|
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: 881.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 1 MFDRYDAGEQAVLVHIYFSQDKDMEDLQEFETLASSAGVEAMQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGASVVLF 80
Cdd:PRK11058 1 MFDRYEAGEQAVLVHIYFSQDKDMEDLQEFESLVSSAGVEALQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGASVVLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 81 DHALSPAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHMATRLVRGWTHLERQKGGIGLRGPGETQL 160
Cdd:PRK11058 81 DHALSPAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPGETQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 161 ETDRRLLRNRIMQILSRLEKVEKQREQGRRSRAKADIPTVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRRID 240
Cdd:PRK11058 161 ETDRRLLRNRIVQILSRLERVEKQREQGRRARIKADVPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 241 VPDVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVIDAADVRVQENIDAVNTVLAEIEADEIPALLVMNKID 320
Cdd:PRK11058 241 VADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVVDAADVRVQENIEAVNTVLEEIDAHEIPTLLVMNKID 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 321 MLDDFEPRIDRDDENKPIRVWLSAQTGVGVPLLFQALTERLSGEVAQHTLRLPPKEGRLRSRFYQLQAIEKEWMEDDGSV 400
Cdd:PRK11058 321 MLDDFEPRIDRDEENKPIRVWLSAQTGAGIPLLFQALTERLSGEVAQHTLRLPPQEGRLRSRFYQLQAIEKEWMEEDGSV 400
|
410 420
....*....|....*....|....*.
gi 490248609 401 SLQVRMPIVDWRRLCKQEPTLVDYVV 426
Cdd:PRK11058 401 SLQVRMPIVDWRRLCKQEPALIDYIV 426
|
|
| HflX |
COG2262 |
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
1-419 |
0e+00 |
|
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 651.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 1 MFDRYDAGEQAVLVHIYFSQD--KDMEDLQEFETLASSAGVEAMQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGASVV 78
Cdd:COG2262 1 MFEREERGERAILVGVDLPGSdeDAEESLEELAELAETAGAEVVGTVTQRRDKPDPATYIGKGKVEELAELVEELEADLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 79 LFDHALSPAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHMATRLVRGWTHLERQKGGIGLRGPGET 158
Cdd:COG2262 81 IFDDELSPSQQRNLEKALGVKVIDRTGLILDIFAQRARTREGKLQVELAQLQYLLPRLVGMWTHLSRQGGGIGTRGPGET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 159 QLETDRRLLRNRIMQILSRLEKVEKQREQGRRSRAKADIPTVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRR 238
Cdd:COG2262 161 QLETDRRLIRDRIARLKRELEKVRKQRELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 239 IDVPDVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVIDAADVRVQENIDAVNTVLAEIEADEIPALLVMNK 318
Cdd:COG2262 241 LELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNEVLEELGADDKPIILVFNK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 319 IDMLDDfePRIDRDDENKPIRVWLSAQTGVGVPLLFQALTERLSGEVAQHTLRLPPKEGRLRSRFYQLQAIEKEWMEDDG 398
Cdd:COG2262 321 IDLLDD--EELERLRAGYPDAVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYSDGDLVAWLHEHGEVLSEEYDEDG 398
|
410 420
....*....|....*....|.
gi 490248609 399 sVSLQVRMPIVDWRRLCKQEP 419
Cdd:COG2262 399 -TLLTVRLPPEDLARLEAYLV 418
|
|
| 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: 604.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 10 QAVLVHIYFSQDKDM-EDLQEFETLASSAGVEAMQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGASVVLFDHALSPAQ 88
Cdd:TIGR03156 1 RAILVGVDLGNEDDEeESLEELAELAETAGAEVVGTVTQKRSRPDPATYIGKGKVEEIAELVEELEADLVIFDHELSPSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 89 ERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHMATRLVRGWTHLERQKGGIGLRGPGETQLETDRRLLR 168
Cdd:TIGR03156 81 ERNLEKALGCRVIDRTGLILDIFAQRARTHEGKLQVELAQLKYLLPRLVGGWTHLSRQGGGIGTRGPGETQLETDRRLIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 169 NRIMQILSRLEKVEKQREQGRRSRAKADIPTVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRRIDVPDVGETV 248
Cdd:TIGR03156 161 ERIAQLKKELEKVEKQRERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGADVYAADQLFATLDPTTRRLDLPDGGEVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 249 LADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVIDAADVRVQENIDAVNTVLAEIEADEIPALLVMNKIDMLDdfEPR 328
Cdd:TIGR03156 241 LTDTVGFIRDLPHELVAAFRATLEEVREADLLLHVVDASDPDREEQIEAVEKVLEELGAEDIPQLLVYNKIDLLD--EPR 318
|
330 340 350
....*....|....*....|....*....|...
