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Conserved domains on  [gi|330443587|ref|NP_012038|]
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putative GTPase MTG2 [Saccharomyces cerevisiae S288C]

Protein Classification

Obg family GTPase( domain architecture ID 1004071)

Obg family GTPase is a P-loop small G protein that may be 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_CgtA super family cl37158
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
91-509 9.55e-73

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]


The actual alignment was detected with superfamily member TIGR02729:

Pssm-ID: 274271 [Multi-domain]  Cd Length: 328  Bit Score: 233.85  E-value: 9.55e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587   91 FVDVRIVKCKSGAGGSGAVSFFR------------DAGRSigppdggdggagGSVYIQAVAGLGSLAKMKTT--YTAEDG 156
Cdd:TIGR02729   1 FVDEAKIFVKAGDGGNGCVSFRRekyvpkggpdggDGGRG------------GSVILEADENLNTLLDFRYQrhFKAENG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  157 EAGAARQLDGMRGRDVLIQVPVGTVVKwclppqkvrelveremrkdnNATLRSILGstavnlsvssgshrkkiqlyrhem 236
Cdd:TIGR02729  69 ENGMGKNRTGKSGEDLVIKVPVGTVVY--------------------DADTGELLA------------------------ 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  237 aeswlfkdkakeyhenkdwfkDLHKKmeaydhsleqselfNDQFPLA-----GLdlnqpmtkpvcllkggqgglGNMHFL 311
Cdd:TIGR02729 105 ---------------------DLTEP--------------GQRFLVAkggrgGL--------------------GNAHFK 129
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  312 TNLIRNPRFSKPGRNGLEQHFLFELKSIADLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQDvFT 391
Cdd:TIGR02729 130 SSTNRAPRFATPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRS-FV 208
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  392 VADIPGIIQGASLDKGMGLEFLRHIERSNGWVFVLDLS---NKNPLNDLQLLIEEVGTL-EKVKTKNILIVCNKVDIDAE 467
Cdd:TIGR02729 209 IADIPGLIEGASEGAGLGHRFLKHIERTRVLLHLIDISpedGSDPVEDYEIIRNELKKYsPELAEKPRIVVLNKIDLLDE 288
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 330443587  468 ksESFAKylQVEKFSKSQEWDCVPISALREENIDVLKKKMFK 509
Cdd:TIGR02729 289 --EELEE--LLKELKKELGKPVFPISALTGEGLDELLDALAE 326
 
Name Accession Description Interval E-value
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
91-509 9.55e-73

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: 233.85  E-value: 9.55e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587   91 FVDVRIVKCKSGAGGSGAVSFFR------------DAGRSigppdggdggagGSVYIQAVAGLGSLAKMKTT--YTAEDG 156
Cdd:TIGR02729   1 FVDEAKIFVKAGDGGNGCVSFRRekyvpkggpdggDGGRG------------GSVILEADENLNTLLDFRYQrhFKAENG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  157 EAGAARQLDGMRGRDVLIQVPVGTVVKwclppqkvrelveremrkdnNATLRSILGstavnlsvssgshrkkiqlyrhem 236
Cdd:TIGR02729  69 ENGMGKNRTGKSGEDLVIKVPVGTVVY--------------------DADTGELLA------------------------ 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  237 aeswlfkdkakeyhenkdwfkDLHKKmeaydhsleqselfNDQFPLA-----GLdlnqpmtkpvcllkggqgglGNMHFL 311
Cdd:TIGR02729 105 ---------------------DLTEP--------------GQRFLVAkggrgGL--------------------GNAHFK 129
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  312 TNLIRNPRFSKPGRNGLEQHFLFELKSIADLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQDvFT 391
Cdd:TIGR02729 130 SSTNRAPRFATPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRS-FV 208
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  392 VADIPGIIQGASLDKGMGLEFLRHIERSNGWVFVLDLS---NKNPLNDLQLLIEEVGTL-EKVKTKNILIVCNKVDIDAE 467
Cdd:TIGR02729 209 IADIPGLIEGASEGAGLGHRFLKHIERTRVLLHLIDISpedGSDPVEDYEIIRNELKKYsPELAEKPRIVVLNKIDLLDE 288
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 330443587  468 ksESFAKylQVEKFSKSQEWDCVPISALREENIDVLKKKMFK 509
Cdd:TIGR02729 289 --EELEE--LLKELKKELGKPVFPISALTGEGLDELLDALAE 326
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
340-510 3.62e-72

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: 226.92  E-value: 3.62e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 340 ADLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQDvFTVADIPGIIQGASLDKGMGLEFLRHIERS 419
Cdd:cd01898    1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRS-FVIADIPGLIEGASEGKGLGHRFLRHIERT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 420 NGWVFVLDLSNK-NPLNDLQLLIEEVGTL-EKVKTKNILIVCNKVDIDAEKSESFAKYlqvEKFSKSQEWDCVPISALRE 497
Cdd:cd01898   80 RVLLHVIDLSGEdDPVEDYETIRNELEAYnPGLAEKPRIVVLNKIDLLDAEERFEKLK---ELLKELKGKKVFPISALTG 156
                        170
                 ....*....|...
gi 330443587 498 ENIDVLKKKMFKC 510
Cdd:cd01898  157 EGLDELLKKLAKL 169
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
91-509 4.36e-71

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: 230.25  E-value: 4.36e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  91 FVD-VRIvKCKSGAGGSGAVSFFR------------DAGRSigppdggdggagGSVYIQAVAGLGSLA--KMKTTYTAED 155
Cdd:COG0536    1 FVDeAKI-YVKAGDGGNGCVSFRRekyvpkggpdggDGGRG------------GDVILVADENLNTLLdfRYKRHFKAEN 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 156 GEAGAARQLDGMRGRDVLIQVPVGTVVKwclppqkvrelveremRKDNNATLrsilgstavnlsvssgshrkkiqlyrHE 235
Cdd:COG0536   68 GENGMGKNRTGKNGEDLVIKVPVGTVVK----------------DAETGEVL--------------------------AD 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 236 MAESwlfkdkakeyhenkdwfkdlhkkmeaydhsleqselfNDQFPLA-----GLdlnqpmtkpvcllkggqgglGNMHF 310
Cdd:COG0536  106 LTED-------------------------------------GQRVVVAkggrgGL--------------------GNAHF 128
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 311 LTNLIRNPRFSKPGRNGLEQHFLFELKSIADLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQDvF 390
Cdd:COG0536  129 KSSTNRAPRFAEPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRS-F 207
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 391 TVADIPGIIQGASLDKGMGLEFLRHIERSNGWVFVLDLS---NKNPLNDLQLLIEEvgtLEK----VKTKNILIVCNKVD 463
Cdd:COG0536  208 VIADIPGLIEGASEGAGLGHRFLRHIERTRVLLHVVDAApldGRDPVEDYEIIRNE---LEAyspeLAEKPRIVVLNKID 284
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 330443587 464 -IDAEKSESFAKYLqvekfsKSQEWDCVPISALREENIDVLKKKMFK 509
Cdd:COG0536  285 lLDAEELEELKAEL------EKLGGPVFPISAVTGEGLDELLYALAE 325
obgE PRK12299
GTPase CgtA; Reviewed
90-509 7.04e-69

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 224.18  E-value: 7.04e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  90 NFVDVRIVKCKSGAGGSGAVSFFR------------DAGRSigppdggdggagGSVYIQAVAGLGSLA--KMKTTYTAED 155
Cdd:PRK12299   1 KFIDEAKIYVKAGDGGNGCVSFRRekfipfggpdggDGGRG------------GSVILEADENLNTLIdfRYKRHFKAEN 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 156 GEAGAARQLDGMRGRDVLIQVPVGTVVKwclppqkvrelveremRKDNNATLrsilgstavnlsvssgshrkkiqlyrHE 235
Cdd:PRK12299  69 GENGMGRNRTGKSGKDLVLKVPVGTQIY----------------DADTGELI--------------------------AD 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 236 MAEswlfkdkakeyhenkdwfkdlhkkmeaydhsleqselFNDQFPLA-----GLdlnqpmtkpvcllkggqgglGNMHF 310
Cdd:PRK12299 107 LTE-------------------------------------HGQRFLVAkggkgGL--------------------GNAHF 129
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 311 LTNLIRNPRFSKPGRNGLEQHFLFELKSIADLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQDvF 390
Cdd:PRK12299 130 KSSTNRAPRYATPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKS-F 208
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 391 TVADIPGIIQGASLDKGMGLEFLRHIERSNGWVFVLDLSNKNPLNDLQLLIEEvgtLEK----VKTKNILIVCNKVDIDA 466
Cdd:PRK12299 209 VIADIPGLIEGASEGAGLGHRFLKHIERTRLLLHLVDIEAVDPVEDYKTIRNE---LEKyspeLADKPRILVLNKIDLLD 285
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 330443587 467 EKSESFAkylQVEKFSKSQEWDCVPISALREENIDVLKKKMFK 509
Cdd:PRK12299 286 EEEEREK---RAALELAALGGPVFLISAVTGEGLDELLRALWE 325
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
341-461 2.72e-26

