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Conserved domains on  [gi|2449300333|ref|NP_001403958|]
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large subunit GTPase 1 homolog isoform 3 [Mus musculus]

Protein Classification

HSR1_MMR1 and RbgA domain-containing protein( domain architecture ID 12923183)

HSR1_MMR1 and RbgA domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 163-429 3.64e-75

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: 236.74  E-value: 3.64e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 163 FWRQLWRVIERSDIVVQIVDARNPLLFRCEDLECYVKEIDAAKENVILINKADLLTAEQRFAWAVHFEKEGVKVIFWSAL 242
Cdd:cd01857     1 VWRQLWRVIERSDVVVQIVDARNPLFFRCPDLEKYVKEVDPSKENVLLLNKADLVTEEQRKAWARYFKKEGIVVLFFSAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 243 AETdhlngdlkevdsvagdtnktesesssldaneiphrdlislseesasdsgdskyedcqedeeedwqtcseedsvpeee 322
Cdd:cd01857    81 NEA----------------------------------------------------------------------------- 83

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 323 egcnadsetqnrknaenqqvnndsylvskqellelfkklhtgkkvkdgqlTVGLVGYPNVGKSSTINTIMGNKKVSVSAT 402
Cdd:cd01857    84 --------------------------------------------------TIGLVGYPNVGKSSLINALVGSKKVSVSST 113

                         250       260
                  ....*....|....*....|....*..
gi 2449300333 403 PGHTKHFQTLYVEPGLCLCDCPGLVMP 429
Cdd:cd01857   114 PGKTKHFQTIFLEPGITLCDCPGLVFP 140
RbgA super family cl34151
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
175-529 1.85e-18

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


The actual alignment was detected with superfamily member COG1161:

Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 85.93  E-value: 1.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 175 DIVVQIVDAR------NPLLfrcedlecyvKEIDAAKENVILINKADLLTAEQRFAWAVHFEKEGVKVIfwsalaetdhl 248
Cdd:COG1161    25 DLVIEVVDARiplssrNPML----------DELVGNKPRLLVLNKADLADPSVTKQWLKYFEKQGVDAL----------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 249 ngdlkevdsvagdtnktesesssldaneiphrdLISlseesasdsgdskyedcqedeeedwqtcseedsvpeeeegcnad 328
Cdd:COG1161    84 ---------------------------------AIS-------------------------------------------- 86

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 329 seTQNRKNAenqqvnndsylvskQELLELFKKLHTGKKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKH 408
Cdd:COG1161    87 --AKKGKGI--------------KELIEAIRELAPEKGIKRRPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKG 150

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 409 FQTLYVEPGLCLCDCPGLVMPSFVS---------TKAemICNGILPIDQ--------MRDHVPpvslvcQNIPRRvlevt 471
Cdd:COG1161   151 QQWIKLDDGLELLDTPGILWPKFEDpevgyklaaTGA--IKDEVLDLEEvalfllgyLARRYP------ELLKER----- 217

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300333 472 YGINIIkprededpyrPPTSEELLTAYGCMRGFMTAHGQPDQPRSARYILKDYVGGKL 529
Cdd:COG1161   218 YKLDEL----------PRTKLELLEAIGRKRGCLLSGGEVDLEKAAEILLTDFRSGKL 265
 
Name Accession Description Interval E-value
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 163-429 3.64e-75

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: 236.74  E-value: 3.64e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 163 FWRQLWRVIERSDIVVQIVDARNPLLFRCEDLECYVKEIDAAKENVILINKADLLTAEQRFAWAVHFEKEGVKVIFWSAL 242
Cdd:cd01857     1 VWRQLWRVIERSDVVVQIVDARNPLFFRCPDLEKYVKEVDPSKENVLLLNKADLVTEEQRKAWARYFKKEGIVVLFFSAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 243 AETdhlngdlkevdsvagdtnktesesssldaneiphrdlislseesasdsgdskyedcqedeeedwqtcseedsvpeee 322
Cdd:cd01857    81 NEA----------------------------------------------------------------------------- 83

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 323 egcnadsetqnrknaenqqvnndsylvskqellelfkklhtgkkvkdgqlTVGLVGYPNVGKSSTINTIMGNKKVSVSAT 402
Cdd:cd01857    84 --------------------------------------------------TIGLVGYPNVGKSSLINALVGSKKVSVSST 113

                         250       260
                  ....*....|....*....|....*..
gi 2449300333 403 PGHTKHFQTLYVEPGLCLCDCPGLVMP 429
Cdd:cd01857   114 PGKTKHFQTIFLEPGITLCDCPGLVFP 140
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
175-529 1.85e-18

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 85.93  E-value: 1.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 175 DIVVQIVDAR------NPLLfrcedlecyvKEIDAAKENVILINKADLLTAEQRFAWAVHFEKEGVKVIfwsalaetdhl 248
Cdd:COG1161    25 DLVIEVVDARiplssrNPML----------DELVGNKPRLLVLNKADLADPSVTKQWLKYFEKQGVDAL----------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 249 ngdlkevdsvagdtnktesesssldaneiphrdLISlseesasdsgdskyedcqedeeedwqtcseedsvpeeeegcnad 328
Cdd:COG1161    84 ---------------------------------AIS-------------------------------------------- 86

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 329 seTQNRKNAenqqvnndsylvskQELLELFKKLHTGKKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKH 408
Cdd:COG1161    87 --AKKGKGI--------------KELIEAIRELAPEKGIKRRPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKG 150

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 409 FQTLYVEPGLCLCDCPGLVMPSFVS---------TKAemICNGILPIDQ--------MRDHVPpvslvcQNIPRRvlevt 471
Cdd:COG1161   151 QQWIKLDDGLELLDTPGILWPKFEDpevgyklaaTGA--IKDEVLDLEEvalfllgyLARRYP------ELLKER----- 217

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300333 472 YGINIIkprededpyrPPTSEELLTAYGCMRGFMTAHGQPDQPRSARYILKDYVGGKL 529
Cdd:COG1161   218 YKLDEL----------PRTKLELLEAIGRKRGCLLSGGEVDLEKAAEILLTDFRSGKL 265
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 175-529 2.05e-17

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: 82.94  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 175 DIVVQIVDARNPLLFRCEDLECYVKEidaaKENVILINKADLLTAEQRFAWAVHFEKEGVKVIFwsalaetdhlngdlke 254
Cdd:TIGR03596  23 DVVIEVLDARIPLSSRNPMIDEIRGN----KPRLIVLNKADLADPAVTKQWLKYFEEKGIKALA---------------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 255 VDSVAGDtnktesessslDANEIphrdlISLSEESASDsgdskyedcqedeeedwqtcseedsvpeeeegcnadsetqnr 334
Cdd:TIGR03596  83 VNAKKGA-----------GVKKI-----IKAAKKLLKE------------------------------------------ 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 335 KNAENQQvnndsylvskqellelfkklhtgKKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKHFQTLYV 414
Cdd:TIGR03596 105 KNEKLKA-----------------------KGLKNRPIRAMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQQWIKL 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 415 EPGLCLCDCPGLVMPSF----VSTK-AemICNGI----LPIDQMRDHVppVSLVCQNIPRRVLEvTYGINIikprEDEDP 485
Cdd:TIGR03596 162 SDNLELLDTPGILWPKFedqeVGLKlA--ATGAIkdeaLDLEDVALFL--LEYLLEHYPELLKE-RYKLDE----LPEDP 232

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2449300333 486 yrpptsEELLTAYGCMRGFMTAHGQPDQPRSARYILKDYVGGKL 529
Cdd:TIGR03596 233 ------VELLEAIAKKRGCLLKGGELDLDRAAEILLNDFRKGKL 270
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 373-427 2.21e-14

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: 69.57  E-value: 2.21e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300333 373 TVGLVGYPNVGKSSTINTIMGnKKVSVSATPGHTKHFQTLYVEPG---LCLCDCPGLV 427
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTG-AKAIVSDYPGTTRDPNEGRLELKgkqIILVDTPGLI 57
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 369-425 2.05e-08

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: 54.40  E-value: 2.05e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2449300333 369 DGQLTVGLVGYPNVGKSSTINTIMGNKKVS-VSATPGHTKH---FQtlyVEPGLCLCDCPG 425
Cdd:TIGR03598  16 DDGPEIAFAGRSNVGKSSLINALTNRKKLArTSKTPGRTQLinfFE---VNDGFRLVDLPG 73
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 374-425 5.29e-08

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


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 53.54  E-value: 5.29e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2449300333 374 VGLVGYPNVGKSSTINTIMGNKK-VSVSATPGHTK---HFQtlyVEPGLCLCDCPG 425
Cdd:COG0218    26 IAFAGRSNVGKSSLINALTNRKKlARTSKTPGKTQlinFFL---INDKFYLVDLPG 78
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 353-406 7.13e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 45.81  E-value: 7.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2449300333 353 ELLELFKKLHTGKKVKDGqLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHT 406
Cdd:PRK00093  156 AILEELPEEEEEDEEDEP-IKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTT 208
 
Name Accession Description Interval E-value
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 163-429 3.64e-75

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: 236.74  E-value: 3.64e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 163 FWRQLWRVIERSDIVVQIVDARNPLLFRCEDLECYVKEIDAAKENVILINKADLLTAEQRFAWAVHFEKEGVKVIFWSAL 242
Cdd:cd01857     1 VWRQLWRVIERSDVVVQIVDARNPLFFRCPDLEKYVKEVDPSKENVLLLNKADLVTEEQRKAWARYFKKEGIVVLFFSAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 243 AETdhlngdlkevdsvagdtnktesesssldaneiphrdlislseesasdsgdskyedcqedeeedwqtcseedsvpeee 322
Cdd:cd01857    81 NEA----------------------------------------------------------------------------- 83

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 323 egcnadsetqnrknaenqqvnndsylvskqellelfkklhtgkkvkdgqlTVGLVGYPNVGKSSTINTIMGNKKVSVSAT 402
Cdd:cd01857    84 --------------------------------------------------TIGLVGYPNVGKSSLINALVGSKKVSVSST 113

                         250       260
                  ....*....|....*....|....*..
gi 2449300333 403 PGHTKHFQTLYVEPGLCLCDCPGLVMP 429
Cdd:cd01857   114 PGKTKHFQTIFLEPGITLCDCPGLVFP 140
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 175-426 1.15e-22

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: 94.37  E-value: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 175 DIVVQIVDARNPLLFRCEDLECYVKEidAAKENVILINKADLLTAEQRFAW-AVHFEKEGVKVIFWSALAetdhlngdlk 253
Cdd:cd01849     1 DVVVEVVDARDPLSSRNPDIEVLINE--KNKKLIMVLNKADLVPKEVLRKWvAELSELYGTKTFFISATN---------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 254 evdsvagdtnktesesssldaneiphrdlislseesasdsgdskyedcqedeeedwqtcseedsvpeeeegcnaDSETQN 333
Cdd:cd01849    69 --------------------------------------------------------------------------GQGILK 74

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 334 RKNAENQQVNndsylvskqellelfkklhtgKKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKHFQTLY 413
Cdd:cd01849    75 LKAEITKQKL---------------------KLKYKKGIRVGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQDVK 133

                         250
                  ....*....|...
gi 2449300333 414 VEPGLCLCDCPGL 426
Cdd:cd01849   134 LDKEIYLYDTPGI 146
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 175-425 2.59e-20

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: 88.40  E-value: 2.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 175 DIVVQIVDARNPLLFRCEDLECYVKEIDAAKENVILINKADLLTAEQRFAWAVHFEKEGVKVIFWSAlaetdhlngdlke 254
Cdd:cd04178     1 DVILEVLDARDPLGCRCPQVERAVLVLGPNKKLVLVLNKIDLVPKENVEKWLKYLRNEFPTVAFKAS------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 255 vdsvagdtnkTESESSSLDANEIPHRDLISLSEESASDSGDskyedcqedeeedwqtcseedsvpeeeegcnadsetqnr 334
Cdd:cd04178    68 ----------TQQQKKNLSRKSKKVKASDDLLSSSACLGAD--------------------------------------- 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 335 knaenqqvnndsylvskqELLELFKKLHTGKKVKDGqLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKHFQTLYV 414
Cdd:cd04178    99 ------------------ALLKLLKNYARNKGIKTS-ITVGVVGYPNVGKSSVINSLKRSRACNVGATPGVTKSMQEVHL 159

                         250
                  ....*....|.
gi 2449300333 415 EPGLCLCDCPG 425
Cdd:cd04178   160 DKHVKLLDSPG 170
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 164-425 4.21e-19

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: 84.68  E-value: 4.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 164 WRQLWRVIERSDIVVQIVDARNPLLFRCEDLECYVKEIDaaKENVILINKADLLTAEQRFAWAVHFEKEGVKVIFWSALA 243
Cdd:cd01859     2 KRLVRRIIKEADVVLEVVDARDPELTRSRKLERMALELG--KKLIIVLNKADLVPREVLEKWKEVFESEGLPVVYVSARE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 244 E--TDHLNGDLKEvdsVAGDtnktesesssldaneiphrdlislseesasdsgdskyedcqedeeedwqtcseedsvpee 321
Cdd:cd01859    80 RlgTRILRRTIKE---LAID------------------------------------------------------------ 96

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 322 eegcnadsetqnrknaenqqvnndsylvskqellelfkklhtGKKVKdgqltVGLVGYPNVGKSSTINTIMGNKKVSVSA 401
Cdd:cd01859    97 ------------------------------------------GKPVI-----VGVVGYPKVGKSSIINALKGRHSASTSP 129

                         250       260
                  ....*....|....*....|....*..
gi 2449300333 402 T---PGHTKHFQTLYVEPGLCLCDCPG 425
Cdd:cd01859   130 IpgsPGYTKGIQLVRIDSKIYLIDTPG 156
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
175-529 1.85e-18

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 85.93  E-value: 1.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 175 DIVVQIVDAR------NPLLfrcedlecyvKEIDAAKENVILINKADLLTAEQRFAWAVHFEKEGVKVIfwsalaetdhl 248
Cdd:COG1161    25 DLVIEVVDARiplssrNPML----------DELVGNKPRLLVLNKADLADPSVTKQWLKYFEKQGVDAL----------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 249 ngdlkevdsvagdtnktesesssldaneiphrdLISlseesasdsgdskyedcqedeeedwqtcseedsvpeeeegcnad 328
Cdd:COG1161    84 ---------------------------------AIS-------------------------------------------- 86

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 329 seTQNRKNAenqqvnndsylvskQELLELFKKLHTGKKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKH 408
Cdd:COG1161    87 --AKKGKGI--------------KELIEAIRELAPEKGIKRRPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKG 150

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 409 FQTLYVEPGLCLCDCPGLVMPSFVS---------TKAemICNGILPIDQ--------MRDHVPpvslvcQNIPRRvlevt 471
Cdd:COG1161   151 QQWIKLDDGLELLDTPGILWPKFEDpevgyklaaTGA--IKDEVLDLEEvalfllgyLARRYP------ELLKER----- 217

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300333 472 YGINIIkprededpyrPPTSEELLTAYGCMRGFMTAHGQPDQPRSARYILKDYVGGKL 529
Cdd:COG1161   218 YKLDEL----------PRTKLELLEAIGRKRGCLLSGGEVDLEKAAEILLTDFRSGKL 265
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
 166-425 4.09e-18

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: 81.58  E-value: 4.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 166 QLWRVIERSDIVVQIVDARNPLLFRCEDLECYVKEIDAAKENVILINKADLLTAEQRFAWAVHFEKEGVKVIFwsalaet 245
Cdd:cd01858     1 ELYKVIDSSDVIIQVLDARDPMGTRCKHVEKYLRKEKPHKHLIFVLNKCDLVPTWVTKRWVKVLSKEYPTLAF------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 246 dhlngdlkevdsvagdtnktesesssldaneiphrdlislseeSASdsgdskyedcqedeeedwqtcseedsvpeeeegc 325
Cdd:cd01858    74 -------------------------------------------HAS---------------------------------- 76

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 326 nadsetqnrknaenqqVNNDSYLVSKQELLELFKKLHTGKKvkdgQLTVGLVGYPNVGKSSTINTiMGNKKV-SVSATPG 404
Cdd:cd01858    77 ----------------ITNPFGKGALINLLRQFAKLHSDKK----QISVGFIGYPNVGKSSVINT-LRSKKVcKVAPIPG 135

                         250       260
                  ....*....|....*....|.
gi 2449300333 405 HTKHFQTLYVEPGLCLCDCPG 425
Cdd:cd01858   136 ETKVWQYITLMKRIYLIDCPG 156
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 175-529 2.05e-17

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: 82.94  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 175 DIVVQIVDARNPLLFRCEDLECYVKEidaaKENVILINKADLLTAEQRFAWAVHFEKEGVKVIFwsalaetdhlngdlke 254
Cdd:TIGR03596  23 DVVIEVLDARIPLSSRNPMIDEIRGN----KPRLIVLNKADLADPAVTKQWLKYFEEKGIKALA---------------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 255 VDSVAGDtnktesessslDANEIphrdlISLSEESASDsgdskyedcqedeeedwqtcseedsvpeeeegcnadsetqnr 334
Cdd:TIGR03596  83 VNAKKGA-----------GVKKI-----IKAAKKLLKE------------------------------------------ 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 335 KNAENQQvnndsylvskqellelfkklhtgKKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKHFQTLYV 414
Cdd:TIGR03596 105 KNEKLKA-----------------------KGLKNRPIRAMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQQWIKL 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 415 EPGLCLCDCPGLVMPSF----VSTK-AemICNGI----LPIDQMRDHVppVSLVCQNIPRRVLEvTYGINIikprEDEDP 485
Cdd:TIGR03596 162 SDNLELLDTPGILWPKFedqeVGLKlA--ATGAIkdeaLDLEDVALFL--LEYLLEHYPELLKE-RYKLDE----LPEDP 232

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2449300333 486 yrpptsEELLTAYGCMRGFMTAHGQPDQPRSARYILKDYVGGKL 529
Cdd:TIGR03596 233 ------VELLEAIAKKRGCLLKGGELDLDRAAEILLNDFRKGKL 270
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 373-427 2.21e-14

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: 69.57  E-value: 2.21e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300333 373 TVGLVGYPNVGKSSTINTIMGnKKVSVSATPGHTKHFQTLYVEPG---LCLCDCPGLV 427
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTG-AKAIVSDYPGTTRDPNEGRLELKgkqIILVDTPGLI 57
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 175-425 3.74e-12

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: 64.86  E-value: 3.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 175 DIVVQIVDARNPLLFRCEDLEcyvkEIDAAKENVILINKADLLTAEQRFAWAVHFEKEGVKVIFwsalaetdhlngdlke 254
Cdd:cd01856    21 DVVIEVRDARIPLSSRNPDLD----KILGNKPRLIVLNKADLADPAKTKKWLKYFKSQGEPVLF---------------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 255 VDSVAGDTNKtesesssldaneiphrdlislseesasdsgdskyedcqedeeedwqtcseedsvpeeeegcnadsetQNR 334
Cdd:cd01856    81 VNAKNGKGVK-------------------------------------------------------------------KLL 93

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 335 KNAENQQVNNDSYLVskqellelfkklhtgKKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKHFQTLYV 414
Cdd:cd01856    94 KKAKKLLKENEKLKA---------------KGLLPRPLRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTRGQQWIRI 158

                         250
                  ....*....|.
gi 2449300333 415 EPGLCLCDCPG 425
Cdd:cd01856   159 GPNIELLDTPG 169
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 374-425 2.13e-09

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: 57.14  E-value: 2.13e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2449300333 374 VGLVGYPNVGKSSTINTIMGNKKVS-VSATPGHTK---HFQtlyVEPGLCLCDCPG 425
Cdd:cd01876     2 VAFAGRSNVGKSSLINALTNRKKLArTSKTPGRTQlinFFN---VGDKFRLVDLPG 54
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 369-425 2.05e-08

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: 54.40  E-value: 2.05e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2449300333 369 DGQLTVGLVGYPNVGKSSTINTIMGNKKVS-VSATPGHTKH---FQtlyVEPGLCLCDCPG 425
Cdd:TIGR03598  16 DDGPEIAFAGRSNVGKSSLINALTNRKKLArTSKTPGRTQLinfFE---VNDGFRLVDLPG 73
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 374-425 5.29e-08

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


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 53.54  E-value: 5.29e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2449300333 374 VGLVGYPNVGKSSTINTIMGNKK-VSVSATPGHTK---HFQtlyVEPGLCLCDCPG 425
Cdd:COG0218    26 IAFAGRSNVGKSSLINALTNRKKlARTSKTPGKTQlinFFL---INDKFYLVDLPG 78
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 375-427 2.46e-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: 50.92  E-value: 2.46e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300333 375 GLVGYPNVGKSSTINTIMGNKKVSVSATPGHT-----KHFQTLYVEPGLCLCDCPGLV 427
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTrdpdvYVKELDKGKVKLVLVDTPGLD 58
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
 351-401 1.23e-06

Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon.