gi 490248609 329 IDRDDENKPIRVWLSAQTGVGVPLLFQALTERL 361
Cdd:TIGR03156 319 IERLEEGYPEAVFVSAKTGEGLDLLLEAIAERL 351
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
157-361 |
1.35e-112 |
|
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: 328.65 E-value: 1.35e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 157 ETQLETDRRLLRNRIMQILSRLEKVEKQREQGRRSRAKADIPTVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTL 236
Cdd:cd01878 1 ETQLETDRRLIRERIAKLRKELEKVKKQRELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 237 RRIDVPDVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVIDAADVRVQENIDAVNTVLAEIEADEIPALLVM 316
Cdd:cd01878 81 RRIKLPGGREVLLTDTVGFIRDLPHQLVEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKELGADDIPIILVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490248609 317 NKIDMLDDFEPRiDRDDENKPIRVWLSAQTGVGVPLLFQALTERL 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 |
1.39e-40 |
|
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: 139.41 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 25 EDLQEFETLASSAGVEAMQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGASVVLFDHALSPAQERNLERLCECRVIDRT 104
Cdd:pfam13167 1 ESLEELEELAETAGAEVVGTVIQKRDKPDPATYIGKGKLEELKELVEALEADLVIFDDELSPSQQRNLEKALGVKVIDRT 80
|
....*..
gi 490248609 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 |
6.41e-40 |
|
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: 137.19 E-value: 6.41e-40
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490248609 114 RARTHEGKLQVELAQLRHMATRLVRGWTHLERQKGGIGLRGPGETQLETDRRLLRNRIMQILSRLEKVEKQREQGRRSR 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 |
1.16e-25 |
|
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: 100.39 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 199 TVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRRIDVPDVgETVLADTVGFIR--HLPHDLVAAFKAtlqeTRQ 276
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGK-QIILVDTPGLIEgaSEGEGLGRAFLA----IIE 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 490248609 277 ATLLLHVIDAadvrvQENIDAVNTVLAEI-EADEIPALLVMNK 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 |
2.86e-21 |
|
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: 94.03 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 195 ADiptVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRRIDVPDVGETVLADTVGFI-----------RHLPHdl 263
Cdd:TIGR02729 158 AD---VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIegasegaglghRFLKH-- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 264 vaafkatLQETRqatLLLHVIDAADVRVQENIDAVNTVLAEIEA-----DEIPALLVMNKIDMLDD--FEPRID--RDDE 334
Cdd:TIGR02729 233 -------IERTR---VLLHLIDISPEDGSDPVEDYEIIRNELKKyspelAEKPRIVVLNKIDLLDEeeLEELLKelKKEL 302
|
170 180
....*....|....*....|....*..
gi 490248609 335 NKPIRVwLSAQTGVGVPLLFQALTERL 361
Cdd:TIGR02729 303 GKPVFP-ISALTGEGLDELLDALAELL 328
|
|
| obgE |
PRK12299 |
GTPase CgtA; Reviewed |
195-367 |
3.01e-20 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 90.90 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 195 ADiptVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRRIDVPDVGETVLADTVGFI-----------RHLPHdl 263
Cdd:PRK12299 159 AD---VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKSFVIADIPGLIegasegaglghRFLKH-- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 264 vaafkatLQETRqatLLLHVIDAADVRVqenIDAVNTVLAEIEA-----DEIPALLVMNKIDMLDD---FEPRIDRDDEN 335
Cdd:PRK12299 234 -------IERTR---LLLHLVDIEAVDP---VEDYKTIRNELEKyspelADKPRILVLNKIDLLDEeeeREKRAALELAA 300
|
170 180 190
....*....|....*....|....*....|...
gi 490248609 336 KPIRVW-LSAQTGVGVPLLFQALTERLSGEVAQ 367
Cdd:PRK12299 301 LGGPVFlISAVTGEGLDELLRALWELLEEARRE 333
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
195-361 |
1.04e-18 |
|
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: 82.86 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 195 ADiptVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRRIDVPDVGETVLADTVG--------------FIRHlp 260
Cdd:cd01898 1 AD---VGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGliegasegkglghrFLRH-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 261 hdlvaafkatLQETRqatLLLHVIDAADvrVQENIDAVNTVLAEIEA-DEI----PALLVMNKIDMLDD------FEPRI 329
Cdd:cd01898 76 ----------IERTR---VLLHVIDLSG--EDDPVEDYETIRNELEAyNPGlaekPRIVVLNKIDLLDAeerfekLKELL 140
|
170 180 190
....*....|....*....|....*....|..