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: 103.08  E-value: 2.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  341 DLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQdvFTVADIPGIIQGASLDKGMGLEFLRHIErSN 420
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQ--IILVDTPGLIEGASEGEGLGRAFLAIIE-AD 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 330443587  421 GWVFVLDLSNKnplndLQLLIEEVGTLEKVKTKNILIVCNK 461
Cdd:pfam01926  78 LILFVVDSEEG-----ITPLDEELLELLRENKKPIILVLNK 113
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
340-475 2.99e-06

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: 47.62  E-value: 2.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587   340 ADLGLIGLPNAGKSTILNKISNAKpkighwqFTTLSPTIGTVS--LGFGQDVFTVADIPGIIQGASLDKGmgleflrHIE 417
Cdd:smart00178  18 AKILFLGLDNAGKTTLLHMLKNDR-------LAQHQPTQHPTSeeLAIGNIKFTTFDLGGHQQARRLWKD-------YFP 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 330443587   418 RSNGWVFVLDLSNKNPLNDLQLLIEEVGTLEKVKTKNILIVCNKVDIDAEKSESFAKY 475
Cdd:smart00178  84 EVNGIVYLVDAYDKERFAESKRELDALLSDEELATVPFLILGNKIDAPYAASEDELRY 141
 
Name Accession Description Interval E-value
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
91-509 9.55e-73

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: 233.85  E-value: 9.55e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587   91 FVDVRIVKCKSGAGGSGAVSFFR------------DAGRSigppdggdggagGSVYIQAVAGLGSLAKMKTT--YTAEDG 156
Cdd:TIGR02729   1 FVDEAKIFVKAGDGGNGCVSFRRekyvpkggpdggDGGRG------------GSVILEADENLNTLLDFRYQrhFKAENG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  157 EAGAARQLDGMRGRDVLIQVPVGTVVKwclppqkvrelveremrkdnNATLRSILGstavnlsvssgshrkkiqlyrhem 236
Cdd:TIGR02729  69 ENGMGKNRTGKSGEDLVIKVPVGTVVY--------------------DADTGELLA------------------------ 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  237 aeswlfkdkakeyhenkdwfkDLHKKmeaydhsleqselfNDQFPLA-----GLdlnqpmtkpvcllkggqgglGNMHFL 311
Cdd:TIGR02729 105 ---------------------DLTEP--------------GQRFLVAkggrgGL--------------------GNAHFK 129
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  312 TNLIRNPRFSKPGRNGLEQHFLFELKSIADLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQDvFT 391
Cdd:TIGR02729 130 SSTNRAPRFATPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRS-FV 208
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  392 VADIPGIIQGASLDKGMGLEFLRHIERSNGWVFVLDLS---NKNPLNDLQLLIEEVGTL-EKVKTKNILIVCNKVDIDAE 467
Cdd:TIGR02729 209 IADIPGLIEGASEGAGLGHRFLKHIERTRVLLHLIDISpedGSDPVEDYEIIRNELKKYsPELAEKPRIVVLNKIDLLDE 288
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 330443587  468 ksESFAKylQVEKFSKSQEWDCVPISALREENIDVLKKKMFK 509
Cdd:TIGR02729 289 --EELEE--LLKELKKELGKPVFPISALTGEGLDELLDALAE 326
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
340-510 3.62e-72

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: 226.92  E-value: 3.62e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 340 ADLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQDvFTVADIPGIIQGASLDKGMGLEFLRHIERS 419
Cdd:cd01898    1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRS-FVIADIPGLIEGASEGKGLGHRFLRHIERT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 420 NGWVFVLDLSNK-NPLNDLQLLIEEVGTL-EKVKTKNILIVCNKVDIDAEKSESFAKYlqvEKFSKSQEWDCVPISALRE 497
Cdd:cd01898   80 RVLLHVIDLSGEdDPVEDYETIRNELEAYnPGLAEKPRIVVLNKIDLLDAEERFEKLK---ELLKELKGKKVFPISALTG 156
                        170
                 ....*....|...
gi 330443587 498 ENIDVLKKKMFKC 510
Cdd:cd01898  157 EGLDELLKKLAKL 169
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
91-509 4.36e-71

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: 230.25  E-value: 4.36e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  91 FVD-VRIvKCKSGAGGSGAVSFFR------------DAGRSigppdggdggagGSVYIQAVAGLGSLA--KMKTTYTAED 155
Cdd:COG0536    1 FVDeAKI-YVKAGDGGNGCVSFRRekyvpkggpdggDGGRG------------GDVILVADENLNTLLdfRYKRHFKAEN 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 156 GEAGAARQLDGMRGRDVLIQVPVGTVVKwclppqkvrelveremRKDNNATLrsilgstavnlsvssgshrkkiqlyrHE 235
Cdd:COG0536   68 GENGMGKNRTGKNGEDLVIKVPVGTVVK----------------DAETGEVL--------------------------AD 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 236 MAESwlfkdkakeyhenkdwfkdlhkkmeaydhsleqselfNDQFPLA-----GLdlnqpmtkpvcllkggqgglGNMHF 310
Cdd:COG0536  106 LTED-------------------------------------GQRVVVAkggrgGL--------------------GNAHF 128
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 311 LTNLIRNPRFSKPGRNGLEQHFLFELKSIADLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQDvF 390
Cdd:COG0536  129 KSSTNRAPRFAEPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRS-F 207
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 391 TVADIPGIIQGASLDKGMGLEFLRHIERSNGWVFVLDLS---NKNPLNDLQLLIEEvgtLEK----VKTKNILIVCNKVD 463
Cdd:COG0536  208 VIADIPGLIEGASEGAGLGHRFLRHIERTRVLLHVVDAApldGRDPVEDYEIIRNE---LEAyspeLAEKPRIVVLNKID 284
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 330443587 464 -IDAEKSESFAKYLqvekfsKSQEWDCVPISALREENIDVLKKKMFK 509
Cdd:COG0536  285 lLDAEELEELKAEL------EKLGGPVFPISAVTGEGLDELLYALAE 325
obgE PRK12299
GTPase CgtA; Reviewed
90-509 7.04e-69

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 224.18  E-value: 7.04e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  90 NFVDVRIVKCKSGAGGSGAVSFFR------------DAGRSigppdggdggagGSVYIQAVAGLGSLA--KMKTTYTAED 155
Cdd:PRK12299   1 KFIDEAKIYVKAGDGGNGCVSFRRekfipfggpdggDGGRG------------GSVILEADENLNTLIdfRYKRHFKAEN 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 156 GEAGAARQLDGMRGRDVLIQVPVGTVVKwclppqkvrelveremRKDNNATLrsilgstavnlsvssgshrkkiqlyrHE 235
Cdd:PRK12299  69 GENGMGRNRTGKSGKDLVLKVPVGTQIY----------------DADTGELI--------------------------AD 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 236 MAEswlfkdkakeyhenkdwfkdlhkkmeaydhsleqselFNDQFPLA-----GLdlnqpmtkpvcllkggqgglGNMHF 310
Cdd:PRK12299 107 LTE-------------------------------------HGQRFLVAkggkgGL--------------------GNAHF 129
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 311 LTNLIRNPRFSKPGRNGLEQHFLFELKSIADLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQDvF 390
Cdd:PRK12299 130 KSSTNRAPRYATPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKS-F 208
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 391 TVADIPGIIQGASLDKGMGLEFLRHIERSNGWVFVLDLSNKNPLNDLQLLIEEvgtLEK----VKTKNILIVCNKVDIDA 466
Cdd:PRK12299 209 VIADIPGLIEGASEGAGLGHRFLKHIERTRLLLHLVDIEAVDPVEDYKTIRNE---LEKyspeLADKPRILVLNKIDLLD 285
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 330443587 467 EKSESFAkylQVEKFSKSQEWDCVPISALREENIDVLKKKMFK 509
Cdd:PRK12299 286 EEEEREK---RAALELAALGGPVFLISAVTGEGLDELLRALWE 325
obgE PRK12297
GTPase CgtA; Reviewed
91-509 3.64e-65

