|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11058 |
PRK11058 |
GTPase HflX; Provisional |
1-426 |
0e+00 |
|
GTPase HflX; Provisional
Pssm-ID: 182934 [Multi-domain] Cd Length: 426 Bit Score: 896.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 1 MFDRYDAGEQAVLVHIYFSQDKDMEDLQEFESLVSSAGVEAMQVITGSRKAPHPKYFVGEGKAVEIADAVKATGASVVLF 80
Cdd:PRK11058 1 MFDRYEAGEQAVLVHIYFSQDKDMEDLQEFESLVSSAGVEALQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGASVVLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 81 DHALSPAQERNLEALCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPGETQL 160
Cdd:PRK11058 81 DHALSPAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPGETQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 161 ETDRRLLRGRITQILSRLERVEKQREQGRRARTKADIPTVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLRRID 240
Cdd:PRK11058 161 ETDRRLLRNRIVQILSRLERVEKQREQGRRARIKADVPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 241 VADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVIDAADVRVQENIDAVNVVLEEIDAHEIPTLLVMNKID 320
Cdd:PRK11058 241 VADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVVDAADVRVQENIEAVNTVLEEIDAHEIPTLLVMNKID 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 321 MLDDFEPRIDRDEENKPIRVWLSAQTGLGVPLLFQALTERLSGEVAQHTLRLPPQEGRLRSRFYQLQAIEKEWMEDDGSV 400
Cdd:PRK11058 321 MLDDFEPRIDRDEENKPIRVWLSAQTGAGIPLLFQALTERLSGEVAQHTLRLPPQEGRLRSRFYQLQAIEKEWMEEDGSV 400
|
410 420
....*....|....*....|....*.
gi 495778339 401 GMQVRMPIVDWRRLCKQEPALVDYIV 426
Cdd:PRK11058 401 SLQVRMPIVDWRRLCKQEPALIDYIV 426
|
|
| HflX |
COG2262 |
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
1-420 |
0e+00 |
|
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 644.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 1 MFDRYDAGEQAVLVHIYFSQD--KDMEDLQEFESLVSSAGVEAMQVITGSRKAPHPKYFVGEGKAVEIADAVKATGASVV 78
Cdd:COG2262 1 MFEREERGERAILVGVDLPGSdeDAEESLEELAELAETAGAEVVGTVTQRRDKPDPATYIGKGKVEELAELVEELEADLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 79 LFDHALSPAQERNLEALCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPGET 158
Cdd:COG2262 81 IFDDELSPSQQRNLEKALGVKVIDRTGLILDIFAQRARTREGKLQVELAQLQYLLPRLVGMWTHLSRQGGGIGTRGPGET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 159 QLETDRRLLRGRITQILSRLERVEKQREQGRRARTKADIPTVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLRR 238
Cdd:COG2262 161 QLETDRRLIRDRIARLKRELEKVRKQRELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 239 IDVADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVIDAADVRVQENIDAVNVVLEEIDAHEIPTLLVMNK 318
Cdd:COG2262 241 LELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNEVLEELGADDKPIILVFNK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 319 IDMLDDfePRIDRDEENKPIRVWLSAQTGLGVPLLFQALTERLSGEVAQHTLRLPPQEGRLRSRFYQLQAIEKEWMEDDG 398
Cdd:COG2262 321 IDLLDD--EELERLRAGYPDAVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYSDGDLVAWLHEHGEVLSEEYDEDG 398
|
410 420
....*....|....*....|..
gi 495778339 399 sVGMQVRMPIVDWRRLCKQEPA 420
Cdd:COG2262 399 -TLLTVRLPPEDLARLEAYLVE 419
|
|
| GTP_HflX |
TIGR03156 |
GTP-binding protein HflX; This protein family is one of a number of homologous small, ... |
10-361 |
0e+00 |
|
GTP-binding protein HflX; This protein family is one of a number of homologous small, well-conserved GTP-binding proteins with pleiotropic effects. Bacterial members are designated HflX, following the naming convention in Escherichia coli where HflX is encoded immediately downstream of the RNA chaperone Hfq, and immediately upstream of HflKC, a membrane-associated protease pair with an important housekeeping function. Over large numbers of other bacterial genomes, the pairing with hfq is more significant than with hflK and hlfC. The gene from Homo sapiens in this family has been named PGPL (pseudoautosomal GTP-binding protein-like). [Unknown function, General]
Pssm-ID: 274455 [Multi-domain] Cd Length: 351 Bit Score: 598.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 10 QAVLVHIYFSQDKDM-EDLQEFESLVSSAGVEAMQVITGSRKAPHPKYFVGEGKAVEIADAVKATGASVVLFDHALSPAQ 88
Cdd:TIGR03156 1 RAILVGVDLGNEDDEeESLEELAELAETAGAEVVGTVTQKRSRPDPATYIGKGKVEEIAELVEELEADLVIFDHELSPSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 89 ERNLEALCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPGETQLETDRRLLR 168
Cdd:TIGR03156 81 ERNLEKALGCRVIDRTGLILDIFAQRARTHEGKLQVELAQLKYLLPRLVGGWTHLSRQGGGIGTRGPGETQLETDRRLIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 169 GRITQILSRLERVEKQREQGRRARTKADIPTVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLRRIDVADVGETV 248
Cdd:TIGR03156 161 ERIAQLKKELEKVEKQRERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGADVYAADQLFATLDPTTRRLDLPDGGEVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 249 LADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVIDAADVRVQENIDAVNVVLEEIDAHEIPTLLVMNKIDMLDdfEPR 328
Cdd:TIGR03156 241 LTDTVGFIRDLPHELVAAFRATLEEVREADLLLHVVDASDPDREEQIEAVEKVLEELGAEDIPQLLVYNKIDLLD--EPR 318
|
330 340 350
....*....|....*....|....*....|...
gi 495778339 329 IDRDEENKPIRVWLSAQTGLGVPLLFQALTERL 361
Cdd:TIGR03156 319 IERLEEGYPEAVFVSAKTGEGLDLLLEAIAERL 351
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
157-361 |
1.24e-110 |
|
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.
Pssm-ID: 206666 [Multi-domain] Cd Length: 204 Bit Score: 323.64 E-value: 1.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 157 ETQLETDRRLLRGRITQILSRLERVEKQREQGRRARTKADIPTVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTL 236
Cdd:cd01878 1 ETQLETDRRLIRERIAKLRKELEKVKKQRELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 237 RRIDVADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVIDAADVRVQENIDAVNVVLEEIDAHEIPTLLVM 316
Cdd:cd01878 81 RRIKLPGGREVLLTDTVGFIRDLPHQLVEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKELGADDIPIILVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495778339 317 NKIDMLDDFEPRiDRDEENKPIRVWLSAQTGLGVPLLFQALTERL 361
Cdd:cd01878 161 NKIDLLDDEELE-ERLRAGRPDAVFISAKTGEGLDLLKEAIEELL 204
|
|
| GTP-bdg_N |
pfam13167 |
GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. ... |
25-111 |
1.05e-39 |
|
GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. The full-length members bind and interact with the 50S ribosome and are GTPases, hydrolysing GTP/GDP/ATP/ADP. This N-terminal region is necessary for stability of the whole protein.
Pssm-ID: 463797 [Multi-domain] Cd Length: 87 Bit Score: 137.10 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 25 EDLQEFESLVSSAGVEAMQVITGSRKAPHPKYFVGEGKAVEIADAVKATGASVVLFDHALSPAQERNLEALCECRVIDRT 104
Cdd:pfam13167 1 ESLEELEELAETAGAEVVGTVIQKRDKPDPATYIGKGKLEELKELVEALEADLVIFDDELSPSQQRNLEKALGVKVIDRT 80
|
....*..
gi 495778339 105 GLILDIF 111
Cdd:pfam13167 81 GLILDIF 87
|
|
| GTP-bdg_M |
pfam16360 |
GTP-binding GTPase Middle Region; This family locates between the N-terminal domain and ... |
114-192 |
3.01e-39 |
|
GTP-binding GTPase Middle Region; This family locates between the N-terminal domain and MMR_HSR1 50S ribosome-binding GTPase of GTP-binding HflX-like proteins. The full-length members bind and interact with the 50S ribosome and are GTPases, hydrolysing GTP/GDP/ATP/ADP. This region is unknown for its function.
Pssm-ID: 465103 [Multi-domain] Cd Length: 79 Bit Score: 135.64 E-value: 3.01e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495778339 114 RARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPGETQLETDRRLLRGRITQILSRLERVEKQREQGRRAR 192
Cdd:pfam16360 1 RARTREAKLQVELAQLKYLLPRLRGMGTHLSRQGGGIGTRGPGETKLETDRRLIRRRIAKLKKELEKVRKQRELQRKRR 79
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
199-318 |
7.40e-26 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 100.77 E-value: 7.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 199 TVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLRRIDVADVgETVLADTVGFIR--HLPHDLVAAFKAtlqeTRQ 276
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGK-QIILVDTPGLIEgaSEGEGLGRAFLA----IIE 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 495778339 277 ATLLLHVIDAadvrvQENIDAVNVVLEEI-DAHEIPTLLVMNK 318
Cdd:pfam01926 76 ADLILFVVDS-----EEGITPLDEELLELlRENKKPIILVLNK 113
|
|
| Obg_CgtA |
TIGR02729 |
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ... |
195-361 |
2.22e-20 |
|
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome GTP-binding protein that associates with ribosomal subunits and appears to play a role in ribosomal RNA maturation. This GTPase, related to the nucleolar protein Obg, is designated CgtA in bacteria. Mutations in this gene are pleiotropic, but it appears that effects on cellular functions such as chromosome partition may be secondary to the effect on ribosome structure. Recent work done in Vibrio cholerae shows an essential role in the stringent response, in which RelA-dependent ability to synthesize the alarmone ppGpp is required for deletion of this GTPase to be lethal. [Protein synthesis, Other]
Pssm-ID: 274271 [Multi-domain] Cd Length: 328 Bit Score: 91.33 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 195 ADiptVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLRRIDVADVGETVLADTVGFI-----------RHLPHdl 263
Cdd:TIGR02729 158 AD---VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIegasegaglghRFLKH-- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 264 vaafkatLQETRqatLLLHVIDAADVRVQENIDAVNVVLEEIDAH-----EIPTLLVMNKIDMLDD--FEPRID--RDEE 334
Cdd:TIGR02729 233 -------IERTR---VLLHLIDISPEDGSDPVEDYEIIRNELKKYspelaEKPRIVVLNKIDLLDEeeLEELLKelKKEL 302
|
170 180
....*....|....*....|....*..
gi 495778339 335 NKPIRVwLSAQTGLGVPLLFQALTERL 361
Cdd:TIGR02729 303 GKPVFP-ISALTGEGLDELLDALAELL 328
|
|
| obgE |
PRK12299 |
GTPase CgtA; Reviewed |
195-367 |
2.38e-19 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 88.59 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 195 ADiptVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLRRIDVADVGETVLADTVGFI-----------RHLPHdl 263
Cdd:PRK12299 159 AD---VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKSFVIADIPGLIegasegaglghRFLKH-- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 264 vaafkatLQETRqatLLLHVIDAADVRVqenIDAVNVVLEEIDAH-----EIPTLLVMNKIDMLDD---FEPRIDRDEEN 335
Cdd:PRK12299 234 -------IERTR---LLLHLVDIEAVDP---VEDYKTIRNELEKYspelaDKPRILVLNKIDLLDEeeeREKRAALELAA 300
|
170 180 190
....*....|....*....|....*....|...
gi 495778339 336 KPIRVW-LSAQTGLGVPLLFQALTERLSGEVAQ 367
Cdd:PRK12299 301 LGGPVFlISAVTGEGLDELLRALWELLEEARRE 333
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
195-361 |
1.70e-17 |
|
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: 79.39 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 195 ADiptVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLRRIDVADVGETVLADTVG--------------FIRHlp 260
Cdd:cd01898 1 AD---VGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGliegasegkglghrFLRH-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 261 hdlvaafkatLQETRqatLLLHVIDAADvrVQENIDAVNVVLEEIDAHEI-----PTLLVMNKIDMLDD------FEPRI 329
Cdd:cd01898 76 ----------IERTR---VLLHVIDLSG--EDDPVEDYETIRNELEAYNPglaekPRIVVLNKIDLLDAeerfekLKELL 140
|
170 180 190
....*....|....*....|....*....|..
gi 495778339 330 DRDEENKPIRVwlSAQTGLGVPLLFQALTERL 361
Cdd:cd01898 141 KELKGKKVFPI--SALTGEGLDELLKKLAKLL 170
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
202-359 |
2.05e-17 |
|
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: 79.04 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 202 LVGYTNAGKSTLFNQITEAQVYAADQLFA-TLDPTLRRIDVADVGETV-LADTVGFIRHLPHDLVAAFKATLqetRQATL 279
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGEVGEVSDVPGtTRDPDVYVKELDKGKVKLvLVDTPGLDEFGGLGREELARLLL---RGADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 280 LLHVIDAADVRVQENIDavNVVLEEIDAHEIPTLLVMNKIDMLD----DFEPRIDRDEENKPIRVW-LSAQTGLGVPLLF 354
Cdd:cd00882 79 ILLVVDSTDRESEEDAK--LLILRRLRKEGIPIILVGNKIDLLEerevEELLRLEELAKILGVPVFeVSAKTGEGVDELF 156
|
....*
gi 495778339 355 QALTE 359
Cdd:cd00882 157 EKLIE 161
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
202-361 |
1.41e-16 |
|
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: 76.52 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 202 LVGYTNAGKSTLFNQITEAQVYA-ADQLFATLDPTLRRIDVADVGETVLADTVGFIRhLPHDLVAAFKATLQETRQATLL 280
Cdd:cd00880 2 IFGRPNVGKSSLLNALLGQNVGIvSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDE-EGGLGRERVEEARQVADRADLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 281 LHVIDAAdvrvqENIDAVNVVLEEIDAHEIPTLLVMNKIDMLDDFEPRIDRDE-------ENKPIRVwlSAQTGLGVPLL 353
Cdd:cd00880 81 LLVVDSD-----LTPVEEEAKLGLLRERGKPVLLVLNKIDLVPESEEEELLRErklellpDLPVIAV--SALPGEGIDEL 153
|
....*...
gi 495778339 354 FQALTERL 361
Cdd:cd00880 154 RKKIAELL 161
|
|
| Obg_like |
cd01881 |
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
202-350 |
5.59e-16 |
|
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified.
Pssm-ID: 206668 [Multi-domain] Cd Length: 167 Bit Score: 75.12 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 202 LVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIRHlPHDLVAAFKATLQETRQATLLL 281
Cdd:cd01881 2 LVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDG-ASEGRGLGEQILAHLYRSDLIL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495778339 282 HVIDAADVRVQENIDAVNVVLEEIDAH-----EIPTLLVMNKIDMLDDFEPRIDR--DEENKPIRVWLSAQTGLGV 350
Cdd:cd01881 81 HVIDASEDCVGDPLEDQKTLNEEVSGSflflkNKPEMIVANKIDMASENNLKRLKldKLKRGIPVVPTSALTRLGL 156
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
163-391 |
4.82e-15 |
|
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: 76.64 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 163 DRRLLRGRITQILSRLERVEKQREQGRRARtkaDIPTVSLVGYTNAGKSTLFNQIteaqvyaadqlfatldptLRRiDVA 242
Cdd:COG0486 182 DREELLERLEELREELEALLASARQGELLR---EGIKVVIVGRPNVGKSSLLNAL------------------LGE-ERA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 243 DV----GET---------------VLADTVGfIRHlPHDLVAAF--KATLQETRQATLLLHVIDAADVRVQENIDavnvV 301
Cdd:COG0486 240 IVtdiaGTTrdvieeriniggipvRLIDTAG-LRE-TEDEVEKIgiERAREAIEEADLVLLLLDASEPLTEEDEE----I 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 302 LEEIDahEIPTLLVMNKIDMLDDFEPRIDRDEENKPIRVwlSAQTGLGVPLLFQALTERLSGevaqhtlRLPPQEGRLRS 381
Cdd:COG0486 314 LEKLK--DKPVIVVLNKIDLPSEADGELKSLPGEPVIAI--SAKTGEGIDELKEAILELVGE-------GALEGEGVLLT 382
|
250
....*....|
gi 495778339 382 RFYQLQAIEK 391
Cdd:COG0486 383 NARHREALER 392
|
|
| obgE |
PRK12298 |
GTPase CgtA; Reviewed |
195-398 |
1.02e-13 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237047 [Multi-domain] Cd Length: 390 Bit Score: 72.21 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 195 ADiptVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLRRIDVADVGETVLADTVGFI-----------RHLPHdl 263
Cdd:PRK12298 160 AD---VGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDERSFVVADIPGLIegasegaglgiRFLKH-- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 264 vaafkatLQETRqatLLLHVIDAADVRVQENIDAVNVVLEEIDAH-----EIPTLLVMNKIDMLDDFE--PRID--RDEE 334
Cdd:PRK12298 235 -------LERCR---VLLHLIDIAPIDGSDPVENARIIINELEKYspklaEKPRWLVFNKIDLLDEEEaeERAKaiVEAL 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495778339 335 NKPIRVWL-SAQTGLGVPLLFQALTERL-SGEVAQHTLRLPPQEGRLRSRFYQLQAIEKEWMEDDG 398
Cdd:PRK12298 305 GWEGPVYLiSAASGLGVKELCWDLMTFIeENPREEAEEAEAPEKVEFMWDDYHREQLEEVEEEDDD 370
|
|
| obgE |
PRK12297 |
GTPase CgtA; Reviewed |
195-398 |
3.59e-13 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237046 [Multi-domain] Cd Length: 424 Bit Score: 70.90 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 195 ADiptVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLRRIDVADVGETVLADTVG--------------FIRHlp 260
Cdd:PRK12297 159 AD---VGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRSFVMADIPGliegasegvglghqFLRH-- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 261 hdlvaafkatLQETRqatLLLHVIDAADVRVQENIDAVNVVLEEIDAH-----EIPTLLVMNKIDMlDDFEPRIDRDEEN 335
Cdd:PRK12297 234 ----------IERTR---VIVHVIDMSGSEGRDPIEDYEKINKELKLYnprllERPQIVVANKMDL-PEAEENLEEFKEK 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495778339 336 KPIRVW-LSAQTGLGVpllfQALTERLSGEVAQHTLRLPPQEGRLRSRFYQLQAIEKEW---MEDDG 398
Cdd:PRK12297 300 LGPKVFpISALTGQGL----DELLYAVAELLEETPEFPLEEEEVEEEVYYKFEEEEKDFtitRDEDG 362
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
161-391 |
3.60e-12 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 67.83 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 161 ETDRRLLRGRITQILSRLERVEKQREQGRRARTKAdipTVSLVGYTNAGKSTLFNqiteaqvyaadqlfatldpTLRRID 240
Cdd:PRK05291 182 FLSDEKILEKLEELIAELEALLASARQGEILREGL---KVVIAGRPNVGKSSLLN-------------------ALLGEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 241 VADV----GET---------------VLADTVGfIRHlPHDLVAA--FKATLQETRQATLLLHVIDAADVRVQENIDavn 299
Cdd:PRK05291 240 RAIVtdiaGTTrdvieehinldgiplRLIDTAG-IRE-TDDEVEKigIERSREAIEEADLVLLVLDASEPLTEEDDE--- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 300 vVLEEIDahEIPTLLVMNKIDMlddfEPRIDRDEENKPIRVWLSAQTGLGVPLLFQALTERLsgevaqHTLRLPPQEGRL 379
Cdd:PRK05291 315 -ILEELK--DKPVIVVLNKADL----TGEIDLEEENGKPVIRISAKTGEGIDELREAIKELA------FGGFGGNQEGVF 381
|
250
....*....|..
gi 495778339 380 RSRFYQLQAIEK 391
Cdd:PRK05291 382 LTNARHLEALER 393
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
200-361 |
7.97e-11 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 62.37 E-value: 7.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 200 VSLVGYTNAGKSTLFNQITE---------AQvyaadqlfatldpTLRR----IDVADVGETVLADTVGFirHLPHD---- 262
Cdd:PRK00089 8 VAIVGRPNVGKSTLLNALVGqkisivspkPQ-------------TTRHrirgIVTEDDAQIIFVDTPGI--HKPKRalnr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 263 -LVAAFKATLQEtrqATLLLHVIDAADvrvqENIDAVNVVLEEIDAHEIPTLLVMNKIDMLDDFE---PRID---RDEEN 335
Cdd:PRK00089 73 aMNKAAWSSLKD---VDLVLFVVDADE----KIGPGDEFILEKLKKVKTPVILVLNKIDLVKDKEellPLLEelsELMDF 145
|
170 180
....*....|....*....|....*.
gi 495778339 336 KPIrVWLSAQTGLGVPLLFQALTERL 361
Cdd:PRK00089 146 AEI-VPISALKGDNVDELLDVIAKYL 170
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
199-361 |
1.19e-10 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 59.82 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 199 TVSLVGYTNAGKSTLFNQIteaqvyaadqlfatldptLRRiDVA----------DVGET---------VLADTVGfIRHL 259
Cdd:cd04164 5 KVVIAGKPNVGKSSLLNAL------------------AGR-DRAivsdiagttrDVIEEeidlggipvRLIDTAG-LRET 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 260 PhDLV--AAFKATLQETRQATLLLHVIDAadvrvQENIDAVNVVLEEIDAhEIPTLLVMNKIDMLDDFEPRIdrdEENKP 337
Cdd:cd04164 65 E-DEIekIGIERAREAIEEADLVLLVVDA-----SEGLDEEDLEILELPA-KKPVIVVLNKSDLLSDAEGIS---ELNGK 134
|
170 180
....*....|....*....|....
gi 495778339 338 IRVWLSAQTGLGVPLLFQALTERL 361
Cdd:cd04164 135 PIIAISAKTGEGIDELKEALLELA 158
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
200-361 |
1.79e-10 |
|
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: 59.40 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 200 VSLVGYTNAGKSTLFNQITE---------AQvyaadqlfatldpTLRR----IDVADVGETVLADTVGFirHLPHD---- 262
Cdd:cd04163 6 VAIIGRPNVGKSTLLNALVGqkisivspkPQ-------------TTRNrirgIYTDDDAQIIFVDTPGI--HKPKKklge 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 263 -LVAAFKATLQEtrqATLLLHVIDAaDVRVQENIDAVnvvLEEIDAHEIPTLLVMNKIDMLDDFEPRIDRDEENKPIRVW 341
Cdd:cd04163 71 rMVKAAWSALKD---VDLVLFVVDA-SEWIGEGDEFI---LELLKKSKTPVILVLNKIDLVKDKEDLLPLLEKLKELHPF 143
|
170 180
....*....|....*....|....*
gi 495778339 342 -----LSAQTGLGVPLLFQALTERL 361
Cdd:cd04163 144 aeifpISALKGENVDELLEYIVEYL 168
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
200-361 |
7.95e-10 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 59.62 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 200 VSLVGYTNAGKSTLFNQ-------IT--EAQvyaadqlfatldpTLRR----IDVADVGETVLADTVGFirHLPHD---- 262
Cdd:COG1159 6 VAIVGRPNVGKSTLLNAlvgqkvsIVspKPQ-------------TTRHrirgIVTREDAQIVFVDTPGI--HKPKRklgr 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 263 -LVAAFKATLQEtrqATLLLHVIDAaDVRVQENIDAVnvvLEEIDAHEIPTLLVMNKIDML--DDFEPRIDRDEENKPIR 339
Cdd:COG1159 71 rMNKAAWSALED---VDVILFVVDA-TEKIGEGDEFI---LELLKKLKTPVILVINKIDLVkkEELLPLLAEYSELLDFA 143
|
170 180
....*....|....*....|....
gi 495778339 340 --VWLSAQTGLGVPLLFQALTERL 361
Cdd:COG1159 144 eiVPISALKGDNVDELLDEIAKLL 167
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
167-364 |
2.27e-09 |
|
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: 58.26 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 167 LRGRITQILSRLERVEKQREQGRRARtkaDIPTVSLVGYTNAGKSTLFNQITEAQVyaadqlfA--------TLDpTLR- 237
Cdd:pfam12631 67 LLERLEELLAELEKLLATADRGRILR---EGIKVVIVGKPNVGKSSLLNALLGEER-------AivtdipgtTRD-VIEe 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 238 RIDVADVgeTV-LADTVGfIRHlPHDLVAAF--KATLQETRQATLLLHVIDAadvrvQENIDAVNVVLEEIDAHEIPTLL 314
Cdd:pfam12631 136 TINIGGI--PLrLIDTAG-IRE-TDDEVEKIgiERAREAIEEADLVLLVLDA-----SRPLDEEDLEILELLKDKKPIIV 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495778339 315 VMNKIDMLDDFEPRIDRDEENkpiRVWLSAQTGLGVPLLFQALTERLSGE 364
Cdd:pfam12631 207 VLNKSDLLGEIDELEELKGKP---VLAISAKTGEGLDELEEAIKELFLAG 253
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
179-341 |
7.56e-09 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 56.70 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 179 ERVEKQREQGRRARTKADIPTVSLVGYTNAGKSTLFNQITEAQVYAADQLFA-TLDPTLRRIDVADVGETVLADTVGF-I 256
Cdd:COG3596 21 VLRELLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPcTREIQRYRLESDGLPGLVLLDTPGLgE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 257 RHLPHdlvAAFKATLQETRQATLLLHVIDAADVRVQENIDAVNVVLEEIDahEIPTLLVMNKIDMLDdfepridrdeenk 336
Cdd:COG3596 101 VNERD---REYRELRELLPEADLILWVVKADDRALATDEEFLQALRAQYP--DPPVLVVLTQVDRLE------------- 162
|
....*
gi 495778339 337 PIRVW 341
Cdd:COG3596 163 PEREW 167
|
|
| PTZ00258 |
PTZ00258 |
GTP-binding protein; Provisional |
187-339 |
4.16e-08 |
|
GTP-binding protein; Provisional
Pssm-ID: 240334 [Multi-domain] Cd Length: 390 Bit Score: 54.95 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 187 QGRRARTKadipTVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLRRIDVAD---------------VGETV-LA 250
Cdd:PTZ00258 15 LGRPGNNL----KMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDerfdwlckhfkpksiVPAQLdIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 251 DTVGFIR--HLPHDLVAAFkatLQETRQATLLLHVI----DAADVRVQENIDAVNvvleeiDAHEIPTLLVMNKIDMLDD 324
Cdd:PTZ00258 91 DIAGLVKgaSEGEGLGNAF---LSHIRAVDGIYHVVrafeDEDITHVEGEIDPVR------DLEIISSELILKDLEFVEK 161
|
170
....*....|....*
gi 495778339 325 FEPRIDRDEENKPIR 339
Cdd:PTZ00258 162 RLDELTKKRKKKKKK 176
|
|
| Rbg1 |
COG1163 |
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; |
167-361 |
7.90e-08 |
|
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440777 [Multi-domain] Cd Length: 368 Bit Score: 54.03 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 167 LRGRITQILSRL-ERVEKQREQGRRARTKADIP-----TVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDP---TLR 237
Cdd:COG1163 27 HIGRLKAKLAELkEELEKRKKKSGGGGEGFAVKksgdaTVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVvpgMLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 238 ----RIDVADV-------------GETVL-----ADTVGFIrhLPHDLVAAFKATLQETRQATLLL-------------- 281
Cdd:COG1163 107 ykgaKIQILDVpgliegaasgkgrGKEVLsvvrnADLILIV--LDVFELEQYDVLKEELYDAGIRLnkpppdvtiekkgk 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 282 ------------------------HVIDAADVRVQENIDavnvvLEE-IDAHE-----IPTLLVMNKIDMLD-DFEPRID 330
Cdd:COG1163 185 ggirvnstgkldldeedikkilreYGIVNADVLIREDVT-----LDDlIDALMgnrvyKPAIVVVNKIDLADeEYVEELK 259
|
250 260 270
....*....|....*....|....*....|...
gi 495778339 331 RD--EENKPIRVwlSAQTGLGvpllFQALTERL 361
Cdd:COG1163 260 SKlpDGVPVIFI--SAEKGIG----LEELKEEI 286
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
193-361 |
2.23e-07 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 53.26 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 193 TKADIPTVSLVGYTNAGKSTLFNQITEAQVYAADQLFA-TLDP--TLRRIDvadvGETVL-ADTVGfIRHLPHDLVAA-F 267
Cdd:PRK09518 446 TPSGLRRVALVGRPNVGKSSLLNQLTHEERAVVNDLAGtTRDPvdEIVEID----GEDWLfIDTAG-IKRRQHKLTGAeY 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 268 KATLQET---RQATLLLHVIDAA------DVRVQENIdavnvvleeIDAHEiPTLLVMNKIDMLDDFE-PRIDRDEENKP 337
Cdd:PRK09518 521 YSSLRTQaaiERSELALFLFDASqpiseqDLKVMSMA---------VDAGR-ALVLVFNKWDLMDEFRrQRLERLWKTEF 590
|
170 180 190
....*....|....*....|....*....|
gi 495778339 338 IRV-W-----LSAQTGLGVPLLFQALTERL 361
Cdd:PRK09518 591 DRVtWarrvnLSAKTGWHTNRLAPAMQEAL 620
|
|
| obgE |
PRK12296 |
GTPase CgtA; Reviewed |
192-376 |
5.13e-07 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237045 [Multi-domain] Cd Length: 500 Bit Score: 51.79 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 192 RTKADiptVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLrriDVADVGETV--LADTVGFI------RHLPHDL 263
Cdd:PRK12296 157 KSVAD---VGLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNL---GVVQAGDTRftVADVPGLIpgasegKGLGLDF 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 264 vaafkatLQETRQATLLLHVIDAA----------DVRVQEN-----IDAVNVVLEEIDAHEIPTLLVMNKID------ML 322
Cdd:PRK12296 231 -------LRHIERCAVLVHVVDCAtlepgrdplsDIDALEAelaayAPALDGDLGLGDLAERPRLVVLNKIDvpdareLA 303
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495778339 323 DDFEPRIdrdeENKPIRVW-LSAQTGLGVpllfQALTERLSGEVAQHTLRLPPQE 376
Cdd:PRK12296 304 EFVRPEL----EARGWPVFeVSAASREGL----RELSFALAELVEEARAAEPEAE 350
|
|
| YchF |
cd01900 |
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ... |
203-254 |
3.85e-06 |
|
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of GTPases: Obg, DRG, Ygr210, and NOG1. Obg is an essential gene that is involved in DNA replication in C. crescentus and Streptomyces griseus and is associated with the ribosome. Several members of the family, including YchF, possess the TGS domain related to the RNA-binding proteins. Experimental data and genomic analysis suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translational factor.
Pssm-ID: 206687 [Multi-domain] Cd Length: 274 Bit Score: 48.22 E-value: 3.85e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 495778339 203 VGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLRRIDVADVGETVLADTVG 254
Cdd:cd01900 4 VGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERLDKLAEIVK 55
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
197-361 |
4.46e-06 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 48.48 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 197 IPTVSLVGYTNAGKSTLFNQIT---EAQVyaADQLFATLDptlRRIDVADVGET--VLADTVGFIRHLPHDLVAAFKA-T 270
Cdd:COG1160 2 SPVVAIVGRPNVGKSTLFNRLTgrrDAIV--DDTPGVTRD---RIYGEAEWGGRefTLIDTGGIEPDDDDGLEAEIREqA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 271 LQETRQATLLLHVIDAadvrvQENIDAVNvvlEEIdAHEI-----PTLLVMNKIDmlddfepriDRDEEN---------- 335
Cdd:COG1160 77 ELAIEEADVILFVVDG-----RAGLTPLD---EEI-AKLLrrsgkPVILVVNKVD---------GPKREAdaaefyslgl 138
|
170 180
....*....|....*....|....*..
gi 495778339 336 -KPIRVwlSAQTGLGVPLLFQALTERL 361
Cdd:COG1160 139 gEPIPI--SAEHGRGVGDLLDAVLELL 163
|
|
| MMR_HSR1_Xtn |
pfam16897 |
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ... |
258-361 |
1.93e-05 |
|
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of the MMR_HSR1 family.
Pssm-ID: 465301 [Multi-domain] Cd Length: 105 Bit Score: 43.18 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 258 HLPHDLVaafKATLQETRqatlllhvIDAADVRVQENIDavnvvLEE-IDAHE-----IPTLLVMNKIDMLD-DFEPRID 330
Cdd:pfam16897 13 KLDEETI---KAILREYK--------IHNADVLIREDVT-----VDDlIDVIEgnrvyIPCLYVYNKIDLISiEELDRLA 76
|
90 100 110
....*....|....*....|....*....|.
gi 495778339 331 RDEENKPIrvwlSAQTGLGVPLLFQALTERL 361
Cdd:pfam16897 77 REPDSVPI----SAEKGLNLDELKERIWEYL 103
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
200-355 |
4.12e-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: 43.51 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 200 VSLVGYTNAGKSTLFNQITEaqvyaaDQLFAT-LDPTLRRIDVADV----GETVLA---DTVGFIRHLPhDLVAAFKATL 271
Cdd:TIGR00231 4 IVIVGHPNVGKSTLLNSLLG------NKGSITeYYPGTTRNYVTTVieedGKTYKFnllDTAGQEDYDA-IRRLYYPQVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 272 QETRQATLLLHVIDAADVRVQEnidavnvvLEEIDAH---EIPTLLVMNKIDMLD-DFEP--RIDRDEENKPIRVWLSAQ 345
Cdd:TIGR00231 77 RSLRVFDIVILVLDVEEILEKQ--------TKEIIHHadsGVPIILVGNKIDLKDaDLKThvASEFAKLNGEPIIPLSAE 148
|
170
....*....|
gi 495778339 346 TGLGVPLLFQ 355
Cdd:TIGR00231 149 TGKNIDSAFK 158
|
|
| GTP1 |
COG0012 |
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ... |
202-326 |
6.50e-05 |
|
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439783 [Multi-domain] Cd Length: 362 Bit Score: 44.63 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 202 LVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIRHLP-----HD---LVA-AFKAT-- 270
Cdd:COG0012 5 IVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPatiefVDiagLVKgASKGEgl 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 271 ----LQETRQATLLLHVidaadVRVQENidaVNVVleeidaHeiptllVMNKIDMLDDFE 326
Cdd:COG0012 85 gnqfLANIREVDAIVHV-----VRCFED---DNVT------H------VEGSVDPLRDIE 124
|
|
| PRK09602 |
PRK09602 |
translation-associated GTPase; Reviewed |
199-286 |
8.11e-05 |
|
translation-associated GTPase; Reviewed
Pssm-ID: 236584 [Multi-domain] Cd Length: 396 Bit Score: 44.41 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 199 TVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDP----TLRRIDVA--DVGETVLADT---VGFIRHLPHDL--VA-- 265
Cdd:PRK09602 3 TIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPnvgvAYVRVECPckELGVKCNPRNgkcIDGTRFIPVELidVAgl 82
|
90 100 110
....*....|....*....|....*....|...
gi 495778339 266 ------------AFkatLQETRQATLLLHVIDA 286
Cdd:PRK09602 83 vpgahegrglgnQF---LDDLRQADALIHVVDA 112
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
196-359 |
1.46e-04 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 42.42 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 196 DIPTVSLVGYTNAGKSTLFNQIT-EAQVYAADQLFATLDPtlrrIDVaDV---GET-VLADTVGfIRHLPH-----DLVA 265
Cdd:cd01895 1 DPIKIAIIGRPNVGKSSLLNALLgEERVIVSDIAGTTRDS----IDV-PFeydGQKyTLIDTAG-IRKKGKvtegiEKYS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 266 AFKaTLQETRQATLLLHVIDAadvrvQENI---DAvnVVLEEIDAHEIPTLLVMNKIDMLDDFEPRIDRDEENkpIR--- 339
Cdd:cd01895 75 VLR-TLKAIERADVVLLVLDA-----SEGIteqDL--RIAGLILEEGKALIIVVNKWDLVEKDEKTMKEFEKE--LRrkl 144
|
170 180
....*....|....*....|....*...
gi 495778339 340 --------VWLSAQTGLGVPLLFQALTE 359
Cdd:cd01895 145 pfldyapiVFISALTGQGVDKLFDAIKE 172
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
283-361 |
2.93e-04 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 41.74 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 283 VIDAADvRVQENIDAVnvvLEEIDAHEIPTLLVMNKIDMLDDFEPR-------------IDRDEENKPIrVWLSAQTGLG 349
Cdd:pfam00009 99 VVDAVE-GVMPQTREH---LRLARQLGVPIIVFINKMDRVDGAELEevveevsrellekYGEDGEFVPV-VPGSALKGEG 173
|
90
....*....|..
gi 495778339 350 VPLLFQALTERL 361
Cdd:pfam00009 174 VQTLLDALDEYL 185
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
202-361 |
3.16e-04 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They 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. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 40.79 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 202 LVGYTNAGKSTLFNQITEAQVYAADQLFA-TLDPTlrRIDVADVGE-TVLADTVGFIRHLPHDLVAAfKATLQETRQATL 279
Cdd:cd11383 2 LMGKTGAGKSSLCNALFGTEVAAVGDRRPtTRAAQ--AYVWQTGGDgLVLLDLPGVGERGRRDREYE-ELYRRLLPEADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 280 LLHVIDAADVRVQENIDavnVVLEEIDAHEIPTLLVMNKIDmlddfepridrdeenkPIrVWLSAQTGLGVPLLFQALTE 359
Cdd:cd11383 79 VLWLLDADDRALAADHD---FYLLPLAGHDAPLLFVLNQVD----------------PV-LAVSARTGWGLDELAEALIT 138
|
..
gi 495778339 360 RL 361
Cdd:cd11383 139 AL 140
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
197-361 |
3.29e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 42.73 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 197 IPTVSLVGYTNAGKSTLFNQIT---EAQVyaADQLFATLDptlRRIDVADVG--ETVLADTVGFIRHlPHDLVAAFKA-T 270
Cdd:PRK00093 1 KPVVAIVGRPNVGKSTLFNRLTgkrDAIV--ADTPGVTRD---RIYGEAEWLgrEFILIDTGGIEPD-DDGFEKQIREqA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 271 LQETRQATLLLHVIDAadvrvQENIDAVNvvlEEIdAHEI-----PTLLVMNKIDmlddfepRIDRDEE---------NK 336
Cdd:PRK00093 75 ELAIEEADVILFVVDG-----RAGLTPAD---EEI-AKILrksnkPVILVVNKVD-------GPDEEADayefyslglGE 138
|
170 180
....*....|....*....|....*
gi 495778339 337 PIRVwlSAQTGLGVPLLFQALTERL 361
Cdd:PRK00093 139 PYPI--SAEHGRGIGDLLDAILEEL 161
|
|
| HflX_C |
pfam19275 |
HflX C-terminal domain; This entry represents the C-terminal domain of the HflX protein. HflX ... |
342-406 |
3.86e-04 |
|
HflX C-terminal domain; This entry represents the C-terminal domain of the HflX protein. HflX binds to the intersubunit face of the 50S subunit. Its C-terminal domain (CTD) predominantly interacts with the NTD of uL11 at the bL12 stalk base. Truncation of the CTD rendered HflX inactive in 70S splitting.
Pssm-ID: 437107 Cd Length: 102 Bit Score: 39.60 E-value: 3.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495778339 342 LSAQTGLGVPLLFQALTERLSGEVAQHTLRLPPQEGRLRSRFYQlQAI--EKEWMEdDGSVGMQVRM 406
Cdd:pfam19275 15 VSAITGEGVDALMDEISRRLSGVLTETTVVLPADKLALLSWVYE-NAIvdGREDNE-DGSVSLDVRL 79
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
199-362 |
3.87e-04 |
|
GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.
Pssm-ID: 206647 [Multi-domain] Cd Length: 183 Bit Score: 41.13 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 199 TVSLVGYTNAGKSTLFNQITE----------AQVYAADQLFA------TLDPTLRRIDVADVGETVLaDTVGfirHLphD 262
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYqtgaidrrgtRKETFLDTLKEerergiTIKTGVVEFEWPKRRINFI-DTPG---HE--D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 263 LVAAFKATLqetRQATLLLHVIDAAD-VRVQeNIDAVNVVLEEIdaheIPTLLVMNKIDMLD--DFE------------- 326
Cdd:cd00881 75 FSKETVRGL---AQADGALLVVDANEgVEPQ-TREHLNIALAGG----LPIIVAVNKIDRVGeeDFDevlreikellkli 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 495778339 327 PRIDRDEENKPIrVWLSAQTGLGVPLLFQALTERLS 362
Cdd:cd00881 147 GFTFLKGKDVPI-IPISALTGEGIEELLDAIVEHLP 181
|
|
| FeoB_N |
pfam02421 |
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ... |
199-357 |
4.87e-04 |
|
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.
Pssm-ID: 460552 [Multi-domain] Cd Length: 156 Bit Score: 40.51 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 199 TVSLVGYTNAGKSTLFNQITEAQVYAADqlFA--TLDPTLRRIDVADVgETVLADtvgfirhLP--HDLVAafkATLQE- 273
Cdd:pfam02421 2 TIALVGNPNVGKTTLFNALTGANQHVGN--WPgvTVEKKEGKFKYKGY-EIEIVD-------LPgiYSLSP---YSEEEr 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 274 -TRQ------ATLLLHVIDAAdvrvqeNID-AVNVVLEEIDAhEIPTLLVMNKIDMLDDFEPRIDRDEENK----PIrVW 341
Cdd:pfam02421 69 vARDyllnekPDVIVNVVDAT------NLErNLYLTLQLLEL-GLPVVLALNMMDEAEKKGIKIDIKKLSEllgvPV-VP 140
|
170
....*....|....*.
gi 495778339 342 LSAQTGLGVPLLFQAL 357
Cdd:pfam02421 141 TSARKGEGIDELLDAI 156
|
|
| Ygr210 |
cd01899 |
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ... |
200-287 |
6.12e-04 |
|
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They are characterized by a distinct glycine-rich motif immediately following the Walker B motif. The Ygr210 and YyaF/YchF subfamilies appear to form one major branch of the Obg-like family. Among eukaryotes, the Ygr210 subfamily is represented only in fungi. These fungal proteins form a tight cluster with their archaeal orthologs, which suggests the possibility of horizontal transfer from archaea to fungi.
Pssm-ID: 206686 [Multi-domain] Cd Length: 318 Bit Score: 41.44 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 200 VSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDP----TLRRIDVADVGETVLA-DTVGF----IRHLPHDL--VAA-- 266
Cdd:cd01899 1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPnvgvGYVRVECPCKELGVSCnPRYGKcidgKRYVPVELidVAGlv 80
|
90 100 110
....*....|....*....|....*....|...
