQQIAVADIPGIIRGAHQNRG----LGSAFLRHIERCrf 130
Cdd:cd01897    7 GYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVG--HFDyKYLRWQVIDTPGILDRPLEERNtiemQAITALAHLRAA-- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 131 LLFVVDLSQpepwTQVDDLKYELEMYEE--GLSERPHAIIANKIDLPEaRANLSQLRDHL---GREVIALSALTGENLEQ 205
Cdd:cd01897   83 VLFFIDPSE----TCGYSIEEQLSLFKEikPLFNKPVIVVLNKIDLLT-EEDLSEIEKELekeGEEVIKISTLTEEGVDE 157

                 .
gi 795566923 206 L 206
Cdd:cd01897  158 L 158
PRK09602 PRK09602
translation-associated GTPase; Reviewed
53-197 2.54e-21

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 91.02  E-value: 2.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  53 GMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGI-------VHYE--------------GHQQIAVA--DIPGIIR 109
Cdd:PRK09602   5 GLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayvrvecPCKElgvkcnprngkcidGTRFIPVEliDVAGLVP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 110 GAHQNRGLGSAFLRHIERCRFLLFVVDLS-------QP-EPWTQ-----VDDLKYELEMY-------------------- 156
Cdd:PRK09602  85 GAHEGRGLGNQFLDDLRQADALIHVVDASgstdeegNPvEPGSHdpvedIKFLEEELDMWiygileknwekfsrkaqaek 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 157 ---EEGLSER--------------------------------------------PHAIIANKIDLPEARANLSQLRDHLG 189
Cdd:PRK09602 165 fdiEEALAEQlsglgineehvkealrelglpedpskwtdedllelarelrkiskPMVIAANKADLPPAEENIERLKEEKY 244

                 ....*...
gi 795566923 190 REVIALSA 197
Cdd:PRK09602 245 YIVVPTSA 252
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
55-207 3.16e-20

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: 83.66  E-value: 3.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  55 VGFPNAGKSSLLRAISNA-RPAVASYPFTTLKPHVGIVHYEGHQ-QIAVADIPGIIRGAHQNRglGSAFLRHIERCRFLL 132
Cdd:cd00882    3 VGRGGVGKSSLLNALLGGeVGEVSDVPGTTRDPDVYVKELDKGKvKLVLVDTPGLDEFGGLGR--EELARLLLRGADLIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 133 FVVDLSQPEpwtQVDDLKYELEMYEEGlSERPHAIIANKIDLPEAR-----ANLSQLRDHLGREVIALSALTGENLEQLL 207
Cdd:cd00882   81 LVVDSTDRE---SEEDAKLLILRRLRK-EGIPIILVGNKIDLLEEReveelLRLEELAKILGVPVFEVSAKTGEGVDELF 156
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
53-138 1.41e-17

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: 79.58  E-value: 1.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  53 GMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHY---------------------EGHQQIAVA--DIPGIIR 109
Cdd:cd01899    2 GLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVGYVrvecpckelgvscnprygkciDGKRYVPVEliDVAGLVP 81
                         90       100
                 ....*....|....*....|....*....
gi 795566923 110 GAHQNRGLGSAFLRHIERCRFLLFVVDLS 138
Cdd:cd01899   82 GAHEGKGLGNQFLDDLRDADVLIHVVDAS 110
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
52-125 1.60e-17

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: 79.04  E-value: 1.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  52 AGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIV------------HYEG----HQQIAVADIPGIIRGAHQNR 115
Cdd:cd01900    1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVpvpderldklaeIVKPkkivPATIEFVDIAGLVKGASKGE 80
                         90
                 ....*....|
gi 795566923 116 GLGSAFLRHI 125
Cdd:cd01900   81 GLGNKFLSHI 90
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
45-207 1.69e-17

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: 77.50  E-value: 1.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  45 ELKTVAhagMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHQQIAVADIPGIIRG-AHQnrgLGSAF-- 121
Cdd:cd01878   40 GVPTVA---LVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTTRRIKLPGGREVLLTDTVGFIRDlPHQ---LVEAFrs 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 122 -LRHIERCRFLLFVVDLSQPEPWTQVDDLKYELEmyEEGLSERPHAIIANKIDLPEARANLSQLRDHLGrEVIALSALTG 200
Cdd:cd01878  114 tLEEVAEADLLLHVVDASDPDREEQIETVEEVLK--ELGADDIPIILVLNKIDLLDDEELEERLRAGRP-DAVFISAKTG 190

                 ....*..
gi 795566923 201 ENLEQLL 207
Cdd:cd01878  191 EGLDLLK 197
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
52-125 7.00e-17

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 78.14  E-value: 7.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  52 AGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIV------------HYEG----HQQIAVADIPGIIRGAHQNR 115
Cdd:COG0012    3 CGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVpvpderldklaeIVKPkkivPATIEFVDIAGLVKGASKGE 82
                         90
                 ....*....|
gi 795566923 116 GLGSAFLRHI 125
Cdd:COG0012   83 GLGNQFLANI 92
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
51-211 9.25e-17

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: 74.81  E-value: 9.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  51 HAGMV---GFPNAGKSSLLRAISNARpaVASypfTTLKPH------VGIVHYEGHQQIAVaDIPGIIRGAHQ-NRGLGSA 120
Cdd:cd04163    2 KSGFVaiiGRPNVGKSTLLNALVGQK--ISI---VSPKPQttrnriRGIYTDDDAQIIFV-DTPGIHKPKKKlGERMVKA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 121 FLRHIERCRFLLFVVDLSQPEPwtqvDDLKYELEMYEEglSERPHAIIANKIDLPEARANLSQLRDHL-----GREVIAL 195
Cdd:cd04163   76 AWSALKDVDLVLFVVDASEWIG----EGDEFILELLKK--SKTPVILVLNKIDLVKDKEDLLPLLEKLkelhpFAEIFPI 149
                        170
                 ....*....|....*.
gi 795566923 196 SALTGENLEQLLLHLK 211
Cdd:cd04163  150 SALKGENVDELLEYIV 165
PTZ00258 PTZ00258
GTP-binding protein; Provisional
38-135 3.91e-15