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 217.28  E-value: 3.64e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  91 FVDVRIVKCKSGAGGSGAVSFFR------------DAGRSigppdggdggagGSVYIQAVAGLGSLA--KMKTTYTAEDG 156
Cdd:PRK12297   2 FIDQAKIYVKAGDGGDGMVSFRRekyvpkggpdggDGGKG------------GSVIFVADEGLRTLLdfRYKRHFKAENG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 157 EAGAARQLDGMRGRDVLIQVPVGTVVKwclppqkvrelveremrkdnNATLRSILGstavnlsvssgshrkkiqlyrhem 236
Cdd:PRK12297  70 ENGMGKNMHGRNGEDLIIKVPVGTVVK--------------------DAETGEVIA------------------------ 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 237 aeswlfkdkakeyhenkdwfkDLHKKmeaydhsleqselfNDQFPLA-------GldlnqpmtkpvcllkggqgglgNMH 309
Cdd:PRK12297 106 ---------------------DLVEP--------------GQEVVVAkggrggrG----------------------NAH 128
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 310 FLTNLIRNPRFSKPGRNGLEQHFLFELKSIADLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQDv 389
Cdd:PRK12297 129 FATSTNQAPRIAENGEPGEERELRLELKLLADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRS- 207
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 390 FTVADIPGIIQGASLDKGMGLEFLRHIERSNGWVFVLDLSN---KNPLNDLQLLIEEVGTL-EKVKTKNILIVCNKVDID 465
Cdd:PRK12297 208 FVMADIPGLIEGASEGVGLGHQFLRHIERTRVIVHVIDMSGsegRDPIEDYEKINKELKLYnPRLLERPQIVVANKMDLP 287
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 330443587 466 --AEKSESFAKYLQVEKFsksqewdcvPISALREENIDVLKKKMFK 509
Cdd:PRK12297 288 eaEENLEEFKEKLGPKVF---------PISALTGQGLDELLYAVAE 324
obgE PRK12298
GTPase CgtA; Reviewed
90-507 1.89e-53

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 185.46  E-value: 1.89e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  90 NFVDVRIVKCKSGAGGSGAVSFFR------------DAGRSigppdggdggagGSVYIQAVAGLGSLAKMKTT--YTAED 155
Cdd:PRK12298   2 KFVDEAKIRVVAGDGGNGCVSFRRekyipkggpdggDGGDG------------GDVYLEADENLNTLIDYRFErhFRAER 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 156 GEAGAARQLDGMRGRDVLIQVPVGTVVKwclppqkvrelveremrkdnNATLRSILGstavnlsvssgshrkkiQLYRHE 235
Cdd:PRK12298  70 GQNGQGRDCTGKRGKDITIKVPVGTRVI--------------------DADTGEVIG-----------------DLTEHG 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 236 MaeSWLFkdkAKeyhenkdwfkdlhkkmeAYDHSLeqselfndqfplaGldlnqpmtkpvcllkggqgglgNMHFLTNLI 315
Cdd:PRK12298 113 Q--RLLV---AK-----------------GGWHGL-------------G----------------------NTRFKSSVN 135
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 316 RNPRFSKPGRNGLEQHFLFELKSIADLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQDvFTVADI 395
Cdd:PRK12298 136 RAPRQKTPGTPGEERELKLELKLLADVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDERS-FVVADI 214
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 396 PGIIQGASLDKGMGLEFLRHIERSNGWVFVLDLS---NKNPLNDLQLLIEEVGTL-EKVKTKNILIVCNKVD-IDAEKSE 470
Cdd:PRK12298 215 PGLIEGASEGAGLGIRFLKHLERCRVLLHLIDIApidGSDPVENARIIINELEKYsPKLAEKPRWLVFNKIDlLDEEEAE 294
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 330443587 471 SfakylQVEKFSKSQEW--DCVPISALREENIDVLKKKM 507
Cdd:PRK12298 295 E-----RAKAIVEALGWegPVYLISAASGLGVKELCWDL 328
obgE PRK12296
GTPase CgtA; Reviewed
318-467 1.58e-39

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 150.02  E-value: 1.58e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 318 PRFSKPGRNGLEQHFLFELKSIADLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSlgFGQDVFTVADIPG 397
Cdd:PRK12296 138 PGFALLGEPGEERDLVLELKSVADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQ--AGDTRFTVADVPG 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 398 IIQGASLDKGMGLEFLRHIERSNGWVFVLDL----SNKNPLNDLQLLIEEV----------GTLEKVKTKNILIVCNKVD 463
Cdd:PRK12296 216 LIPGASEGKGLGLDFLRHIERCAVLVHVVDCatlePGRDPLSDIDALEAELaayapaldgdLGLGDLAERPRLVVLNKID 295

                 ....*
gi 330443587 464 I-DAE 467
Cdd:PRK12296 296 VpDAR 300
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
343-504 3.76e-30

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: 115.57  E-value: 3.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 343 GLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQDvFTVADIPGIIQGASLDKGMGLEFLRHIERSNGW 422
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVD-IQIIDLPGLLDGASEGRGLGEQILAHLYRSDLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 423 VFVLDLSNK---NPLNDLQLLIEEV-GTLEKVKTKNILIVCNKVDIDAEKSESFAKylqveKFSKSQEWDCVPISALREE 498
Cdd:cd01881   80 LHVIDASEDcvgDPLEDQKTLNEEVsGSFLFLKNKPEMIVANKIDMASENNLKRLK-----LDKLKRGIPVVPTSALTRL 154

                 ....*.
gi 330443587 499 NIDVLK 504
Cdd:cd01881  155 GLDRVI 160
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
341-461 2.72e-26

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: 103.08  E-value: 2.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  341 DLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQdvFTVADIPGIIQGASLDKGMGLEFLRHIErSN 420
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQ--IILVDTPGLIEGASEGEGLGRAFLAIIE-AD 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 330443587  421 GWVFVLDLSNKnplndLQLLIEEVGTLEKVKTKNILIVCNK 461
Cdd:pfam01926  78 LILFVVDSEEG-----ITPLDEELLELLRENKKPIILVLNK 113
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
343-509 1.06e-21

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: 91.75  E-value: 1.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 343 GLIGLPNAGKSTILNKISNAKPKI-GHWQFTTLSPTIGTVSLGFGQDVFTVADIPGIIQGAslDKGMGLEFLRHIERSNG 421
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEvSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFG--GLGREELARLLLRGADL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 422 WVFVLDLSNKNPLNDLQLLIEEvgTLEKVKtKNILIVCNKVDIDAEKSESFAKYLQVEKFSKsqEWDCVPISALREENID 501
Cdd:cd00882   79 ILLVVDSTDRESEEDAKLLILR--RLRKEG-IPIILVGNKIDLLEEREVEELLRLEELAKIL--GVPVFEVSAKTGEGVD 153

                 ....*...
gi 330443587 502 VLKKKMFK 509
Cdd:cd00882  154 ELFEKLIE 161
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
344-509 1.34e-20

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 93.32  E-value: 1.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQdvFTVADIPGIIQGASLDKGMGLEFLRHIERSNGWV 423
Cdd:COG1163   68 LVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLEYKGAK--IQILDVPGLIEGAASGKGRGKEVLSVVRNADLIL 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 424 FVLDLSNKNPLNDLQLLIEEVG----------TLEKVKT------------------KNIL------------------- 456
Cdd:COG1163  146 IVLDVFELEQYDVLKEELYDAGirlnkpppdvTIEKKGKggirvnstgkldldeediKKILreygivnadvliredvtld 225
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 457 ----------------IVCNKVD-IDAEKSESFAKYLqvekfskSQEWDCVPISALREENIDVLKKKMFK 509
Cdd:COG1163  226 dlidalmgnrvykpaiVVVNKIDlADEEYVEELKSKL-------PDGVPVIFISAEKGIGLEELKEEIFE 288
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
343-509 4.00e-20

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: 87.30  E-value: 4.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 343 GLIGLPNAGKSTILNKISNAKPKI-GHWQFTTLSPTIGTVSLGFGQDVfTVADIPGIIQGASLDKGMGLEFLRHIERSNG 421
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIvSPIPGTTRDPVRKEWELLPLGPV-VLIDTPGLDEEGGLGRERVEEARQVADRADL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 422 WVFVLDlsnknplNDLQLLIEEVGTLEKVKTKN-ILIVCNKVDIDAEKSEsfAKYLQVEKFSKSQEWDCVPISALREENI 500
Cdd:cd00880   80 VLLVVD-------SDLTPVEEEAKLGLLRERGKpVLLVLNKIDLVPESEE--EELLRERKLELLPDLPVIAVSALPGEGI 150

                 ....*....
gi 330443587 501 DVLKKKMFK 509
Cdd:cd00880  151 DELRKKIAE 159
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
340-510 6.15e-17

Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding protein (DRG) subfamily is an uncharacterized member of the Obg family, an evolutionary branch of GTPase superfamily proteins. GTPases act as molecular switches regulating diverse cellular processes. DRG2 and DRG1 comprise the DRG subfamily in eukaryotes. In view of their widespread expression in various tissues and high conservation among distantly related species in eukaryotes and archaea, DRG proteins may regulate fundamental cellular processes. It is proposed that the DRG subfamily proteins play their physiological roles through RNA binding.