Pssm-ID: 206652  Cd Length: 248  Bit Score: 50.01  E-value: 1.23e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2449300333 351 KQELLELfkkLHTGKKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSA 401
Cdd:cd01853    14 QTKLHEL---EAKLKKELDFSLTILVLGKTGVGKSSTINSIFGERKVSVSA 61
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
368-427 2.95e-06

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 49.80  E-value: 2.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300333 368 KDGQLTVGLVGYPNVGKSSTINTiMGNKKVSVSATPghtkhFQTLYVEPGLC--------LCDCPGLV 427
Cdd:COG1163    60 KSGDATVVLVGFPSVGKSTLLNK-LTNAKSEVGAYE-----FTTLDVVPGMLeykgakiqILDVPGLI 121
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 351-406 9.67e-06

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: 47.86  E-value: 9.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2449300333 351 KQELLELFKKLHTGKKVKDGqLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHT 406
Cdd:pfam12631  75 LAELEKLLATADRGRILREG-IKVVIVGKPNVGKSSLLNALLGEERAIVTDIPGTT 129
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 375-408 1.55e-05

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: 45.70  E-value: 1.55e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2449300333 375 GLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKH 408
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRD 34
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 372-406 1.73e-05

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: 45.50  E-value: 1.73e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2449300333 372 LTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHT 406
Cdd:cd01895     3 IKIAIIGRPNVGKSSLLNALLGEERVIVSDIAGTT 37
YeeP COG3596
Predicted GTPase [General function prediction only];
356-426 2.17e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 47.07  E-value: 2.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2449300333 356 ELFKKLHTgKKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKHFQtLYV-----EPGLCLCDCPGL 426
Cdd:COG3596    25 LLAEALER-LLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQ-RYRlesdgLPGLVLLDTPGL 98
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 171-242 2.90e-05

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: 44.72  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 171 IERSDIVVQIVDA---RNPLlfrcEDLECYVKEIDAAKEN------VILINKADLLTAEQRFAWAVHFEKE--GVKVIFW 239
Cdd:cd01898    76 IERTRVLLHVIDLsgeDDPV----EDYETIRNELEAYNPGlaekprIVVLNKIDLLDAEERFEKLKELLKElkGKKVFPI 151


                  ...
gi 2449300333 240 SAL 242
Cdd:cd01898   152 SAL 154
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 374-415 3.36e-05

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: 44.67  E-value: 3.36e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2449300333 374 VGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKHFQTLYVE 415
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIE 45
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 374-429 6.79e-05

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: 43.60  E-value: 6.79e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2449300333 374 VGLVGYPNVGKSSTINTIMGnKKVS-VSATPGHTKH----------FQTLYVepglclcDCPGLVMP 429
Cdd:cd04163     6 VAIIGRPNVGKSTLLNALVG-QKISiVSPKPQTTRNrirgiytdddAQIIFV-------DTPGIHKP 64
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 353-406 7.13e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 45.81  E-value: 7.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2449300333 353 ELLELFKKLHTGKKVKDGqLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHT 406
Cdd:PRK00093  156 AILEELPEEEEEDEEDEP-IKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTT 208
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 351-406 7.21e-05

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: 45.82  E-value: 7.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2449300333 351 KQELLELFKKLHTGKKVKDGqLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHT 406
Cdd:COG0486   194 REELEALLASARQGELLREG-IKVVIVGRPNVGKSSLLNALLGEERAIVTDIAGTT 248
3a0901s02IAP34 TIGR00991
GTP-binding protein (Chloroplast Envelope Protein Translocase); [Transport and binding ...
 350-436 1.02e-04

GTP-binding protein (Chloroplast Envelope Protein Translocase); [Transport and binding proteins, Nucleosides, purines and pyrimidines]


Pssm-ID: 130064  Cd Length: 313  Bit Score: 44.89  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 350 SKQELLELFKKLhtgKKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSAtpghtkhFQTLYVEP----------GLC 419
Cdd:TIGR00991  20 TQTKLLELLGKL---KEEDVSSLTILVMGKGGVGKSSTVNSIIGERIATVSA-------FQSEGLRPmmvsrtragfTLN 89

                          90
                  ....*....|....*..
gi 2449300333 420 LCDCPGLVMPSFVSTKA 436
Cdd:TIGR00991  90 IIDTPGLIEGGYINDQA 106
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
353-406 1.83e-04