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 73.44  E-value: 3.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  38 QRRVLHLELktvahaGMVGFPNAGKSSLLRAISN-ARPAvASYPFTTLKPHVGIV----------------HYEGHQQIA 100
Cdd:PTZ00258  16 GRPGNNLKM------GIVGLPNVGKSTTFNALCKqQVPA-ENFPFCTIDPNTARVnvpderfdwlckhfkpKSIVPAQLD 88
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 795566923 101 VADIPGIIRGAHQNRGLGSAFLRHIERCRFLLFVV 135
Cdd:PTZ00258  89 ITDIAGLVKGASEGEGLGNAFLSHIRAVDGIYHVV 123
era PRK00089
GTPase Era; Reviewed
55-211 6.10e-15

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 72.00  E-value: 6.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  55 VGFPNAGKSSLLRAISNARPA-VASYPFTTLKPHVGIVHYEGHQQIAVaDIPGIIRGAHQ-NRGLGSAFLRHIERCRFLL 132
Cdd:PRK00089  11 VGRPNVGKSTLLNALVGQKISiVSPKPQTTRHRIRGIVTEDDAQIIFV-DTPGIHKPKRAlNRAMNKAAWSSLKDVDLVL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 133 FVVDLSqpEPWTQVDdlKYELEMYEEglSERPHAIIANKIDLPEARANLSQLRDHLGR-----EVIALSALTGENLEQLL 207
Cdd:PRK00089  90 FVVDAD--EKIGPGD--EFILEKLKK--VKTPVILVLNKIDLVKDKEELLPLLEELSElmdfaEIVPISALKGDNVDELL 163

                 ....
gi 795566923 208 LHLK 211
Cdd:PRK00089 164 DVIA 167
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
45-222 3.20e-14

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 70.89  E-value: 3.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  45 ELKTVAhagMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHQQIAVADIPGIIRG-AHQnrgLGSAF-- 121
Cdd:COG2262  198 GIPTVA---LVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRRLELPDGRPVLLTDTVGFIRKlPHQ---LVEAFrs 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 122 -LRHIERCRFLLFVVDLSQPEPWTQ---VDDLKYELemyeeGLSERPHAIIANKIDL--PEARANLSQLRDHlgreVIAL 195
Cdd:COG2262  272 tLEEVREADLLLHVVDASDPDFEEQietVNEVLEEL-----GADDKPIILVFNKIDLldDEELERLRAGYPD----AVFI 342
                        170       180
                 ....*....|....*....|....*...
gi 795566923 196 SALTGENLEQLLLHL-KVLHDAYVEAEL 222
Cdd:COG2262  343 SAKTGEGIDELLEAIeERLPEDRVEVEL 370
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
55-211 6.23e-14

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: 66.75  E-value: 6.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  55 VGFPNAGKSSLLRAISNaRPA--VASYPFTT---LkphvgivhyegHQQIAVADIP-------GI-----------IRGA 111
Cdd:cd04164    9 AGKPNVGKSSLLNALAG-RDRaiVSDIAGTTrdvI-----------EEEIDLGGIPvrlidtaGLretedeiekigIERA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 112 HQnrglgsaflrHIERCRFLLFVVDLSQPepWTQVDDLKYELemyeegLSERPHAIIANKIDLPEARANLSqlrDHLGRE 191
Cdd:cd04164   77 RE----------AIEEADLVLLVVDASEG--LDEEDLEILEL------PAKKPVIVVLNKSDLLSDAEGIS---ELNGKP 135
                        170       180
                 ....*....|....*....|
gi 795566923 192 VIALSALTGENLEQLLLHLK 211
Cdd:cd04164  136 IIAISAKTGEGIDELKEALL 155
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
55-207 5.74e-13

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 66.55  E-value: 5.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  55 VGFPNAGKSSLLRAISNARPA-VASYPFTTLKPHVGIVHYEGHQQIAVaDIPGIIRGAHQ-NRGLGSAFLRHIERCRFLL 132
Cdd:COG1159    9 VGRPNVGKSTLLNALVGQKVSiVSPKPQTTRHRIRGIVTREDAQIVFV-DTPGIHKPKRKlGRRMNKAAWSALEDVDVIL 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795566923 133 FVVDLSqpEPWTQVDdlKYELEMYEEglSERPHAIIANKIDL---PEARANLSQLRDHLG-REVIALSALTGENLEQLL 207
Cdd:COG1159   88 FVVDAT--EKIGEGD--EFILELLKK--LKTPVILVINKIDLvkkEELLPLLAEYSELLDfAEIVPISALKGDNVDELL 160
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
54-210 2.51e-12