gi 490248609 330 DRDDENKPIRVwlSAQTGVGVPLLFQALTERL 361
Cdd:cd01898 141 KELKGKKVFPI--SALTGEGLDELLKKLAKLL 170
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
202-361 |
2.10e-17 |
|
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: 79.21 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 202 LVGYTNAGKSTLFNQITAAEVYA-ANQLFATLDPTLRRIDVPDVGETVLADTVGFIRhLPHDLVAAFKATLQETRQATLL 280
Cdd:cd00880 2 IFGRPNVGKSSLLNALLGQNVGIvSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDE-EGGLGRERVEEARQVADRADLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 281 LHVIDAADVRVQENIdavntVLAEIEADEIPALLVMNKIDMLDDFEPRIDRDD-------ENKPIRVwlSAQTGVGVPLL 353
Cdd:cd00880 81 LLVVDSDLTPVEEEA-----KLGLLRERGKPVLLVLNKIDLVPESEEEELLRErklellpDLPVIAV--SALPGEGIDEL 153
|
....*...
gi 490248609 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 |
3.98e-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: 75.51 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 202 LVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRRIDVPDVGETVLADTVGFIRHlPHDLVAAFKATLQETRQATLLL 281
Cdd:cd01881 2 LVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDG-ASEGRGLGEQILAHLYRSDLIL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490248609 282 HVIDAADVRVQ---ENIDAVNTVLAE--IEADEIPALLVMNKIDMLDDFEPRIDRDDENKP--IRVWLSAQTGVGV 350
Cdd:cd01881 81 HVIDASEDCVGdplEDQKTLNEEVSGsfLFLKNKPEMIVANKIDMASENNLKRLKLDKLKRgiPVVPTSALTRLGL 156
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
202-359 |
9.61e-16 |
|
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: 74.42 E-value: 9.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 202 LVGYTNAGKSTLFNQITAAEVYAANQLFA-TLDPTLRRIDVPDVGETV-LADTVGFIRHLPHDLVAAFKATLqetRQATL 279
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGEVGEVSDVPGtTRDPDVYVKELDKGKVKLvLVDTPGLDEFGGLGREELARLLL---RGADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 280 LLHVIDAADVRVQENIDavNTVLAEIEADEIPALLVMNKIDMLDDFEPRIDRDDE----NKPIRVW-LSAQTGVGVPLLF 354
Cdd:cd00882 79 ILLVVDSTDRESEEDAK--LLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEelakILGVPVFeVSAKTGEGVDELF 156
|
....*
gi 490248609 355 QALTE 359
Cdd:cd00882 157 EKLIE 161
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
163-367 |
2.93e-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: 77.41 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 163 DRRLLRNRIMQILSRLEKVEKQREQGRRSRakaDIPTVSLVGYTNAGKSTLFNQITAAEvyaanqlfatldptlRRI--D 240
Cdd:COG0486 182 DREELLERLEELREELEALLASARQGELLR---EGIKVVIVGRPNVGKSSLLNALLGEE---------------RAIvtD 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 241 VP----DVGETV---------LADTVGfIRHlPHDLVAAF--KATLQETRQATLLLHVIDAADVRVQENIDavntVLAEI 305
Cdd:COG0486 244 IAgttrDVIEERiniggipvrLIDTAG-LRE-TEDEVEKIgiERAREAIEEADLVLLLLDASEPLTEEDEE----ILEKL 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490248609 306 EadEIPALLVMNKIDMLDDFEPRIDRDDENKPIRVwlSAQTGVGVPLLFQALTERLSGEVAQ 367
Cdd:COG0486 318 K--DKPVIVVLNKIDLPSEADGELKSLPGEPVIAI--SAKTGEGIDELKEAILELVGEGALE 375
|
|
| obgE |
PRK12297 |
GTPase CgtA; Reviewed |
195-398 |
4.36e-14 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237046 [Multi-domain] Cd Length: 424 Bit Score: 73.60 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 195 ADiptVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRRIDVPDVGETVLADTVG--------------FIRHlp 260
Cdd:PRK12297 159 AD---VGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRSFVMADIPGliegasegvglghqFLRH-- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 261 hdlvaafkatLQETRqatLLLHVIDAADVRVQENIDAVNTVLAEIEA-----DEIPALLVMNKIDMlDDFEPRIDRDDEN 335
