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Conserved domains on  [gi|1858589270|ref|NP_001371276|]
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mitochondrial ribosome-associated GTPase 2 isoform 1 [Homo sapiens]

Protein Classification

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 ...
90-403 1.69e-109

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: 325.53  E-value: 1.69e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270  90 FVDYRRVLVCGGNGGAGASCFHSEPRKEFGGPDGGDGGNGGHVILRVDQQVKSLSSVlsRYQGF----SGEDGGSKNCFG 165
Cdd:TIGR02729   1 FVDEAKIFVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGSVILEADENLNTLLDF--RYQRHfkaeNGENGMGKNRTG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 166 RSGAVLYIRVPVGTLVK--EGGRVVADLSCVGDEYIAALGGAGGKGNRFFLANNNRAPVTCTPGQPGQQRVLHLELKTVA 243
Cdd:TIGR02729  79 KSGEDLVIKVPVGTVVYdaDTGELLADLTEPGQRFLVAKGGRGGLGNAHFKSSTNRAPRFATPGEPGEERWLRLELKLLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 244 HAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRF 323
Cdd:TIGR02729 159 DVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 324 LLFVVDLSQPEPWTQVDDLKY---ELEMYEKGLSARPHAIVANKIDLP---EAQANLSQLRDHLGQEVIVLSALTGENLE 397
Cdd:TIGR02729 239 LLHLIDISPEDGSDPVEDYEIirnELKKYSPELAEKPRIVVLNKIDLLdeeELEELLKELKKELGKPVFPISALTGEGLD 318

                  ....*.
gi 1858589270 398 QLLLHL 403
Cdd:TIGR02729 319 ELLDAL 324
 
Name Accession Description Interval E-value
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
90-403 1.69e-109

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: 325.53  E-value: 1.69e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270  90 FVDYRRVLVCGGNGGAGASCFHSEPRKEFGGPDGGDGGNGGHVILRVDQQVKSLSSVlsRYQGF----SGEDGGSKNCFG 165
Cdd:TIGR02729   1 FVDEAKIFVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGSVILEADENLNTLLDF--RYQRHfkaeNGENGMGKNRTG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 166 RSGAVLYIRVPVGTLVK--EGGRVVADLSCVGDEYIAALGGAGGKGNRFFLANNNRAPVTCTPGQPGQQRVLHLELKTVA 243
Cdd:TIGR02729  79 KSGEDLVIKVPVGTVVYdaDTGELLADLTEPGQRFLVAKGGRGGLGNAHFKSSTNRAPRFATPGEPGEERWLRLELKLLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 244 HAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRF 323
Cdd:TIGR02729 159 DVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 324 LLFVVDLSQPEPWTQVDDLKY---ELEMYEKGLSARPHAIVANKIDLP---EAQANLSQLRDHLGQEVIVLSALTGENLE 397
Cdd:TIGR02729 239 LLHLIDISPEDGSDPVEDYEIirnELKKYSPELAEKPRIVVLNKIDLLdeeELEELLKELKKELGKPVFPISALTGEGLD 318

                  ....*.
gi 1858589270 398 QLLLHL 403
Cdd:TIGR02729 319 ELLDAL 324
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
90-414 1.72e-109

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: 325.78  E-value: 1.72e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270  90 FVDYRRVLVCGGNGGAGASCFHSEPRKEFggpdggdggnggHVILRVDQQVKSLSSVlsRYQGF----SGEDGGSKNCFG 165
Cdd:COG0536     1 FVDEAKIYVKAGDGGNGCVSFRREKYVPKggpdggdggrggDVILVADENLNTLLDF--RYKRHfkaeNGENGMGKNRTG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 166 RSGAVLYIRVPVGTLVK--EGGRVVADLSCVGDEYIaalggaggkgNRFFLANNNRAPVTCTPGQPGQQRVLHLELKTVA 243
Cdd:COG0536    79 KNGEDLVIKVPVGTVVKdaETGEVLADLTEDGQRVVvakggrgglgNAHFKSSTNRAPRFAEPGEPGEERWLRLELKLLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 244 HAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRF 323
Cdd:COG0536   159 DVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRSFVIADIPGLIEGASEGAGLGHRFLRHIERTRV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 324 LLFVVDLSQPE---PWTQVDDLKYELEMYEKGLSARPHAIVANKIDLPEAQ--ANLSQLRDHLGQEVIVLSALTGENLEQ 398
Cdd:COG0536   239 LLHVVDAAPLDgrdPVEDYEIIRNELEAYSPELAEKPRIVVLNKIDLLDAEelEELKAELEKLGGPVFPISAVTGEGLDE 318
                         330
                  ....*....|....*.
gi 1858589270 399 LLLHLKVLYDAYAEAE 414
Cdd:COG0536   319 LLYALAELLEELRAEE 334
obgE PRK12297
GTPase CgtA; Reviewed
90-415 4.98e-105

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 317.43  E-value: 4.98e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270  90 FVDYRRVLVCGGNGGAGASCFHSE---PR---------KefggpdggdggnGGHVILRVDQQVKSLSSVlsRYQGF---- 153
Cdd:PRK12297    2 FIDQAKIYVKAGDGGDGMVSFRREkyvPKggpdggdggK------------GGSVIFVADEGLRTLLDF--RYKRHfkae 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 154 SGEDGGSKNCFGRSGAVLYIRVPVGTLVK--EGGRVVADLSCVGDEYIAALGGAGGKGNRFFLANNNRAPVTCTPGQPGQ 231
Cdd:PRK12297   68 NGENGMGKNMHGRNGEDLIIKVPVGTVVKdaETGEVIADLVEPGQEVVVAKGGRGGRGNAHFATSTNQAPRIAENGEPGE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 232 QRVLHLELKTVAHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLG 311
Cdd:PRK12297  148 ERELRLELKLLADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRSFVMADIPGLIEGASEGVGLG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 312 SAFLRHIERCRFLLFVVDLSQPE---PWTQVDDLKYELEMYEKGLSARPHAIVANKIDLPEAQANLSQLRDHLGQEVIVL 388
Cdd:PRK12297  228 HQFLRHIERTRVIVHVIDMSGSEgrdPIEDYEKINKELKLYNPRLLERPQIVVANKMDLPEAEENLEEFKEKLGPKVFPI 307
                         330       340
                  ....*....|....*....|....*..
gi 1858589270 389 SALTGENLEQLLLHLKVLYDAYAEAEL 415
Cdd:PRK12297  308 SALTGQGLDELLYAVAELLEETPEFPL 334
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
243-403 2.26e-84

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: 255.43  E-value: 2.26e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 243 AHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCR 322
Cdd:cd01898     1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 323 FLLFVVDLSQPE-PWTQVDDLKYELEMYEKGLSARPHAIVANKIDLPEAQANLSQLRDHL----GQEVIVLSALTGENLE 397
Cdd:cd01898    81 VLLHVIDLSGEDdPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELLkelkGKKVFPISALTGEGLD 160

                  ....*.
gi 1858589270 398 QLLLHL 403
Cdd:cd01898   161 ELLKKL 166
GTP1_OBG pfam01018
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ...
91-241 1.08e-32

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: 120.53  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270  91 VDYRRVLVCGGNGGAGASCFHSEPRKEFGGPDGGDGGNGGHVILRVDQQVKSLSSVLSR--YQGFSGEDGGSKNCFGRSG 168
Cdd:pfam01018   1 VDRAKIKVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGDVILVADENLNTLLDFRYKrhFKAENGENGGGKNCHGKNG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1858589270 169 AVLYIRVPVGTLVK--EGGRVVADLSCVGDEYIAALGGAGGKGNRFFLANNNRAPVTCTPGQPGQQRVLHLELKT 241
Cdd:pfam01018  81 EDLIIKVPVGTVVKdaETGEVLADLTEPGQRVLVAKGGRGGRGNAHFKTSTNQAPRFAEPGEPGEERWLELELKL 155
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
244-382 2.15e-04

