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Conserved domains on  [gi|7019419|ref|NP_037417|]
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nucleolar GTP-binding protein 2 isoform 1 [Homo sapiens]

Protein Classification

nucleolar GTP-binding protein 2( domain architecture ID 10548123)

nucleolar GTP-binding protein 2 is a GTPase that associates with pre-60S ribosomal subunits in the nucleolus and is required for their nuclear export and maturation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
 209-365 1.44e-123

A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; Autoantigen NGP-1 (Nucleolar G-protein gene 1) has been shown to localize in the nucleolus and nucleolar organizers in all cell types analyzed, which is indicative of a function in ribosomal assembly. NGP-1 and its homologs show 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 NKXD motif) are relocated to the N terminus.


:

Pssm-ID: 206751 [Multi-domain]  Cd Length: 157  Bit Score: 365.08  E-value: 1.44e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  209 ELYKVIDSSDVVVQVLDARDPMGTRSPHIETYLKKEKPWKHLIFVLNKCDLVPTWATKRWVAVLSQDYPTLAFHASLTNP 288
Cdd:cd01858   1 ELYKVIDSSDVIIQVLDARDPMGTRCKHVEKYLRKEKPHKHLIFVLNKCDLVPTWVTKRWVKVLSKEYPTLAFHASITNP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7019419  289 FGKGAFIQLLRQFGKLHTDKKQISVGFIGYPNVGKSSVINTLRSKKVCNVAPIAGETKVWQYITLMRRIFLIDCPGV 365
Cdd:cd01858  81 FGKGALINLLRQFAKLHSDKKQISVGFIGYPNVGKSSVINTLRSKKVCKVAPIPGETKVWQYITLMKRIYLIDCPGV 157
NGP1NT pfam08153
NGP1NT (NUC091) domain; This N terminal domain is found in a subfamily of hypothetical ...
 43-174 4.62e-62

NGP1NT (NUC091) domain; This N terminal domain is found in a subfamily of hypothetical nucleolar GTP-binding proteins similar to human NGP1.


:

Pssm-ID: 462379  Cd Length: 129  Bit Score: 203.60  E-value: 4.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419     43 MYR-QKERRNSRGKIIKPLQYQSTVAsgTVARVEPNIKWFGNTRVIKQSSLQKFQEEMDTVMKDPYKVVMKQSKLPMSLL 121
Cdd:pfam08153   1 MYKsGKPKRNAKGKIIKAAPFQSKDT--PTARIEPDRRWFGNTRVISQDALEKFREEMGEKVKDPYQVLLKRNKLPMSLL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 7019419    122 HDRIRPHnlKVHILDTESFETTFGPKSQRKRPNLFASDMQSLIENAEMSTESY 174
Cdd:pfam08153  79 QDKTKKA--RVHILETEPFEDTFGPKAQRKRPKLSVSSLEELAKKAEESQDSY 129
 
Name Accession Description Interval E-value
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
 209-365 1.44e-123

A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; Autoantigen NGP-1 (Nucleolar G-protein gene 1) has been shown to localize in the nucleolus and nucleolar organizers in all cell types analyzed, which is indicative of a function in ribosomal assembly. NGP-1 and its homologs show 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 NKXD motif) are relocated to the N terminus.


Pssm-ID: 206751 [Multi-domain]  Cd Length: 157  Bit Score: 365.08  E-value: 1.44e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  209 ELYKVIDSSDVVVQVLDARDPMGTRSPHIETYLKKEKPWKHLIFVLNKCDLVPTWATKRWVAVLSQDYPTLAFHASLTNP 288
Cdd:cd01858   1 ELYKVIDSSDVIIQVLDARDPMGTRCKHVEKYLRKEKPHKHLIFVLNKCDLVPTWVTKRWVKVLSKEYPTLAFHASITNP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7019419  289 FGKGAFIQLLRQFGKLHTDKKQISVGFIGYPNVGKSSVINTLRSKKVCNVAPIAGETKVWQYITLMRRIFLIDCPGV 365
Cdd:cd01858  81 FGKGALINLLRQFAKLHSDKKQISVGFIGYPNVGKSSVINTLRSKKVCKVAPIPGETKVWQYITLMKRIYLIDCPGV 157
NGP1NT pfam08153
NGP1NT (NUC091) domain; This N terminal domain is found in a subfamily of hypothetical ...
 43-174 4.62e-62

NGP1NT (NUC091) domain; This N terminal domain is found in a subfamily of hypothetical nucleolar GTP-binding proteins similar to human NGP1.