Pssm-ID: 206683 [Multi-domain]  Cd Length: 233  Bit Score: 79.90  E-value: 6.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 340 ADLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLgfgQDV-FTVADIPGIIQGASLDKGMGLEFLRHIER 418
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEY---KGAkIQLLDLPGIIEGASDGKGRGRQVIAVART 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 419 SNGWVFVLDLSnkNPLNDLQLL---IEEVG----------TLEKVKT-------------------KNIL---------- 456
Cdd:cd01896   78 ADLILIVLDAT--KPEGQREILereLEGVGirlnkkppnvTIKKKKKgginitstvpltkldektvKAILreykihnadv 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 457 -------------------------IVCNKVD-IDAEKSESFAKYLqvekfsksqewDCVPISALREENIDVLKKKMFKC 510
Cdd:cd01896  156 lireditvddlidviegnrvyipclYVYNKIDlISIEELDRLARIP-----------NSVVISAEKDLNLDELLERIWDY 224
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
346-512 1.84e-15

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 77.57  E-value: 1.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 346 GLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQdvFTVADIPGIiqgasLDKGMG------------LEFL 413
Cdd:COG1084  167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGR--YQVIDTPGL-----LDRPLSerneierqailaLKHL 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 414 RHIersngWVFVLDLSNKN--PLNDlQL-LIEEVGTLEKVKtknILIVCNKVDIDAEKSESFAKYLQVekfsksqewdcV 490
Cdd:COG1084  240 ADV-----ILFLFDPSETCgySLEE-QLnLLEEIRSLFDVP---VIVVINKIDLSDEEELKEAEEEAD-----------I 299
                        170       180
                 ....*....|....*....|..
gi 330443587 491 PISALREENIDVLKKKMFKCAR 512
Cdd:COG1084  300 KISALTGEGVDELLDELIEALE 321
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
344-509 2.30e-15

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: 73.65  E-value: 2.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKISNAK-----PKIghwQfTTLSPTIGTVSLGFGQDVFTvaDIPGIIQG-ASLDKGMGLEFLRHIE 417
Cdd:cd04163    8 IIGRPNVGKSTLLNALVGQKisivsPKP---Q-TTRNRIRGIYTDDDAQIIFV--DTPGIHKPkKKLGERMVKAAWSALK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 418 RSNGWVFVLDLSNKNPLNDLQLLieevGTLEKVKTKNILIVcNKVDIDAEKSESFAKYLQVEKfsKSQEWDCVPISALRE 497
Cdd:cd04163   82 DVDLVLFVVDASEWIGEGDEFIL----ELLKKSKTPVILVL-NKIDLVKDKEDLLPLLEKLKE--LHPFAEIFPISALKG 154
                        170
                 ....*....|..
gi 330443587 498 ENIDVLKKKMFK 509
Cdd:cd04163  155 ENVDELLEYIVE 166
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
346-509 5.66e-15

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: 72.59  E-value: 5.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 346 GLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQdvFTVADIPGIiqgasLDKGMG----LEF-----LRHI 416
Cdd:cd01897    7 GYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLR--WQVIDTPGI-----LDRPLEerntIEMqaitaLAHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 417 ErsNGWVFVLDLSNK--NPLNDLQLLIEEVGTLEKvktKNILIVCNKVDIdaeKSESFAKYLQVEKFSKSQEWdcVPISA 494
Cdd:cd01897   80 R--AAVLFFIDPSETcgYSIEEQLSLFKEIKPLFN---KPVIVVLNKIDL---LTEEDLSEIEKELEKEGEEV--IKIST 149
                        170
                 ....*....|....*
gi 330443587 495 LREENIDVLKKKMFK 509
Cdd:cd01897  150 LTEEGVDELKNKACE 164
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
344-501 3.07e-13

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: 67.60  E-value: 3.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKIsnaKPKighwQFTTLSPTIGT--VSLGFGQDVFTVADIpGiiqgasldkgmGLEFLRHI----- 416
Cdd:cd00878    4 MLGLDGAGKTTILYKL---KLG----EVVTTIPTIGFnvETVEYKNVKFTVWDV-G-----------GQDKIRPLwkhyy 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 417 ERSNGWVFVLDLSNKNPLNDLQLLIEEVGTLEKVKTKNILIVCNKVD-IDAEKSESFAKYLQVEKFsKSQEWDCVPISAL 495
Cdd:cd00878   65 ENTDGLIFVVDSSDRERIEEAKNELHKLLNEEELKGAPLLILANKQDlPGALTESELIELLGLESI-KGRRWHIQPCSAV 143

                 ....*.
gi 330443587 496 REENID 501
Cdd:cd00878  144 TGDGLD 149
GTP1_OBG pfam01018
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ...
92-183 3.12e-13

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: 67.37  E-value: 3.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587   92 VDVRIVKCKSGAGGSGAVSFFRDA-----------GrsigppdggdgGAGGSVYIQAVAGLGSLA--KMKTTYTAEDGEA 158
Cdd:pfam01018   1 VDRAKIKVKAGDGGNGCVSFRREKyvpkggpdggdG-----------GRGGDVILVADENLNTLLdfRYKRHFKAENGEN 69
                          90       100
                  ....*....|....*....|....*
gi 330443587  159 GAARQLDGMRGRDVLIQVPVGTVVK 183
Cdd:pfam01018  70 GGGKNCHGKNGEDLIIKVPVGTVVK 94
era PRK00089
GTPase Era; Reviewed
344-509 3.49e-12

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 66.99  E-value: 3.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKISNAK-----PKIghwQfTTLSPTIGTVSLGFGQDVFTvaDIPGIIQGAS-LDKGMGLEFLRHIE 417
Cdd:PRK00089  10 IVGRPNVGKSTLLNALVGQKisivsPKP---Q-TTRHRIRGIVTEDDAQIIFV--DTPGIHKPKRaLNRAMNKAAWSSLK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 418 RSNGWVFVLDlSNKNPLNDLQLLIEEvgtLEKVKTKNILIVcNKVDIDAEKSESFAKYLQVEKfsKSQEWDCVPISALRE 497
Cdd:PRK00089  84 DVDLVLFVVD-ADEKIGPGDEFILEK---LKKVKTPVILVL-NKIDLVKDKEELLPLLEELSE--LMDFAEIVPISALKG 156
                        170
                 ....*....|..
gi 330443587 498 ENIDVLKKKMFK 509
Cdd:PRK00089 157 DNVDELLDVIAK 168
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
342-509 4.46e-12

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: 64.32  E-value: 4.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  342 LGLIGLPNAGKSTILNKISNAKPKIghwqfTTLSPTIG--TVSLGFGQD----VFTVADIPGIIQGASLDKGMGLEFLRH 415
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSI-----TEYYPGTTrnYVTTVIEEDgktyKFNLLDTAGQEDYDAIRRLYYPQVERS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  416 IERSNGWVFVLDLSNKnplndlqlLIEEVGTLEKVKTKN--ILIVCNKVDIdaeKSESFaKYLQVEKFSKSQEWDCVPIS 493
Cdd:TIGR00231  79 LRVFDIVILVLDVEEI--------LEKQTKEIIHHADSGvpIILVGNKIDL---KDADL-KTHVASEFAKLNGEPIIPLS 146
                         170
                  ....*....|....*.
gi 330443587  494 ALREENIDVLKKKMFK 509
Cdd:TIGR00231 147 AETGKNIDSAFKIVEA 162
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
342-444 7.88e-12

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: 66.48  E-value: 7.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 342 LGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTvslGFGQD-----VFTVA--------------------DIP 396
Cdd:cd01899    1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGV---GYVRVecpckELGVScnprygkcidgkryvpveliDVA 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330443587 397 GIIQGASLDKGMGLEFLRHIERSNGWVFVLDLS-------------NKNPLNDLQLLIEEV 444
Cdd:cd01899   78 GLVPGAHEGKGLGNQFLDDLRDADVLIHVVDASggtdaegngvetgGYDPLEDIEFLENEI 138
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
344-509 2.44e-11

