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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 153 DVILEVLDARDPLGTRCIDMEKMVRKADPSKRIVLLLNKIDLVPKESVEKWLTYLREEMPTVAFKCNTQEQRTKLGWKSS 232
Cdd:cd04178     1 DVILEVLDARDPLGCRCPQVERAVLVLGPNKKLVLVLNKIDLVPKENVEKWLKYLRNEFPTVAFKASTQQQKKNLSRKSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 233 KIDKSSNIPQSSDCLGAENLIKLLKNYSRSHELKLAITVGIVGLPNVGKSSLINSLKRSRVVNVGSTPGVTRSMQEVQLD 312
Cdd:cd04178    81 KVKASDDLLSSSACLGADALLKLLKNYARNKGIKTSITVGVVGYPNVGKSSVINSLKRSRACNVGATPGVTKSMQEVHLD 160

                         170
                  ....*....|.
gi 1002233346 313 KKVKLLDCPGV 323
Cdd:cd04178   161 KHVKLLDSPGV 171

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 269 ITVGIVGLPNVGKSSLINSLKRSRVVNVGSTPGVTRS--MQEVQLD---KKVKLLDCPGVV----MLKSSNSGVSVALRN 339
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNyvTTVIEEDgktYKFNLLDTAGQEdydaIRRLYYPQVERSLRV 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002233346 340 C---KRVEKMEDPISP-VKEILDLCPHEKLLSLYrvptFTSVD----DFLQKVATLRGKLKKGGIVDVEAAARI 405
Cdd:TIGR00231  82 FdivILVLDVEEILEKqTKEIIHHADSGVPIILV----GNKIDlkdaDLKTHVASEFAKLNGEPIIPLSAETGK 151

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 153 DVILEVLDARDPLGTRCIDMEKMVRKADPSKRIVLLLNKIDLVPKESVEKWLTYLREEMPTVAFKCNTQEQRTKLGWKSS 232
Cdd:cd04178     1 DVILEVLDARDPLGCRCPQVERAVLVLGPNKKLVLVLNKIDLVPKENVEKWLKYLRNEFPTVAFKASTQQQKKNLSRKSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 233 KIDKSSNIPQSSDCLGAENLIKLLKNYSRSHELKLAITVGIVGLPNVGKSSLINSLKRSRVVNVGSTPGVTRSMQEVQLD 312
Cdd:cd04178    81 KVKASDDLLSSSACLGADALLKLLKNYARNKGIKTSITVGVVGYPNVGKSSVINSLKRSRACNVGATPGVTKSMQEVHLD 160

                         170
                  ....*....|.
gi 1002233346 313 KKVKLLDCPGV 323
Cdd:cd04178   161 KHVKLLDSPGV 171

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 143 KELVKVIeasDVILEVLDARDPLGTRCIDMEKMVRKadpsKRIVLLLNKIDLVPKESVEKWLTYLREE-MPTVAFKCNTQ 221
Cdd:COG1161    18 KEILKLV---DLVIEVVDARIPLSSRNPMLDELVGN----KPRLLVLNKADLADPSVTKQWLKYFEKQgVDALAISAKKG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 222 EqrtklgwksskidkssnipqssdclGAENLIKLLKNYSRSHELKL-AITVGIVGLPNVGKSSLINSLKRSRVVNVGSTP 300
Cdd:COG1161    91 K-------------------------GIKELIEAIRELAPEKGIKRrPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNKP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 301 GVTRSMQEVQLDKKVKLLDCPGVVMLK--SSNSGVSVAlrnckrvekmedPISPVK-EILD-----------LCPH--EK 364
Cdd:COG1161   146 GVTKGQQWIKLDDGLELLDTPGILWPKfeDPEVGYKLA------------ATGAIKdEVLDleevalfllgyLARRypEL 213

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002233346 365 LLSLYRVPTF-TSVDDFLQKVATLRGKLKKGGIVDVEAAARIVLHDWNEGKI 415
Cdd:COG1161   214 LKERYKLDELpRTKLELLEAIGRKRGCLLSGGEVDLEKAAEILLTDFRSGKL 265

GNL3L/Grn1 putative GTPase; Grn1 (yeast) and GNL3L (human) are putative GTPases which are required for growth and play a role in processing of nucleolar pre-rRNA. This family contains a potential nuclear localization signal.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002233346  15 LRQKHKVLRKVKEHHRKKRKEAKKEGKSHRKKvEKDPGIPNEWPFKEQELKALEARRAQALQELELKKEARKERARKR 92
Cdd:pfam08701   1 LRKRYKIEKKVAEHHRKERKEAKKNPTWKSKK-KKDPGIPNSFPFKEEILAEIEEKKRKKEEEKERRKEAKKAERAEA 77