Pssm-ID: 462379  Cd Length: 129  Bit Score: 203.60  E-value: 4.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419     43 MYR-QKERRNSRGKIIKPLQYQSTVAsgTVARVEPNIKWFGNTRVIKQSSLQKFQEEMDTVMKDPYKVVMKQSKLPMSLL 121
Cdd:pfam08153   1 MYKsGKPKRNAKGKIIKAAPFQSKDT--PTARIEPDRRWFGNTRVISQDALEKFREEMGEKVKDPYQVLLKRNKLPMSLL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 7019419    122 HDRIRPHnlKVHILDTESFETTFGPKSQRKRPNLFASDMQSLIENAEMSTESY 174
Cdd:pfam08153  79 QDKTKKA--RVHILETEPFEDTFGPKAQRKRPKLSVSSLEELAKKAEESQDSY 129
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
218-456 4.99e-36

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 137.16  E-value: 4.99e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  218 DVVVQVLDARDPMGTRSPHIETyLKKEKPwkhLIFVLNKCDLVPTWATKRWVAVL-SQDYPTLAFhaSLTNPFGKGAFIQ 296
Cdd:COG1161  25 DLVIEVVDARIPLSSRNPMLDE-LVGNKP---RLLVLNKADLADPSVTKQWLKYFeKQGVDALAI--SAKKGKGIKELIE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  297 LLRQ-FGKLHTDKKQISVGFIGYPNVGKSSVINTLRSKKVCNVAPIAGETKVWQYITLMRRIFLIDCPGVVYPSEDSETD 375
Cdd:COG1161  99 AIRElAPEKGIKRRPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKGQQWIKLDDGLELLDTPGILWPKFEDPEV 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  376 ---IVLKG-----VVQVEKIKSpedHIGAVLERAKPEYISKTYKIDSW-ENAEDFLEKLAFRTGKLLKGGEPDLQTVGKM 446
Cdd:COG1161 179 gykLAATGaikdeVLDLEEVAL---FLLGYLARRYPELLKERYKLDELpRTKLELLEAIGRKRGCLLSGGEVDLEKAAEI 255

                       250
                ....*....|
gi 7019419  447 VLNDWQRGRI 456
Cdd:COG1161 256 LLTDFRSGKL 265
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 218-456 4.54e-34

ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members. [Protein synthesis, Other]


Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 131.48  E-value: 4.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419    218 DVVVQVLDARDPMGTRSPHIETYLKkEKPwkhLIFVLNKCDLVPTWATKRWVAVLSQDyPTLAFHASLTNPFGKGAFIQL 297
Cdd:TIGR03596  23 DVVIEVLDARIPLSSRNPMIDEIRG-NKP---RLIVLNKADLADPAVTKQWLKYFEEK-GIKALAVNAKKGAGVKKIIKA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419    298 LRQFGKlHTDKKQISVGF---------IGYPNVGKSSVINTLRSKKVCNVAPIAGETKVWQYITLMRRIFLIDCPGVVYP 368
Cdd:TIGR03596  98 AKKLLK-EKNEKLKAKGLknrpiramiVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQQWIKLSDNLELLDTPGILWP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419    369 SEDSETD---IVLKGVVQVEKIksPEDHIGA----VLERAKPEYISKTYKIDS-WENAEDFLEKLAFRTGKLLKGGEPDL 440
Cdd:TIGR03596 177 KFEDQEVglkLAATGAIKDEAL--DLEDVALflleYLLEHYPELLKERYKLDElPEDPVELLEAIAKKRGCLLKGGELDL 254