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 64.62  E-value: 2.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILN-----KIS--NAKPkighwQfTTLSPTIGTVSLGFGQDVFTvaDIPGIIQGAS-LDKGMGLEFLRH 415
Cdd:COG1159    8 IVGRPNVGKSTLLNalvgqKVSivSPKP-----Q-TTRHRIRGIVTREDAQIVFV--DTPGIHKPKRkLGRRMNKAAWSA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 416 IERSNGWVFVLDLSNKNPLNDlQLLIEEvgtLEKVKTKNILIVcNKVD-IDAEKSESFAKYLQvekfSKSQEWDCVPISA 494
Cdd:COG1159   80 LEDVDVILFVVDATEKIGEGD-EFILEL---LKKLKTPVILVI-NKIDlVKKEELLPLLAEYS----ELLDFAEIVPISA 150
                        170
                 ....*....|....*
gi 330443587 495 LREENIDVLKKKMFK 509
Cdd:COG1159  151 LKGDNVDELLDEIAK 165
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
344-506 4.88e-11

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: 60.93  E-value: 4.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGfGQDvFTVADIPGI--IQGASLDKGMGLEFLRHiERSNG 421
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLG-GKE-IEIVDLPGTysLTPYSEDEKVARDFLLG-EEPDL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 422 WVFVLDLSN--KNplndLQLLIE--EVGtlekvktKNILIVCNKVD--------IDAEKsesFAKYLQVEkfsksqewdC 489
Cdd:cd01879   79 IVNVVDATNleRN----LYLTLQllELG-------LPVVVALNMIDeaekrgikIDLDK---LSELLGVP---------V 135
                        170
                 ....*....|....*..
gi 330443587 490 VPISALREENIDVLKKK 506
Cdd:cd01879  136 VPTSARKGEGIDELLDA 152
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
344-511 1.33e-10

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: 59.82  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKISnakpkighwqfttlsptigtvslgfGQDVFTVADIPG----IIQgASLD-KGMGLEF-----L 413
Cdd:cd04164    8 IAGKPNVGKSSLLNALA-------------------------GRDRAIVSDIAGttrdVIE-EEIDlGGIPVRLidtagL 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 414 RH---------IERSngW---------VFVLDLSNKNPLNDLQLlieevgtLEKVKTKNILIVCNKVDIDAEKSESFAKY 475
Cdd:cd04164   62 REtedeiekigIERA--ReaieeadlvLLVVDASEGLDEEDLEI-------LELPAKKPVIVVLNKSDLLSDAEGISELN 132
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 330443587 476 LQvekfsksqewDCVPISALREENIDVLKKKMFKCA 511
Cdd:cd04164  133 GK----------PIIAISAKTGEGIDELKEALLELA 158
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
335-509 5.27e-10

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: 59.01  E-value: 5.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 335 ELKSIAdlgLIGLPNAGKSTILNKISNA----KPKIghwqFTTLSPTIGTVSLGFGQDVfTVADIPGIIQG--------- 401
Cdd:cd01878   40 GVPTVA---LVGYTNAGKSTLFNALTGAdvlaEDQL----FATLDPTTRRIKLPGGREV-LLTDTVGFIRDlphqlveaf 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 402 -ASLDKGMGLEFLRHiersngwvfVLDLSNKNPLNDLQL---LIEEVGtlekVKTKNILIVCNKVD-IDAEKSESFAKYL 476
Cdd:cd01878  112 rSTLEEVAEADLLLH---------VVDASDPDREEQIETveeVLKELG----ADDIPIILVLNKIDlLDDEELEERLRAG 178
                        170       180       190
                 ....*....|....*....|....*....|...
gi 330443587 477 QVekfsksqewDCVPISALREENIDVLKKKMFK 509
Cdd:cd01878  179 RP---------DAVFISAKTGEGLDLLKEAIEE 202
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
343-516 5.58e-10

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: 60.09  E-value: 5.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  343 GLIGLPNAGKSTILNKISNAKPKI-GHWQFTTLSPTIGTVSLGFGQDVFTvaDIPGI-IQGASLDKGMGLEFLRHIERSN 420
Cdd:TIGR00436   4 AILGRPNVGKSTLLNQLHGQKISItSPKAQTTRNRISGIHTTGASQIIFI--DTPGFhEKKHSLNRLMMKEARSAIGGVD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  421 GWVFVLDLSNKNPLNDLQLLIeevgtLEKVKTKNILIVcNKVD-IDAEKSES-FAKYLQVEKFSksqewDCVPISALREE 498
Cdd:TIGR00436  82 LILFVVDSDQWNGDGEFVLTK-----LQNLKRPVVLTR-NKLDnKFKDKLLPlIDKYAILEDFK-----DIVPISALTGD 150
                         170
                  ....*....|....*...
gi 330443587  499 NIDVLKKKMFKCARQSEF 516
Cdd:TIGR00436 151 NTSFLAAFIEVHLPEGPF 168
Arl2 cd04154
Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind ...
344-501 1.16e-09

Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind GDP and GTP with very low affinity. Unlike most Arf family proteins, Arl2 is not myristoylated at its N-terminal helix. The protein PDE-delta, first identified in photoreceptor rod cells, binds specifically to Arl2 and is structurally very similar to RhoGDI. Despite the high structural similarity between Arl2 and Rho proteins and between PDE-delta and RhoGDI, the interactions between the GTPases and their effectors are very different. In its GTP bound form, Arl2 interacts with the protein Binder of Arl2 (BART), and the complex is believed to play a role in mitochondrial adenine nucleotide transport. In its GDP bound form, Arl2 interacts with tubulin- folding Cofactor D; this interaction is believed to play a role in regulation of microtubule dynamics that impact the cytoskeleton, cell division, and cytokinesis.


Pssm-ID: 206720 [Multi-domain]  Cd Length: 173  Bit Score: 57.33  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKISNAkpkighwQFTTLSPTigtvsLGFgqDVFTVadipgIIQGASL---DKGmGLEFLR-----H 415
Cdd:cd04154   19 MLGLDNAGKTTILKKFNGE-------DISTISPT-----LGF--NIKTL-----EYNGYKLniwDVG-GQKSLRsywrnY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 416 IERSNGWVFVLDLSNKNPLND----LQLLIEEvgtlEKVKTKNILIVCNKVDID-AEKSESFAKYLQVEKFsKSQEWDCV 490
Cdd:cd04154   79 FESTDALIWVVDSSDRARLEDckreLQKLLVE----ERLAGATLLIFANKQDLPgALSPEEIREVLELDSI-KSHHWRIF 153
                        170
                 ....*....|.
gi 330443587 491 PISALREENID 501
Cdd:cd04154  154 GCSAVTGENLL 164
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
343-500 2.02e-09

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: 58.62  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 343 GLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLgfgQD------------------VFTVADIPGIIQGASL 404
Cdd:cd01900    2 GIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPV---PDerldklaeivkpkkivpaTIEFVDIAGLVKGASK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 405 DKGMGLEFLRHIERSNGWVFVL------DLS----NKNPLNDLQL----LI--------------------------EEV 444
Cdd:cd01900   79 GEGLGNKFLSHIREVDAIAHVVrcfeddDIThvegSVDPVRDIEIinteLIladletiekrlerlekkaksgdkeakEEL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 445 GTLEKVK-----------------------------TKNILIVCNkVDiDAEKSESFAKYLQVEKFSKSQEWDCVPISAL 495
Cdd:cd01900  159 ELLEKIKehleegkpartleltdeeikilkslqlltAKPVIYVAN-VS-EDDLIRGNNKVLKVREIAAKEGAEVIPISAK 236

                 ....*
gi 330443587 496 REENI 500
Cdd:cd01900  237 LEAEL 241
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
344-501 2.18e-09

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 56.46  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  344 LIGLPNAGKSTILNK-----ISNAKPKIGhwqFTTLSPTIGTVSlgfgqdvFTVADIPGIIQGASLDKgmgleflRHIER 418
Cdd:pfam00025   5 ILGLDNAGKTTILYKlklgeIVTTIPTIG---FNVETVTYKNVK-------FTVWDVGGQESLRPLWR-------NYFPN 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  419 SNGWVFVLDLSNKNPLND----LQLLIEEvgtlEKVKTKNILIVCNKVDIDAEKSESFAKYLQVEKFSKSQEWDCVPISA 494
Cdd:pfam00025  68 TDAVIFVVDSADRDRIEEakeeLHALLNE----EELADAPLLILANKQDLPGAMSEAEIRELLGLHELKDRPWEIQGCSA 143

                  ....*..
gi 330443587  495 LREENID 501
Cdd:pfam00025 144 VTGEGLD 150
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
342-510 2.58e-09