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: 41.84  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270  244 HAGMV--GFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIvhyeGHLQIAVADIpgiirGAHQN-RGLGSAFLRHIER 320
Cdd:smart00178  17 HAKILflGLDNAGKTTLLHMLKNDRLAQHQPTQHPTSEELAI----GNIKFTTFDL-----GGHQQaRRLWKDYFPEVNG 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1858589270  321 crfLLFVVDLSQPEpwtQVDDLKYELE--MYEKGLSARPHAIVANKIDLPEAqANLSQLRDHLG 382
Cdd:smart00178  88 ---IVYLVDAYDKE---RFAESKRELDalLSDEELATVPFLILGNKIDAPYA-ASEDELRYALG 144
 
Name Accession Description Interval E-value
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
90-403 1.69e-109

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: 325.53  E-value: 1.69e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270  90 FVDYRRVLVCGGNGGAGASCFHSEPRKEFGGPDGGDGGNGGHVILRVDQQVKSLSSVlsRYQGF----SGEDGGSKNCFG 165
Cdd:TIGR02729   1 FVDEAKIFVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGSVILEADENLNTLLDF--RYQRHfkaeNGENGMGKNRTG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 166 RSGAVLYIRVPVGTLVK--EGGRVVADLSCVGDEYIAALGGAGGKGNRFFLANNNRAPVTCTPGQPGQQRVLHLELKTVA 243
Cdd:TIGR02729  79 KSGEDLVIKVPVGTVVYdaDTGELLADLTEPGQRFLVAKGGRGGLGNAHFKSSTNRAPRFATPGEPGEERWLRLELKLLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 244 HAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRF 323
Cdd:TIGR02729 159 DVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 324 LLFVVDLSQPEPWTQVDDLKY---ELEMYEKGLSARPHAIVANKIDLP---EAQANLSQLRDHLGQEVIVLSALTGENLE 397
Cdd:TIGR02729 239 LLHLIDISPEDGSDPVEDYEIirnELKKYSPELAEKPRIVVLNKIDLLdeeELEELLKELKKELGKPVFPISALTGEGLD 318

                  ....*.
gi 1858589270 398 QLLLHL 403
Cdd:TIGR02729 319 ELLDAL 324
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
90-414 1.72e-109

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: 325.78  E-value: 1.72e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270  90 FVDYRRVLVCGGNGGAGASCFHSEPRKEFggpdggdggnggHVILRVDQQVKSLSSVlsRYQGF----SGEDGGSKNCFG 165
Cdd:COG0536     1 FVDEAKIYVKAGDGGNGCVSFRREKYVPKggpdggdggrggDVILVADENLNTLLDF--RYKRHfkaeNGENGMGKNRTG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 166 RSGAVLYIRVPVGTLVK--EGGRVVADLSCVGDEYIaalggaggkgNRFFLANNNRAPVTCTPGQPGQQRVLHLELKTVA 243
Cdd:COG0536    79 KNGEDLVIKVPVGTVVKdaETGEVLADLTEDGQRVVvakggrgglgNAHFKSSTNRAPRFAEPGEPGEERWLRLELKLLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 244 HAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRF 323
Cdd:COG0536   159 DVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRSFVIADIPGLIEGASEGAGLGHRFLRHIERTRV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 324 LLFVVDLSQPE---PWTQVDDLKYELEMYEKGLSARPHAIVANKIDLPEAQ--ANLSQLRDHLGQEVIVLSALTGENLEQ 398
Cdd:COG0536   239 LLHVVDAAPLDgrdPVEDYEIIRNELEAYSPELAEKPRIVVLNKIDLLDAEelEELKAELEKLGGPVFPISAVTGEGLDE 318
                         330
                  ....*....|....*.
gi 1858589270 399 LLLHLKVLYDAYAEAE 414
Cdd:COG0536   319 LLYALAELLEELRAEE 334
obgE PRK12297
GTPase CgtA; Reviewed
90-415 4.98e-105

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 317.43  E-value: 4.98e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270  90 FVDYRRVLVCGGNGGAGASCFHSE---PR---------KefggpdggdggnGGHVILRVDQQVKSLSSVlsRYQGF---- 153
Cdd:PRK12297    2 FIDQAKIYVKAGDGGDGMVSFRREkyvPKggpdggdggK------------GGSVIFVADEGLRTLLDF--RYKRHfkae 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 154 SGEDGGSKNCFGRSGAVLYIRVPVGTLVK--EGGRVVADLSCVGDEYIAALGGAGGKGNRFFLANNNRAPVTCTPGQPGQ 231
Cdd:PRK12297   68 NGENGMGKNMHGRNGEDLIIKVPVGTVVKdaETGEVIADLVEPGQEVVVAKGGRGGRGNAHFATSTNQAPRIAENGEPGE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 232 QRVLHLELKTVAHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLG 311
Cdd:PRK12297  148 ERELRLELKLLADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRSFVMADIPGLIEGASEGVGLG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 312 SAFLRHIERCRFLLFVVDLSQPE---PWTQVDDLKYELEMYEKGLSARPHAIVANKIDLPEAQANLSQLRDHLGQEVIVL 388
Cdd:PRK12297  228 HQFLRHIERTRVIVHVIDMSGSEgrdPIEDYEKINKELKLYNPRLLERPQIVVANKMDLPEAEENLEEFKEKLGPKVFPI 307
                         330       340
                  ....*....|....*....|....*..
gi 1858589270 389 SALTGENLEQLLLHLKVLYDAYAEAEL 415
Cdd:PRK12297  308 SALTGQGLDELLYAVAELLEETPEFPL 334
obgE PRK12299
GTPase CgtA; Reviewed
90-400 8.18e-105

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 313.55  E-value: 8.18e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270  90 FVDYRRVLVCGGNGGAGASCFHSEPRKEFggpdggdggnggHVILRVDQQVKSLSSVlsRYQGF----SGEDGGSKNCFG 165
Cdd:PRK12299    2 FIDEAKIYVKAGDGGNGCVSFRREKFIPFggpdggdggrggSVILEADENLNTLIDF--RYKRHfkaeNGENGMGRNRTG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 166 RSGAVLYIRVPVGTLVK--EGGRVVADLSCVGDEYIAALGGAGGKGNRFFLANNNRAPVTCTPGQPGQQRVLHLELKTVA 243
Cdd:PRK12299   80 KSGKDLVLKVPVGTQIYdaDTGELIADLTEHGQRFLVAKGGKGGLGNAHFKSSTNRAPRYATPGEPGEERWLRLELKLLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 244 HAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRF 323
Cdd:PRK12299  160 DVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKSFVIADIPGLIEGASEGAGLGHRFLKHIERTRL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 324 LLFVVDLSQPEPWTQVDDLKYELEMYEKGLSARPHAIVANKIDLP----EAQANLSQLRDHLGQEVIVLSALTGENLEQL 399
Cdd:PRK12299  240 LLHLVDIEAVDPVEDYKTIRNELEKYSPELADKPRILVLNKIDLLdeeeEREKRAALELAALGGPVFLISAVTGEGLDEL 319

                  .
gi 1858589270 400 L 400
Cdd:PRK12299  320 L 320
obgE PRK12298
GTPase CgtA; Reviewed
90-414 1.79e-85