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 63.08  E-value: 2.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  54 MVGFPNAGKSSLLRAISNARPAVASYpfttLKPHvGIVHY-------EGHQQIAVADIPGI--IRGAHQNrglgsaFLRH 124
Cdd:COG1100    8 VVGTGGVGKTSLVNRLVGDIFSLEKY----LSTN-GVTIDkkelkldGLDVDLVIWDTPGQdeFRETRQF------YARQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 125 IERCRFLLFVVDLSQPEPWTqvdDLKYELEMYEEGLSERPHAIIANKIDL--PEARANLSQLR----DHLGREVIALSAL 198
Cdd:COG1100   77 LTGASLYLFVVDGTREETLQ---SLYELLESLRRLGKKSPIILVLNKIDLydEEEIEDEERLKealsEDNIVEVVATSAK 153
                        170
                 ....*....|..
gi 795566923 199 TGENLEQLLLHL 210
Cdd:COG1100  154 TGEGVEELFAAL 165
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
54-216 2.81e-12

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: 62.47  E-value: 2.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  54 MVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHqQIAVADIPGI--IRGAHQNRGLGSAFLRHiERCRFL 131
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGK-EIEIVDLPGTysLTPYSEDEKVARDFLLG-EEPDLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 132 LFVVDLSQPE---PWT-QVddlkyeLEMyeeglsERPHAIIANKIDLPEARA---NLSQLRDHLGREVIALSALTGENLE 204
Cdd:cd01879   80 VNVVDATNLErnlYLTlQL------LEL------GLPVVVALNMIDEAEKRGikiDLDKLSELLGVPVVPTSARKGEGID 147
                        170
                 ....*....|..
gi 795566923 205 QLLLHLKVLHDA 216
Cdd:cd01879  148 ELLDAIAKLAES 159
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
38-211 2.91e-12

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 65.13  E-value: 2.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  38 QRRVLHLELKTVahagMVGFPNAGKSSLL-------RAIsnarpaVASYPFTT---LkphvgivhyegHQQIAVADIP-- 105
Cdd:PRK05291 208 QGEILREGLKVV----IAGRPNVGKSSLLnallgeeRAI------VTDIAGTTrdvI-----------EEHINLDGIPlr 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 106 -----GI-----------IRGAHQnrglgsaflrHIERCRFLLFVVDLSQPepWTQVDDLKYELemyeegLSERPHAIIA 169
Cdd:PRK05291 267 lidtaGIretddevekigIERSRE----------AIEEADLVLLVLDASEP--LTEEDDEILEE------LKDKPVIVVL 328
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 795566923 170 NKIDLPEAranlSQLRDHLGREVIALSALTGENLEQLLLHLK 211
Cdd:PRK05291 329 NKADLTGE----IDLEEENGKPVIRISAKTGEGIDELREAIK 366
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
52-225 1.64e-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: 62.02  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923   52 AGMVGFPNAGKSSLLRAISNARPAVAS-YPFTTLKPHVGIvHYEGHQQIAVADIPGIIRGAHQ-NRGLGSAFLRHIERCR 129
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISITSpKAQTTRNRISGI-HTTGASQIIFIDTPGFHEKKHSlNRLMMKEARSAIGGVD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  130 FLLFVVDLSQpepWTQVDdlkyelEMYEEGL--SERPHAIIANKIDLPEARANLSQLRDHLGRE----VIALSALTGENL 203
Cdd:TIGR00436  82 LILFVVDSDQ---WNGDG------EFVLTKLqnLKRPVVLTRNKLDNKFKDKLLPLIDKYAILEdfkdIVPISALTGDNT 152
                         170       180
                  ....*....|....*....|..
gi 795566923  204 EQLLlhlkvlhdAYVEAELGKG 225
Cdd:TIGR00436 153 SFLA--------AFIEVHLPEG 166
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
54-207 2.02e-11

ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 60.28  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  54 MVGFPNAGKSSLLRAIsnarpavASYPFTTLKPHVG----IVHYEGHQqIAVADIPGiirgahQNRglgsafLRHI---- 125
Cdd:cd00878    4 MLGLDGAGKTTILYKL-------KLGEVVTTIPTIGfnveTVEYKNVK-FTVWDVGG------QDK------IRPLwkhy 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 126 -ERCRFLLFVVDLSQPEpwtQVDDLKYELE--MYEEGLSERPHAIIANKIDLPEAR-----ANLSQLRDHLGRE--VIAL 195
Cdd:cd00878   64 yENTDGLIFVVDSSDRE---RIEEAKNELHklLNEEELKGAPLLILANKQDLPGALteselIELLGLESIKGRRwhIQPC 140
                        170
                 ....*....|..
gi 795566923 196 SALTGENLEQLL 207
Cdd:cd00878  141 SAVTGDGLDEGL 152
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
38-211 2.95e-11

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: 62.39  E-value: 2.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  38 QRRVLHLELKTVahagMVGFPNAGKSSLL-------RAIsnarpaVASYPFTT---LKPHVgivHYEGHQqIAVADIPGI 107
Cdd:COG0486  206 QGELLREGIKVV----IVGRPNVGKSSLLnallgeeRAI------VTDIAGTTrdvIEERI---NIGGIP-VRLIDTAGL 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 108 -----------IRGAHQnrglgsaflrHIERCRFLLFVVDLSQPepwtqvddLKYELEMYEEGLSERPHAIIANKIDLPE 176
Cdd:COG0486  272 retedevekigIERARE----------AIEEADLVLLLLDASEP--------LTEEDEEILEKLKDKPVIVVLNKIDLPS 333
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 795566923 177 ARAnlSQLRDHLGREVIALSALTGENLEQLLLHLK 211
Cdd:COG0486  334 EAD--GELKSLPGEPVIAISAKTGEGIDELKEAIL 366
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
53-206 5.12e-11