                         250
                  ....*....|....*.
gi 7019419    441 QTVGKMVLNDWQRGRI 456
Cdd:TIGR03596 255 DRAAEILLNDFRKGKL 270
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 313-406 5.49e-15

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: 71.50  E-value: 5.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419    313 VGFIGYPNVGKSSVINTLrSKKVCNVAPIAGETKVWQYITLM---RRIFLIDCPGVVYPSED-----------SETDIVL 378
Cdd:pfam01926   2 VALVGRPNVGKSTLINAL-TGAKAIVSDYPGTTRDPNEGRLElkgKQIILVDTPGLIEGASEgeglgraflaiIEADLIL 80

                          90       100
                  ....*....|....*....|....*...
gi 7019419    379 KGVVQVEKIKSPEDHIGAVLERAKPEYI 406
Cdd:pfam01926  81 FVVDSEEGITPLDEELLELLRENKKPII 108
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 214-345 8.55e-07

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 51.97  E-value: 8.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419   214 IDSSDVVVQVLDARDPMgtrSP---HIETYLKKEKpwKHLIFVLNKCDlvptwatkrwvavlSQDYPTLA--FHA-SLTN 287
Cdd:PRK00093  78 IEEADVILFVVDGRAGL---TPadeEIAKILRKSN--KPVILVVNKVD--------------GPDEEADAyeFYSlGLGE 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419   288 PF------GKG------AFIQLLRQFGKLHTDKKQISVGFIGYPNVGKSSVINTLRSKKVCNVAPIAGET 345
Cdd:PRK00093 139 PYpisaehGRGigdlldAILEELPEEEEEDEEDEPIKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTT 208
 
Name Accession Description Interval E-value
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
 209-365 1.44e-123

A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; Autoantigen NGP-1 (Nucleolar G-protein gene 1) has been shown to localize in the nucleolus and nucleolar organizers in all cell types analyzed, which is indicative of a function in ribosomal assembly. NGP-1 and its homologs show 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 NKXD motif) are relocated to the N terminus.


Pssm-ID: 206751 [Multi-domain]  Cd Length: 157  Bit Score: 365.08  E-value: 1.44e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  209 ELYKVIDSSDVVVQVLDARDPMGTRSPHIETYLKKEKPWKHLIFVLNKCDLVPTWATKRWVAVLSQDYPTLAFHASLTNP 288
Cdd:cd01858   1 ELYKVIDSSDVIIQVLDARDPMGTRCKHVEKYLRKEKPHKHLIFVLNKCDLVPTWVTKRWVKVLSKEYPTLAFHASITNP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7019419  289 FGKGAFIQLLRQFGKLHTDKKQISVGFIGYPNVGKSSVINTLRSKKVCNVAPIAGETKVWQYITLMRRIFLIDCPGV 365
Cdd:cd01858  81 FGKGALINLLRQFAKLHSDKKQISVGFIGYPNVGKSSVINTLRSKKVCKVAPIPGETKVWQYITLMKRIYLIDCPGV 157
NGP1NT pfam08153
NGP1NT (NUC091) domain; This N terminal domain is found in a subfamily of hypothetical ...
 43-174 4.62e-62

NGP1NT (NUC091) domain; This N terminal domain is found in a subfamily of hypothetical nucleolar GTP-binding proteins similar to human NGP1.


Pssm-ID: 462379  Cd Length: 129  Bit Score: 203.60  E-value: 4.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419     43 MYR-QKERRNSRGKIIKPLQYQSTVAsgTVARVEPNIKWFGNTRVIKQSSLQKFQEEMDTVMKDPYKVVMKQSKLPMSLL 121
Cdd:pfam08153   1 MYKsGKPKRNAKGKIIKAAPFQSKDT--PTARIEPDRRWFGNTRVISQDALEKFREEMGEKVKDPYQVLLKRNKLPMSLL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 7019419    122 HDRIRPHnlKVHILDTESFETTFGPKSQRKRPNLFASDMQSLIENAEMSTESY 174
Cdd:pfam08153  79 QDKTKKA--RVHILETEPFEDTFGPKAQRKRPKLSVSSLEELAKKAEESQDSY 129
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 218-365 3.22e-56