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 265.96  E-value: 1.79e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270  90 FVDYRRVLVCGGNGGAGASCFHSEPRKEFGGPDGGDGGNGGHVILRVDQQVKSLssVLSRYQGF----SGEDGGSKNCFG 165
Cdd:PRK12298    3 FVDEAKIRVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVYLEADENLNTL--IDYRFERHfraeRGQNGQGRDCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 166 RSGAVLYIRVPVGTLVK--EGGRVVADLSCVGDEYIAALGGAGGKGNRFFLANNNRAPVTCTPGQPGQQRVLHLELKTVA 243
Cdd:PRK12298   81 KRGKDITIKVPVGTRVIdaDTGEVIGDLTEHGQRLLVAKGGWHGLGNTRFKSSVNRAPRQKTPGTPGEERELKLELKLLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 244 HAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRF 323
Cdd:PRK12298  161 DVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDERSFVVADIPGLIEGASEGAGLGIRFLKHLERCRV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 324 LLFVVDLS---QPEPWTQVDDLKYELEMYEKGLSARPHAIVANKIDL---PEAQANLSQLRDHLGQE--VIVLSALTGEN 395
Cdd:PRK12298  241 LLHLIDIApidGSDPVENARIIINELEKYSPKLAEKPRWLVFNKIDLldeEEAEERAKAIVEALGWEgpVYLISAASGLG 320
                         330
                  ....*....|....*....
gi 1858589270 396 LEQLLLHLKVLYDAYAEAE 414
Cdd:PRK12298  321 VKELCWDLMTFIEENPREE 339
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
243-403 2.26e-84

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: 255.43  E-value: 2.26e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 243 AHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCR 322
Cdd:cd01898     1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 323 FLLFVVDLSQPE-PWTQVDDLKYELEMYEKGLSARPHAIVANKIDLPEAQANLSQLRDHL----GQEVIVLSALTGENLE 397
Cdd:cd01898    81 VLLHVIDLSGEDdPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELLkelkGKKVFPISALTGEGLD 160

                  ....*.
gi 1858589270 398 QLLLHL 403
Cdd:cd01898   161 ELLKKL 166
obgE PRK12296
GTPase CgtA; Reviewed
90-414 5.80e-70

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 229.37  E-value: 5.80e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270  90 FVDYRRVLVCGGNGGAGASCFHSEPRKEFGGPDGGDGGNGGHVILRVDQQVKSLssVLSRYQGF----SGEDGGSKNCFG 165
Cdd:PRK12296    4 FVDRVVLHVKAGDGGNGCASVHREKFKPLGGPDGGNGGRGGSVVLVVDPQVTTL--LDFHFRPHrkatNGKPGMGDNRDG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 166 RSGAVLYIRVPVGTLVK-EGGRVVADLSCVGDEYIAALGGAGGKGNRFfLANNNR-APVTCTPGQPGQQRVLHLELKTVA 243
Cdd:PRK12296   82 AAGEDLVLPVPDGTVVLdEDGEVLADLVGAGTRFVAAAGGRGGLGNAA-LASKARkAPGFALLGEPGEERDLVLELKSVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 244 HAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYeGHLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRF 323
Cdd:PRK12296  161 DVGLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQA-GDTRFTVADVPGLIPGASEGKGLGLDFLRHIERCAV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 324 LLFVVDLSQPE----PWTQVDDLKYELEMYE---------KGLSARPHAIVANKIDLPEAQANLSQLRDHL---GQEVIV 387
Cdd:PRK12296  240 LVHVVDCATLEpgrdPLSDIDALEAELAAYApaldgdlglGDLAERPRLVVLNKIDVPDARELAEFVRPELearGWPVFE 319
                         330       340
                  ....*....|....*....|....*..
gi 1858589270 388 LSALTGENLEQLLLHLKVLYDAYAEAE 414
Cdd:PRK12296  320 VSAASREGLRELSFALAELVEEARAAE 346
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
246-400 1.59e-39

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: 139.45  E-value: 1.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 246 GMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRFLL 325
Cdd:cd01881     1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 326 FVVDLSQPEPWTQVDDLK---YELEMYEKGLSARPHAIVANKIDLPEAQANLSQLRDHLGQE--VIVLSALTGENLEQLL 400
Cdd:cd01881    81 HVIDASEDCVGDPLEDQKtlnEEVSGSFLFLKNKPEMIVANKIDMASENNLKRLKLDKLKRGipVVPTSALTRLGLDRVI 160
GTP1_OBG pfam01018
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ...
91-241 1.08e-32

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: 120.53  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270  91 VDYRRVLVCGGNGGAGASCFHSEPRKEFGGPDGGDGGNGGHVILRVDQQVKSLSSVLSR--YQGFSGEDGGSKNCFGRSG 168
Cdd:pfam01018   1 VDRAKIKVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGDVILVADENLNTLLDFRYKrhFKAENGENGGGKNCHGKNG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1858589270 169 AVLYIRVPVGTLVK--EGGRVVADLSCVGDEYIAALGGAGGKGNRFFLANNNRAPVTCTPGQPGQQRVLHLELKT 241
Cdd:pfam01018  81 EDLIIKVPVGTVVKdaETGEVLADLTEPGQRVLVAKGGRGGRGNAHFKTSTNQAPRFAEPGEPGEERWLELELKL 155
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
244-364 4.79e-31

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 115.02  E-value: 4.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 244 HAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHlQIAVADIPGIIRGAHQNRGLGSAFLRHIErCRF 323
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGK-QIILVDTPGLIEGASEGEGLGRAFLAIIE-ADL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1858589270 324 LLFVVDLSqpEPWTQVDdlkyeLEMYEKGLSA-RPHAIVANK 364
Cdd:pfam01926  79 ILFVVDSE--EGITPLD-----EELLELLRENkKPIILVLNK 113
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
243-347 1.18e-27

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


Pssm-ID: 206683 [Multi-domain]  Cd Length: 233  Bit Score: 109.56  E-value: 1.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 243 AHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGhLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCR 322
Cdd:cd01896     1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKG-AKIQLLDLPGIIEGASDGKGRGRQVIAVARTAD 79
                          90       100
                  ....*....|....*....|....*
gi 1858589270 323 FLLFVVDLSQPEpwTQVDDLKYELE 347
Cdd:cd01896    80 LILIVLDATKPE--GQREILERELE 102
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
241-399 1.38e-27

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 112.58  E-value: 1.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 241 TVAhagMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGhLQIAVADIPGIIRGAHQNRGLGSAFLRHIER 320
Cdd:COG1163    65 TVV---LVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLEYKG-AKIQILDVPGLIEGAASGKGRGKEVLSVVRN 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 321 CRFLLFVVDLSQPEpwtQVDDLKYELE-----------------------------------------MYEKGL-SAR-- 356
Cdd:COG1163   141 ADLILIVLDVFELE---QYDVLKEELYdagirlnkpppdvtiekkgkggirvnstgkldldeedikkiLREYGIvNADvl 217
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1858589270 357 ---------------------PHAIVANKIDLPEAQaNLSQLRDHLGQ--EVIVLSALTGENLEQL 399
Cdd:COG1163   218 iredvtlddlidalmgnrvykPAIVVVNKIDLADEE-YVEELKSKLPDgvPVIFISAEKGIGLEEL 282
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
246-400 5.22e-24

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: 97.32  E-value: 5.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 246 GMVGFPNAGKSSLLRAISNARPA-VASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRFL 324
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVGiVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 325 LFVVDLSQpepwTQVDDLKYELEMYEKGLsarPHAIVANKIDLPEAQANLSQLRD-----HLGQEVIVLSALTGENLEQL 399
Cdd:cd00880    81 LLVVDSDL----TPVEEEAKLGLLRERGK---PVLLVLNKIDLVPESEEEELLRErklelLPDLPVIAVSALPGEGIDEL 153

                  .
gi 1858589270 400 L 400
Cdd:cd00880   154 R 154
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
238-414 2.25e-23