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: 59.31  E-value: 5.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923   53 GMVGFPNAGKSSLLRAIS-NARPAVASYPFTTLKPHVGIVHYEGHQ-QIAVADIPGIIRGAHQNRGLGSAFLRHIERCRF 130
Cdd:TIGR00231   5 VIVGHPNVGKSTLLNSLLgNKGSITEYYPGTTRNYVTTVIEEDGKTyKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFDI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  131 LLFVVDLSQ-PEPWTQVddLKYELEMyeeglsERPHAIIANKIDLPEAR---------ANLSQLRdhlgreVIALSALTG 200
Cdd:TIGR00231  85 VILVLDVEEiLEKQTKE--IIHHADS------GVPIILVGNKIDLKDADlkthvasefAKLNGEP------IIPLSAETG 150

                  ....*.
gi 795566923  201 ENLEQL 206
Cdd:TIGR00231 151 KNIDSA 156
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
55-211 3.12e-10

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: 59.03  E-value: 3.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923   55 VGFPNAGKSSLL-------RAIsnarpaVASYPFTT---LKPHVgivHYEGHQqIAVADIPGI-----------IRGAHQ 113
Cdd:pfam12631 100 VGKPNVGKSSLLnallgeeRAI------VTDIPGTTrdvIEETI---NIGGIP-LRLIDTAGIretddevekigIERARE 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  114 nrglgsaflrHIERCRFLLFVVDLSQPepWTQVDDLKYELemyeegLSERPHAI-IANKIDLPEAranLSQLRDHLGREV 192
Cdd:pfam12631 170 ----------AIEEADLVLLVLDASRP--LDEEDLEILEL------LKDKKPIIvVLNKSDLLGE---IDELEELKGKPV 228
                         170
                  ....*....|....*....
gi 795566923  193 IALSALTGENLEQLLLHLK 211
Cdd:pfam12631 229 LAISAKTGEGLDELEEAIK 247
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
54-210 3.98e-10

Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in high-risk familial breast cancer.


Pssm-ID: 133356 [Multi-domain]  Cd Length: 160  Bit Score: 56.65  E-value: 3.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  54 MVGFPNAGKSSLLRAISNARPavasypFTTLkPHVG----IVHYEGHQQIAVADIPGiirgahQNRgLGSAFLRHIERCR 129
Cdd:cd04156    4 LLGLDSAGKSTLLYKLKHAEL------VTTI-PTVGfnveMLQLEKHLSLTVWDVGG------QEK-MRTVWKCYLENTD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 130 FLLFVVDLSQPEpwtQVDDLKYELE--MYEEGLSERPHAIIANKIDLPEA--------RANLSQLRDHLGREVIALSALT 199
Cdd:cd04156   70 GLVYVVDSSDEA---RLDESQKELKhiLKNEHIKGVPVVLLANKQDLPGAltaeeitrRFKLKKYCSDRDWYVQPCSAVT 146
                        170
                 ....*....|.
gi 795566923 200 GENLEQLLLHL 210
Cdd:cd04156  147 GEGLAEAFRKL 157
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
54-207 2.25e-08

ADP-ribosylation factor family; Pfam combines a number of different Prosite families together


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 51.84  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923   54 MVGFPNAGKSSLLRAISNARpAVASYPftTLKPHVGIVHYEGHQqIAVADIpgiirGAHQNrglgsafLRHIERCRF--- 130
Cdd:pfam00025   5 ILGLDNAGKTTILYKLKLGE-IVTTIP--TIGFNVETVTYKNVK-FTVWDV-----GGQES-------LRPLWRNYFpnt 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  131 --LLFVVDLSQPEpwtQVDDLKYELE--MYEEGLSERPHAIIANKIDLPEArANLSQLRDHLGR--------EVIALSAL 198
Cdd:pfam00025  69 daVIFVVDSADRD---RIEEAKEELHalLNEEELADAPLLILANKQDLPGA-MSEAEIRELLGLhelkdrpwEIQGCSAV 144

                  ....*....
gi 795566923  199 TGENLEQLL 207
Cdd:pfam00025 145 TGEGLDEGL 153
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
54-207 8.57e-08

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: 50.51  E-value: 8.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  54 MVGFPNAGKSSLLRAISNA-RPAVASYPFTTLKPHVGIVHYEGhQQIAVADIPGIIRGAHQNRGL-----GSAfLRHIER 127
Cdd:cd01895    7 IIGRPNVGKSSLLNALLGEeRVIVSDIAGTTRDSIDVPFEYDG-QKYTLIDTAGIRKKGKVTEGIekysvLRT-LKAIER 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 128 CRFLLFVVDLSqpEPWTQVDdlKYELEM-YEEGlseRPHAIIANKIDL-PEARANLSQLRDHLGRE--------VIALSA 197
Cdd:cd01895   85 ADVVLLVLDAS--EGITEQD--LRIAGLiLEEG---KALIIVVNKWDLvEKDEKTMKEFEKELRRKlpfldyapIVFISA 157
                        170
                 ....*....|
gi 795566923 198 LTGENLEQLL 207
Cdd:cd01895  158 LTGQGVDKLF 167
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
52-207 1.54e-07

Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from a human cancer-derived EST dataset. No functional information about the subfamily is available at the current time, but crystal structures of human Arl10b and Arl10c have been solved.