Cdd:PRK12297 234 ----------IERTR---VIVHVIDMSGSEGRDPIEDYEKINKELKLynprlLERPQIVVANKMDL-PEAEENLEEFKEK 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490248609 336 KPIRVW-LSAQTGVGVpllfQALTERLSGEVAQHTLRLPPKEGRLRSRFYQLQAIEKEW---MEDDG 398
Cdd:PRK12297 300 LGPKVFpISALTGQGL----DELLYAVAELLEETPEFPLEEEEVEEEVYYKFEEEEKDFtitRDEDG 362
|
|
| obgE |
PRK12298 |
GTPase CgtA; Reviewed |
195-398 |
2.36e-13 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237047 [Multi-domain] Cd Length: 390 Bit Score: 71.05 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 195 ADiptVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRRIDVPDVGETVLADTVGFI-----------RHLPHdl 263
Cdd:PRK12298 160 AD---VGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDERSFVVADIPGLIegasegaglgiRFLKH-- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 264 vaafkatLQETRqatLLLHVIDAADVRVQENIDAVNTVLAEIEA-----DEIPALLVMNKIDMLDDFEPR------IDRD 332
Cdd:PRK12298 235 -------LERCR---VLLHLIDIAPIDGSDPVENARIIINELEKyspklAEKPRWLVFNKIDLLDEEEAEerakaiVEAL 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490248609 333 DENKPIRVwLSAQTGVGVPLLFQALTERL-SGEVAQHTLRLPPKEGRLRSRFYQLQAIEKEWMEDDG 398
Cdd:PRK12298 305 GWEGPVYL-ISAASGLGVKELCWDLMTFIeENPREEAEEAEAPEKVEFMWDDYHREQLEEVEEEDDD 370
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
161-391 |
1.23e-11 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 65.90 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 161 ETDRRLLRNRIMQILSRLEKVEKQREQGRRSRakaDIPTVSLVGYTNAGKSTLFNQITAAEvyaanqlfatldptlRRI- 239
Cdd:PRK05291 182 FLSDEKILEKLEELIAELEALLASARQGEILR---EGLKVVIAGRPNVGKSSLLNALLGEE---------------RAIv 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 240 -DVP----DVGET---------VLADTVGfIRHlPHDLVAA--FKATLQETRQATLLLHVIDAADVRVQENIDAVntvla 303
Cdd:PRK05291 244 tDIAgttrDVIEEhinldgiplRLIDTAG-IRE-TDDEVEKigIERSREAIEEADLVLLVLDASEPLTEEDDEIL----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 304 eIEADEIPALLVMNKIDMLDDFEPRIDRDDEnkpiRVWLSAQTGVGVPLLFQALTERLSGEVAQHTlrlppkEGRLRSRF 383
Cdd:PRK05291 317 -EELKDKPVIVVLNKADLTGEIDLEEENGKP----VIRISAKTGEGIDELREAIKELAFGGFGGNQ------EGVFLTNA 385
|
....*...
gi 490248609 384 YQLQAIEK 391
Cdd:PRK05291 386 RHLEALER 393
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
167-364 |
1.78e-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: 61.73 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 167 LRNRIMQILSRLEKVEKQREQGRRSRakaDIPTVSLVGYTNAGKSTLFNQITAAEvyaanqlfatldptlRRI--DVP-- 242
Cdd:pfam12631 67 LLERLEELLAELEKLLATADRGRILR---EGIKVVIVGKPNVGKSSLLNALLGEE---------------RAIvtDIPgt 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 243 --DVGETV---------LADTVGfIRHlPHDLVAAF--KATLQETRQATLLLHVIDAadvrvQENIDAVNTVLAEIEADE 309
Cdd:pfam12631 129 trDVIEETiniggiplrLIDTAG-IRE-TDDEVEKIgiERAREAIEEADLVLLVLDA-----SRPLDEEDLEILELLKDK 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490248609 310 IPALLVMNKIDMLDDFEPRIDRDDENkpiRVWLSAQTGVGVPLLFQALTERLSGE 364
Cdd:pfam12631 202 KPIIVVLNKSDLLGEIDELEELKGKP---VLAISAKTGEGLDELEEAIKELFLAG 253
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
200-361 |
3.00e-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: 58.63 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 200 VSLVGYTNAGKSTLFNQITAAEVYA----ANqlfatldpTLRR----IDVPDVGETVLADTVGFirHLPHD-----LVAA 266
Cdd:cd04163 6 VAIIGRPNVGKSTLLNALVGQKISIvspkPQ--------TTRNrirgIYTDDDAQIIFVDTPGI--HKPKKklgerMVKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 267 FKATLQEtrqATLLLHVIDAADvrvqENIDAVNTVLAEIEADEIPALLVMNKIDMLDDFE---PRIDR---DDENKPIrV 340
Cdd:cd04163 76 AWSALKD---VDLVLFVVDASE----WIGEGDEFILELLKKSKTPVILVLNKIDLVKDKEdllPLLEKlkeLHPFAEI-F 147
|
170 180
....*....|....*....|.