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 99.91  E-value: 2.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 238 ELKTVAHAGMvgfPNAGKSSLLRAISNARPAVASYPFTTLKPHVGivHYE-GHLQIAVADIPGII------RGAHQNRGL 310
Cdd:COG1084   159 DLPTIVVAGY---PNVGKSSLVSKVTSAKPEIASYPFTTKGIIVG--HFErGHGRYQVIDTPGLLdrplseRNEIERQAI 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 311 gSAfLRHIERCrfLLFVVDLSQpepwTQVDDLKYELEMYE--KGLSARPHAIVANKIDLPEAQanlsQLRDHLGQEVIVL 388
Cdd:COG1084   234 -LA-LKHLADV--ILFLFDPSE----TCGYSLEEQLNLLEeiRSLFDVPVIVVINKIDLSDEE----ELKEAEEEADIKI 301
                         170       180
                  ....*....|....*....|....*.
gi 1858589270 389 SALTGENLEQLLLHLKVLYDAYAEAE 414
Cdd:COG1084   302 SALTGEGVDELLDELIEALEEEPELP 327
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
249-399 3.44e-23

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: 95.32  E-value: 3.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 249 GFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGivHYE-GHLQIAVADIPGIIRGAHQNRG----LGSAFLRHIERCrf 323
Cdd:cd01897     7 GYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVG--HFDyKYLRWQVIDTPGILDRPLEERNtiemQAITALAHLRAA-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 324 LLFVVDLSQpepwTQVDDLKYELEMYE--KGLSARPHAIVANKIDLPEaQANLSQLRDHL---GQEVIVLSALTGENLEQ 398
Cdd:cd01897    83 VLFFIDPSE----TCGYSIEEQLSLFKeiKPLFNKPVIVVLNKIDLLT-EEDLSEIEKELekeGEEVIKISTLTEEGVDE 157

                  .
gi 1858589270 399 L 399
Cdd:cd01897   158 L 158
PRK09602 PRK09602
translation-associated GTPase; Reviewed
246-390 2.34e-19

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 89.10  E-value: 2.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 246 GMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGI-------VHYEGHLQ--------------IAVA--DIPGIIR 302
Cdd:PRK09602    5 GLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayvrvecPCKELGVKcnprngkcidgtrfIPVEliDVAGLVP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 303 GAHQNRGLGSAFLRHIERCRFLLFVVDLS-------QP-EPWTQ-----VDDLKYELEMY-------------------- 349
Cdd:PRK09602   85 GAHEGRGLGNQFLDDLRQADALIHVVDASgstdeegNPvEPGSHdpvedIKFLEEELDMWiygileknwekfsrkaqaek 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 350 ---EKGLS--------------------------------------------ARPHAIVANKIDLPEAQANLSQLRDHLG 382
Cdd:PRK09602  165 fdiEEALAeqlsglgineehvkealrelglpedpskwtdedllelarelrkiSKPMVIAANKADLPPAEENIERLKEEKY 244

                  ....*...
gi 1858589270 383 QEVIVLSA 390
Cdd:PRK09602  245 YIVVPTSA 252
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
248-400 1.60e-18

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: 82.12  E-value: 1.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 248 VGFPNAGKSSLLRAISNA-RPAVASYPFTTLKPHVGIVHYEGHL-QIAVADIPGIIRGAHQNRglGSAFLRHIERCRFLL 325
Cdd:cd00882     3 VGRGGVGKSSLLNALLGGeVGEVSDVPGTTRDPDVYVKELDKGKvKLVLVDTPGLDEFGGLGR--EELARLLLRGADLIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 326 FVVDLSQPEpwtQVDDLKYELEMYEKGLSArPHAIVANKIDLP-----EAQANLSQLRDHLGQEVIVLSALTGENLEQLL 400
Cdd:cd00882    81 LVVDSTDRE---SEEDAKLLILRRLRKEGI-PIILVGNKIDLLeerevEELLRLEELAKILGVPVFEVSAKTGEGVDELF 156
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
238-400 7.98e-18

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: 81.35  E-value: 7.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 238 ELKTVAhagMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRG-AHQnrgLGSAF-- 314
Cdd:cd01878    40 GVPTVA---LVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTTRRIKLPGGREVLLTDTVGFIRDlPHQ---LVEAFrs 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 315 -LRHIERCRFLLFVVDLSQPEPWTQVDDLKYELEmyEKGLSARPHAIVANKIDLPEAQANLSQLRDHLGqEVIVLSALTG 393
Cdd:cd01878   114 tLEEVAEADLLLHVVDASDPDREEQIETVEEVLK--ELGADDIPIILVLNKIDLLDDEELEERLRAGRP-DAVFISAKTG 190

                  ....*..
gi 1858589270 394 ENLEQLL 400
Cdd:cd01878   191 EGLDLLK 197
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
246-331 1.42e-16

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


Pssm-ID: 206686 [Multi-domain]  Cd Length: 318  Bit Score: 79.96  E-value: 1.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 246 GMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHY---------------------EG--HLQIAVADIPGIIR 302
Cdd:cd01899     2 GLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVGYVrvecpckelgvscnprygkciDGkrYVPVELIDVAGLVP 81
                          90       100
                  ....*....|....*....|....*....
gi 1858589270 303 GAHQNRGLGSAFLRHIERCRFLLFVVDLS 331
Cdd:cd01899    82 GAHEGKGLGNQFLDDLRDADVLIHVVDAS 110
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
245-318 2.12e-16

YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of GTPases: Obg, DRG, Ygr210, and NOG1. Obg is an essential gene that is involved in DNA replication in C. crescentus and Streptomyces griseus and is associated with the ribosome. Several members of the family, including YchF, possess the TGS domain related to the RNA-binding proteins. Experimental data and genomic analysis suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translational factor.


Pssm-ID: 206687 [Multi-domain]  Cd Length: 274  Bit Score: 78.65  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 245 AGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIV------------HYEG----HLQIAVADIPGIIRGAHQNR 308
Cdd:cd01900     1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVpvpderldklaeIVKPkkivPATIEFVDIAGLVKGASKGE 80
                          90
                  ....*....|
gi 1858589270 309 GLGSAFLRHI 318
Cdd:cd01900    81 GLGNKFLSHI 90
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
245-318 4.62e-16

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 78.91  E-value: 4.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 245 AGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIV------------HYEG----HLQIAVADIPGIIRGAHQNR 308
Cdd:COG0012     3 CGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVpvpderldklaeIVKPkkivPATIEFVDIAGLVKGASKGE 82
                          90
                  ....*....|
gi 1858589270 309 GLGSAFLRHI 318
Cdd:COG0012    83 GLGNQFLANI 92
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
244-404 3.52e-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: 72.88  E-value: 3.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 244 HAGMV---GFPNAGKSSLLRAISNARpaVASypfTTLKPH------VGIVHYEGHlQIAVADIPGIIRGAHQ-NRGLGSA 313
Cdd:cd04163     2 KSGFVaiiGRPNVGKSTLLNALVGQK--ISI---VSPKPQttrnriRGIYTDDDA-QIIFVDTPGIHKPKKKlGERMVKA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 314 FLRHIERCRFLLFVVDLSQPEPwtqvDDLKYELEMYEKglSARPHAIVANKIDLPEAQANLSQLRDHL-----GQEVIVL 388
Cdd:cd04163    76 AWSALKDVDLVLFVVDASEWIG----EGDEFILELLKK--SKTPVILVLNKIDLVKDKEDLLPLLEKLkelhpFAEIFPI 149
                         170
                  ....*....|....*.
gi 1858589270 389 SALTGENLEQLLLHLK 404
Cdd:cd04163   150 SALKGENVDELLEYIV 165
PTZ00258 PTZ00258
GTP-binding protein; Provisional
246-328 4.04e-14