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 269 ITVGIVGLPNVGKSSLINSLKRSRVVNVGSTPGVTRS--MQEVQLD---KKVKLLDCPGVV----MLKSSNSGVSVALRN 339
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNyvTTVIEEDgktYKFNLLDTAGQEdydaIRRLYYPQVERSLRV 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002233346 340 C---KRVEKMEDPISP-VKEILDLCPHEKLLSLYrvptFTSVD----DFLQKVATLRGKLKKGGIVDVEAAARI 405
Cdd:TIGR00231  82 FdivILVLDVEEILEKqTKEIIHHADSGVPIILV----GNKIDlkdaDLKTHVASEFAKLNGEPIIPLSAETGK 151

Dynamin family;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 271 VGIVGLPNVGKSSLINSLKRSRVVNVGSTPgVTRSMQEVQLDKKVKLLDCPGVVMLKSSNSGVS--VALRN--CKRVEKM 346
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGP-TTRRPTVLRLGESPGASEGAVKVEYKDGEKKFEdfSELREeiEKETEKI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1002233346 347 E---DPISPVKEILDLC-PHEKLLSLYRVPTFTSVDDFLQKVA 385
Cdd:pfam00350  80 AgtgKGISSEPIVLEILsPLVPGLTLVDTPGLDSVAVGDQELT 122

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 153 DVILEVLDARDPLGTRCIDMEKMVRKADPSKRIVLLLNKIDLVPKESVEKWLTYLREEMPTVAFKCNTQEQRTKLGWKSS 232
Cdd:cd04178     1 DVILEVLDARDPLGCRCPQVERAVLVLGPNKKLVLVLNKIDLVPKENVEKWLKYLRNEFPTVAFKASTQQQKKNLSRKSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 233 KIDKSSNIPQSSDCLGAENLIKLLKNYSRSHELKLAITVGIVGLPNVGKSSLINSLKRSRVVNVGSTPGVTRSMQEVQLD 312
Cdd:cd04178    81 KVKASDDLLSSSACLGADALLKLLKNYARNKGIKTSITVGVVGYPNVGKSSVINSLKRSRACNVGATPGVTKSMQEVHLD 160

                         170
                  ....*....|.
gi 1002233346 313 KKVKLLDCPGV 323
Cdd:cd04178   161 KHVKLLDSPGV 171

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 141 FYKELVKVIEASDVILEVLDARDPLGTRCIDMEKMVRKADPSKRIVLLLNKIDLVPKESVEKWLTYLREEMPTVAFKcnt 220
Cdd:cd01857     1 VWRQLWRVIERSDVVVQIVDARNPLFFRCPDLEKYVKEVDPSKENVLLLNKADLVTEEQRKAWARYFKKEGIVVLFF--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 221 qeqrtklgwksskidkssnipqssdclgaenlikllknysrshELKLAITVGIVGLPNVGKSSLINSLKRSRVVNVGSTP 300
Cdd:cd01857    78 -------------------------------------------SALNEATIGLVGYPNVGKSSLINALVGSKKVSVSSTP 114

                         170       180
                  ....*....|....*....|....*
gi 1002233346 301 GVTRSMQEVQLDKKVKLLDCPGVVM 325
Cdd:cd01857   115 GKTKHFQTIFLEPGITLCDCPGLVF 139

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 143 KELVKVIeasDVILEVLDARDPLGTRCIDMEKMVrkadPSKRIVLLLNKIDLVPKESVEKWLTYLREEmPTVAFKCNTQE 222
Cdd:TIGR03596  16 KENLKLV---DVVIEVLDARIPLSSRNPMIDEIR----GNKPRLIVLNKADLADPAVTKQWLKYFEEK-GIKALAVNAKK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 223 QRTKLgwksskidkssNIPQSSDCLGAEnliKLLKNYSRSHELKlAITVGIVGLPNVGKSSLINSLKRSRVVNVGSTPGV 302
Cdd:TIGR03596  88 GAGVK-----------KIIKAAKKLLKE---KNEKLKAKGLKNR-PIRAMIVGIPNVGKSTLINRLAGKKVAKVGNRPGV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 303 TRSMQEVQLDKKVKLLDCPGVVMLKSSN--SGVSVALRNCKRVEKMEDP---ISPVKEILDLCPhEKLLSLYRVPTF-TS 376
Cdd:TIGR03596 153 TKGQQWIKLSDNLELLDTPGILWPKFEDqeVGLKLAATGAIKDEALDLEdvaLFLLEYLLEHYP-ELLKERYKLDELpED 231