gi 490248609 341 WLSAQTGVGVPLLFQALTERL 361
Cdd:cd04163 148 PISALKGENVDELLEYIVEYL 168
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
182-341 |
4.05e-10 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 60.55 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 182 EKQREQGRRSRAKADIPTVSLVGYTNAGKSTLFNQITAAEVYAANQLFAT------------LDPTLRRIDVPDVGETVL 249
Cdd:COG3596 24 ELLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCtreiqryrlesdGLPGLVLLDTPGLGEVNE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 250 ADtvgfirhlphdlvAAFKATLQETRQATLLLHVIDAADVRVQENIDAVNTVLAEIEadEIPALLVMNKIDMLDdfepri 329
Cdd:COG3596 104 RD-------------REYRELRELLPEADLILWVVKADDRALATDEEFLQALRAQYP--DPPVLVVLTQVDRLE------ 162
|
170
....*....|..
gi 490248609 330 drddenkPIRVW 341
Cdd:COG3596 163 -------PEREW 167
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
200-361 |
6.00e-10 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 60.06 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 200 VSLVGYTNAGKSTLFNQ-------ITAAEVyaanQlfatldpTLRR----IDVPDVGETVLADTVGFirHLPHD-----L 263
Cdd:PRK00089 8 VAIVGRPNVGKSTLLNAlvgqkisIVSPKP----Q-------TTRHrirgIVTEDDAQIIFVDTPGI--HKPKRalnraM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 264 VAAFKATLQEtrqATLLLHVIDAADvrvqENIDAVNTVLAEIEADEIPALLVMNKIDMLDDFE---PRID---RDDENKP 337
Cdd:PRK00089 75 NKAAWSSLKD---VDLVLFVVDADE----KIGPGDEFILEKLKKVKTPVILVLNKIDLVKDKEellPLLEelsELMDFAE 147
|
170 180
....*....|....*....|....
gi 490248609 338 IrVWLSAQTGVGVPLLFQALTERL 361
Cdd:PRK00089 148 I-VPISALKGDNVDELLDVIAKYL 170
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
199-361 |
7.57e-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: 57.50 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 199 TVSLVGYTNAGKSTLFNQITAAEvyaanqlfatldptlRRI--DVP----DVGET---------VLADTVGfIRHLPhDL 263
Cdd:cd04164 5 KVVIAGKPNVGKSSLLNALAGRD---------------RAIvsDIAgttrDVIEEeidlggipvRLIDTAG-LRETE-DE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 264 V--AAFKATLQETRQATLLLHVIDAadvrvQENIDAVNTVLAEIEADeIPALLVMNKIDMLDDFEPRIdrdDENKPIRVW 341
Cdd:cd04164 68 IekIGIERAREAIEEADLVLLVVDA-----SEGLDEEDLEILELPAK-KPVIVVLNKSDLLSDAEGIS---ELNGKPIIA 138
|
170 180
....*....|....*....|
gi 490248609 342 LSAQTGVGVPLLFQALTERL 361
Cdd:cd04164 139 ISAKTGEGIDELKEALLELA 158
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
200-361 |
3.66e-09 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 57.31 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 200 VSLVGYTNAGKSTLFNQ-------ITAAEVyaanQlfaTldpTLRRI----DVPDvGETVLADTVGFirHLPHD-----L 263
Cdd:COG1159 6 VAIVGRPNVGKSTLLNAlvgqkvsIVSPKP----Q---T---TRHRIrgivTRED-AQIVFVDTPGI--HKPKRklgrrM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 264 VAAFKATLQEtrqATLLLHVIDAADVRVQENidavNTVLAEIEADEIPALLVMNKIDML--DDFEPRIDRDDENKPIR-- 339
Cdd:COG1159 73 NKAAWSALED---VDVILFVVDATEKIGEGD----EFILELLKKLKTPVILVINKIDLVkkEELLPLLAEYSELLDFAei 145
|
170 180
....*....|....*....|..