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 73.44  E-value: 4.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 246 GMVGFPNAGKSSLLRAISN-ARPAvASYPFTTLKPHVGIV----------------HYEGHLQIAVADIPGIIRGAHQNR 308
Cdd:PTZ00258   25 GIVGLPNVGKSTTFNALCKqQVPA-ENFPFCTIDPNTARVnvpderfdwlckhfkpKSIVPAQLDITDIAGLVKGASEGE 103
                          90       100
                  ....*....|....*....|
gi 1858589270 309 GLGSAFLRHIERCRFLLFVV 328
Cdd:PTZ00258  104 GLGNAFLSHIRAVDGIYHVV 123
era PRK00089
GTPase Era; Reviewed
244-404 4.52e-14

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 72.39  E-value: 4.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 244 HAGMV---GFPNAGKSSLLRAISNARPA-VASYPFTTLKPHVGIVHyEGHLQIAVADIPGIIRGAHQ-NRGLGSAFLRHI 318
Cdd:PRK00089    4 KSGFVaivGRPNVGKSTLLNALVGQKISiVSPKPQTTRHRIRGIVT-EDDAQIIFVDTPGIHKPKRAlNRAMNKAAWSSL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 319 ERCRFLLFVVDLSqpEPWTQVDdlKYELEMYEKglSARPHAIVANKIDLPEAQANLSQLRDHLGQ-----EVIVLSALTG 393
Cdd:PRK00089   83 KDVDLVLFVVDAD--EKIGPGD--EFILEKLKK--VKTPVILVLNKIDLVKDKEELLPLLEELSElmdfaEIVPISALKG 156
                         170
                  ....*....|.
gi 1858589270 394 ENLEQLLLHLK 404
Cdd:PRK00089  157 DNVDELLDVIA 167
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
247-415 7.54e-14

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 69.24  E-value: 7.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 247 MVGFPNAGKSSLLRAISNARPAVASYpfttLKPHvGIVHYEGHLQIAVA-------DIPGI--IRGAHQNrglgsaFLRH 317
Cdd:COG1100     8 VVGTGGVGKTSLVNRLVGDIFSLEKY----LSTN-GVTIDKKELKLDGLdvdlviwDTPGQdeFRETRQF------YARQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 318 IERCRFLLFVVDLSQPEPWTQVDDLKYELEMYEKglsARPHAIVANKIDL--PEAQANLSQLR----DHLGQEVIVLSAL 391
Cdd:COG1100    77 LTGASLYLFVVDGTREETLQSLYELLESLRRLGK---KSPIILVLNKIDLydEEEIEDEERLKealsEDNIVEVVATSAK 153
                         170       180
                  ....*....|....*....|....
gi 1858589270 392 TGENLEQLLLHLKVLYDAYAEAEL 415
Cdd:COG1100   154 TGEGVEELFAALAEILRGEGDSLD 177
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
248-404 1.70e-13

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: 67.90  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 248 VGFPNAGKSSLLRAISNaRPA--VASYPFTT---LkphvgivhyEGHLQIA-----VADIPGI-----------IRGAHQ 306
Cdd:cd04164     9 AGKPNVGKSSLLNALAG-RDRaiVSDIAGTTrdvI---------EEEIDLGgipvrLIDTAGLretedeiekigIERARE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 307 nrglgsaflrHIERCRFLLFVVDLSQPepWTQVDDLKYELemyekgLSARPHAIVANKIDLPEAQANLSqlrDHLGQEVI 386
Cdd:cd04164    79 ----------AIEEADLVLLVVDASEG--LDEEDLEILEL------PAKKPVIVVLNKSDLLSDAEGIS---ELNGKPII 137
                         170
                  ....*....|....*...
gi 1858589270 387 VLSALTGENLEQLLLHLK 404
Cdd:cd04164   138 AISAKTGEGIDELKEALL 155
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
231-415 1.07e-12

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 69.35  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 231 QQRVLH------LELKTVAhagMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRG- 303
Cdd:COG2262   185 KQRELQrkrrkrSGIPTVA---LVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRRLELPDGRPVLLTDTVGFIRKl 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 304 AHQnrgLGSAF---LRHIERCRFLLFVVDLSQPEPWTQVDDLKYELEmyEKGLSARPHAIVANKIDL--PEAQANLSQLR 378
Cdd:COG2262   262 PHQ---LVEAFrstLEEVREADLLLHVVDASDPDFEEQIETVNEVLE--ELGADDKPIILVFNKIDLldDEELERLRAGY 336
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1858589270 379 DHlgqeVIVLSALTGENLEQLLLHL-KVLYDAYAEAEL 415
Cdd:COG2262   337 PD----AVFISAKTGEGIDELLEAIeERLPEDRVEVEL 370
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
244-400 1.80e-12

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 67.32  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 244 HAGMV---GFPNAGKSSLLRAISNARPA-VASYPFTTLKPHVGIVHYEGHlQIAVADIPGIIRGAHQ-NRGLGSAFLRHI 318
Cdd:COG1159     2 RSGFVaivGRPNVGKSTLLNALVGQKVSiVSPKPQTTRHRIRGIVTREDA-QIVFVDTPGIHKPKRKlGRRMNKAAWSAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 319 ERCRFLLFVVDLSqpEPWTQVDdlKYELEMYEKglSARPHAIVANKID------LPEAQANLSQLRDHlgQEVIVLSALT 392
Cdd:COG1159    81 EDVDVILFVVDAT--EKIGEGD--EFILELLKK--LKTPVILVINKIDlvkkeeLLPLLAEYSELLDF--AEIVPISALK 152

                  ....*...
gi 1858589270 393 GENLEQLL 400
Cdd:COG1159   153 GDNVDELL 160
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
248-404 5.62e-12

MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 66.35  E-value: 5.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 248 VGFPNAGKSSLL-------RAIsnarpaVASYPFTT---LkphvgivhyEGHLQIAvaDIP-------GI---------- 300
Cdd:pfam12631 100 VGKPNVGKSSLLnallgeeRAI------VTDIPGTTrdvI---------EETINIG--GIPlrlidtaGIretddeveki 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 301 -IRGAHQnrglgsaflrHIERCRFLLFVVDLSQPepWTQVDDLKYELemyekgLSARPHAI-VANKIDLPEAQANLSQLR 378
Cdd:pfam12631 163 gIERARE----------AIEEADLVLLVLDASRP--LDEEDLEILEL------LKDKKPIIvVLNKSDLLGEIDELEELK 224
                         170       180
                  ....*....|....*....|....*.
gi 1858589270 379 DHlgqEVIVLSALTGENLEQLLLHLK 404
Cdd:pfam12631 225 GK---PVLAISAKTGEGLDELEEAIK 247
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
248-404 1.14e-11

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 66.29  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 248 VGFPNAGKSSLL-------RAIsnarpaVASYPFTT---LkphvgivhyEGHLQIA-----VADIPGI-----------I 301
Cdd:PRK05291  221 AGRPNVGKSSLLnallgeeRAI------VTDIAGTTrdvI---------EEHINLDgiplrLIDTAGIretddevekigI 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 302 RGAHQnrglgsaflrHIERCRFLLFVVDLSQPepWTQVDDLKYELemyekgLSARPHAIVANKIDLPEAqanlSQLRDHL 381
Cdd:PRK05291  286 ERSRE----------AIEEADLVLLVLDASEP--LTEEDDEILEE------LKDKPVIVVLNKADLTGE----IDLEEEN 343
                         170       180
                  ....*....|....*....|...
gi 1858589270 382 GQEVIVLSALTGENLEQLLLHLK 404
Cdd:PRK05291  344 GKPVIRISAKTGEGIDELREAIK 366
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
247-404 1.85e-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: 62.09  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 247 MVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHlQIAVADIPGI--IRGAHQNRGLGSAFLRHiERCRFL 324
Cdd:cd01879     2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGK-EIEIVDLPGTysLTPYSEDEKVARDFLLG-EEPDLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 325 LFVVDLSQPE---PWTqvddlkyeLEMYEKGLsarPHAIVANKIDlpEAQA-----NLSQLRDHLGQEVIVLSALTGENL 396
Cdd:cd01879    80 VNVVDATNLErnlYLT--------LQLLELGL---PVVVALNMID--EAEKrgikiDLDKLSELLGVPVVPTSARKGEGI 146