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1002233346 377 VDDFLQKVATLRGKLKKGGIVDVEAAARIVLHDWNEGKI 415
Cdd:TIGR03596 232 PVELLEAIAKKRGCLLKGGELDLDRAAEILLNDFRKGKL 270

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 143 KELVKVIeasDVILEVLDARDPLGTRCIDMEKMVRKadpsKRIVLLLNKIDLVPKESVEKWLTYLREEMPTVAFKCNTQe 222
Cdd:cd01856    14 KEKLKLV---DVVIEVRDARIPLSSRNPDLDKILGN----KPRLIVLNKADLADPAKTKKWLKYFKSQGEPVLFVNAKN- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 223 qrtklGWKSSKIDKSsnipqssdclgAENLIKLLKNYSRSHELKLAITVGIVGLPNVGKSSLINSLKRSRVVNVGSTPGV 302
Cdd:cd01856    86 -----GKGVKKLLKK-----------AKKLLKENEKLKAKGLLPRPLRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPGV 149

                         170       180
                  ....*....|....*....|.
gi 1002233346 303 TRSMQEVQLDKKVKLLDCPGV 323
Cdd:cd01856   150 TRGQQWIRIGPNIELLDTPGI 170

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002233346 270 TVGIVGLPNVGKSSLINSLKRSRVVnVGSTPGVTRSMQEVQL---DKKVKLLDCPGVVMLKSSNSGVSVALRNCKRVE 344
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAI-VSDYPGTTRDPNEGRLelkGKQIILVDTPGLIEGASEGEGLGRAFLAIIEAD 77

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 139 RAFYKELVKVIEASD-VILEVLDARDPLGTRCIDMEKMVRKadpsKRIVLLLNKIDLVPKES----VEKWL-TYLReemp 212
Cdd:cd01855    20 DEDFLEILSTLLNDNaLVVHVVDIFDFPGSLIPGLAELIGA----KPVILVGNKIDLLPKDVkpnrLKQWVkKRLK---- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 213 tvafkcntqeqrtKLGWKSSKI-----DKSSNIpqssdclgaENLIKLLKNYsrsheLKLAITVGIVGLPNVGKSSLINS 287
Cdd:cd01855    92 -------------IGGLKIKDVilvsaKKGWGV---------EELIEEIKKL-----AKYRGDVYVVGATNVGKSTLINA 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1002233346 288 L--------KRSRVVNVGST---PGVTRSMQEVQLDKKVKLLDCPGV 323
Cdd:cd01855   145 LlksnggkvQAQALVQRLTVspiPGTTLGLIKIPLGEGKKLYDTPGI 191

ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of GTPases involved in ribosome biogenesis. Like YqlF, it shows a cyclical permutation relative to GTPases EngA (in which the GTPase domain is duplicated), Era, and others. Members of this protein family are found in a relatively small number of bacterial species, including Bacillus subtilis but not Escherichia coli. [Protein synthesis, Other]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 141 FYKELVKVIEASDVILEVLDARDPLGTRCIDMEKMVRKadpsKRIVLLLNKIDLVPKES-VEKWLTYLREEmptvaFKcn 219
Cdd:TIGR03597  53 FLNLLNSLGDSNALIVYVVDIFDFEGSLIPELKRFVGG----NPVLLVGNKIDLLPKSVnLSKIKEWMKKR-----AK-- 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 220 tqeqrtKLGWKSSKID-KSSNIPQSSDclgaeNLIKLLKNYSRSHElklaitVGIVGLPNVGKSSLINSL-----KRSRV 293
Cdd:TIGR03597 122 ------ELGLKPVDIIlVSAKKGNGID-----ELLDKIKKARNKKD------VYVVGVTNVGKSSLINKLlkqnnGDKDV 184

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1002233346 294 VNVGSTPGVTRSMQEVQLDKKVKLLDCPGVV 324
Cdd:TIGR03597 185 ITTSPFPGTTLDLIEIPLDDGHSLYDTPGII 215

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002233346 273 IVGLPNVGKSSLINSLKRSRVVNVGSTPGVTRSMQEVQ---LDKKVKLLDCPGVV 324
Cdd:cd01894     2 IVGRPNVGKSTLFNRLTGRRDAIVSDTPGVTRDRKYGEaewGGREFILIDTGGIE 56