gi 490248609 340 VWLSAQTGVGVPLLFQALTERL 361
Cdd:COG1159 146 VPISALKGDNVDELLDEIAKLL 167
|
|
| PTZ00258 |
PTZ00258 |
GTP-binding protein; Provisional |
187-339 |
4.70e-09 |
|
GTP-binding protein; Provisional
Pssm-ID: 240334 [Multi-domain] Cd Length: 390 Bit Score: 57.65 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 187 QGRRSRAKadipTVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRRIDVPD---------------VGETV-LA 250
Cdd:PTZ00258 15 LGRPGNNL----KMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDerfdwlckhfkpksiVPAQLdIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 251 DTVGFIR--HLPHDLVAAFkatLQETRQATLLLHVI----DAADVRVQENIDAVNTVlaEIEADEipalLVMNKIDMLDD 324
Cdd:PTZ00258 91 DIAGLVKgaSEGEGLGNAF---LSHIRAVDGIYHVVrafeDEDITHVEGEIDPVRDL--EIISSE----LILKDLEFVEK 161
|
170
....*....|....*
gi 490248609 325 FEPRIDRDDENKPIR 339
Cdd:PTZ00258 162 RLDELTKKRKKKKKK 176
|
|
| Rbg1 |
COG1163 |
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; |
175-361 |
2.04e-08 |
|
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440777 [Multi-domain] Cd Length: 368 Bit Score: 55.57 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 175 LSRL-EKVEKQREQGRRSRAKADIP-----TVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDP----------TLRR 238
Cdd:COG1163 35 LAELkEELEKRKKKSGGGGEGFAVKksgdaTVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVvpgmleykgaKIQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 239 IDVP----------DVGETVL-----ADTVGFIrhLPHDLVAAFKATLQETRQATLLL---------------------- 281
Cdd:COG1163 115 LDVPgliegaasgkGRGKEVLsvvrnADLILIV--LDVFELEQYDVLKEELYDAGIRLnkpppdvtiekkgkggirvnst 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 282 ----------------HVIDAADVRVQEN------IDAV--NTVLaeieadeIPALLVMNKIDMLD-DFEPRIDRD--DE 334
Cdd:COG1163 193 gkldldeedikkilreYGIVNADVLIREDvtlddlIDALmgNRVY-------KPAIVVVNKIDLADeEYVEELKSKlpDG 265
|
250 260
....*....|....*....|....*..
gi 490248609 335 NKPIRVwlSAQTGVGvpllFQALTERL 361
Cdd:COG1163 266 VPVIFI--SAEKGIG----LEELKEEI 286
|
|
| YchF |
cd01900 |
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ... |
203-254 |
6.42e-08 |
|
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: 53.62 E-value: 6.42e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 490248609 203 VGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRRIDVPDVGETVLADTVG 254
Cdd:cd01900 4 VGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERLDKLAEIVK 55
|
|
| GTP1 |
COG0012 |
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ... |
202-326 |
1.06e-07 |
|
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439783 [Multi-domain] Cd Length: 362 Bit Score: 53.49 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 202 LVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRRIDVPDVGETVLADTVGFIRHLP-----HD---LVA-AFKAT-- 270
Cdd:COG0012 5 IVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVPVPDERLDKLAEIVKPKKIVPatiefVDiagLVKgASKGEgl 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 271 ----LQETRQATLLLHVidaadVRVQENidavntvlaeieaDEIPalLVMNKIDMLDDFE 326
Cdd:COG0012 85 gnqfLANIREVDAIVHV-----VRCFED-------------DNVT--HVEGSVDPLRDIE 124
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
198-361 |
2.12e-07 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 53.26 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 198 PTVSLVGYTNAGKSTLFNQITAAEVYAANQLFA-TLDP--TLRRIDvpdvGETVL-ADTVGfIRHLPHDLVAA-FKATLQ 272
Cdd:PRK09518 451 RRVALVGRPNVGKSSLLNQLTHEERAVVNDLAGtTRDPvdEIVEID----GEDWLfIDTAG-IKRRQHKLTGAeYYSSLR 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 273 ET---RQATLLLHVIDAA------DVRVQENI-DAVNTVlaeieadeipaLLVMNKIDMLDDFE-PRIDRDDENKPIRV- 340
Cdd:PRK09518 526 TQaaiERSELALFLFDASqpiseqDLKVMSMAvDAGRAL-----------VLVFNKWDLMDEFRrQRLERLWKTEFDRVt 594
|
170 180
....*....|....*....|....*.
gi 490248609 341 W-----LSAQTGVGVPLLFQALTERL 361
Cdd:PRK09518 595 WarrvnLSAKTGWHTNRLAPAMQEAL 620
|
|
| obgE |
PRK12296 |
GTPase CgtA; Reviewed |
195-376 |
3.88e-06 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237045 [Multi-domain] Cd Length: 500 Bit Score: 49.10 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 195 ADiptVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRRIDVPDVGETVlADTVGFI------RHLPHDLvaafk 268
Cdd:PRK12296 160 AD---VGLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQAGDTRFTV-ADVPGLIpgasegKGLGLDF----- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 269 atLQETRQATLLLHVIDAADVRVQEN----IDAVNTVLAE-----------IEADEIPALLVMNKID------MLDDFEP 327
Cdd:PRK12296 231 --LRHIERCAVLVHVVDCATLEPGRDplsdIDALEAELAAyapaldgdlglGDLAERPRLVVLNKIDvpdareLAEFVRP 308
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490248609 328 RIdrddENKPIRVW-LSAQTGVGVpllfQALTERLSGEVAQHTLRLPPKE 376
Cdd:PRK12296 309 EL----EARGWPVFeVSAASREGL----RELSFALAELVEEARAAEPEAE 350
|
|
| PRK09602 |
PRK09602 |
translation-associated GTPase; Reviewed |
199-286 |
5.52e-06 |
|
translation-associated GTPase; Reviewed
Pssm-ID: 236584 [Multi-domain] Cd Length: 396 Bit Score: 48.27 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 199 TVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDP----TLRRIDVP--DVGETVLADT---VGFIRHLPHDL--VA-- 265
Cdd:PRK09602 3 TIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPnvgvAYVRVECPckELGVKCNPRNgkcIDGTRFIPVELidVAgl 82
|
90 100 110
....*....|....*....|....*....|...
gi 490248609 266 ------------AFkatLQETRQATLLLHVIDA 286
Cdd:PRK09602 83 vpgahegrglgnQF---LDDLRQADALIHVVDA 112
|
|
| NOG |
cd01897 |
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ... |
198-362 |
2.29e-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: 44.47 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 198 PTVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDPTLRRIDVPDVGETVLaDTVGFirhLPHDLvaafkatlqETR-- 275
Cdd:cd01897 1 RTLVIAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVI-DTPGI---LDRPL---------EERnt 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 276 ---QATLLLHVIDAADVRVqenIDAVNTVLAEIEA-----DEI------PALLVMNKIDMLDDFEPRIDRDDENKPIRVW 341
Cdd:cd01897 68 iemQAITALAHLRAAVLFF---IDPSETCGYSIEEqlslfKEIkplfnkPVIVVLNKIDLLTEEDLSEIEKELEKEGEEV 144
|
170 180
....*....|....*....|...