                  ....*...
gi 1858589270 397 EQLLLHLK 404
Cdd:cd01879   147 DELLDAIA 154
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
248-404 2.83e-11

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


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 65.08  E-value: 2.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 248 VGFPNAGKSSLL-------RAIsnarpaVASYPFTT---LkphvgivhyEGHLQIA-----VADIPGI-----------I 301
Cdd:COG0486   219 VGRPNVGKSSLLnallgeeRAI------VTDIAGTTrdvI---------EERINIGgipvrLIDTAGLretedevekigI 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 302 RGAHQnrglgsaflrHIERCRFLLFVVDLSQPEPwtqvDDLKYELEMyekgLSARPHAIVANKIDLPEAQAnlSQLRDHL 381
Cdd:COG0486   284 ERARE----------AIEEADLVLLLLDASEPLT----EEDEEILEK----LKDKPVIVVLNKIDLPSEAD--GELKSLP 343
                         170       180
                  ....*....|....*....|...
gi 1858589270 382 GQEVIVLSALTGENLEQLLLHLK 404
Cdd:COG0486   344 GEPVIAISAKTGEGIDELKEAIL 366
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
246-399 1.35e-10

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 59.69  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 246 GMVGFPNAGKSSLLRAIS-NARPAVASYPFTTLKPHVGIVHYEG-HLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRF 323
Cdd:TIGR00231   5 VIVGHPNVGKSTLLNSLLgNKGSITEYYPGTTRNYVTTVIEEDGkTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFDI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 324 LLFVVDLSQ-PEPWTQVddLKYELEMyekglsARPHAIVANKIDLPEAQANLSQ--LRDHLGQEVIV-LSALTGENLEQL 399
Cdd:TIGR00231  85 VILVLDVEEiLEKQTKE--IIHHADS------GVPIILVGNKIDLKDADLKTHVasEFAKLNGEPIIpLSAETGKNIDSA 156
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
245-400 1.23e-09

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: 58.55  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 245 AGMVGFPNAGKSSLLRAISNARPAVAS-YPFTTLKPHVGIvHYEGHLQIAVADIPGIIRGAHQ-NRGLGSAFLRHIERCR 322
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISITSpKAQTTRNRISGI-HTTGASQIIFIDTPGFHEKKHSlNRLMMKEARSAIGGVD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 323 FLLFVVDLSQpepWTQVDDLKYELEMYEKglsaRPHAIVANKIDLPEAQANLSQLRDHLGQE----VIVLSALTGENLEQ 398
Cdd:TIGR00436  82 LILFVVDSDQ---WNGDGEFVLTKLQNLK----RPVVLTRNKLDNKFKDKLLPLIDKYAILEdfkdIVPISALTGDNTSF 154

                  ..
gi 1858589270 399 LL 400
Cdd:TIGR00436 155 LA 156
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
247-400 3.17e-09

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: 55.66  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 247 MVGFPNAGKSSLLRAIsnarpavASYPFTTLKPHVG----IVHYeGHLQIAVADIPGiirgahQNRglgsafLRHI---- 318
Cdd:cd00878     4 MLGLDGAGKTTILYKL-------KLGEVVTTIPTIGfnveTVEY-KNVKFTVWDVGG------QDK------IRPLwkhy 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 319 -ERCRFLLFVVDLSQPEpwtQVDDLKYELE--MYEKGLSARPHAIVANKIDLPEA--QANLSQ---LRDHLGQEVIVL-- 388
Cdd:cd00878    64 yENTDGLIFVVDSSDRE---RIEEAKNELHklLNEEELKGAPLLILANKQDLPGAltESELIEllgLESIKGRRWHIQpc 140
                         170
                  ....*....|..
gi 1858589270 389 SALTGENLEQLL 400
Cdd:cd00878   141 SAVTGDGLDEGL 152
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
247-403 4.89e-08

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: 52.03  E-value: 4.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 247 MVGFPNAGKSSLLRAISNARPavasypFTTLkPHVG----IVHYEGHLQIAVADIPGiirgahQNRgLGSAFLRHIERCR 322
Cdd:cd04156     4 LLGLDSAGKSTLLYKLKHAEL------VTTI-PTVGfnveMLQLEKHLSLTVWDVGG------QEK-MRTVWKCYLENTD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 323 FLLFVVDLSQPEpwtQVDDLKYELE--MYEKGLSARPHAIVANKIDLPEA--------QANLSQLRDHLGQEVIVLSALT 392
Cdd:cd04156    70 GLVYVVDSSDEA---RLDESQKELKhiLKNEHIKGVPVVLLANKQDLPGAltaeeitrRFKLKKYCSDRDWYVQPCSAVT 146
                         170
                  ....*....|.
gi 1858589270 393 GENLEQLLLHL 403
Cdd:cd04156   147 GEGLAEAFRKL 157
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
247-400 1.17e-07

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 51.07  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 247 MVGFPNAGKSSLLRAISNARpAVASYPftTLKPHVGIVHYEGhLQIAVADIpgiirGAHQNrglgsafLRHIERCRF--- 323
Cdd:pfam00025   5 ILGLDNAGKTTILYKLKLGE-IVTTIP--TIGFNVETVTYKN-VKFTVWDV-----GGQES-------LRPLWRNYFpnt 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 324 --LLFVVDLSQPEpwtQVDDLKYELE--MYEKGLSARPHAIVANKIDLPEAqANLSQLRDHLGQ--------EVIVLSAL 391
Cdd:pfam00025  69 daVIFVVDSADRD---RIEEAKEELHalLNEEELADAPLLILANKQDLPGA-MSEAEIRELLGLhelkdrpwEIQGCSAV 144

                  ....*....
gi 1858589270 392 TGENLEQLL 400
Cdd:pfam00025 145 TGEGLDEGL 153
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
247-407 5.72e-07

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: 49.35  E-value: 5.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 247 MVGFPNAGKSSLLRAISNA-RPAVASYPFTTLKPHVGIVHYEGHLQIAVaDIPGIIRGAHQNRGL-----GSAfLRHIER 320
Cdd:cd01895     7 IIGRPNVGKSSLLNALLGEeRVIVSDIAGTTRDSIDVPFEYDGQKYTLI-DTAGIRKKGKVTEGIekysvLRT-LKAIER 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 321 CRFLLFVVDLSqpEPWTQVDdlKYELEM-YEKGlsaRPHAIVANKIDLPEAQANL-----SQLRDHLGQ----EVIVLSA 390
Cdd:cd01895    85 ADVVLLVLDAS--EGITEQD--LRIAGLiLEEG---KALIIVVNKWDLVEKDEKTmkefeKELRRKLPFldyaPIVFISA 157
                         170
                  ....*....|....*..
gi 1858589270 391 LTGENLEQLLLHLKVLY 407
Cdd:cd01895   158 LTGQGVDKLFDAIKEVY 174
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
245-400 9.29e-07