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002233346 272 GIVGLPNVGKSSLINSLKRSRVVNVGSTPGVTRSMQ----EVQLDKKVKLLDCPGV 323
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVrkewELLPLGPVVLIDTPGL 56

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002233346 272 GIVGLPNVGKSSLINSLKRSRVVNVGSTPGVTR-----SMQEVQLDKKVKLLDCPG 322
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRdpdvyVKELDKGKVKLVLVDTPG 56

GTP-binding protein Der; Reviewed

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002233346 270 TVGIVGLPNVGKSSLINSLKRSRVVNVGSTPGVTRSMQEVQ---LDKKVKLLDCPGVV 324
Cdd:PRK00093    3 VVAIVGRPNVGKSTLFNRLTGKRDAIVADTPGVTRDRIYGEaewLGREFILIDTGGIE 60

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 268 AITVGIVGLPNVGKSSLINSL-KRSRVVnVGSTPGVTRSMQEVQL---DKKVKLLDCPGV 323
Cdd:cd01895     2 PIKIAIIGRPNVGKSSLLNALlGEERVI-VSDIAGTTRDSIDVPFeydGQKYTLIDTAGI 60

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002233346 273 IVGLPNVGKSSLINSLKRSRvVNVGSTPGVT--RSMQEVQL-DKKVKLLDCPGV 323
Cdd:cd01879     2 LVGNPNVGKTTLFNALTGAR-QKVGNWPGVTveKKEGEFKLgGKEIEIVDLPGT 54

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1002233346 278 NVGKSSLINSL-KRSRVVNVGSTPGVTRSMQEVQLDKKVKLLDCPG 322
Cdd:COG0218    33 NVGKSSLINALtNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPG 78

GTPase CgtA; Reviewed

                          10        20
                  ....*....|....*....|....*....
gi 1002233346 264 ELKLAITVGIVGLPNVGKSSLINSLKRSR 292
Cdd:PRK12299  154 ELKLLADVGLVGLPNAGKSTLISAVSAAK 182

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002233346 269 ITVGIVGLPNVGKSSLINSLKRSRVVNVGSTPGVTRSMQEVQLD---KKVKLLD 319
Cdd:cd04164     4 IKVVIAGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDVIEEEIDlggIPVRLID 57

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233346 135 DHSERAFYKELVKVIEASDVILEVLDARdplGTRCIDMEKMVRKADPSKRIVLLLNKIDLVPkESVEKWLTYLREEM--- 211
Cdd:cd00880    60 GGLGRERVEEARQVADRADLVLLVVDSD---LTPVEEEAKLGLLRERGKPVLLVLNKIDLVP-ESEEEELLRERKLEllp 135

                          90       100
                  ....*....|....*....|.
gi 1002233346 212 --PTVAFKCNTQEQRTKLGWK 230
Cdd:cd00880   136 dlPVIAVSALPGEGIDELRKK 156

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.

                          10        20
                  ....*....|....*....|..
gi 1002233346 271 VGIVGLPNVGKSSLINSLKRSR 292
Cdd:cd01898     3 VGLVGLPNAGKSTLLSAISNAK 24

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002233346 250 ENLIKLLKNYSRSHELKLAITVGIVGLPNVGKSSLINSL-KRSR--VVNVgstPGVTRSMQEVQLD---KKVKLLD 319
Cdd:COG0486   195 EELEALLASARQGELLREGIKVVIVGRPNVGKSSLLNALlGEERaiVTDI---AGTTRDVIEERINiggIPVRLID 267

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002233346 250 ENLIKLLKNYSRSHELKLAITVGIVGLPNVGKSSLINSL-KRSRVVnVGSTPGVTRSMQEVQLD---KKVKLLD 319
Cdd:pfam12631  76 AELEKLLATADRGRILREGIKVVIVGKPNVGKSSLLNALlGEERAI-VTDIPGTTRDVIEETINiggIPLRLID 148

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002233346 272 GIVGLPNVGKSSLINSLKRSRvVNVGSTPGVTRSMQEVQLD----KKVKLLDCPGVV 324
Cdd:cd01881     1 GLVGLPNVGKSTLLSALTSAK-VEIASYPFTTLEPNVGVFEfgdgVDIQIIDLPGLL 56

Predicted GTPase [General function prediction only];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002233346 254 KLLKNYSRSHELKLAITVGIVGLPNVGKSSLINSLKRSRVVNVGSTPGVTRSMQEVQL----DKKVKLLDCPGV 323
Cdd:COG3596    25 LLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLesdgLPGLVLLDTPGL 98