|
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: 882.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 1 MFDRYDAGEQAVLVHIYFTQDKDMEDLQEFESLVSSAGVEALQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGASVVLF 80
Cdd:PRK11058 1 MFDRYEAGEQAVLVHIYFSQDKDMEDLQEFESLVSSAGVEALQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGASVVLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 81 DHALSPAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPGETQL 160
Cdd:PRK11058 81 DHALSPAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPGETQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 161 ETDRRLLRNRIVQIQSRLERVEKQREQGRQSRIKADVPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRID 240
Cdd:PRK11058 161 ETDRRLLRNRIVQILSRLERVEKQREQGRRARIKADVPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 241 VADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVIDAADVRVQENIEAVNTVLEEIDAHEIPTLLVMNKID 320
Cdd:PRK11058 241 VADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVVDAADVRVQENIEAVNTVLEEIDAHEIPTLLVMNKID 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 321 MLEDFEPRIDRDEENKPNRVWLSAQTGAGIPQLFQALTERLSGEVAQHTLRLPPQEGRLRSRFYQLQAIEKEWMEEDGSV 400
Cdd:PRK11058 321 MLDDFEPRIDRDEENKPIRVWLSAQTGAGIPLLFQALTERLSGEVAQHTLRLPPQEGRLRSRFYQLQAIEKEWMEEDGSV 400
|
410 420
....*....|....*....|....*.
gi 16131995 401 SLQVRMPIVDWRRLCKQEPALIDYLI 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: 654.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 1 MFDRYDAGEQAVLVHIYFTQD--KDMEDLQEFESLVSSAGVEALQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGASVV 78
Cdd:COG2262 1 MFEREERGERAILVGVDLPGSdeDAEESLEELAELAETAGAEVVGTVTQRRDKPDPATYIGKGKVEELAELVEELEADLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 79 LFDHALSPAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPGET 158
Cdd:COG2262 81 IFDDELSPSQQRNLEKALGVKVIDRTGLILDIFAQRARTREGKLQVELAQLQYLLPRLVGMWTHLSRQGGGIGTRGPGET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 159 QLETDRRLLRNRIVQIQSRLERVEKQREQGRQSRIKADVPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRR 238
Cdd:COG2262 161 QLETDRRLIRDRIARLKRELEKVRKQRELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 239 IDVADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVIDAADVRVQENIEAVNTVLEEIDAHEIPTLLVMNK 318
Cdd:COG2262 241 LELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNEVLEELGADDKPIILVFNK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 319 IDMLEDfePRIDRDEENKPNRVWLSAQTGAGIPQLFQALTERLSGEVAQHTLRLPPQEGRLRSRFYQLQAIEKEWMEEDG 398
Cdd:COG2262 321 IDLLDD--EELERLRAGYPDAVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYSDGDLVAWLHEHGEVLSEEYDEDG 398
|
410 420
....*....|....*....|..
gi 16131995 399 sVSLQVRMPIVDWRRLCKQEPA 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: 603.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 10 QAVLVHIYFTQDKDM-EDLQEFESLVSSAGVEALQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGASVVLFDHALSPAQ 88
Cdd:TIGR03156 1 RAILVGVDLGNEDDEeESLEELAELAETAGAEVVGTVTQKRSRPDPATYIGKGKVEEIAELVEELEADLVIFDHELSPSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 89 ERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPGETQLETDRRLLR 168
Cdd:TIGR03156 81 ERNLEKALGCRVIDRTGLILDIFAQRARTHEGKLQVELAQLKYLLPRLVGGWTHLSRQGGGIGTRGPGETQLETDRRLIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 169 NRIVQIQSRLERVEKQREQGRQSRIKADVPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETV 248
Cdd:TIGR03156 161 ERIAQLKKELEKVEKQRERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGADVYAADQLFATLDPTTRRLDLPDGGEVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 249 LADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVIDAADVRVQENIEAVNTVLEEIDAHEIPTLLVMNKIDMLEdfEPR 328
Cdd:TIGR03156 241 LTDTVGFIRDLPHELVAAFRATLEEVREADLLLHVVDASDPDREEQIEAVEKVLEELGAEDIPQLLVYNKIDLLD--EPR 318
|
330 340 350
....*....|....*....|....*....|...
gi 16131995 329 IDRDEENKPNRVWLSAQTGAGIPQLFQALTERL 361
Cdd:TIGR03156 319 IERLEEGYPEAVFVSAKTGEGLDLLLEAIAERL 351
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
157-361 |
6.20e-113 |
|
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: 329.42 E-value: 6.20e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 157 ETQLETDRRLLRNRIVQIQSRLERVEKQREQGRQSRIKADVPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTL 236
Cdd:cd01878 1 ETQLETDRRLIRERIAKLRKELEKVKKQRELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 237 RRIDVADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVIDAADVRVQENIEAVNTVLEEIDAHEIPTLLVM 316
Cdd:cd01878 81 RRIKLPGGREVLLTDTVGFIRDLPHQLVEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKELGADDIPIILVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131995 317 NKIDMLEDFEPRiDRDEENKPNRVWLSAQTGAGIPQLFQALTERL 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 |
9.84e-41 |
|
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: 139.79 E-value: 9.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 25 EDLQEFESLVSSAGVEALQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGASVVLFDHALSPAQERNLERLCECRVIDRT 104
Cdd:pfam13167 1 ESLEELEELAETAGAEVVGTVIQKRDKPDPATYIGKGKLEELKELVEALEADLVIFDDELSPSQQRNLEKALGVKVIDRT 80
|
....*..
gi 16131995 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 |
3.72e-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: 135.26 E-value: 3.72e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131995 114 RARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPGETQLETDRRLLRNRIVQIQSRLERVEKQREQGRQSR 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 |
1.38e-27 |
|
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: 105.78 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 199 TVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVgETVLADTVGFIR--HLPHDLVAAFKAtlqeTRQ 276
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGK-QIILVDTPGLIEgaSEGEGLGRAFLA----IIE 75
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 16131995 277 ATLLLHVIDAADvRVQENIEAVNTVLEEidaHEIPTLLVMNK 318
Cdd:pfam01926 76 ADLILFVVDSEE-GITPLDEELLELLRE---NKKPIILVLNK 113
|
|
| Obg_CgtA |
TIGR02729 |
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ... |
195-361 |
3.51e-22 |
|
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: 96.34 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 195 ADVptvSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFI-----------RHLPHdl 263
Cdd:TIGR02729 158 ADV---GLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIegasegaglghRFLKH-- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 264 vaafkatLQETRqatLLLHVIDAADVRVQENIEAVNTVLEEIDAH-----EIPTLLVMNKIDML--EDFEPRIDRDEENK 336
Cdd:TIGR02729 233 -------IERTR---VLLHLIDISPEDGSDPVEDYEIIRNELKKYspelaEKPRIVVLNKIDLLdeEELEELLKELKKEL 302
|
170 180
....*....|....*....|....*.
gi 16131995 337 PNRVW-LSAQTGAGIPQLFQALTERL 361
Cdd:TIGR02729 303 GKPVFpISALTGEGLDELLDALAELL 328
|
|
| obgE |
PRK12299 |
GTPase CgtA; Reviewed |
195-367 |
3.01e-21 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 93.98 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 195 ADVptvSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFI-----------RHLPHdl 263
Cdd:PRK12299 159 ADV---GLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKSFVIADIPGLIegasegaglghRFLKH-- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 264 vaafkatLQETRqatLLLHVIDAADVRVqenIEAVNTVLEEIDAH-----EIPTLLVMNKIDMLEDFEPRIDRDEENKPN 338
Cdd:PRK12299 234 -------IERTR---LLLHLVDIEAVDP---VEDYKTIRNELEKYspelaDKPRILVLNKIDLLDEEEEREKRAALELAA 300
|
170 180 190
....*....|....*....|....*....|...
gi 16131995 339 R----VWLSAQTGAGIPQLFQALTERLSGEVAQ 367
Cdd:PRK12299 301 LggpvFLISAVTGEGLDELLRALWELLEEARRE 333
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
195-361 |
2.68e-19 |
|
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: 84.78 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 195 ADVptvSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVG--------------FIRHlp 260
Cdd:cd01898 1 ADV---GLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGliegasegkglghrFLRH-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 261 hdlvaafkatLQETRqatLLLHVIDAADvrVQENIEAVNTVLEEIDAHEI-----PTLLVMNKIDMLED---FEPRIDRD 332
Cdd:cd01898 76 ----------IERTR---VLLHVIDLSG--EDDPVEDYETIRNELEAYNPglaekPRIVVLNKIDLLDAeerFEKLKELL 140
|
170 180 190
....*....|....*....|....*....|
gi 16131995 333 EENKPNRVW-LSAQTGAGIPQLFQALTERL 361
Cdd:cd01898 141 KELKGKKVFpISALTGEGLDELLKKLAKLL 170
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
202-359 |
1.18e-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: 79.81 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 202 LVGYTNAGKSTLFNRITEARVYAADQLFA-TLDPTLRRIDVADVGETV-LADTVGFIRHLPHDLVAAFKATLqetRQATL 279
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGEVGEVSDVPGtTRDPDVYVKELDKGKVKLvLVDTPGLDEFGGLGREELARLLL---RGADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 280 LLHVIDAADVRVQENIEavNTVLEEIDAHEIPTLLVMNKIDMLE----DFEPRIDRDEENKPNRVW-LSAQTGAGIPQLF 354
Cdd:cd00882 79 ILLVVDSTDRESEEDAK--LLILRRLRKEGIPIILVGNKIDLLEerevEELLRLEELAKILGVPVFeVSAKTGEGVDELF 156
|
....*
gi 16131995 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 |
2.34e-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: 76.13 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 202 LVGYTNAGKSTLFNRITEARVYA-ADQLFATLDPTLRRIDVADVGETVLADTVGFIRhLPHDLVAAFKATLQETRQATLL 280
Cdd:cd00880 2 IFGRPNVGKSSLLNALLGQNVGIvSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDE-EGGLGRERVEEARQVADRADLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 281 LHVIDAAdvrvqENIEAVNTVLEEIDAHEIPTLLVMNKIDMLEDFE----PRIDRDEENKPNR-VWLSAQTGAGIPQLFQ 355
Cdd:cd00880 81 LLVVDSD-----LTPVEEEAKLGLLRERGKPVLLVLNKIDLVPESEeeelLRERKLELLPDLPvIAVSALPGEGIDELRK 155
|
....*.
gi 16131995 356 ALTERL 361
Cdd:cd00880 156 KIAELL 161
|
|
| Obg_like |
cd01881 |
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
202-353 |
2.83e-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: 75.89 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 202 LVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIRHlPHDLVAAFKATLQETRQATLLL 281
Cdd:cd01881 2 LVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDG-ASEGRGLGEQILAHLYRSDLIL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131995 282 HVIDAADVRVQENIEAVNTVLEEIDAH-----EIPTLLVMNKIDMLEDFEPRIDR--DEENKPNRVWLSAQTGAGIPQL 353
Cdd:cd01881 81 HVIDASEDCVGDPLEDQKTLNEEVSGSflflkNKPEMIVANKIDMASENNLKRLKldKLKRGIPVVPTSALTRLGLDRV 159
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
163-391 |
3.84e-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: 77.02 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 163 DRRLLRNRIVQIQSRLERVEKQREQGRQSRikaDVPTVSLVGYTNAGKSTLFNRIteARVYAA----------DQLFATL 232
Cdd:COG0486 182 DREELLERLEELREELEALLASARQGELLR---EGIKVVIVGRPNVGKSSLLNAL--LGEERAivtdiagttrDVIEERI 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 233 DptLRRIDVadvgetVLADTVGfIRHlPHDLVAAF--KATLQETRQATLLLHVIDAADVRVQENIEavntVLEEIDahEI 310
Cdd:COG0486 257 N--IGGIPV------RLIDTAG-LRE-TEDEVEKIgiERAREAIEEADLVLLLLDASEPLTEEDEE----ILEKLK--DK 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 311 PTLLVMNKIDMLEDFEPRIDrdEENKPNRVWLSAQTGAGIPQLFQALTERLSGevaqhtlRLPPQEGRLRSRFYQLQAIE 390
Cdd:COG0486 321 PVIVVLNKIDLPSEADGELK--SLPGEPVIAISAKTGEGIDELKEAILELVGE-------GALEGEGVLLTNARHREALE 391
|
.
gi 16131995 391 K 391
Cdd:COG0486 392 R 392
|
|
| obgE |
PRK12297 |
GTPase CgtA; Reviewed |
195-362 |
5.24e-15 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237046 [Multi-domain] Cd Length: 424 Bit Score: 76.29 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 195 ADVptvSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVG--------------FIRHlp 260
Cdd:PRK12297 159 ADV---GLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRSFVMADIPGliegasegvglghqFLRH-- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 261 hdlvaafkatLQETRqatLLLHVIDAADVRVQENIEAVNTVLEEIDAH-----EIPTLLVMNKIDMlEDFEPRIDRDEEN 335
Cdd:PRK12297 234 ----------IERTR---VIVHVIDMSGSEGRDPIEDYEKINKELKLYnprllERPQIVVANKMDL-PEAEENLEEFKEK 299
|
170 180
....*....|....*....|....*...
gi 16131995 336 KPNRVW-LSAQTGAGIPQLFQALTERLS 362
Cdd:PRK12297 300 LGPKVFpISALTGQGLDELLYAVAELLE 327
|
|
| obgE |
PRK12298 |
GTPase CgtA; Reviewed |
195-398 |
2.35e-14 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237047 [Multi-domain] Cd Length: 390 Bit Score: 74.13 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 195 ADVptvSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFI-----------RHLPHdl 263
Cdd:PRK12298 160 ADV---GLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDERSFVVADIPGLIegasegaglgiRFLKH-- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 264 vaafkatLQETRqatLLLHVIDAADVRVQENIEAVNTVLEEIDAH-----EIPTLLVMNKIDMLEDfEPRIDRDEENKPN 338
Cdd:PRK12298 235 -------LERCR---VLLHLIDIAPIDGSDPVENARIIINELEKYspklaEKPRWLVFNKIDLLDE-EEAEERAKAIVEA 303
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131995 339 RVW------LSAQTGAGIPQLFQALTERL-SGEVAQHTLRLPPQEGRLRSRFYQLQAIEKEWMEEDG 398
Cdd:PRK12298 304 LGWegpvylISAASGLGVKELCWDLMTFIeENPREEAEEAEAPEKVEFMWDDYHREQLEEVEEEDDD 370
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
161-391 |
1.47e-13 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 72.07 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 161 ETDRRLLRNRIVQIQSRLERVEKQREQGRQSR--IKadvptVSLVGYTNAGKSTLFNRItearvyaadqlfatldptLRR 238
Cdd:PRK05291 182 FLSDEKILEKLEELIAELEALLASARQGEILRegLK-----VVIAGRPNVGKSSLLNAL------------------LGE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 239 iDVADV----GET---------------VLADTVGfIRHlPHDLVAA--FKATLQETRQATLLLHVIDAADVRVQENIEa 297
Cdd:PRK05291 239 -ERAIVtdiaGTTrdvieehinldgiplRLIDTAG-IRE-TDDEVEKigIERSREAIEEADLVLLVLDASEPLTEEDDE- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 298 vntVLEEIDahEIPTLLVMNKIDMLEDfeprIDRDEENKPNRVWLSAQTGAGIPQLFQALTERLsgevaqHTLRLPPQEG 377
Cdd:PRK05291 315 ---ILEELK--DKPVIVVLNKADLTGE----IDLEEENGKPVIRISAKTGEGIDELREAIKELA------FGGFGGNQEG 379
|
250
....*....|....
gi 16131995 378 RLRSRFYQLQAIEK 391
Cdd:PRK05291 380 VFLTNARHLEALER 393
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
200-361 |
4.10e-12 |
|
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: 64.02 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 200 VSLVGYTNAGKSTLFNRITEARVYAA---DQlfatldpTLRR----IDVADVGETVLADTVGFirHLPHD-----LVAAF 267
Cdd:cd04163 6 VAIIGRPNVGKSTLLNALVGQKISIVspkPQ-------TTRNrirgIYTDDDAQIIFVDTPGI--HKPKKklgerMVKAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 268 KATLQEtrqATLLLHVIDAaDVRVQENIEavnTVLEEIDAHEIPTLLVMNKIDMLEDFEPRIDRDEENKPNRVW-----L 342
Cdd:cd04163 77 WSALKD---VDLVLFVVDA-SEWIGEGDE---FILELLKKSKTPVILVLNKIDLVKDKEDLLPLLEKLKELHPFaeifpI 149
|
170
....*....|....*....
gi 16131995 343 SAQTGAGIPQLFQALTERL 361
Cdd:cd04163 150 SALKGENVDELLEYIVEYL 168
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
199-361 |
5.24e-12 |
|
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: 63.67 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 199 TVSLVGYTNAGKSTLFNRItearvyaadqlfatldptLRRiDVA----------DVGET---------VLADTVGfIRHL 259
Cdd:cd04164 5 KVVIAGKPNVGKSSLLNAL------------------AGR-DRAivsdiagttrDVIEEeidlggipvRLIDTAG-LRET 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 260 PhDLV--AAFKATLQETRQATLLLHVIDAadvrvQENIEAVNTVLEEIDAhEIPTLLVMNKIDMLEDFEPRIdrdEENKP 337
Cdd:cd04164 65 E-DEIekIGIERAREAIEEADLVLLVVDA-----SEGLDEEDLEILELPA-KKPVIVVLNKSDLLSDAEGIS---ELNGK 134
|
170 180
....*....|....*....|....
gi 16131995 338 NRVWLSAQTGAGIPQLFQALTERL 361
Cdd:cd04164 135 PIIAISAKTGEGIDELKEALLELA 158
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
200-361 |
2.20e-11 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 64.30 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 200 VSLVGYTNAGKSTLFNRITEARVyaadqlfATLDP---TLRR----IDVADVGETVLADTVGFirHLPHD-----LVAAF 267
Cdd:PRK00089 8 VAIVGRPNVGKSTLLNALVGQKI-------SIVSPkpqTTRHrirgIVTEDDAQIIFVDTPGI--HKPKRalnraMNKAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 268 KATLQEtrqATLLLHVIDAADvrvqENIEAVNTVLEEIDAHEIPTLLVMNKIDML---EDFEPRIDRDEENKPNR--VWL 342
Cdd:PRK00089 79 WSSLKD---VDLVLFVVDADE----KIGPGDEFILEKLKKVKTPVILVLNKIDLVkdkEELLPLLEELSELMDFAeiVPI 151
|
170
....*....|....*....
gi 16131995 343 SAQTGAGIPQLFQALTERL 361
Cdd:PRK00089 152 SALKGDNVDELLDVIAKYL 170
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
200-361 |
1.51e-10 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 61.54 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 200 VSLVGYTNAGKSTLFNR-------ITEARVyaadQlfatldpTLRR----IDVADVGETVLADTVGFirHLPHD-----L 263
Cdd:COG1159 6 VAIVGRPNVGKSTLLNAlvgqkvsIVSPKP----Q-------TTRHrirgIVTREDAQIVFVDTPGI--HKPKRklgrrM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 264 VAAFKATLQEtrqATLLLHVIDAaDVRVQENIEAVntvLEEIDAHEIPTLLVMNKIDML--EDFEPRIDRDEENKPNR-- 339
Cdd:COG1159 73 NKAAWSALED---VDVILFVVDA-TEKIGEGDEFI---LELLKKLKTPVILVINKIDLVkkEELLPLLAEYSELLDFAei 145
|
170 180
....*....|....*....|..
gi 16131995 340 VWLSAQTGAGIPQLFQALTERL 361
Cdd:COG1159 146 VPISALKGDNVDELLDEIAKLL 167
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
167-364 |
2.75e-10 |
|
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: 61.34 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 167 LRNRIVQIQSRLERVEKQREQGRQSR--IKadvptVSLVGYTNAGKSTLFNRIT-EARvyaadqlfA--------TLDpT 235
Cdd:pfam12631 67 LLERLEELLAELEKLLATADRGRILRegIK-----VVIVGKPNVGKSSLLNALLgEER--------AivtdipgtTRD-V 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 236 LR-RIDVADVgeTV-LADTVGfIRHlPHDLVAAF--KATLQETRQATLLLHVIDAADVRVQENIEavntvLEEIDAHEIP 311
Cdd:pfam12631 133 IEeTINIGGI--PLrLIDTAG-IRE-TDDEVEKIgiERAREAIEEADLVLLVLDASRPLDEEDLE-----ILELLKDKKP 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131995 312 TLLVMNKIDMLEDFEPRIDRDEEnkpNRVWLSAQTGAGIPQLFQALTERLSGE 364
Cdd:pfam12631 204 IIVVLNKSDLLGEIDELEELKGK---PVLAISAKTGEGLDELEEAIKELFLAG 253
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
179-323 |
3.35e-10 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 60.94 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 179 ERVEKQREQGRQSRIKADVPTVSLVGYTNAGKSTLFNRITEARVYAADQLFA-TLDPTLRRIDVADVGETVLADTVGF-I 256
Cdd:COG3596 21 VLRELLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPcTREIQRYRLESDGLPGLVLLDTPGLgE 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131995 257 RHLPHdlvAAFKATLQETRQATLLLHVIDAADVRVQENIEAVNTVLEEIDahEIPTLLVMNKIDMLE 323
Cdd:COG3596 101 VNERD---REYRELRELLPEADLILWVVKADDRALATDEEFLQALRAQYP--DPPVLVVLTQVDRLE 162
|
|
| obgE |
PRK12296 |
GTPase CgtA; Reviewed |
195-376 |
1.19e-08 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237045 [Multi-domain] Cd Length: 500 Bit Score: 56.80 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 195 ADVptvSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLrriDVADVGETV--LADTVGFI------RHLPHDLvaa 266
Cdd:PRK12296 160 ADV---GLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNL---GVVQAGDTRftVADVPGLIpgasegKGLGLDF--- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 267 fkatLQETRQATLLLHVIDAA----------DVRVQEN-----IEAVNTVLEEIDAHEIPTLLVMNKID------MLEDF 325
Cdd:PRK12296 231 ----LRHIERCAVLVHVVDCAtlepgrdplsDIDALEAelaayAPALDGDLGLGDLAERPRLVVLNKIDvpdareLAEFV 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131995 326 EPRIdrdeENKPNRVW-LSAQTGAGIPQLFQALTERlsgeVAQHTLRLPPQE 376
Cdd:PRK12296 307 RPEL----EARGWPVFeVSAASREGLRELSFALAEL----VEEARAAEPEAE 350
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
198-361 |
4.56e-08 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 55.19 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 198 PTVSLVGYTNAGKSTLFNRIT-EARVYAADQLFATLDP--TLRRIDvadvGETVL-ADTVGfIRHLPHDLVAA-FKATLQ 272
Cdd:PRK09518 451 RRVALVGRPNVGKSSLLNQLThEERAVVNDLAGTTRDPvdEIVEID----GEDWLfIDTAG-IKRRQHKLTGAeYYSSLR 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 273 ET---RQATLLLHVIDAADVRVQENIEAVNTVLEEIDAheipTLLVMNKIDMLEDFE-PRIDRDEENKPNRV-W-----L 342
Cdd:PRK09518 526 TQaaiERSELALFLFDASQPISEQDLKVMSMAVDAGRA----LVLVFNKWDLMDEFRrQRLERLWKTEFDRVtWarrvnL 601
|
170
....*....|....*....
gi 16131995 343 SAQTGAGIPQLFQALTERL 361
Cdd:PRK09518 602 SAKTGWHTNRLAPAMQEAL 620
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
196-359 |
1.83e-07 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 50.89 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 196 DVPTVSLVGYTNAGKSTLFNRIT-EARVYAADQLFATLDPtlrrIDVaDV---GET-VLADTVGfIRHLPH-----DLVA 265
Cdd:cd01895 1 DPIKIAIIGRPNVGKSSLLNALLgEERVIVSDIAGTTRDS----IDV-PFeydGQKyTLIDTAG-IRKKGKvtegiEKYS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 266 AFKaTLQETRQATLLLHVIDAadvrvQENIEAVN-TVLEEIDAHEIPTLLVMNKIDMLEDFEPRIDRDEENKPNR----- 339
Cdd:cd01895 75 VLR-TLKAIERADVVLLVLDA-----SEGITEQDlRIAGLILEEGKALIIVVNKWDLVEKDEKTMKEFEKELRRKlpfld 148
|
170 180
....*....|....*....|....
gi 16131995 340 ----VWLSAQTGAGIPQLFQALTE 359
Cdd:cd01895 149 yapiVFISALTGQGVDKLFDAIKE 172
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
198-361 |
2.74e-07 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 52.33 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 198 PTVSLVGYTNAGKSTLFNRITEARVyA--ADQLFATLDptlRRIDVADVGET--VLADTVGFIRHLPHDLVAAFKA-TLQ 272
Cdd:COG1160 3 PVVAIVGRPNVGKSTLFNRLTGRRD-AivDDTPGVTRD---RIYGEAEWGGRefTLIDTGGIEPDDDDGLEAEIREqAEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 273 ETRQATLLLHVIDAadvrvqenIEAVNTVLEEIdAHEI-----PTLLVMNKID------MLEDF------EPridrdeen 335
Cdd:COG1160 79 AIEEADVILFVVDG--------RAGLTPLDEEI-AKLLrrsgkPVILVVNKVDgpkreaDAAEFyslglgEP-------- 141
|
170 180
....*....|....*....|....*.
gi 16131995 336 kpnrVWLSAQTGAGIPQLFQALTERL 361
Cdd:COG1160 142 ----IPISAEHGRGVGDLLDAVLELL 163
|
|
| Rbg1 |
COG1163 |
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; |
164-361 |
1.06e-06 |
|
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440777 [Multi-domain] Cd Length: 368 Bit Score: 50.57 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 164 RRLLRNRIVQIQSRLERvEKQREQGRQSRI---KADVPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDP---TLR 237
Cdd:COG1163 28 IGRLKAKLAELKEELEK-RKKKSGGGGEGFavkKSGDATVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVvpgMLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 238 ----RIDVADV-------------GETVL-----ADTVGFIrhLPHDLVAAFKATLQETRQATLLL-------------- 281
Cdd:COG1163 107 ykgaKIQILDVpgliegaasgkgrGKEVLsvvrnADLILIV--LDVFELEQYDVLKEELYDAGIRLnkpppdvtiekkgk 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 282 ------------------------HVIDAADVRVQENIeavnTVLEEIDAHE-----IPTLLVMNKIDML-EDFEPRIDR 331
Cdd:COG1163 185 ggirvnstgkldldeedikkilreYGIVNADVLIREDV----TLDDLIDALMgnrvyKPAIVVVNKIDLAdEEYVEELKS 260
|
250 260 270
....*....|....*....|....*....|
gi 16131995 332 DEENKPNRVWLSAQTGAGIPQLFQALTERL 361
Cdd:COG1163 261 KLPDGVPVIFISAEKGIGLEELKEEIFEEL 290
|
|
| HflX_C |
pfam19275 |
HflX C-terminal domain; This entry represents the C-terminal domain of the HflX protein. HflX ... |
334-406 |
1.62e-06 |
|
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: 46.15 E-value: 1.62e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131995 334 ENKPNRVWLSAQTGAGIPQLFQALTERLSGEVAQHTLRLPPQEGRLRSRFYQlQAI--EKEWMeEDGSVSLQVRM 406
Cdd:pfam19275 7 AGRENVIAVSAITGEGVDALMDEISRRLSGVLTETTVVLPADKLALLSWVYE-NAIvdGREDN-EDGSVSLDVRL 79
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
200-355 |
4.87e-06 |
|
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: 46.21 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 200 VSLVGYTNAGKSTLFNRITEarvyaaDQLFAT-LDPTLRRIDVADV----GETVLA---DTVGFIRHLPhDLVAAFKATL 271
Cdd:TIGR00231 4 IVIVGHPNVGKSTLLNSLLG------NKGSITeYYPGTTRNYVTTVieedGKTYKFnllDTAGQEDYDA-IRRLYYPQVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 272 QETRQATLLLHVIDAADVrVQENIEAVNTVLEEidahEIPTLLVMNKIDML-EDFEP--RIDRDEENKPNRVWLSAQTGA 348
Cdd:TIGR00231 77 RSLRVFDIVILVLDVEEI-LEKQTKEIIHHADS----GVPIILVGNKIDLKdADLKThvASEFAKLNGEPIIPLSAETGK 151
|
....*..
gi 16131995 349 GIPQLFQ 355
Cdd:TIGR00231 152 NIDSAFK 158
|
|
| PTZ00258 |
PTZ00258 |
GTP-binding protein; Provisional |
200-323 |
7.31e-06 |
|
GTP-binding protein; Provisional
Pssm-ID: 240334 [Multi-domain] Cd Length: 390 Bit Score: 48.02 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 200 VSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVAD---------------VGETV-LADTVGFIR--HLPH 261
Cdd:PTZ00258 24 MGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDerfdwlckhfkpksiVPAQLdITDIAGLVKgaSEGE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131995 262 DLVAAFkatLQETRQATLLLHVI----DAADVRVQENIEAVNtvleeiDAHEIPTLLVMNKIDMLE 323
Cdd:PTZ00258 104 GLGNAF---LSHIRAVDGIYHVVrafeDEDITHVEGEIDPVR------DLEIISSELILKDLEFVE 160
|
|
| FeoB_N |
pfam02421 |
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ... |
199-357 |
8.48e-06 |
|
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: 45.52 E-value: 8.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 199 TVSLVGYTNAGKSTLFNRITEARVYAADqlFA--TLDPTLRRIDVADVgETVLADtvgfirhLP--HDLVAafkATLQE- 273
Cdd:pfam02421 2 TIALVGNPNVGKTTLFNALTGANQHVGN--WPgvTVEKKEGKFKYKGY-EIEIVD-------LPgiYSLSP---YSEEEr 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 274 -TRQ------ATLLLHVIDAAdvrvqeNIE-AVNTVLEEIDAhEIPTLLVMNKIDMLEDFEPRIDRDE-ENKPNR--VWL 342
Cdd:pfam02421 69 vARDyllnekPDVIVNVVDAT------NLErNLYLTLQLLEL-GLPVVLALNMMDEAEKKGIKIDIKKlSELLGVpvVPT 141
|
170
....*....|....*
gi 16131995 343 SAQTGAGIPQLFQAL 357
Cdd:pfam02421 142 SARKGEGIDELLDAI 156
|
|
| NOG |
cd01897 |
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ... |
198-362 |
1.84e-05 |
|
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: 44.86 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 198 PTVSLVGYTNAGKSTLFNRITEARVYAADQLFAT-------LDPTLRRIDVADV-G--------------ETVLAdtvgf 255
Cdd:cd01897 1 RTLVIAGYPNVGKSSLVNKLTRAKPEVAPYPFTTkslfvghFDYKYLRWQVIDTpGildrpleerntiemQAITA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 256 IRHLphdlvaafkatlqetrqATLLLHVIDAAD-----VRVQENIeavntvLEEIDAH-EIPTLLVMNKIDMLEDFEPRI 329
Cdd:cd01897 76 LAHL-----------------RAAVLFFIDPSEtcgysIEEQLSL------FKEIKPLfNKPVIVVLNKIDLLTEEDLSE 132
|
170 180 190
....*....|....*....|....*....|....*
gi 16131995 330 DRDEENKPNRVWL--SAQTGAGIPQLFQALTERLS 362
Cdd:cd01897 133 IEKELEKEGEEVIkiSTLTEEGVDELKNKACELLL 167
|
|
| YchF |
cd01900 |
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ... |
203-254 |
3.43e-05 |
|
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: 45.14 E-value: 3.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 16131995 203 VGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVG 254
Cdd:cd01900 4 VGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERLDKLAEIVK 55
|
|
| 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 |
4.49e-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: 42.41 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 258 HLPHDLVaafKATLQETRqatlllhvIDAADVRVQENIeavnTVLEEIDAHE-----IPTLLVMNKIDML-EDFEPRIDR 331
Cdd:pfam16897 13 KLDEETI---KAILREYK--------IHNADVLIREDV----TVDDLIDVIEgnrvyIPCLYVYNKIDLIsIEELDRLAR 77
|
90 100 110
....*....|....*....|....*....|
gi 16131995 332 deenKPNRVWLSAQTGAGIPQLFQALTERL 361
Cdd:pfam16897 78 ----EPDSVPISAEKGLNLDELKERIWEYL 103
|
|
| PRK09602 |
PRK09602 |
translation-associated GTPase; Reviewed |
199-306 |
5.36e-05 |
|
translation-associated GTPase; Reviewed
Pssm-ID: 236584 [Multi-domain] Cd Length: 396 Bit Score: 45.18 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 199 TVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDP----TLRRIDVA--DVGETVLADT---VGFIRHLPHDL--VA-- 265
Cdd:PRK09602 3 TIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPnvgvAYVRVECPckELGVKCNPRNgkcIDGTRFIPVELidVAgl 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131995 266 ------------AFkatLQETRQATLLLHVIDAA----------DVRVQENIEAVNTVLEEID 306
Cdd:PRK09602 83 vpgahegrglgnQF---LDDLRQADALIHVVDASgstdeegnpvEPGSHDPVEDIKFLEEELD 142
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
196-359 |
6.54e-05 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 45.01 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 196 DVPTVSLVGYTNAGKSTLFNRIT-EARVYAADQlfA--TLDPtlrrIDVaDV---GET-VLADTVGfIRHlphdlvaafK 268
Cdd:COG1160 174 DPIKIAIVGRPNVGKSSLINALLgEERVIVSDI--AgtTRDS----IDT-PFerdGKKyTLIDTAG-IRR---------K 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 269 ATLQE---------TRQAtlllhvIDAADVrvqenieavntVLEEIDAHEIPT-----------------LLVMNKIDML 322
Cdd:COG1160 237 GKVDEgiekysvlrTLRA------IERADV-----------VLLVIDATEGITeqdlkiaglaleagkalVIVVNKWDLV 299
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131995 323 EDFEPRIDRDEE---------NKPNRVWLSAQTGAGIPQLFQALTE 359
Cdd:COG1160 300 EKDRKTREELEKeirrrlpflDYAPIVFISALTGQGVDKLLEAVDE 345
|
|
| FeoB |
cd01879 |
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
202-363 |
8.92e-05 |
|
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.
Pssm-ID: 206667 [Multi-domain] Cd Length: 159 Bit Score: 42.44 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 202 LVGYTNAGKSTLFNRITEARVY----------AADQLFATLDPTLRRIDV----------ADvgETVladTVGFIRHLPH 261
Cdd:cd01879 2 LVGNPNVGKTTLFNALTGARQKvgnwpgvtveKKEGEFKLGGKEIEIVDLpgtysltpysED--EKV---ARDFLLGEEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 262 DLVaafkatlqetrqatllLHVIDAAdvrvqeNIE-AVNTVLEEIDAhEIPTLLVMNKIDMLEDFEPRIDRD---EENKP 337
Cdd:cd01879 77 DLI----------------VNVVDAT------NLErNLYLTLQLLEL-GLPVVVALNMIDEAEKRGIKIDLDklsELLGV 133
|
170 180
....*....|....*....|....*.
gi 16131995 338 NRVWLSAQTGAGIPQLFQALTERLSG 363
Cdd:cd01879 134 PVVPTSARKGEGIDELLDAIAKLAES 159
|
|
| Arf_Arl |
cd00878 |
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
202-360 |
1.34e-04 |
|
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.
Pssm-ID: 206644 [Multi-domain] Cd Length: 158 Bit Score: 42.18 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 202 LVGYTNAGKSTLFNRItearvyaADQLFATLDPTL-----------RRIDVADVGEtvlADTvgfIRHL-PHDlvaaFKA 269
Cdd:cd00878 4 MLGLDGAGKTTILYKL-------KLGEVVTTIPTIgfnvetveyknVKFTVWDVGG---QDK---IRPLwKHY----YEN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 270 TlqetrQAtlLLHVIDAADV-RVQENIEAVNTVLEEIDAHEIPTLLVMNKIDMLEDFEPRIDRDE---ENKPNRVWL--- 342
Cdd:cd00878 67 T-----DG--LIFVVDSSDReRIEEAKNELHKLLNEEELKGAPLLILANKQDLPGALTESELIELlglESIKGRRWHiqp 139
|
170
....*....|....*....
gi 16131995 343 -SAQTGAGIPQLFQALTER 360
Cdd:cd00878 140 cSAVTGDGLDEGLDWLIEQ 158
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
196-361 |
1.60e-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: 42.51 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 196 DVPTVSLVGYTNAGKSTLFNRITEA------RVYAADQLFATLD--PTLRR----IDVADV---GETV---LADTVGfir 257
Cdd:pfam00009 2 RHRNIGIIGHVDHGKTTLTDRLLYYtgaiskRGEVKGEGEAGLDnlPEERErgitIKSAAVsfeTKDYlinLIDTPG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 258 hlpHdlvAAF-KATLQETRQATLLLHVIDAADvRVQENIEavnTVLEEIDAHEIPTLLVMNKIDMLEDFEPRIDRDE--- 333
Cdd:pfam00009 79 ---H---VDFvKEVIRGLAQADGAILVVDAVE-GVMPQTR---EHLRLARQLGVPIIVFINKMDRVDGAELEEVVEEvsr 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131995 334 -------ENKPNRVWL--SAQTGAGIPQLFQALTERL 361
Cdd:pfam00009 149 ellekygEDGEFVPVVpgSALKGEGVQTLLDALDEYL 185
|
|
| DRG |
cd01896 |
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ... |
199-361 |
1.61e-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: 42.92 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 199 TVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDP---TLR----RIDVADV-------------GETVLA-------- 250
Cdd:cd01896 2 RVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCvpgVMEykgaKIQLLDLpgiiegasdgkgrGRQVIAvartadli 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 251 --------------------DTVGfIR---------------------------HLPHDLVaafKATLQETRqatlllhv 283
Cdd:cd01896 82 livldatkpegqreilerelEGVG-IRlnkkppnvtikkkkkgginitstvpltKLDEKTV---KAILREYK-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 284 IDAADVRVQENIeavnTVLEEIDAHE-----IPTLLVMNKIDMLEdfEPRIDRDEEnKPNRVWLSAQTGAGIPQLFQALT 358
Cdd:cd01896 150 IHNADVLIREDI----TVDDLIDVIEgnrvyIPCLYVYNKIDLIS--IEELDRLAR-IPNSVVISAEKDLNLDELLERIW 222
|
...
gi 16131995 359 ERL 361
Cdd:cd01896 223 DYL 225
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
198-361 |
1.75e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 43.50 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 198 PTVSLVGYTNAGKSTLFNRITEARVyA--ADQLFATLDptlRRIDVADVG--ETVLADTVGFIRHlPHDLVAAFKA-TLQ 272
Cdd:PRK00093 2 PVVAIVGRPNVGKSTLFNRLTGKRD-AivADTPGVTRD---RIYGEAEWLgrEFILIDTGGIEPD-DDGFEKQIREqAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 273 ETRQATLLLHVIDA------ADvrvqenieavntvlEEIdAHEI-----PTLLVMNKID------MLEDF------EPri 329
Cdd:PRK00093 77 AIEEADVILFVVDGragltpAD--------------EEI-AKILrksnkPVILVVNKVDgpdeeaDAYEFyslglgEP-- 139
|
170 180 190
....*....|....*....|....*....|..
gi 16131995 330 drdeenkpnrVWLSAQTGAGIPQLFQALTERL 361
Cdd:PRK00093 140 ----------YPISAEHGRGIGDLLDAILEEL 161
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
202-361 |
1.84e-04 |
|
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: 41.65 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 202 LVGYTNAGKSTLFNRITEAR---VyaADQLFATLDptlRRIDVADVGET--VLADTVGFIRHLPHDLVAAFKATLQETRQ 276
Cdd:cd01894 2 IVGRPNVGKSTLFNRLTGRRdaiV--SDTPGVTRD---RKYGEAEWGGRefILIDTGGIEPDDEGISKEIREQAEIAIEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 277 ATLLLHVIDAADVRVQENIEavntVLEEIDAHEIPTLLVMNKIDmleDFEPRIDRDEENK---PNRVWLSAQTGAGIPQL 353
Cdd:cd01894 77 ADVILFVVDGREGLTPADEE----IAKYLRKSKKPVILVVNKID---NIKEEEEAAEFYSlgfGEPIPISAEHGRGIGDL 149
|
....*...
gi 16131995 354 FQALTERL 361
Cdd:cd01894 150 LDAILELL 157
|
|
| GTP1 |
COG0012 |
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ... |
202-243 |
2.12e-04 |
|
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439783 [Multi-domain] Cd Length: 362 Bit Score: 43.09 E-value: 2.12e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 16131995 202 LVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVAD 243
Cdd:COG0012 5 IVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPD 46
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
200-363 |
6.66e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 41.88 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 200 VSLVGYTNAGKSTLFNRIT-EARVYAADQLFATLDPTLRRIDVAdvGET-VLADTVGFIRHLPHDLVAAFKATLQeTRQA 277
Cdd:PRK03003 214 VALVGKPNVGKSSLLNKLAgEERSVVDDVAGTTVDPVDSLIELG--GKTwRFVDTAGLRRRVKQASGHEYYASLR-THAA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 278 tlllhvIDAADVRV----------QENIEAVNTVLEEIDAheipTLLVMNKIDMLED-----FEPRIDRDEENKP--NRV 340
Cdd:PRK03003 291 ------IEAAEVAVvlidasepisEQDQRVLSMVIEAGRA----LVLAFNKWDLVDEdrryyLEREIDRELAQVPwaPRV 360
|
170 180
....*....|....*....|...
gi 16131995 341 WLSAQTGAGIPQLFQALTERLSG 363
Cdd:PRK03003 361 NISAKTGRAVDKLVPALETALES 383
|
|
| Ygr210 |
cd01899 |
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ... |
200-287 |
8.96e-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: 41.06 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 200 VSLVGYTNAGKSTLFNRITEARVYAADQLFATLDP----TLRRIDVADVGETVLA-DTVGF----IRHLPHDL--VAA-- 266
Cdd:cd01899 1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPnvgvGYVRVECPCKELGVSCnPRYGKcidgKRYVPVELidVAGlv 80
|
90 100 110
....*....|....*....|....*....|...
gi 16131995 267 ------------FkatLQETRQATLLLHVIDAA 287
Cdd:cd01899 81 pgahegkglgnqF---LDDLRDADVLIHVVDAS 110
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
199-387 |
1.16e-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: 39.84 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 199 TVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADvgETVLADTVGF---IRHlpHDLVaafkaTLQETR 275
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAVITVLRYGLLK--GVVLVDTPGLnstIEH--HTEI-----TESFLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 276 QATLLLHVIDAADVRVQENIEAVNTVLeeiDAHEIPTLLVMNKIDMLEDfEPRIDRDEENKpnRVWLSAQTGAGIPQLFq 355
Cdd:cd09912 73 RADAVIFVLSADQPLTESEREFLKEIL---KWSGKKIFFVLNKIDLLSE-EELEEVLEYSR--EELGVLELGGGEPRIF- 145
|
170 180 190
....*....|....*....|....*....|..
gi 16131995 356 alteRLSGEVAQHTLRLPPQEGRLRSRFYQLQ 387
Cdd:cd09912 146 ----PVSAKEALEARLQGDEELLEQSGFEELE 173
|
|
| FeoB |
COG0370 |
Fe2+ transporter FeoB [Inorganic ion transport and metabolism]; |
198-368 |
2.07e-03 |
|
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
Pssm-ID: 440139 [Multi-domain] Cd Length: 662 Bit Score: 40.49 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 198 PTVSLVGYTNAGKSTLFNRITEARVYAA-------DQLFATLDPTLRRIDVADV-G----------ETVladTVGFIRHL 259
Cdd:COG0370 4 ITIALVGNPNVGKTTLFNALTGSRQKVGnwpgvtvEKKEGKFKLKGKEIELVDLpGtyslsayspdEKV---ARDFLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 260 PHDLVaafkatlqetrqatllLHVIDAadvrvqenieavnTVLE-------EIDAHEIPTLLVMNKIDMLEDFEPRIDRD 332
Cdd:COG0370 81 KPDVV----------------VNVVDA-------------TNLErnlyltlQLLELGIPVVLALNMMDEAEKKGIKIDVE 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131995 333 EenkpnrvwLS-----------AQTGAGIPQLFQALTERLSGEVAQH 368
Cdd:COG0370 132 K--------LSkllgvpvvptsARKGKGIDELKEAIIEAAEGKKPRP 170
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
202-361 |
2.90e-03 |
|
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: 37.70 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 202 LVGYTNAGKSTLFNRITEARVYAADQLFA-TLDPTlrRIDVADVGE-TVLADTVGFIRHLPHDLVAAfKATLQETRQATL 279
Cdd:cd11383 2 LMGKTGAGKSSLCNALFGTEVAAVGDRRPtTRAAQ--AYVWQTGGDgLVLLDLPGVGERGRRDREYE-ELYRRLLPEADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 280 LLHVIDAADVRVQENIEavnTVLEEIDAHEIPTLLVMNKIDmledfepridrdeenkpNRVWLSAQTGAGIPQLFQALTE 359
Cdd:cd11383 79 VLWLLDADDRALAADHD---FYLLPLAGHDAPLLFVLNQVD-----------------PVLAVSARTGWGLDELAEALIT 138
|
..
gi 16131995 360 RL 361
Cdd:cd11383 139 AL 140
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
199-362 |
4.40e-03 |
|
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: 38.04 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 199 TVSLVGYTNAGKSTLFNRIT-------EARVYAADQLFA---------TLDPTLRRIDVADVGETVLaDTVGfirHLphD 262
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLyqtgaidRRGTRKETFLDTlkeerergiTIKTGVVEFEWPKRRINFI-DTPG---HE--D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131995 263 LVAAFKATLqetRQATLLLHVIDAAD-VRVQeNIEAVNTVLEEIdaheIPTLLVMNKIDML--EDFE------------- 326
Cdd:cd00881 75 FSKETVRGL---AQADGALLVVDANEgVEPQ-TREHLNIALAGG----LPIIVAVNKIDRVgeEDFDevlreikellkli 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 16131995 327 PRIDRDEENkPNRVWLSAQTGAGIPQLFQALTERLS 362
Cdd:cd00881 147 GFTFLKGKD-VPIIPISALTGEGIEELLDAIVEHLP 181
|
|
| |