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


Pssm-ID: 206724 [Multi-domain]  Cd Length: 159  Bit Score: 48.47  E-value: 9.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 245 AGMVGFPNAGKSSLLRAISNARPAVASYPftTLKPHVGIVHyEGHLQIAVADIPGiirgahQNRglgsaFLRHIER-CR- 322
Cdd:cd04159     2 ITLVGLQNSGKTTLVNVIASGQFSEDTIP--TVGFNMRKVT-KGNVTIKVWDLGG------QPR-----FRSMWERyCRg 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 323 --FLLFVVDLSQPEPWTQVddlKYELE--MYEKGLSARPHAIVANKIDLPEA--------QANLSQLRDhlgQEVIV--L 388
Cdd:cd04159    68 vnAIVYVVDAADREKLEVA---KNELHdlLEKPSLEGIPLLVLGNKNDLPGAlsvdelieQMNLKSITD---REVSCysI 141
                         170
                  ....*....|..
gi 1858589270 389 SALTGENLEQLL 400
Cdd:cd04159   142 SAKEKTNIDIVL 153
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
248-403 1.59e-06

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


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 47.89  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 248 VGFPNAGKSSLLRAISN----ARpaVASYPFTTLKphvgIVHYEGHLQIAVADIPG--------IIRGAHQNrgLGSAFL 315
Cdd:cd01876     5 AGRSNVGKSSLINALTNrkklAR--TSKTPGRTQL----INFFNVGDKFRLVDLPGygyakvskEVREKWGK--LIEEYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 316 RHIERCRFLLFVVDLSQPepwtqvdDLKYELEMYEKgLSAR--PHAIVANKID-LP--EAQANLSQLRDHLGQ-----EV 385
Cdd:cd01876    77 ENRENLKGVVLLIDARHG-------PTPIDLEMLEF-LEELgiPFLIVLTKADkLKksELAKVLKKIKEELNLfnilpPV 148
                         170
                  ....*....|....*...
gi 1858589270 386 IVLSALTGENLEQLLLHL 403
Cdd:cd01876   149 ILFSSKKGTGIDELRALI 166
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
240-424 1.99e-06

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 50.12  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 240 KTVAhagMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHlQIAVADIPGIIrgahqnrGLGSA------ 313
Cdd:COG0370     4 ITIA---LVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGK-EIELVDLPGTY-------SLSAYspdekv 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 314 ---FLRHiERCRFLLFVVDLSQPEP----WTQVddlkyeLEMYekglsaRPHAIVANKIDLPEAQA---NLSQLRDHLGQ 383
Cdd:COG0370    73 ardFLLE-EKPDVVVNVVDATNLERnlylTLQL------LELG------IPVVLALNMMDEAEKKGikiDVEKLSKLLGV 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1858589270 384 EVIVLSALTGENLEQLL------------LHLKVLYDAYAEAELGQ--------GRQPLRW 424
Cdd:COG0370   140 PVVPTSARKGKGIDELKeaiieaaegkkpRPLRIDYPEEIEEAIEEleelleedGPYPSRW 200
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
248-400 3.06e-06

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


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 46.66  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 248 VGFPNAGKSSLLRAISNARPA-VASYPFTTLKPHVGIVHYEGHlQIAVADIPGIIrgaHQNRGLGSAFLRH----IERCR 322
Cdd:cd01894     3 VGRPNVGKSTLFNRLTGRRDAiVSDTPGVTRDRKYGEAEWGGR-EFILIDTGGIE---PDDEGISKEIREQaeiaIEEAD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 323 FLLFVVDLSQpepwtQVDDLKYEL-EMYEKglSARPHAIVANKIDLPEAQANLSQLRdHLG-QEVIVLSALTGENLEQLL 400
Cdd:cd01894    79 VILFVVDGRE-----GLTPADEEIaKYLRK--SKKPVILVVNKIDNIKEEEEAAEFY-SLGfGEPIPISAEHGRGIGDLL 150
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
247-398 3.38e-06

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: 47.01  E-value: 3.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 247 MVGFPNAGKSSLLRAISNarpAVASYPFTTLKPHVGIVHYEGhLQIAVADIPGiirgahqNRGLGSAFLRHIERCRFLLF 326
Cdd:cd04155    20 LLGLDNAGKTTILKQLAS---EDISHITPTQGFNIKNVQADG-FKLNVWDIGG-------QRKIRPYWRNYFENTDVLIY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 327 VVDLSQPEpwtQVDDLKYELE--MYEKGLSARPHAIVANKIDLPEAQA--------NLSQLRDHLGQeVIVLSALTGENL 396
Cdd:cd04155    89 VIDSADRK---RFEEAGQELVelLEEEKLAGVPVLVFANKQDLLTAAPaeevaealNLHDIRDRSWH-IQACSAKTGEGL 164

                  ..
gi 1858589270 397 EQ 398
Cdd:cd04155   165 QE 166
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
247-384 5.88e-06

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: 46.50  E-value: 5.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 247 MVGFPNAGKSSLLRAISNARpaVASY-PftTLKPHVGIVHYeGHLQIAVADIpgiirGAHQnrglgsAFLR----HIERC 321
Cdd:cd00879    24 FLGLDNAGKTTLLHMLKDDR--LAQHvP--TLHPTSEELTI-GNVKFTTFDL-----GGHE------QARRvwkdYFPEV 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1858589270 322 RFLLFVVDLSQPEpwtQVDDLKYELE--MYEKGLSARPHAIVANKIDLPEAqANLSQLRDHLGQE 384
Cdd:cd00879    88 DGIVFLVDAADPE---RFQESKEELDslLNDEELANVPILILGNKIDKPGA-VSEEELREALGLY 148
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
247-367 8.77e-06

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 47.87  E-value: 8.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 247 MVGFPNAGKSSLLRAISNARPAVAS-YPFTTLKPHVGIVHYEGHLQIAVaDIPGIIRGAHQNRGLG-SAFLRH---IERC 321
Cdd:PRK09518  455 LVGRPNVGKSSLLNQLTHEERAVVNdLAGTTRDPVDEIVEIDGEDWLFI-DTAGIKRRQHKLTGAEyYSSLRTqaaIERS 533
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1858589270 322 RFLLFVVDLSQPepwTQVDDLKYELEMYEKGlsaRPHAIVANKIDL 367
Cdd:PRK09518  534 ELALFLFDASQP---ISEQDLKVMSMAVDAG---RALVLVFNKWDL 573
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
248-398 3.05e-05

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: 43.96  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 248 VGFPNAGKSSLLRAI--SNARPAvasypftTLKPHVGIV---HYEGHLQIAVADIPGiirgAHQNRGLGSAFLrhiERCR 322
Cdd:cd04157     5 LGLDNSGKTTIINQLkpSNAQSQ-------NIVPTVGFNvesFKKGNLSFTAFDMSG----QGKYRGLWEHYY---KNIQ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 323 FLLFVVDLSqpepwtqvDDL-----KYELEMY--EKGLSAR--PHAIVANKIDLPEAQA--------NLSQLRDHLGQeV 385
Cdd:cd04157    71 GIIFVIDSS--------DRLrmvvaKDELELLlnHPDIKHRriPILFYANKMDLPDALTavkitqllCLENIKDKPWH-I 141
                         170
                  ....*....|...
gi 1858589270 386 IVLSALTGENLEQ 398
Cdd:cd04157   142 FASSALTGEGLDE 154
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
358-422 3.65e-05

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


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 45.78  E-value: 3.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 358 HA-------IVA-NKIDLPEAQAN--LSQLRDH------LGQEVIV--LSALTGENLEQLL---------LHLKVLYDAY 410
Cdd:COG0532    98 HAkaagvpiIVAiNKIDKPGANPDrvKQELAEHglvpeeWGGDTIFvpVSAKTGEGIDELLemillqaevLELKANPDRP 177
                          90
                  ....*....|....*..
gi 1858589270 411 A-----EAELGQGRQPL 422
Cdd:COG0532   178 ArgtviEAKLDKGRGPV 194
Arl2l1_Arl13_like cd04161
Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a ...
246-370 9.23e-05

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


Pssm-ID: 133361 [Multi-domain]  Cd Length: 167  Bit Score: 42.77  E-value: 9.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 246 GMVGFPNAGKSSLLRAI-----SNARPAVASYPfTTLKphvgivhyEGHLQIAVADIPGIIRGahqnRGlgsAFLRHIER 320
Cdd:cd04161     3 LTVGLDNAGKTTLVSALqgeipKKVAPTVGFTP-TKLR--------LDKYEVCIFDLGGGANF----RG---IWVNYYAE 66
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1858589270 321 CRFLLFVVDLSQPEPWTQVDDLKYELeMYEKGLSARPHAIVANKIDLPEA 370
Cdd:cd04161    67 AHGLVFVVDSSDDDRVQEVKEILREL-LQHPRVSGKPILVLANKQDKKNA 115
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
247-400 1.15e-04

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


Pssm-ID: 133353 [Multi-domain]  Cd Length: 174  Bit Score: 42.72  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 247 MVGFPNAGKSSLLRAISnARPAVASYPftTLKPHVGIVHYEGhLQIAVADIPGiirgahQNRgLGSAFLRHIERCRFLLF 326
Cdd:cd04153    20 IVGLDNAGKTTILYQFL-LGEVVHTSP--TIGSNVEEIVYKN-IRFLMWDIGG------QES-LRSSWNTYYTNTDAVIL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 327 VVDLSQPEPWTQVDDLKYELEMYEKgLSARPHAIVANKIDLPEA--------QANLSQLRDHLGQeVIVLSALTGENLEQ 398
Cdd:cd04153    89 VIDSTDRERLPLTKEELYKMLAHED-LRKAVLLVLANKQDLKGAmtpaeiseSLGLTSIRDHTWH-IQGCCALTGEGLPE 166

                  ..
gi 1858589270 399 LL 400
Cdd:cd04153   167 GL 168
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
238-300 1.58e-04

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


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 42.25  E-value: 1.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1858589270 238 ELKTVAHAG----MVGFPNAGKSSLLRAI------------SNARPAVASYPFTTLkphvGIVHYEGHLQIAVADIPGI 300
Cdd:cd01855   117 EIKKLAKYRgdvyVVGATNVGKSTLINALlksnggkvqaqaLVQRLTVSPIPGTTL----GLIKIPLGEGKKLYDTPGI 191
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
244-382 2.15e-04

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: 41.84  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270  244 HAGMV--GFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIvhyeGHLQIAVADIpgiirGAHQN-RGLGSAFLRHIER 320
Cdd:smart00178  17 HAKILflGLDNAGKTTLLHMLKNDRLAQHQPTQHPTSEELAI----GNIKFTTFDL-----GGHQQaRRLWKDYFPEVNG 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1858589270  321 crfLLFVVDLSQPEpwtQVDDLKYELE--MYEKGLSARPHAIVANKIDLPEAqANLSQLRDHLG 382
Cdd:smart00178  88 ---IVYLVDAYDKE---RFAESKRELDalLSDEELATVPFLILGNKIDAPYA-ASEDELRYALG 144
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
247-403 2.64e-04

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: 41.29  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 247 MVGFPNAGKSSLL-RAISNArpavasypFT-TLKPHVGI------VHYEGH---LQI---AvadipgiirGAHQNRGLGS 312
Cdd:cd00154     5 LIGDSGVGKTSLLlRFVDNK--------FSeNYKSTIGVdfksktIEVDGKkvkLQIwdtA---------GQERFRSITS 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 313 AFLRHierCRFLLFVVDLSQPEPWTQVDDLKYELEMYekglsARPHA---IVANKIDLPEAQANLS----QLRDHLGQEV 385
Cdd:cd00154    68 SYYRG---AHGAILVYDVTNRESFENLDKWLNELKEY-----APPNIpiiLVGNKSDLEDERQVSTeeaqQFAKENGLLF 139
                         170
                  ....*....|....*...
gi 1858589270 386 IVLSALTGENLEQLLLHL 403
Cdd:cd00154   140 FETSAKTGENVDEAFESL 157
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
246-300 3.65e-04

Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 40.45  E-value: 3.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1858589270 246 GMVGFPNAGKSSLLRAISNARPAVASY--PFTTLKPHVGIVHyeghlQIAVADIPGI 300
Cdd:cd01849    95 GVVGLPNVGKSSFINALLNKFKLKVGSipGTTKLQQDVKLDK-----EIYLYDTPGI 146
PRK00098 PRK00098
GTPase RsgA; Reviewed
360-404 5.38e-04

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 41.73  E-value: 5.38e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1858589270 360 IVANKIDLPEAQANLSQLRDH---LGQEVIVLSALTGENLEQLLLHLK 404
Cdd:PRK00098  116 IVLNKIDLLDDLEEARELLALyraIGYDVLELSAKEGEGLDELKPLLA 163
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
248-398 1.10e-03

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: 39.63  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 248 VGFPNAGKSSLLRAI-SNARPAVASYPFTTLKPHVGivhyeghLQIAVADIPGII-----RGAHQnrGLGSAFLRHIERC 321
Cdd:cd04160     5 LGLDNAGKTTFLEQTkTKFSKNYKGLNPSKITPTVG-------LNIGTIEVGKARlmfwdLGGQE--ELRSLWDKYYAES 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 322 RFLLFVVDLSQPEpwtQVDDLKYELE--MYEKGLSARPHAIVANKIDLPEAQA------NLSQLRDHLGQE---VIVLSA 390
Cdd:cd04160    76 HGVIYVIDSTDRE---RFNESKSAFEkvINNEALEGVPLLVLANKQDLPDALSvaeikeVFDDCIALIGRRdclVQPVSA 152

                  ....*...
gi 1858589270 391 LTGENLEQ 398
Cdd:cd04160   153 LEGEGVEE 160
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
324-404 1.11e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 40.07  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858589270 324 LLFVVDLSQPEP-WTQVDdlKYELEMYEKGLSArphAIVANKIDL---PEAQANLSQLRDhLGQEVIVLSALTGENLEQL 399
Cdd:cd01854     6 VLIVFSLKEPFFnLRLLD--RYLVAAEASGIEP---VIVLNKADLvddEELEELLEIYEK-LGYPVLAVSAKTGEGLDEL 79

                  ....*
gi 1858589270 400 LLHLK 404
Cdd:cd01854    80 RELLK 84
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
243-262 6.11e-03

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


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 36.83  E-value: 6.11e-03
                          10        20
                  ....*....|....*....|
gi 1858589270 243 AHAGMVGFPNAGKSSLLRAI 262
Cdd:cd01857    83 ATIGLVGYPNVGKSSLINAL 102
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
361-400 6.95e-03

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


Pssm-ID: 206677 [Multi-domain]  Cd Length: 179  Bit Score: 37.51  E-value: 6.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1858589270 361 VANKIDLPEAQAN--LSQLRDHLG---QEVIVLSALTGENLEQLL 400
Cdd:cd01890   125 VINKIDLPAADPDrvKQEIEDVLGldaSEAILVSAKTGLGVEDLL 169
MMR_HSR1_C pfam08438
GTPase of unknown function C-terminal; This domain is found at the C-terminus of pfam01926 in ...
361-392 8.80e-03

GTPase of unknown function C-terminal; This domain is found at the C-terminus of pfam01926 in archaeal and eukaryotic GTP-binding proteins. The C-terminal domain of the GTP-binding proteins is necessary 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 nucleotides.


Pssm-ID: 429998 [Multi-domain]  Cd Length: 109  Bit Score: 35.97  E-value: 8.80e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1858589270 361 VANKIDLPEAQANLSQLRDHLGQEVIVL-SALT 392
Cdd:pfam08438   1 AANKADLPAADENIEKLKEKYPDHIVVPtSAEA 33
 
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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