Pssm-ID: 206724 [Multi-domain]  Cd Length: 159  Bit Score: 49.24  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  52 AGMVGFPNAGKSSLLRAISNARPAVASYPftTLKPHVGIVHyEGHQQIAVADIPGiirgahQNRglgsaFLRHIER-CR- 129
Cdd:cd04159    2 ITLVGLQNSGKTTLVNVIASGQFSEDTIP--TVGFNMRKVT-KGNVTIKVWDLGG------QPR-----FRSMWERyCRg 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 130 --FLLFVVDLSQPEPWTQVddlKYELE--MYEEGLSERPHAIIANKIDLPEA--------RANLSQLRDhlgREV--IAL 195
Cdd:cd04159   68 vnAIVYVVDAADREKLEVA---KNELHdlLEKPSLEGIPLLVLGNKNDLPGAlsvdelieQMNLKSITD---REVscYSI 141
                        170
                 ....*....|..
gi 795566923 196 SALTGENLEQLL 207
Cdd:cd04159  142 SAKEKTNIDIVL 153
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
54-205 1.67e-07

Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most Arf family members in the N-terminal extension. In is inactive, GDP-bound form, the N-terminal extension forms an elongated loop that is hydrophobically anchored into the membrane surface; however, it has been proposed that this region might form a helix in the GTP-bound form. The delta subunit of the rod-specific cyclic GMP phosphodiesterase type 6 (PDEdelta) is an Arl3 effector. Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis via interactions with retinitis pigmentosa 2 (RP2). It has been proposed that RP2 functions in concert with Arl3 to link the cell membrane and the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery. In mice, the absence of Arl3 is associated with abnormal epithelial cell proliferation and cyst formation.


Pssm-ID: 206721 [Multi-domain]  Cd Length: 174  Bit Score: 49.70  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  54 MVGFPNAGKSSLLRAISNarpAVASYPFTTLKPHVGIVHYEGhQQIAVADIPGiirgahqNRGLGSAFLRHIERCRFLLF 133
Cdd:cd04155   20 LLGLDNAGKTTILKQLAS---EDISHITPTQGFNIKNVQADG-FKLNVWDIGG-------QRKIRPYWRNYFENTDVLIY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 134 VVDLSQPEpwtQVDDLKYELE--MYEEGLSERPHAIIANKIDLPEARA--------NLSQLRDHLGrEVIALSALTGENL 203
Cdd:cd04155   89 VIDSADRK---RFEEAGQELVelLEEEKLAGVPVLVFANKQDLLTAAPaeevaealNLHDIRDRSW-HIQACSAKTGEGL 164

                 ..
gi 795566923 204 EQ 205
Cdd:cd04155  165 QE 166
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
54-189 1.67e-07

Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII vesicle coats involved in export of cargo from the ER. The GTPase activity of Sar1 functions as a molecular switch to control protein-protein and protein-lipid interactions that direct vesicle budding from the ER. Activation of the GDP to the GTP-bound form of Sar1 involves the membrane-associated guanine nucleotide exchange factor (GEF) Sec12. Sar1 is unlike all Ras superfamily GTPases that use either myristoyl or prenyl groups to direct membrane association and function, in that Sar1 lacks such modification. Instead, Sar1 contains a unique nine-amino-acid N-terminal extension. This extension contains an evolutionarily conserved cluster of bulky hydrophobic amino acids, referred to as the Sar1-N-terminal activation recruitment (STAR) motif. The STAR motif mediates the recruitment of Sar1 to ER membranes and facilitates its interaction with mammalian Sec12 GEF leading to activation.


Pssm-ID: 206645 [Multi-domain]  Cd Length: 191  Bit Score: 49.97  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  54 MVGFPNAGKSSLLRAISNARpaVASY-PftTLKPH-----VGIVHYE-----GHQQIA------VADIPGIIrgahqnrg 116
Cdd:cd00879   24 FLGLDNAGKTTLLHMLKDDR--LAQHvP--TLHPTseeltIGNVKFTtfdlgGHEQARrvwkdyFPEVDGIV-------- 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795566923 117 lgsaflrhiercrfllFVVDLSQPEpwtQVDDLKYELE--MYEEGLSERPHAIIANKIDLPEArANLSQLRDHLG 189
Cdd:cd00879   92 ----------------FLVDAADPE---RFQESKEELDslLNDEELANVPILILGNKIDKPGA-VSEEELREALG 146
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
55-210 1.97e-07

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: 49.43  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  55 VGFPNAGKSSLLRAISN----ARpaVASYPFTTLKphvgIVHYEGHQQIAVADIPG--------IIRGAHQNrgLGSAFL 122
Cdd:cd01876    5 AGRSNVGKSSLINALTNrkklAR--TSKTPGRTQL----INFFNVGDKFRLVDLPGygyakvskEVREKWGK--LIEEYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 123 RHIERCRFLLFVVDLSQPepwtqvdDLKYELEMYEEgLSER--PHAIIANKID-LP--EARANLSQLRDHLGR-----EV 192
Cdd:cd01876   77 ENRENLKGVVLLIDARHG-------PTPIDLEMLEF-LEELgiPFLIVLTKADkLKksELAKVLKKIKEELNLfnilpPV 148
                        170
                 ....*....|....*...
gi 795566923 193 IALSALTGENLEQLLLHL 210
Cdd:cd01876  149 ILFSSKKGTGIDELRALI 166
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
47-210 4.53e-07

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 49.73  E-value: 4.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  47 KTVAhagMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHqQIAVADIPGIIrgahqnrGLGSA------ 120
Cdd:COG0370    4 ITIA---LVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGK-EIELVDLPGTY-------SLSAYspdekv 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 121 ---FLRHiERCRFLLFVVDLSQPEP----WTQVddlkyeLEMyeeglsERPhAIIA-NKIDlpEARA-----NLSQLRDH 187
Cdd:COG0370   73 ardFLLE-EKPDVVVNVVDATNLERnlylTLQL------LEL------GIP-VVLAlNMMD--EAEKkgikiDVEKLSKL 136
                        170       180
                 ....*....|....*....|...
gi 795566923 188 LGREVIALSALTGENLEQLLLHL 210
Cdd:COG0370  137 LGVPVVPTSARKGKGIDELKEAI 159
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
37-206 4.86e-07

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 49.79  E-value: 4.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  37 GQRRVlhlelktvahaGMVGFPNAGKSSLLRAISNARPAVAS-YPFTTLKPHVGIVHYEGHQQIAVaDIPGIIRGAHQNR 115
Cdd:PRK09518 449 GLRRV-----------ALVGRPNVGKSSLLNQLTHEERAVVNdLAGTTRDPVDEIVEIDGEDWLFI-DTAGIKRRQHKLT 516
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 116 GLG-SAFLRH---IERCRFLLFVVDLSQPepwTQVDDLKYeLEMYEEglSERPHAIIANKIDL-PEARanlsqlRDHLGR 190
Cdd:PRK09518 517 GAEyYSSLRTqaaIERSELALFLFDASQP---ISEQDLKV-MSMAVD--AGRALVLVFNKWDLmDEFR------RQRLER 584
                        170       180
                 ....*....|....*....|....*...
gi 795566923 191 EV------------IALSALTGENLEQL 206
Cdd:PRK09518 585 LWktefdrvtwarrVNLSAKTGWHTNRL 612
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
55-205 2.58e-06

Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a membrane-associated Arf family member that lacks the N-terminal myristoylation motif. Arfrp1 is mainly associated with the trans-Golgi compartment and the trans-Golgi network, where it regulates the targeting of Arl1 and the GRIP domain-containing proteins, golgin-97 and golgin-245, onto Golgi membranes. It is also involved in the anterograde transport of the vesicular stomatitis virus G protein from the Golgi to the plasma membrane, and in the retrograde transport of TGN38 and Shiga toxin from endosomes to the trans-Golgi network. Arfrp1 also inhibits Arf/Sec7-dependent activation of phospholipase D. Deletion of Arfrp1 in mice causes embryonic lethality at the gastrulation stage and apoptosis of mesodermal cells, indicating its importance in development.


Pssm-ID: 206725 [Multi-domain]  Cd Length: 168  Bit Score: 46.18  E-value: 2.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  55 VGFPNAGKSSLLRAI-SNARPAVASYPFTTLKPHVGivhyeghQQIAVADIPGII-----RGAHQnrGLGSAFLRHIERC 128
Cdd:cd04160    5 LGLDNAGKTTFLEQTkTKFSKNYKGLNPSKITPTVG-------LNIGTIEVGKARlmfwdLGGQE--ELRSLWDKYYAES 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 129 RFLLFVVDLSQPEpwtQVDDLKYELE--MYEEGLSERPHAIIANKIDLP------EARANLSQLRDHLGRE---VIALSA 197
Cdd:cd04160   76 HGVIYVIDSTDRE---RFNESKSAFEkvINNEALEGVPLLVLANKQDLPdalsvaEIKEVFDDCIALIGRRdclVQPVSA 152

                 ....*...
gi 795566923 198 LTGENLEQ 205
Cdd:cd04160  153 LEGEGVEE 160
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
54-210 1.11e-05

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 43.98  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  54 MVGFPNAGKSSLL-RAISNArpavasypFT-TLKPHVGI------VHYEGHQ-QIAVADIPGIIRgahqNRGLGSAFLRH 124
Cdd:cd00154    5 LIGDSGVGKTSLLlRFVDNK--------FSeNYKSTIGVdfksktIEVDGKKvKLQIWDTAGQER----FRSITSSYYRG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 125 ierCRFLLFVVDLSQPEPWTQVDDLKYELEMYeeGLSERPHAIIANKIDLPEARANLS----QLRDHLGREVIALSALTG 200
Cdd:cd00154   73 ---AHGAILVYDVTNRESFENLDKWLNELKEY--APPNIPIILVGNKSDLEDERQVSTeeaqQFAKENGLLFFETSAKTG 147
                        170
                 ....*....|
gi 795566923 201 ENLEQLLLHL 210
Cdd:cd00154  148 ENVDEAFESL 157
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
51-189 2.21e-05

Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene required for transport of secretory proteins from the endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 197556 [Multi-domain]  Cd Length: 184  Bit Score: 43.77  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923    51 HAGMV--GFPNAGKSSLLRAISNARPAVASypfTTLKPhvgivhyeGHQQIAVADI--PGIIRGAHQN-RGLGSAFLRHI 125
Cdd:smart00178  17 HAKILflGLDNAGKTTLLHMLKNDRLAQHQ---PTQHP--------TSEELAIGNIkfTTFDLGGHQQaRRLWKDYFPEV 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795566923   126 ERcrfLLFVVDLSQPEpwtQVDDLKYELE--MYEEGLSERPHAIIANKIDLPEArANLSQLRDHLG 189
Cdd:smart00178  86 NG---IVYLVDAYDKE---RFAESKRELDalLSDEELATVPFLILGNKIDAPYA-ASEDELRYALG 144
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
54-207 7.06e-05

Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like Arl4 and Arl7, are localized to the nucleus and nucleolus. Arl5 is developmentally regulated during embryogenesis in mice. Human Arl5 interacts with the heterochromatin protein 1-alpha (HP1alpha), a nonhistone chromosomal protein that is associated with heterochromatin and telomeres, and prevents telomere fusion. Arl5 may also play a role in embryonic nuclear dynamics and/or signaling cascades. Arl8 was identified from a fetal cartilage cDNA library. It is found in brain, heart, lung, cartilage, and kidney. No function has been assigned for Arl8 to date.