gi 495778339 267 ------------FkatLQETRQATLLLHVIDAA 287
Cdd:cd01899 81 pgahegkglgnqF---LDDLRDADVLIHVVDAS 110
|
|
| PRK04213 |
PRK04213 |
GTP-binding protein EngB; |
198-331 |
8.24e-04 |
|
GTP-binding protein EngB;
Pssm-ID: 179790 [Multi-domain] Cd Length: 201 Bit Score: 40.29 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 198 PTVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTlrRIDVADVgetVLADTVGFirhlphDLVAAFKATLQEtRQA 277
Cdd:PRK04213 10 PEIVFVGRSNVGKSTLVRELTGKKVRVGKRPGVTRKPN--HYDWGDF---ILTDLPGF------GFMSGVPKEVQE-KIK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 278 TLLLHVI-DAADvrvqeNID-AVNVV-----LEEIDAHE-------------------IPTLLVMNKIDMLDDFEPRIDR 331
Cdd:PRK04213 78 DEIVRYIeDNAD-----RILaAVLVVdgksfIEIIERWEgrgeipidvemfdflrelgIPPIVAVNKMDKIKNRDEVLDE 152
|
|
| DRG |
cd01896 |
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ... |
199-234 |
8.29e-04 |
|
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: 40.61 E-value: 8.29e-04
10 20 30
....*....|....*....|....*....|....*.
gi 495778339 199 TVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDP 234
Cdd:cd01896 2 RVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTC 37
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
200-363 |
1.54e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 40.72 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 200 VSLVGYTNAGKSTLFNQIT-EAQVYAADQLFATLDPTLRRIDVAdvGET-VLADTVGFIRHLPHDLVAAFKATLQeTRQA 277
Cdd:PRK03003 214 VALVGKPNVGKSSLLNKLAgEERSVVDDVAGTTVDPVDSLIELG--GKTwRFVDTAGLRRRVKQASGHEYYASLR-THAA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 278 tlllhvIDAADVRVQEnIDAVNVVLEE--------IDAHEiPTLLVMNKIDMLDD-----FEPRIDRDEENKP--IRVWL 342
Cdd:PRK03003 291 ------IEAAEVAVVL-IDASEPISEQdqrvlsmvIEAGR-ALVLAFNKWDLVDEdrryyLEREIDRELAQVPwaPRVNI 362
|
170 180
....*....|....*....|.
gi 495778339 343 SAQTGLGVPLLFQALTERLSG 363
Cdd:PRK03003 363 SAKTGRAVDKLVPALETALES 383
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
202-361 |
2.16e-03 |
|
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206681 [Multi-domain] Cd Length: 157 Bit Score: 38.57 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 202 LVGYTNAGKSTLFNQIT---EAQVyaADQLFATLDptlRRIDVADVGET--VLADTVGFIrhlphdlvaAFKATLQE--T 274
Cdd:cd01894 2 IVGRPNVGKSTLFNRLTgrrDAIV--SDTPGVTRD---RKYGEAEWGGRefILIDTGGIE---------PDDEGISKeiR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 275 RQATLllhVIDAAD-----VRVQENIDAVNV-VLEEIDAHEIPTLLVMNKIDMLDDFEpriDRDEEN-----KPIRVwlS 343
Cdd:cd01894 68 EQAEI---AIEEADvilfvVDGREGLTPADEeIAKYLRKSKKPVILVVNKIDNIKEEE---EAAEFYslgfgEPIPI--S 139
|
170
....*....|....*...
gi 495778339 344 AQTGLGVPLLFQALTERL 361
Cdd:cd01894 140 AEHGRGIGDLLDAILELL 157
|
|
| FeoB |
COG0370 |
Fe2+ transporter FeoB [Inorganic ion transport and metabolism]; |
198-368 |
3.70e-03 |
|
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
Pssm-ID: 440139 [Multi-domain] Cd Length: 662 Bit Score: 39.72 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 198 PTVSLVGYTNAGKSTLFNQITEAQVYaadqlfatldptlrridvadVGE----TVlADTVGFIRHLPHDlvaafkatlqe 273
Cdd:COG0370 4 ITIALVGNPNVGKTTLFNALTGSRQK--------------------VGNwpgvTV-EKKEGKFKLKGKE----------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 274 trqatllLHVID----------------AADVRVQENIDA-VNVV----LE-------EIDAHEIPTLLVMNKIDMLDDF 325
Cdd:COG0370 52 -------IELVDlpgtyslsayspdekvARDFLLEEKPDVvVNVVdatnLErnlyltlQLLELGIPVVLALNMMDEAEKK 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495778339 326 EPRIDRDE-ENK---PIrVWLSAQTGLGVPLLFQALTERLSGEVAQH 368
Cdd:COG0370 125 GIKIDVEKlSKLlgvPV-VPTSARKGKGIDELKEAIIEAAEGKKPRP 170
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
199-387 |
6.03e-03 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 37.53 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 199 TVSLVGYTNAGKSTLFNQITEAQVYAADQLFATLDPTLRRIDVADvgETVLADTVGF---IRHlpHDLVaafkaTLQETR 275
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAVITVLRYGLLK--GVVLVDTPGLnstIEH--HTEI-----TESFLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 276 QATLLLHVIDAADVRVQENIDavnvVLEEI-DAHEIPTLLVMNKIDMLDDfEPRIDRDEENKpiRVWLSAQTGLGVPLLF 354
Cdd:cd09912 73 RADAVIFVLSADQPLTESERE----FLKEIlKWSGKKIFFVLNKIDLLSE-EELEEVLEYSR--EELGVLELGGGEPRIF 145
|
170 180 190
....*....|....*....|....*....|...
gi 495778339 355 qalteRLSGEVAQHTLRLPPQEGRLRSRFYQLQ 387
Cdd:cd09912 146 -----PVSAKEALEARLQGDEELLEQSGFEELE 173
|
|
| ATP_bind_1 |
pfam03029 |
Conserved hypothetical ATP binding protein; Members of this family are found in a range of ... |
220-342 |
8.04e-03 |
|
Conserved hypothetical ATP binding protein; Members of this family are found in a range of archaea and eukaryotes and have hypothesized ATP binding activity.
Pssm-ID: 397252 [Multi-domain] Cd Length: 238 Bit Score: 37.74 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778339 220 AQVYAADQLFATLDPTLRRIDVADVgeTVLADTVGFIRHLPH--DLVAAFKATlqETRQATLLLHVIDAadVRVQENIDA 297
Cdd:pfam03029 67 ALTVAMDFGRITLDWLDEELKREDD--YYLFDTPGQIELFTHwdSLAIIVEAL--ESRGALGAVYLVDT--RRLTDPTDF 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 495778339 298 VNVVLEEIDA---HEIPTLLVMNKIDMLD---------DFEPRIDRDEENKPIRVWL 342
Cdd:pfam03029 141 FSGLLYALSImlrLGLPFVVALNKFDLLSlefalkwftDPEDLQLLLELDDGKYRKL 197
|
|
| |