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: 56.29  E-value: 2.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 342 LGLIGLPNAGKSTILNKISNAKPKIghwqfttLSPTIGT------VSLGFGQDVFTVADIPGIIQGASLDKgmGLEF--- 412
Cdd:cd01895    5 IAIIGRPNVGKSSLLNALLGEERVI-------VSDIAGTtrdsidVPFEYDGQKYTLIDTAGIRKKGKVTE--GIEKysv 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 413 ---LRHIERSNGWVFVLDLSNKNPLNDLQL--LIEEVGtlekvktKNILIVCNKVDIDAEKSESFAKYLQV--EKFSKSQ 485
Cdd:cd01895   76 lrtLKAIERADVVLLVLDASEGITEQDLRIagLILEEG-------KALIIVVNKWDLVEKDEKTMKEFEKElrRKLPFLD 148
                        170       180
                 ....*....|....*....|....*
gi 330443587 486 EWDCVPISALREENIDVLKKKMFKC 510
Cdd:cd01895  149 YAPIVFISALTGQGVDKLFDAIKEV 173
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
345-501 4.52e-09

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: 55.51  E-value: 4.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 345 IGLPNAGKSTILNKISNAKPkighwQFTTLSPTIGTVSLGF--GQDVFTVADIPGIIQGASLdkgmgleFLRHIERSNGW 422
Cdd:cd04157    5 LGLDNSGKTTIINQLKPSNA-----QSQNIVPTVGFNVESFkkGNLSFTAFDMSGQGKYRGL-------WEHYYKNIQGI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 423 VFVLDLSNKNPL----NDLQLLIEEVGTleKVKTKNILIVCNKVDI-DAEKSESFAKYLQVEKFsKSQEWDCVPISALRE 497
Cdd:cd04157   73 IFVIDSSDRLRMvvakDELELLLNHPDI--KHRRIPILFYANKMDLpDALTAVKITQLLCLENI-KDKPWHIFASSALTG 149

                 ....
gi 330443587 498 ENID 501
Cdd:cd04157  150 EGLD 153
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
344-501 5.43e-09

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: 55.11  E-value: 5.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKISnakpkigHWQFTTLSPTIGtvslgfgqdvFTVA--DIPGIIQGASLDKGmGLEFLR-----HI 416
Cdd:cd04156    4 LLGLDSAGKSTLLYKLK-------HAELVTTIPTVG----------FNVEmlQLEKHLSLTVWDVG-GQEKMRtvwkcYL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 417 ERSNGWVFVLDLSNKNPLNDLQLLIEEVGTLEKVKTKNILIVCNKVDI-DAEKSESFAKYLQVEKFSKSQEWDCVPISAL 495
Cdd:cd04156   66 ENTDGLVYVVDSSDEARLDESQKELKHILKNEHIKGVPVVLLANKQDLpGALTAEEITRRFKLKKYCSDRDWYVQPCSAV 145

                 ....*.
gi 330443587 496 REENID 501
Cdd:cd04156  146 TGEGLA 151
PTZ00258 PTZ00258
GTP-binding protein; Provisional
342-497 6.67e-09

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 57.65  E-value: 6.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 342 LGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLG----------FG-----QDVFTVADIPGIIQGASLDK 406
Cdd:PTZ00258  24 MGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPderfdwlckhFKpksivPAQLDITDIAGLVKGASEGE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 407 GMGLEFLRHIERSNGWVFVL------DLS----NKNPLNDLQ-----LLIEEVGTLEKVKTKNILIVCNKVDIDAEKSE- 470
Cdd:PTZ00258 104 GLGNAFLSHIRAVDGIYHVVrafedeDIThvegEIDPVRDLEiisseLILKDLEFVEKRLDELTKKRKKKKKKKEEKVEl 183
                        170       180       190
                 ....*....|....*....|....*....|.
gi 330443587 471 ----SFAKYLQVEKFSKSQEWDCVPISALRE 497
Cdd:PTZ00258 184 dvlkKVLEWLEEGKPVRDGDWTDKEIEILNE 214
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
342-416 9.22e-09

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 57.34  E-value: 9.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 342 LGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVS-----LGFGQDVF--------TV--ADIPGIIQGASLDK 406
Cdd:COG0012    3 CGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPvpderLDKLAEIVkpkkivpaTIefVDIAGLVKGASKGE 82
                         90
                 ....*....|
gi 330443587 407 GMGLEFLRHI 416
Cdd:COG0012   83 GLGNQFLANI 92
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
344-515 2.73e-08

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 56.28  E-value: 2.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGfGQDVfTVADIPGI--IQGASLDKGMGLEFLRHiERSNG 421
Cdd:COG0370    8 LVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLK-GKEI-ELVDLPGTysLSAYSPDEKVARDFLLE-EKPDV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 422 WVFVLDLSN--KNplndLQLLIE--EVGtlekvktKNILIVCNKVD--------IDAEKsesFAKYLQVEkfsksqewdC 489
Cdd:COG0370   85 VVNVVDATNleRN----LYLTLQllELG-------IPVVLALNMMDeaekkgikIDVEK---LSKLLGVP---------V 141
                        170       180
                 ....*....|....*....|....*.
gi 330443587 490 VPISALREENIDVLKKKMFKCARQSE 515
Cdd:COG0370  142 VPTSARKGKGIDELKEAIIEAAEGKK 167
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
344-507 5.28e-08

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 55.09  E-value: 5.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKISNA----KPKIghwqFTTLSPTIGTVSLGFGQDVfTVADIPGIIQ------------------G 401
Cdd:COG2262  204 LVGYTNAGKSTLFNRLTGAdvlaEDKL----FATLDPTTRRLELPDGRPV-LLTDTVGFIRklphqlveafrstleevrE 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 402 ASLdkgmglefLRHiersngwvfVLDLSNKNP---LNDLQLLIEEVGtlekVKTKNILIVCNKVD-IDAEKSESFAKYLQ 477
Cdd:COG2262  279 ADL--------LLH---------VVDASDPDFeeqIETVNEVLEELG----ADDKPIILVFNKIDlLDDEELERLRAGYP 337
                        170       180       190
                 ....*....|....*....|....*....|
gi 330443587 478 vekfsksqewDCVPISALREENIDVLKKKM 507
Cdd:COG2262  338 ----------DAVFISAKTGEGIDELLEAI 357
PRK09602 PRK09602
translation-associated GTPase; Reviewed
342-444 9.61e-08

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 54.04  E-value: 9.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 342 LGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIG-----------------TVSLGFGQD------VfTVADIPGI 398
Cdd:PRK09602   4 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGvayvrvecpckelgvkcNPRNGKCIDgtrfipV-ELIDVAGL 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 330443587 399 IQGASLDKGMGLEFLRHIERSNGWVFVLDLSNK-------------NPLNDLQLLIEEV 444
Cdd:PRK09602  83 VPGAHEGRGLGNQFLDDLRQADALIHVVDASGStdeegnpvepgshDPVEDIKFLEEEL 141
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
343-507 1.18e-07

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


Pssm-ID: 274455 [Multi-domain]  Cd Length: 351  Bit Score: 53.63  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  343 GLIGLPNAGKSTILNKISNA----KPKIghwqFTTLSPTIGTVSLGFGQDVfTVADIPGIIQG----------ASLDKGM 408
Cdd:TIGR03156 193 ALVGYTNAGKSTLFNALTGAdvyaADQL----FATLDPTTRRLDLPDGGEV-LLTDTVGFIRDlphelvaafrATLEEVR 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587  409 GLEFLRHiersngwvfVLDLSNKNPLN---DLQLLIEEVGtlekVKTKNILIVCNKVDidaEKSESFAKYLQvekfskSQ 485
Cdd:TIGR03156 268 EADLLLH---------VVDASDPDREEqieAVEKVLEELG----AEDIPQLLVYNKID---LLDEPRIERLE------EG 325
                         170       180
                  ....*....|....*....|..
gi 330443587  486 EWDCVPISALREENIDVLKKKM 507
Cdd:TIGR03156 326 YPEAVFVSAKTGEGLDLLLEAI 347
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
344-509 1.08e-06

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: 48.61  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKISNAKpkighwqFT-TLSPTIGtvsLGFGQDVFTVADIPGIIQgasL-DKGmGLEFLRHIERS-- 419
Cdd:cd00154    5 LIGDSGVGKTSLLLRFVDNK-------FSeNYKSTIG---VDFKSKTIEVDGKKVKLQ---IwDTA-GQERFRSITSSyy 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 420 ---NGWVFVLDLSNKNPLNDLQLLIEEVgtlEKVKTKN--ILIVCNKVDIDAEKSESFAkylQVEKFSKSQEWDCVPISA 494
Cdd:cd00154   71 rgaHGAILVYDVTNRESFENLDKWLNEL---KEYAPPNipIILVGNKSDLEDERQVSTE---EAQQFAKENGLLFFETSA 144
                        170
                 ....*....|....*
gi 330443587 495 LREENIDVLKKKMFK 509
Cdd:cd00154  145 KTGENVDEAFESLAR 159
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
340-475 2.99e-06