Pssm-ID: 133353 [Multi-domain]  Cd Length: 174  Bit Score: 41.95  E-value: 7.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  54 MVGFPNAGKSSLLRAISnARPAVASYPftTLKPHVGIVHYEGhQQIAVADIPGiirgahQNRgLGSAFLRHIERCRFLLF 133
Cdd:cd04153   20 IVGLDNAGKTTILYQFL-LGEVVHTSP--TIGSNVEEIVYKN-IRFLMWDIGG------QES-LRSSWNTYYTNTDAVIL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 134 VVDLSQPEPWTQVDDLKYELEMYEEgLSERPHAIIANKIDLPEARA--------NLSQLRDHlGREVIALSALTGENLEQ 205
Cdd:cd04153   89 VIDSTDRERLPLTKEELYKMLAHED-LRKAVLLVLANKQDLKGAMTpaeiseslGLTSIRDH-TWHIQGCCALTGEGLPE 166

                 ..
gi 795566923 206 LL 207
Cdd:cd04153  167 GL 168
Arl2l1_Arl13_like cd04161
Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a ...
53-179 8.64e-05

Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a subfamily of the Arf family of small GTPases. Arl2l1 was identified in human cells during a search for the gene(s) responsible for Bardet-Biedl syndrome (BBS). Like Arl6, the identified BBS gene, Arl2l1 is proposed to have cilia-specific functions. Arl13 is found on the X chromosome, but its expression has not been confirmed; it may be a pseudogene.


Pssm-ID: 133361 [Multi-domain]  Cd Length: 167  Bit Score: 41.61  E-value: 8.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  53 GMVGFPNAGKSSLLRAI-----SNARPAVASYPfTTLKphvgivhyEGHQQIAVADIPGIIRGahqnRGlgsAFLRHIER 127
Cdd:cd04161    3 LTVGLDNAGKTTLVSALqgeipKKVAPTVGFTP-TKLR--------LDKYEVCIFDLGGGANF----RG---IWVNYYAE 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 795566923 128 CRFLLFVVDLSQPEPWTQVDDLKYELeMYEEGLSERPHAIIANKIDLPEARA 179
Cdd:cd04161   67 AHGLVFVVDSSDDDRVQEVKEILREL-LQHPRVSGKPILVLANKQDKKNALL 117
GTP1_OBG pfam01018
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ...
16-48 8.77e-05

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: 41.56  E-value: 8.77e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 795566923   16 GNRFFLANDNRAPVTCTPGRPGQRRVLHLELKT 48
Cdd:pfam01018 123 GNAHFKTSTNQAPRFAEPGEPGEERWLELELKL 155
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
45-107 1.40e-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: 41.48  E-value: 1.40e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795566923  45 ELKTVAHAG----MVGFPNAGKSSLLRAI------------SNARPAVASYPFTTLkphvGIVHYEGHQQIAVADIPGI 107
Cdd:cd01855  117 EIKKLAKYRgdvyVVGATNVGKSTLINALlksnggkvqaqaLVQRLTVSPIPGTTL----GLIKIPLGEGKKLYDTPGI 191
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
53-107 1.57e-04

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: 40.45  E-value: 1.57e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 795566923  53 GMVGFPNAGKSSLLRAISNARPAVASY--PFTTLKPHVGIVHyeghqQIAVADIPGI 107
Cdd:cd01849   95 GVVGLPNVGKSSFINALLNKFKLKVGSipGTTKLQQDVKLDK-----EIYLYDTPGI 146
PRK00098 PRK00098
GTPase RsgA; Reviewed
167-211 1.74e-04

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 41.73  E-value: 1.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 795566923 167 IIANKIDLPEARANLSQLRDH---LGREVIALSALTGENLEQLLLHLK 211
Cdd:PRK00098 116 IVLNKIDLLDDLEEARELLALyraIGYDVLELSAKEGEGLDELKPLLA 163
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
55-205 3.04e-04

Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small GTPases. Arl6 expression is limited to the brain and kidney in adult mice, but it is expressed in the neural plate and somites during embryogenesis, suggesting a possible role for Arl6 in early development. Arl6 is also believed to have a role in cilia or flagella function. Several proteins have been identified that bind Arl6, including Arl6 interacting protein (Arl6ip), and SEC61beta, a subunit of the heterotrimeric conducting channel SEC61p. Based on Arl6 binding to these effectors, Arl6 is also proposed to play a role in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. At least three specific homozygous Arl6 mutations in humans have been found to cause Bardet-Biedl syndrome, a disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, and hypogenitalism. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.


Pssm-ID: 206722 [Multi-domain]  Cd Length: 162  Bit Score: 40.11  E-value: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  55 VGFPNAGKSSLLRAI--SNARPAvasypftTLKPHVGIV---HYEGHQQIAVADIPGiirgAHQNRGLGSAFLrhiERCR 129
Cdd:cd04157    5 LGLDNSGKTTIINQLkpSNAQSQ-------NIVPTVGFNvesFKKGNLSFTAFDMSG----QGKYRGLWEHYY---KNIQ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 130 FLLFVVDLSqpepwtqvDDL-----KYELEMYEE--GLSER--PHAIIANKIDLPEARA--------NLSQLRDHlGREV 192
Cdd:cd04157   71 GIIFVIDSS--------DRLrmvvaKDELELLLNhpDIKHRriPILFYANKMDLPDALTavkitqllCLENIKDK-PWHI 141
                        170
                 ....*....|...
gi 795566923 193 IALSALTGENLEQ 205
Cdd:cd04157  142 FASSALTGEGLDE 154
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
165-229 3.64e-04

Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 41.15  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 165 HA-------IIA-NKIDLPEARAN--LSQLRDH------LGREVIA--LSALTGENLEQLL---------LHLKVLHDAY 217
Cdd:COG0532   98 HAkaagvpiIVAiNKIDKPGANPDrvKQELAEHglvpeeWGGDTIFvpVSAKTGEGIDELLemillqaevLELKANPDRP 177
                         90
                 ....*....|....*..
gi 795566923 218 -----VEAELGKGRQPL 229
Cdd:COG0532  178 argtvIEAKLDKGRGPV 194
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
54-207 5.14e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 40.42  E-value: 5.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  54 MVGFPNAGKSSLLRAISNARPAVAS-YPFTTLKPhvgI---VHYEGhQQIAVADIPGIIRGAHQNRGL-----GSAfLRH 124
Cdd:PRK00093 178 IIGRPNVGKSSLINALLGEERVIVSdIAGTTRDS---IdtpFERDG-QKYTLIDTAGIRRKGKVTEGVekysvIRT-LKA 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 125 IERCRFLLFVVDLSQP--EpwtQvdDLK---YeleMYEEGlseRPHAIIANKIDL--PEARANL-SQLRDHLGR----EV 192
Cdd:PRK00093 253 IERADVVLLVIDATEGitE---Q--DLRiagL---ALEAG---RALVIVVNKWDLvdEKTMEEFkKELRRRLPFldyaPI 321
                        170
                 ....*....|....*
gi 795566923 193 IALSALTGENLEQLL 207
Cdd:PRK00093 322 VFISALTGQGVDKLL 336
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
162-207 9.24e-04

LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.


Pssm-ID: 206677 [Multi-domain]  Cd Length: 179  Bit Score: 38.67  E-value: 9.24e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 795566923 162 ERPHAIIA--NKIDLPEARAN--LSQLRDHLG---REVIALSALTGENLEQLL 207
Cdd:cd01890  117 ENNLEIIPviNKIDLPAADPDrvKQEIEDVLGldaSEAILVSAKTGLGVEDLL 169
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
37-206 1.14e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 39.57  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  37 GQRRVlhlelktvahaGMVGFPNAGKSSLLRAISNA-RPAVASYPFTTLKPHVGIVHYEGHQQIAVaDIPGIIRGAHQNR 115
Cdd:PRK03003 210 GPRRV-----------ALVGKPNVGKSSLLNKLAGEeRSVVDDVAGTTVDPVDSLIELGGKTWRFV-DTAGLRRRVKQAS 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923 116 GLG-SAFLRH---IERCRFLLFVVDLSQPepwTQVDDLKYeLEMYEEglSERPHAIIANKIDL-PEARanlsqlRDHLGR 190
Cdd:PRK03003 278 GHEyYASLRThaaIEAAEVAVVLIDASEP---ISEQDQRV-LSMVIE--AGRALVLAFNKWDLvDEDR------RYYLER 345
                        170       180
                 ....*....|....*....|....*...
gi 795566923 191 EV------------IALSALTGENLEQL 206
Cdd:PRK03003 346 EIdrelaqvpwaprVNISAKTGRAVDKL 373
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
50-88 1.48e-03

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


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 37.60  E-value: 1.48e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 795566923  50 AHAGMVGFPNAGKSSLLRAISNA-RPAVASYP-----FTT--LKPHV 88
Cdd:cd01857   83 ATIGLVGYPNVGKSSLINALVGSkKVSVSSTPgktkhFQTifLEPGI 129
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
55-194 4.69e-03

Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first identified as part of the Human Cancer Genome Project. It maps to chromosome 4q12 and is sometimes referred to as Arfrp2 (Arf-related protein 2). This is a novel subfamily identified in human cancers that is uncharacterized to date.


Pssm-ID: 133362 [Multi-domain]  Cd Length: 164  Bit Score: 36.66  E-value: 4.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795566923  55 VGFPNAGKSSLLRAISNARPAVASYPfTTLKPHVGIVHyeGHQQIAVADIPgiirGAHQNRGLGSAFLrhiERCRFLLFV 134
Cdd:cd04162    5 LGLDGAGKTSLLHSLSSERSLESVVP-TTGFNSVAIPT--QDAIMELLEIG----GSQNLRKYWKRYL---SGSQGLIFV 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795566923 135 VDLSQPE--PWTqvddlKYELEMYEEGLSERPHAIIANKIDLPEARAnLSQLRDHLGREVIA 194
Cdd:cd04162   75 VDSADSErlPLA-----RQELHQLLQHPPDLPLVVLANKQDLPAARS-VQEIHKELELEPIA 130
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
45-83 8.14e-03

A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein that functions as a regulator of cell growth and proliferation in stem cells and in several types of cancer cells, but is not expressed in the differentiated cells of most mammalian adult tissues. NS shuttles between the nucleolus and nucleoplasm bidirectionally at a rate that is fast and independent of cell type. Lowering GTP levels decreases the nucleolar retention of NS, and expression of NS is abruptly down-regulated during differentiation prior to terminal cell division. Found only in eukaryotes, NS consists of an N-terminal basic domain, a coiled-coil domain, a GTP-binding domain, an intermediate domain, and a C-terminal acidic domain. Experimental evidence indicates that NS uses its GTP-binding property as a molecular switch to control the transition between the nucleolus and nucleoplasm, and this process involves interaction between the basic, GTP-binding, and intermediate domains of the protein.


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 36.01  E-value: 8.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 795566923  45 ELKTVAHAGMVGFPNAGKSSLLRAISNARP-AVASYP-FTT 83
Cdd:cd04178  112 GIKTSITVGVVGYPNVGKSSVINSLKRSRAcNVGATPgVTK 152
 
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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