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: 188.36  E-value: 3.22e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  218 DVVVQVLDARDPMGTRSPHIEtyLKKEKPWKHLIFVLNKCDLVPTWATKRWVAVLSQDYPTLAFHASLTNPFGKGAFIQL 297
Cdd:cd01849   1 DVVVEVVDARDPLSSRNPDIE--VLINEKNKKLIMVLNKADLVPKEVLRKWVAELSELYGTKTFFISATNGQGILKLKAE 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7019419  298 LRQFGKLHTDKKQISVGFIGYPNVGKSSVINTLRSKKVCNVAPIAGETKVWQYITLMRRIFLIDCPGV 365
Cdd:cd01849  79 ITKQKLKLKYKKGIRVGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQDVKLDKEIYLYDTPGI 146
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 218-365 7.08e-49

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


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 169.29  E-value: 7.08e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  218 DVVVQVLDARDPMGTRSPHIETYLKKEKPWKHLIFVLNKCDLVPTWATKRWVAVLSQDYPTLAFHAS------------- 284
Cdd:cd04178   1 DVILEVLDARDPLGCRCPQVERAVLVLGPNKKLVLVLNKIDLVPKENVEKWLKYLRNEFPTVAFKAStqqqkknlsrksk 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  285 ----------LTNPFGKGAFIQLLRQFGKLHTDKKQISVGFIGYPNVGKSSVINTLRSKKVCNVAPIAGETKVWQYITLM 354
Cdd:cd04178  81 kvkasddllsSSACLGADALLKLLKNYARNKGIKTSITVGVVGYPNVGKSSVINSLKRSRACNVGATPGVTKSMQEVHLD 160

                       170
                ....*....|.
gi 7019419  355 RRIFLIDCPGV 365
Cdd:cd04178 161 KHVKLLDSPGV 171
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 206-368 1.55e-36

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: 133.90  E-value: 1.55e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  206 IWGELYKVIDSSDVVVQVLDARDPMGTRSPHIETYLKKEKPWKHLIFVLNKCDLVPTWATKRWVAVLSQDYPTLAFHASL 285
Cdd:cd01857   1 VWRQLWRVIERSDVVVQIVDARNPLFFRCPDLEKYVKEVDPSKENVLLLNKADLVTEEQRKAWARYFKKEGIVVLFFSAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  286 tnpfgkgafiqllrqfgklhtdkKQISVGFIGYPNVGKSSVINTLRSKKVCNVAPIAGETKVWQYITLMRRIFLIDCPGV 365
Cdd:cd01857  81 -----------------------NEATIGLVGYPNVGKSSLINALVGSKKVSVSSTPGKTKHFQTIFLEPGITLCDCPGL 137


                ...
gi 7019419  366 VYP 368
Cdd:cd01857 138 VFP 140
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 207-365 2.77e-36

An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 133.98  E-value: 2.77e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  207 WGELYKVIDS-SDVVVQVLDARDPMGTRSPHIETYLKKEKpwKHLIFVLNKCDLVPTWATKRWVAVL-SQDYPTLAFHAs 284
Cdd:cd01859   1 WKRLVRRIIKeADVVLEVVDARDPELTRSRKLERMALELG--KKLIIVLNKADLVPREVLEKWKEVFeSEGLPVVYVSA- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  285 lTNPFGkgaFIQLLRQFGKLHTDKKQISVGFIGYPNVGKSSVINTLRSKKVCNVAPI---AGETKVWQYITLMRRIFLID 361
Cdd:cd01859  78 -RERLG---TRILRRTIKELAIDGKPVIVGVVGYPKVGKSSIINALKGRHSASTSPIpgsPGYTKGIQLVRIDSKIYLID 153