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: 47.62  E-value: 2.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587   340 ADLGLIGLPNAGKSTILNKISNAKpkighwqFTTLSPTIGTVS--LGFGQDVFTVADIPGIIQGASLDKGmgleflrHIE 417
Cdd:smart00178  18 AKILFLGLDNAGKTTLLHMLKNDR-------LAQHQPTQHPTSeeLAIGNIKFTTFDLGGHQQARRLWKD-------YFP 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 330443587   418 RSNGWVFVLDLSNKNPLNDLQLLIEEVGTLEKVKTKNILIVCNKVDIDAEKSESFAKY 475
Cdd:smart00178  84 EVNGIVYLVDAYDKERFAESKRELDALLSDEELATVPFLILGNKIDAPYAASEDELRY 141
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
441-503 5.49e-06

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 47.26  E-value: 5.49e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330443587 441 IEEVGTLEKVKTKNILIVCNKVDIdAEKSESFAKYLQVEKFSKSQEWD---CVPISALREENIDVL 503
Cdd:cd01888  120 SEHLAALEIMGLKHIIILQNKIDL-VKEEQALENYEQIKEFVKGTIAEnapIIPISAQLKYNIDVL 184
Arl2l1_Arl13_like cd04161
Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a ...
342-497 7.27e-06

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: 46.23  E-value: 7.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 342 LGLIGLPNAGKSTILNKISNAKPKighwqftTLSPTIGTVSLGFGQDVFTVAdipgiiqgaSLDKGMGLEF----LRHIE 417
Cdd:cd04161    2 LLTVGLDNAGKTTLVSALQGEIPK-------KVAPTVGFTPTKLRLDKYEVC---------IFDLGGGANFrgiwVNYYA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 418 RSNGWVFVLDLSNKNPLNDLQLLIEEVGTLEKVKTKNILIVCNKVDI-DAEKSESFAKYLQVEKFSKSQEWDCV--PISA 494
Cdd:cd04161   66 EAHGLVFVVDSSDDDRVQEVKEILRELLQHPRVSGKPILVLANKQDKkNALLGADVIEYLSLEKLVNENKSLCHiePCSA 145

                 ...
gi 330443587 495 LRE 497
Cdd:cd04161  146 IEG 148
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
342-505 1.13e-05

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 48.17  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 342 LGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGFGQdvFTVADIPG------IIQGASLDKGMGLEFLRH 415
Cdd:PRK09554   6 IGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTDHQ--VTLVDLPGtyslttISSQTSLDEQIACHYILS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 416 IErSNGWVFVLDLSN--KNPLNDLQLLieEVGtlekvktknilIVC----NKVDIdAEKsesfaKYLQVEKFSKSQEWDC 489
Cdd:PRK09554  84 GD-ADLLINVVDASNleRNLYLTLQLL--ELG-----------IPCivalNMLDI-AEK-----QNIRIDIDALSARLGC 143
                        170
                 ....*....|....*...
gi 330443587 490 --VPISALREENIDVLKK 505
Cdd:PRK09554 144 pvIPLVSTRGRGIEALKL 161
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
344-511 2.25e-05

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: 44.81  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKISNAK--PKIGHWQFTTLSPTIGTVSlgfgqDVFTVADIPGIIqGASLDKGMGLEFLRHIE---- 417
Cdd:cd01876    4 FAGRSNVGKSSLINALTNRKklARTSKTPGRTQLINFFNVG-----DKFRLVDLPGYG-YAKVSKEVREKWGKLIEeyle 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 418 -RSN--GWVFVLDLSNKNPLNDLQLL--IEEVGtlekvktKNILIVCNKVD-IDaeKSESFAKYLQVEKFSKSQEWDC-- 489
Cdd:cd01876   78 nRENlkGVVLLIDARHGPTPIDLEMLefLEELG-------IPFLIVLTKADkLK--KSELAKVLKKIKEELNLFNILPpv 148
                        170       180
                 ....*....|....*....|..
gi 330443587 490 VPISALREENIDVLKKKMFKCA 511
Cdd:cd01876  149 ILFSSKKGTGIDELRALIAEWL 170
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
344-501 2.29e-05

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: 45.03  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKI-SNAKPKIGHWQFTTLSPTIGtvslgfgqdvFTVADIPgiIQGASL---DKGmGLEFLRHI--- 416
Cdd:cd04160    4 ILGLDNAGKTTFLEQTkTKFSKNYKGLNPSKITPTVG----------LNIGTIE--VGKARLmfwDLG-GQEELRSLwdk 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 417 --ERSNGWVFVLDLSNKNPLNDLQLLIEEVGTLEKVKTKNILIVCNKVDI-DAEKSESFAKYLQvEKFSKSQEWDC--VP 491
Cdd:cd04160   71 yyAESHGVIYVIDSTDRERFNESKSAFEKVINNEALEGVPLLVLANKQDLpDALSVAEIKEVFD-DCIALIGRRDClvQP 149
                        170
                 ....*....|
gi 330443587 492 ISALREENID 501
Cdd:cd04160  150 VSALEGEGVE 159
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
332-471 3.28e-05

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: 44.96  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 332 FLFELKSIADLGLIGLPNAGKSTILNKISNAKPKIgH---WQFTTLSPTIGTVSlgfgqdvFTVADIPGIIQGASLDKgm 408
Cdd:cd00879   12 SLGLYKKEAKIVFLGLDNAGKTTLLHMLKDDRLAQ-HvptLHPTSEELTIGNVK-------FTTFDLGGHEQARRVWK-- 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443587 409 gleflRHIERSNGWVFVLDLSNKNPLNDLQLLIEEVGTLEKVKTKNILIVCNKVDIDAEKSES 471
Cdd:cd00879   82 -----DYFPEVDGIVFLVDAADPERFQESKEELDSLLNDEELANVPILILGNKIDKPGAVSEE 139
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
344-474 3.54e-05

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 45.00  E-value: 3.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKISNAKPKIGHwqfTTLSPTIGTVSLGFGQDV-FTVADIPGiiqGASLdKGMGLEFLRHIERsnGW 422
Cdd:cd04105    5 LLGPSDSGKTALFTKLTTGKVRSTV---TSIEPNVASFYSNSSKGKkLTLVDVPG---HEKL-RDKLLEYLKASLK--AI 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 330443587 423 VFVLDLS--NKNpLNDLQLLIEEVGT-LEKVKTK-NILIVCNKVDIDAEKSESFAK 474
Cdd:cd04105   76 VFVVDSAtfQKN-IRDVAEFLYDILTdLEKIKNKiPILIACNKQDLFTAKPAKKIK 130
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
456-509 1.55e-04

C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of the MMR_HSR1 family.


Pssm-ID: 465301 [Multi-domain]  Cd Length: 105  Bit Score: 40.87  E-value: 1.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 330443587  456 LIVCNKVD-IDAEKSESFAKylqvekfsksqEWDCVPISALREENIDVLKKKMFK 509
Cdd:pfam16897  58 LYVYNKIDlISIEELDRLAR-----------EPDSVPISAEKGLNLDELKERIWE 101
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
447-503 1.78e-04

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 44.07  E-value: 1.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330443587 447 LEKVKTKNILIVCNKVDIdAEKSESFAKYLQVEKFSKSqEWD----CVPISALREENIDVL 503
Cdd:PRK04000 134 LDIIGIKNIVIVQNKIDL-VSKERALENYEQIKEFVKG-TVAenapIIPVSALHKVNIDAL 192
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
344-464 2.57e-04

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 42.14  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKIsnakpKIGhwQFTTLSPTIG--TVSLGFGQDVFTVADIPGiiqgasLDKGMGLefLRH-IERSN 420
Cdd:PTZ00133  22 MVGLDAAGKTTILYKL-----KLG--EVVTTIPTIGfnVETVEYKNLKFTMWDVGG------QDKLRPL--WRHyYQNTN 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 330443587 421 GWVFVLDLSNKNPLNDLQLLIEEVGTLEKVKTKNILIVCNKVDI 464
Cdd:PTZ00133  87 GLIFVVDSNDRERIGDAREELERMLSEDELRDAVLLVFANKQDL 130
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
415-510 4.54e-04

Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206642 [Multi-domain]  Cd Length: 160  Bit Score: 40.97  E-value: 4.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 415 HIERSNGWVFVLDLSNKNPLNDLQLLIEEvgtLEKVKTKN---ILIVCNKVDIDAEKSESfakYLQVEKFSKsqEWDC-- 489
Cdd:cd00876   67 YIRNGDGFILVYSITSRESFEEIKNIREQ---ILRVKDKEdvpIVLVGNKCDLENERQVS---TEEGEALAE--EWGCpf 138
                         90       100
                 ....*....|....*....|.
gi 330443587 490 VPISALREENIDvlkkKMFKC 510
Cdd:cd00876  139 LETSAKTNINID----ELFNT 155
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
349-518 8.71e-04

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


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 40.22  E-value: 8.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 349 NAGKSTILNKISNAK--P-KIGHwqfTTLSPTIgtVSLGFGQDVfTVADIPGIiqgASLDKGMGLEFLRHIERSNGWVFV 425
Cdd:cd09912   10 SAGKSTLLNALLGEEvlPtGVTP---TTAVITV--LRYGLLKGV-VLVDTPGL---NSTIEHHTEITESFLPRADAVIFV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 426 LDLSNknplndlQLLIEEVGTLEKVK---TKNILIVCNKVDI--DAEKSESFAKYLQVEKFSKSQEWDCV--PISAlREE 498
Cdd:cd09912   81 LSADQ-------PLTESEREFLKEILkwsGKKIFFVLNKIDLlsEEELEEVLEYSREELGVLELGGGEPRifPVSA-KEA 152
                        170       180
                 ....*....|....*....|
gi 330443587 499 NIDVLKKKmFKCARQSEFDK 518
Cdd:cd09912  153 LEARLQGD-EELLEQSGFEE 171
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
344-501 1.02e-03

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: 40.07  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKISNAkpkighwQFTTLSPTIG-----TVSLGFGqdvFTVADIPGiiQGASldkgmgLEFLRH-IE 417
Cdd:cd04155   20 LLGLDNAGKTTILKQLASE-------DISHITPTQGfniknVQADGFK---LNVWDIGG--QRKI------RPYWRNyFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 418 RSNGWVFVLDLSNKNPLNDLQLLIEEVGTLEKVKTKNILIVCNKVDI-DAEKSESFAKYLQVEKFsKSQEWDCVPISALR 496
Cdd:cd04155   82 NTDVLIYVIDSADRKRFEEAGQELVELLEEEKLAGVPVLVFANKQDLlTAAPAEEVAEALNLHDI-RDRSWHIQACSAKT 160

                 ....*
gi 330443587 497 EENID 501
Cdd:cd04155  161 GEGLQ 165
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
344-495 1.20e-03

ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins localize to the plasma membrane, where they perform a wide variety of functions. In its active, GTP-bound form, Arf6 is involved in cell spreading, Rac-induced formation of plasma membrane ruffles, cell migration, wound healing, and Fc-mediated phagocytosis. Arf6 appears to change the actin structure at the plasma membrane by activating Rac, a Rho family protein involved in membrane ruffling. Arf6 is required for and enhances Rac formation of ruffles. Arf6 can regulate dendritic branching in hippocampal neurons, and in yeast it localizes to the growing bud, where it plays a role in polarized growth and bud site selection. In leukocytes, Arf6 is required for chemokine-stimulated migration across endothelial cells. Arf6 also plays a role in down-regulation of beta2-adrenergic receptors and luteinizing hormone receptors by facilitating the release of sequestered arrestin to allow endocytosis. Arf6 is believed to function at multiple sites on the plasma membrane through interaction with a specific set of GEFs, GAPs, and effectors. Arf6 has been implicated in breast cancer and melanoma cell invasion, and in actin remodelling at the invasion site of Chlamydia infection.


Pssm-ID: 206716  Cd Length: 168  Bit Score: 39.76  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKIsnakpKIGhwQFTTLSPTIG----TVSLgfgQDV-FTVADIPGiiqgasLDKGMGLefLRH-IE 417
Cdd:cd04149   14 MLGLDAAGKTTILYKL-----KLG--QSVTTIPTVGfnveTVTY---KNVkFNVWDVGG------QDKIRPL--WRHyYT 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330443587 418 RSNGWVFVLDLSNKNPLNDLQLLIEEVGTLEKVKTKNILIVCNKVDI-DAEKSESFAKYLQVEKfSKSQEWDCVPISAL 495
Cdd:cd04149   76 GTQGLIFVVDSADRDRIDEARQELHRIINDREMRDALLLVFANKQDLpDAMKPHEIQEKLGLTR-IRDRNWYVQPSCAT 153
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
344-464 1.33e-03

ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular transport. Activator 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. Contains ATP/GTP-binding motif (P-loop).


Pssm-ID: 128474 [Multi-domain]  Cd Length: 175  Bit Score: 39.90  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587   344 LIGLPNAGKSTILNKIsnakpKIGhwQFTTLSPTIG----TVSlgFGQDVFTVADIPGiiqgasLDKGMGLefLRHIER- 418
Cdd:smart00177  18 MVGLDAAGKTTILYKL-----KLG--ESVTTIPTIGfnveTVT--YKNISFTVWDVGG------QDKIRPL--WRHYYTn 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 330443587   419 SNGWVFVLDLSNKNPLNDLQLLIEEVGTLEKVKTKNILIVCNKVDI 464
Cdd:smart00177  81 TQGLIFVVDSNDRDRIDEAREELHRMLNEDELRDAVILVFANKQDL 126
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
442-503 3.43e-03

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 39.99  E-value: 3.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330443587 442 EEVGTLEKVKTKNILIVCNKVDIdAEKSESFAKYLQVEKFSKSQEWD---CVPISALREENIDVL 503
Cdd:PTZ00327 161 EHLAAVEIMKLKHIIILQNKIDL-VKEAQAQDQYEEIRNFVKGTIADnapIIPISAQLKYNIDVV 224
Arf1_5_like cd04150
ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like ...
344-464 4.25e-03

ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like subfamily contains Arf1, Arf2, Arf3, Arf4, Arf5, and related proteins. Arfs1-5 are soluble proteins that are crucial for assembling coat proteins during vesicle formation. Each contains an N-terminal myristoylated amphipathic helix that is folded into the protein in the GDP-bound state. GDP/GTP exchange exposes the helix, which anchors to the membrane. Following GTP hydrolysis, the helix dissociates from the membrane and folds back into the protein. A general feature of Arf1-5 signaling may be the cooperation of two Arfs at the same site. Arfs1-5 are generally considered to be interchangeable in function and location, but some specific functions have been assigned. Arf1 localizes to the early/cis-Golgi, where it is activated by GBF1 and recruits the coat protein COPI. It also localizes to the trans-Golgi network (TGN), where it is activated by BIG1/BIG2 and recruits the AP1, AP3, AP4, and GGA proteins. Humans, but not rodents and other lower eukaryotes, lack Arf2. Human Arf3 shares 96% sequence identity with Arf1 and is believed to generally function interchangeably with Arf1. Human Arf4 in the activated (GTP-bound) state has been shown to interact with the cytoplasmic domain of epidermal growth factor receptor (EGFR) and mediate the EGF-dependent activation of phospholipase D2 (PLD2), leading to activation of the activator protein 1 (AP-1) transcription factor. Arf4 has also been shown to recognize the C-terminal sorting signal of rhodopsin and regulate its incorporation into specialized post-Golgi rhodopsin transport carriers (RTCs). There is some evidence that Arf5 functions at the early-Golgi and the trans-Golgi to affect Golgi-associated alpha-adaptin homology Arf-binding proteins (GGAs).


Pssm-ID: 206717 [Multi-domain]  Cd Length: 159  Bit Score: 38.16  E-value: 4.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443587 344 LIGLPNAGKSTILNKIsnakpKIGhwQFTTLSPTIG----TVSlgFGQDVFTVADIPGiiqgasLDKGMGLefLRH-IER 418
Cdd:cd04150    5 MVGLDAAGKTTILYKL-----KLG--EIVTTIPTIGfnveTVE--YKNISFTVWDVGG------QDKIRPL--WRHyFQN 67
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 330443587 419 SNGWVFVLDLSNKNPLND----LQLLIEEvgtlEKVKTKNILIVCNKVDI 464
Cdd:cd04150   68 TQGLIFVVDSNDRERIGEareeLQRMLNE----DELRDAVLLVFANKQDL 113
PRK11058 PRK11058
GTPase HflX; Provisional
339-400 4.49e-03

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 39.32  E-value: 4.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330443587 339 IADLGLIGLPNAGKSTILNKISNAKPKIGHWQFTTLSPTIGTVSLGfgqDVFTV--ADIPGIIQ 400
Cdd:PRK11058 197 VPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVA---DVGETvlADTVGFIR 257
 
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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