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 44.24  E-value: 1.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2449300333 353 ELLELFKKlHTGKKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHT 406
Cdd:COG1160   158 AVLELLPE-EEEEEEEDDPIKIAIVGRPNVGKSSLINALLGEERVIVSDIAGTT 210
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 356-426 1.92e-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: 43.02  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 356 ELFKKLHTGKKVKDgqlTVGLVGYPNVGKSSTINTI-----------MGNKKVSVSATPGHTKHFQTLYVEPGLCLCDCP 424
Cdd:cd01855   113 ELIEEIKKLAKYRG---DVYVVGATNVGKSTLINALlksnggkvqaqALVQRLTVSPIPGTTLGLIKIPLGEGKKLYDTP 189


                  ..
gi 2449300333 425 GL 426
Cdd:cd01855   190 GI 191
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
351-406 3.81e-04

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 43.18  E-value: 3.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2449300333 351 KQELLELFKKLHTGKKVKDGqLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHT 406
Cdd:PRK05291  196 IAELEALLASARQGEILREG-LKVVIAGRPNVGKSSLLNALLGEERAIVTDIAGTT 250
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 373-407 8.87e-04

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 42.47  E-value: 8.87e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2449300333 373 TVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTK 407
Cdd:PRK09518  277 VVAIVGRPNVGKSTLVNRILGRREAVVEDTPGVTR 311
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 374-391 9.27e-04

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: 40.49  E-value: 9.27e-04
                          10
                  ....*....|....*...
gi 2449300333 374 VGLVGYPNVGKSSTINTI 391
Cdd:cd01898     3 VGLVGLPNAGKSTLLSAI 20
obgE PRK12297
GTPase CgtA; Reviewed
 374-412 1.10e-03

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 42.01  E-value: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2449300333 374 VGLVGYPNVGKSSTINtimgnkKVSvSATPghtK----HFQTL 412
Cdd:PRK12297  161 VGLVGFPNVGKSTLLS------VVS-NAKP---KianyHFTTL 193
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 168-242 1.18e-03

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: 40.14  E-value: 1.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2449300333 168 WRVIERSDIVVQIVDARNPLlfrCEDLECYVKEIDAAKENVIL-INKADLLTAEQRFAWAVHFEKEG---VKVIFWSAL 242
Cdd:cd04163    77 WSALKDVDLVLFVVDASEWI---GEGDEFILELLKKSKTPVILvLNKIDLVKDKEDLLPLLEKLKELhpfAEIFPISAL 152
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 373-418 1.44e-03

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: 39.85  E-value: 1.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2449300333 373 TVGLVGYPNVGKSSTINTIMgNKKVSVSATPGHTK-----HFQTLYVE------PGL 418
Cdd:cd01897     2 TLVIAGYPNVGKSSLVNKLT-RAKPEVAPYPFTTKslfvgHFDYKYLRwqvidtPGI 57
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 353-406 1.52e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 41.49  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2449300333 353 ELLELFKKLHTGKKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHT 406
Cdd:PRK03003  193 AVLAALPEVPRVGSASGGPRRVALVGKPNVGKSSLLNKLAGEERSVVDDVAGTT 246
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 373-407 1.86e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 41.11  E-value: 1.86e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2449300333 373 TVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTK 407
Cdd:PRK03003   40 VVAVVGRPNVGKSTLVNRILGRREAVVEDVPGVTR 74
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 168-242 2.01e-03

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: 39.40  E-value: 2.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2449300333 168 WRVIERSDIVVQIVDARNPLLfrCEDLEcyVKEIDAAKENVILINKADLLTAEQRFAwavhfEKEGVKVIFWSAL 242
Cdd:cd04164    77 REAIEEADLVLLVVDASEGLD--EEDLE--ILELPAKKPVIVVLNKSDLLSDAEGIS-----ELNGKPIIAISAK 142
era PRK00089
GTPase Era; Reviewed
 374-429 2.42e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 40.42  E-value: 2.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2449300333 374 VGLVGYPNVGKSSTINTIMGnKKVS-VSATPG----------HTKHFQTLYVepglclcDCPGLVMP 429
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVG-QKISiVSPKPQttrhrirgivTEDDAQIIFV-------DTPGIHKP 66
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 169-242 2.50e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 40.80  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 169 RVIERSDIVVQIVDARNPllfrcedlecyVKEID------AAKEN---VILINKADLLTAEQRfawaVHFEKE------- 232
Cdd:PRK00093  251 KAIERADVVLLVIDATEG-----------ITEQDlriaglALEAGralVIVVNKWDLVDEKTM----EEFKKElrrrlpf 315

                          90
                  ....*....|..
gi 2449300333 233 --GVKVIFWSAL 242
Cdd:PRK00093  316 ldYAPIVFISAL 327
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
374-408 2.96e-03

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 39.97  E-value: 2.96e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2449300333 374 VGLVGYPNVGKSSTINTIMGnKKVS-VSATPGHTKH 408
Cdd:COG1159     6 VAIVGRPNVGKSTLLNALVG-QKVSiVSPKPQTTRH 40
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 373-427 3.19e-03

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: 39.45  E-value: 3.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2449300333 373 TVGLVGYPNVGKSSTINTiMGNKKVSVSATPghtkhFQTLYVEPGLC--------LCDCPGLV 427
Cdd:cd01896     2 RVALVGFPSVGKSTLLSK-LTNTKSEVAAYE-----FTTLTCVPGVMeykgakiqLLDLPGII 58
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 168-242 4.73e-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: 38.38  E-value: 4.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2449300333 168 WRVIERSDIVVQIVDARNPllfRCEDLECYVKEIDAAKENVILINKADLLTAEQRFAWAVHFEKE---GVKVIFWSAL 242
Cdd:cd00880    71 RQVADRADLVLLVVDSDLT---PVEEEAKLGLLRERGKPVLLVLNKIDLVPESEEEELLRERKLEllpDLPVIAVSAL 145
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 208-255 5.51e-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: 38.29  E-value: 5.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2449300333 208 VILINKADLLTAEQRF-AWAVHFEKEGVKVIFWSALAETDHLngDLKEV 255
Cdd:pfam03193  57 VIVLNKIDLLDEEEELeELLKIYRAIGYPVLFVSAKTGEGIE--ALKEL 103
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 168-242 5.60e-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: 39.39  E-value: 5.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2449300333 168 WRVIERSDIVVQIVDARNPLLfrCEDLECYvKEIDAAKENVILINKADLLTAEQRFAwavhfEKEGVKVIFWSAL 242
Cdd:pfam12631 168 REAIEEADLVLLVLDASRPLD--EEDLEIL-ELLKDKKPIIVVLNKSDLLGEIDELE-----ELKGKPVLAISAK 234
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 169-242 5.89e-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: 38.18  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 169 RVIERSDIVVQIVDARNPllFRCEDLecyvKEIDAAKEN----VILINKADLLTAEQRFAWavHFEKE---------GVK 235
Cdd:cd01895    80 KAIERADVVLLVLDASEG--ITEQDL----RIAGLILEEgkalIIVVNKWDLVEKDEKTMK--EFEKElrrklpfldYAP 151


                  ....*..
gi 2449300333 236 VIFWSAL 242
Cdd:cd01895   152 IVFISAL 158
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 372-391 6.57e-03

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 39.16  E-value: 6.57e-03
                          10        20
                  ....*....|....*....|
gi 2449300333 372 LTVGLVGYPNVGKSSTINTI 391
Cdd:PTZ00258   22 LKMGIVGLPNVGKSTTFNAL 41
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 208-242 7.14e-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: 38.15  E-value: 7.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2449300333 208 VILINKADLLTAEQRFAWAVHFEKEGVKVIFWSAL 242
Cdd:cd01854    37 VIVLNKADLVDDEELEELLEIYEKLGYPVLAVSAK 71
obgE PRK12299
GTPase CgtA; Reviewed
 171-243 9.27e-03

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 38.51  E-value: 9.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449300333 171 IERSDIVVQIVDA--RNPLlfrcEDLECYVKEIDA------AKENVILINKADLLTAEQRFAWAVHFEKE--GVKVIFWS 240
Cdd:PRK12299  234 IERTRLLLHLVDIeaVDPV----EDYKTIRNELEKyspelaDKPRILVLNKIDLLDEEEEREKRAALELAalGGPVFLIS 309


                  ...
gi 2449300333 241 ALA 243
Cdd:PRK12299  310 AVT 312
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 374-426 9.92e-03

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: 38.52  E-value: 9.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2449300333 374 VGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKH-FQTLYVEPG--LCLCDCPGL 426
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNrISGIHTTGAsqIIFIDTPGF 58
 
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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