                ....
gi 7019419  362 CPGV 365
Cdd:cd01859 154 TPGV 157
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
218-456 4.99e-36

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 137.16  E-value: 4.99e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  218 DVVVQVLDARDPMGTRSPHIETyLKKEKPwkhLIFVLNKCDLVPTWATKRWVAVL-SQDYPTLAFhaSLTNPFGKGAFIQ 296
Cdd:COG1161  25 DLVIEVVDARIPLSSRNPMLDE-LVGNKP---RLLVLNKADLADPSVTKQWLKYFeKQGVDALAI--SAKKGKGIKELIE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  297 LLRQ-FGKLHTDKKQISVGFIGYPNVGKSSVINTLRSKKVCNVAPIAGETKVWQYITLMRRIFLIDCPGVVYPSEDSETD 375
Cdd:COG1161  99 AIRElAPEKGIKRRPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKGQQWIKLDDGLELLDTPGILWPKFEDPEV 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  376 ---IVLKG-----VVQVEKIKSpedHIGAVLERAKPEYISKTYKIDSW-ENAEDFLEKLAFRTGKLLKGGEPDLQTVGKM 446
Cdd:COG1161 179 gykLAATGaikdeVLDLEEVAL---FLLGYLARRYPELLKERYKLDELpRTKLELLEAIGRKRGCLLSGGEVDLEKAAEI 255

                       250
                ....*....|
gi 7019419  447 VLNDWQRGRI 456
Cdd:COG1161 256 LLTDFRSGKL 265
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 218-456 4.54e-34

ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members. [Protein synthesis, Other]


Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 131.48  E-value: 4.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419    218 DVVVQVLDARDPMGTRSPHIETYLKkEKPwkhLIFVLNKCDLVPTWATKRWVAVLSQDyPTLAFHASLTNPFGKGAFIQL 297
Cdd:TIGR03596  23 DVVIEVLDARIPLSSRNPMIDEIRG-NKP---RLIVLNKADLADPAVTKQWLKYFEEK-GIKALAVNAKKGAGVKKIIKA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419    298 LRQFGKlHTDKKQISVGF---------IGYPNVGKSSVINTLRSKKVCNVAPIAGETKVWQYITLMRRIFLIDCPGVVYP 368
Cdd:TIGR03596  98 AKKLLK-EKNEKLKAKGLknrpiramiVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQQWIKLSDNLELLDTPGILWP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419    369 SEDSETD---IVLKGVVQVEKIksPEDHIGA----VLERAKPEYISKTYKIDS-WENAEDFLEKLAFRTGKLLKGGEPDL 440
Cdd:TIGR03596 177 KFEDQEVglkLAATGAIKDEAL--DLEDVALflleYLLEHYPELLKERYKLDElPEDPVELLEAIAKKRGCLLKGGELDL 254

                         250
                  ....*....|....*.
gi 7019419    441 QTVGKMVLNDWQRGRI 456
Cdd:TIGR03596 255 DRAAEILLNDFRKGKL 270
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 218-365 1.07e-26

Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 106.84  E-value: 1.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  218 DVVVQVLDARDPMGTRSPHIETYLKKeKPwkHLIfVLNKCDLVPTWATKRWVAVL-SQDYPTLAFHASltNPFGKGAFIQ 296
Cdd:cd01856  21 DVVIEVRDARIPLSSRNPDLDKILGN-KP--RLI-VLNKADLADPAKTKKWLKYFkSQGEPVLFVNAK--NGKGVKKLLK 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7019419  297 LLRQFGKL-------HTDKKQISVGFIGYPNVGKSSVINTLRSKKVCNVAPIAGETKVWQYITLMRRIFLIDCPGV 365
Cdd:cd01856  95 KAKKLLKEneklkakGLLPRPLRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTRGQQWIRIGPNIELLDTPGI 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 313-406 5.49e-15

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: 71.50  E-value: 5.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419    313 VGFIGYPNVGKSSVINTLrSKKVCNVAPIAGETKVWQYITLM---RRIFLIDCPGVVYPSED-----------SETDIVL 378
Cdd:pfam01926   2 VALVGRPNVGKSTLINAL-TGAKAIVSDYPGTTRDPNEGRLElkgKQIILVDTPGLIEGASEgeglgraflaiIEADLIL 80

                          90       100
                  ....*....|....*....|....*...
gi 7019419    379 KGVVQVEKIKSPEDHIGAVLERAKPEYI 406
Cdd:pfam01926  81 FVVDSEEGITPLDEELLELLRENKKPII 108
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 212-365 7.07e-11

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: 61.90  E-value: 7.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  212 KVIDSSDVVVQVLDARDPMGTRSPHIETYLKKEKpwkhLIFVLNKCDLVPT----WATKRWVAVLSQDYPTLAFHASLTN 287
Cdd:cd01855  29 TLLNDNALVVHVVDIFDFPGSLIPGLAELIGAKP----VILVGNKIDLLPKdvkpNRLKQWVKKRLKIGGLKIKDVILVS 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  288 PFgKGAFI-QLLRQFGKLHTDKKQisVGFIGYPNVGKSSVINTLRSKKVCN-----------VAPIAGETKVWQYITLMR 355
Cdd:cd01855 105 AK-KGWGVeELIEEIKKLAKYRGD--VYVVGATNVGKSTLINALLKSNGGKvqaqalvqrltVSPIPGTTLGLIKIPLGE 181

                       170
                ....*....|
gi 7019419  356 RIFLIDCPGV 365
Cdd:cd01855 182 GKKLYDTPGI 191
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 314-373 4.11e-07

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: 50.32  E-value: 4.11e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7019419  314 GFIGYPNVGKSSVINTLRSKKVCNVAPIAGETKVWQY----ITLMRRIFLIDCPGVVYPSEDSE 373
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRkeweLLPLGPVVLIDTPGLDEEGGLGR 64
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 314-381 6.86e-07

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: 49.76  E-value: 6.86e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7019419  314 GFIGYPNVGKSSVINTLRSKKVCNVAPIAGET-----KVWQYITLMRRIFLIDCPGVV---YPSEDSETDIVLKGV 381
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTrdpdvYVKELDKGKVKLVLVDTPGLDefgGLGREELARLLLRGA 76
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 214-345 8.55e-07

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 51.97  E-value: 8.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419   214 IDSSDVVVQVLDARDPMgtrSP---HIETYLKKEKpwKHLIFVLNKCDlvptwatkrwvavlSQDYPTLA--FHA-SLTN 287
Cdd:PRK00093  78 IEEADVILFVVDGRAGL---TPadeEIAKILRKSN--KPVILVVNKVD--------------GPDEEADAyeFYSlGLGE 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419   288 PF------GKG------AFIQLLRQFGKLHTDKKQISVGFIGYPNVGKSSVINTLRSKKVCNVAPIAGET 345
Cdd:PRK00093 139 PYpisaehGRGigdlldAILEELPEEEEEDEEDEPIKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTT 208
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
214-345 9.54e-06

Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 48.87  E-value: 9.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  214 IDSSDVVVQVLDARDPMgtrSP---HIETYLKKEKpwKHLIFVLNKCDlvptwatkrwvavlSQDYPTLA--FHA-SLTN 287
Cdd:COG1160  80 IEEADVILFVVDGRAGL---TPldeEIAKLLRRSG--KPVILVVNKVD--------------GPKREADAaeFYSlGLGE 140

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7019419  288 PF------GKG------AFIQLLRQFGKLHTDKKQISVGFIGYPNVGKSSVINTL----RSKkvcnVAPIAGET 345
Cdd:COG1160 141 PIpisaehGRGvgdlldAVLELLPEEEEEEEEDDPIKIAIVGRPNVGKSSLINALlgeeRVI----VSDIAGTT 210
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 251-330 2.24e-05

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: 46.24  E-value: 2.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  251 IFVLNKCDLVPTWATKRWVAVLSQ-DYPTLAfhASLTNPFGKGAFIQLLrqfgklhtdKKQISVgFIGYPNVGKSSVINT 329
Cdd:cd01854  37 VIVLNKADLVDDEELEELLEIYEKlGYPVLA--VSAKTGEGLDELRELL---------KGKTSV-LVGQSGVGKSTLLNA 104


                .
gi 7019419  330 L 330
Cdd:cd01854 105 L 105
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 313-364 7.40e-05

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


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 44.04  E-value: 7.40e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 7019419  313 VGFIGYPNVGKSSVINTL-RSKKVCNVAPIAGETKVWQYITLMRRIFLIDCPG 364
Cdd:cd01876   2 VAFAGRSNVGKSSLINALtNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPG 54
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 317-365 1.76e-04

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: 42.55  E-value: 1.76e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 7019419  317 GYPNVGKSSVINTLRSKKVcNVAPIAGETK---VWQYITLMRRIFLIDCPGV 365
Cdd:cd01897   7 GYPNVGKSSLVNKLTRAKP-EVAPYPFTTKslfVGHFDYKYLRWQVIDTPGI 57
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 180-261 3.13e-04

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: 43.90  E-value: 3.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  180 RDLVTE------------DT-GVRnEAQEEIYKKGQSKRIwgelyKVIDSSDVVVQVLDARDPMGTRSPHIETYLKKekp 246
Cdd:COG0486 249 RDVIEEriniggipvrliDTaGLR-ETEDEVEKIGIERAR-----EAIEEADLVLLLLDASEPLTEEDEEILEKLKD--- 319

                        90
                ....*....|....*
gi 7019419  247 wKHLIFVLNKCDLVP 261
Cdd:COG0486 320 -KPVIVVLNKIDLPS 333
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 180-261 8.81e-04

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: 40.56  E-value: 8.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  180 RDLVTE------------DT-GVRnEAQEEIYKKGQsKRIWgelyKVIDSSDVVVQVLDARDPMGtrSPHIETYLKKEKp 246
Cdd:cd04164  39 RDVIEEeidlggipvrliDTaGLR-ETEDEIEKIGI-ERAR----EAIEEADLVLLVVDASEGLD--EEDLEILELPAK- 109

                        90
                ....*....|....*
gi 7019419  247 wKHLIFVLNKCDLVP 261
Cdd:cd04164 110 -KPVIVVLNKSDLLS 123
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 311-345 9.16e-04

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: 40.88  E-value: 9.16e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 7019419  311 ISVGFIGYPNVGKSSVINTLRSKKVCNVAPIAGET 345
Cdd:cd01895   3 IKIAIIGRPNVGKSSLLNALLGEERVIVSDIAGTT 37
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 314-366 1.12e-03

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: 40.46  E-value: 1.12e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7019419  314 GFIGYPNVGKSSVINTLRSKKVcNVAPIAGETK-----VWQYITLmRRIFLIDCPGVV 366
Cdd:cd01881   1 GLVGLPNVGKSTLLSALTSAKV-EIASYPFTTLepnvgVFEFGDG-VDIQIIDLPGLL 56
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
180-265 1.51e-03

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 41.63  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419   180 RDLVTE------------DT-GVRnEAQEEIYKKGQSKRiwgelYKVIDSSDVVVQVLDARDPMgTRSPHIETYLKKEKP 246
Cdd:PRK05291 251 RDVIEEhinldgiplrliDTaGIR-ETDDEVEKIGIERS-----REAIEEADLVLLVLDASEPL-TEEDDEILEELKDKP 323

                         90
                 ....*....|....*....
gi 7019419   247 wkhLIFVLNKCDLVPTWAT 265
Cdd:PRK05291 324 ---VIVVLNKADLTGEIDL 339
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
309-364 1.63e-03

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 42.01  E-value: 1.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 7019419   309 KQISVGFIGYPNVGKSSVINTLRS--KKVCNVAPIAGETKVWQYITLMRRIFLIDCPG 364
Cdd:PRK09554   2 KKLTIGLIGNPNSGKTTLFNQLTGarQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPG 59
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 249-365 1.68e-03

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


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 39.83  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419    249 HLIFVLNKCDLVPTWAT-KRWVAVLSQ-DYPTlaFHASLTNPFGKGAFIQLLrqfgklhtdKKQISVgFIGYPNVGKSSV 326
Cdd:pfam03193  55 EPVIVLNKIDLLDEEEElEELLKIYRAiGYPV--LFVSAKTGEGIEALKELL---------KGKTTV-LAGQSGVGKSTL 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 7019419    327 INTLRSKKVCNVAPIAGETKVWQYITLMRRIF-------LIDCPGV 365
Cdd:pfam03193 123 LNALLPELDLRTGEISEKLGRGRHTTTHVELFplpggglLIDTPGF 168
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 217-346 2.17e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 41.32  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419   217 SDVVVQVLDARDPMGTRSPHIETYLKKEKpwKHLIFVLNKCDLVPTW--ATKRWVAVLSQDYPTLAFHasltnpfGKGA- 293
Cdd:PRK09518 355 ADAVVFVVDGQVGLTSTDERIVRMLRRAG--KPVVLAVNKIDDQASEydAAEFWKLGLGEPYPISAMH-------GRGVg 425

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7019419   294 ---------FIQLLRQFGKLhTDKKQISVGFIGYPNVGKSSVINTLRSKKVCNVAPIAGETK 346
Cdd:PRK09518 426 dlldealdsLKVAEKTSGFL-TPSGLRRVALVGRPNVGKSSLLNQLTHEERAVVNDLAGTTR 486
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 180-261 2.25e-03

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


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 40.93  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419    180 RDLVTE------------DT-GVRnEAQEEIYKKGQSKRIwgelyKVIDSSDVVVQVLDARDPMgtrSPHIETYLKKEKP 246
Cdd:pfam12631 130 RDVIEEtiniggiplrliDTaGIR-ETDDEVEKIGIERAR-----EAIEEADLVLLVLDASRPL---DEEDLEILELLKD 200

                          90
                  ....*....|....*
gi 7019419    247 WKHLIFVLNKCDLVP 261
Cdd:pfam12631 201 KKPIIVVLNKSDLLG 215
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 178-258 2.27e-03

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


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 39.34  E-value: 2.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019419  178 KDRDLVTEDT-GV---RNEAQEEIY---------------KKGQSKRIWGELYKVIDSSDVVVQVLDARDPMGTRSPHIE 238
Cdd:cd01894  19 GRRDAIVSDTpGVtrdRKYGEAEWGgrefilidtggiepdDEGISKEIREQAEIAIEEADVILFVVDGREGLTPADEEIA 98

                        90       100
                ....*....|....*....|
gi 7019419  239 TYLKKEKpwKHLIFVLNKCD 258
Cdd:cd01894  99 KYLRKSK--KPVILVVNKID 116
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 212-261 2.40e-03

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


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 39.34  E-value: 2.40e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 7019419  212 KVIDSSDVVVQVLDARDPMGTRSPHIETYLKKEKpwKHLIFVLNKCDLVP 261
Cdd:cd01895  80 KAIERADVVLLVLDASEGITEQDLRIAGLILEEG--KALIIVVNKWDLVE 127
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 197-261 2.89e-03

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: 39.15  E-value: 2.89e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7019419  197 IYKKGQSKRIWGEL-YKVIDSSDVVVQVLDARDPMGTRSPHIETYLKKEKPwkhLIFVLNKCDLVP 261
Cdd:cd00880  56 LDEEGGLGRERVEEaRQVADRADLVLLVVDSDLTPVEEEAKLGLLRERGKP---VLLVLNKIDLVP 118
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 313-330 7.15e-03

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 38.22  E-value: 7.15e-03
                          10
                  ....*....|....*...
gi 7019419    313 VGFIGYPNVGKSSVINTL 330
Cdd:TIGR03598  21 IAFAGRSNVGKSSLINAL 38
 
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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