gi 490248609 342 L--SAQTGVGVPLLFQALTERLS 362
Cdd:cd01897 145 IkiSTLTEEGVDELKNKACELLL 167
|
|
| feoB |
TIGR00437 |
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ... |
204-360 |
2.33e-05 |
|
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane protein required for iron(II) update, is encoded in an operon with FeoA (75 amino acids), which is also required, and is regulated by Fur. There appear to be two copies in Archaeoglobus fulgidus and Clostridium acetobutylicum. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273077 [Multi-domain] Cd Length: 591 Bit Score: 46.66 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 204 GYTNAGKSTLFNQITAAEVYAANQLFATLDptLRRIDVPDVGETV-LADTVGFirhlpHDLVAafkATLQE--------T 274
Cdd:TIGR00437 1 GNPNVGKSTLFNALTGANQTVGNWPGVTVE--KKEGKLGFQGEDIeIVDLPGI-----YSLTT---FSLEEevardyllN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 275 RQATLLLHVIDAAdvrvqeNIDAVNTVLAEIEADEIPALLVMNKIDMLDDFEPRIDRDDENK----PIrVWLSAQTGVGV 350
Cdd:TIGR00437 71 EKPDLVVNVVDAS------NLERNLYLTLQLLELGIPMILALNLVDEAEKKGIRIDEEKLEErlgvPV-VPTSATEGRGI 143
|
170
....*....|
gi 490248609 351 PLLFQALTER 360
Cdd:TIGR00437 144 ERLKDAIRKA 153
|
|
| HflX_C |
pfam19275 |
HflX C-terminal domain; This entry represents the C-terminal domain of the HflX protein. HflX ... |
342-406 |
5.96e-05 |
|
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: 41.91 E-value: 5.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490248609 342 LSAQTGVGVPLLFQALTERLSGEVAQHTLRLPPKEGRLRSRFYQlQAI--EKEWMEdDGSVSLQVRM 406
Cdd:pfam19275 15 VSAITGEGVDALMDEISRRLSGVLTETTVVLPADKLALLSWVYE-NAIvdGREDNE-DGSVSLDVRL 79
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
196-359 |
5.97e-05 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 43.58 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 196 DIPTVSLVGYTNAGKSTLFNQITAAE-VYAANQLFATLDPtlrrIDVPDV--GET-VLADTVGfIRHLPH-----DLVAA 266
Cdd:cd01895 1 DPIKIAIIGRPNVGKSSLLNALLGEErVIVSDIAGTTRDS----IDVPFEydGQKyTLIDTAG-IRKKGKvtegiEKYSV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 267 FKaTLQETRQATLLLHVIDAadvrvQENIDAVNTVLAE-IEADEIPALLVMNKIDMLDDFEPRID---RDDENK------ 336
Cdd:cd01895 76 LR-TLKAIERADVVLLVLDA-----SEGITEQDLRIAGlILEEGKALIIVVNKWDLVEKDEKTMKefeKELRRKlpfldy 149
|
170 180
....*....|....*....|....
gi 490248609 337 -PIrVWLSAQTGVGVPLLFQALTE 359
Cdd:cd01895 150 aPI-VFISALTGQGVDKLFDAIKE 172
|
|
| Ygr210 |
cd01899 |
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ... |
200-287 |
6.08e-05 |
|
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: 44.53 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 200 VSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDP----TLRRIDVPDVGETVLA-DTVGF----IRHLPHDL--VAA-- 266
Cdd:cd01899 1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPnvgvGYVRVECPCKELGVSCnPRYGKcidgKRYVPVELidVAGlv 80
|
90 100 110
....*....|....*....|....*....|...
gi 490248609 267 ------------FkatLQETRQATLLLHVIDAA 287
Cdd:cd01899 81 pgahegkglgnqF---LDDLRDADVLIHVVDAS 110
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
200-355 |
7.63e-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: 42.74 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 200 VSLVGYTNAGKSTLFNQITaaevyaANQLFAT-LDPTLRRIDVPDV----GETVLA---DTVGFIRHLPhDLVAAFKATL 271
Cdd:TIGR00231 4 IVIVGHPNVGKSTLLNSLL------GNKGSITeYYPGTTRNYVTTVieedGKTYKFnllDTAGQEDYDA-IRRLYYPQVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 272 QETRQATLLLHVIDAADVRVQEnidavnTVLAEIEAD-EIPALLVMNKIDMLD-DFEP--RIDRDDENKPIRVWLSAQTG 347
Cdd:TIGR00231 77 RSLRVFDIVILVLDVEEILEKQ------TKEIIHHADsGVPIILVGNKIDLKDaDLKThvASEFAKLNGEPIIPLSAETG 150
|
....*...
gi 490248609 348 VGVPLLFQ 355
Cdd:TIGR00231 151 KNIDSAFK 158
|
|
| 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 |
2.05e-04 |
|
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: 40.49 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 258 HLPHDLVaafKATLQETRqatlllhvIDAADVRVQEN------IDAV--NTVLaeieadeIPALLVMNKIDMLD-DFEPR 328
Cdd:pfam16897 13 KLDEETI---KAILREYK--------IHNADVLIREDvtvddlIDVIegNRVY-------IPCLYVYNKIDLISiEELDR 74
|
90 100 110
....*....|....*....|....*....|...
gi 490248609 329 IDRDDENKPIrvwlSAQTGVGVPLLFQALTERL 361
Cdd:pfam16897 75 LAREPDSVPI----SAEKGLNLDELKERIWEYL 103
|
|
| FeoB_N |
pfam02421 |
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ... |
199-357 |
2.65e-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: 41.28 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 199 TVSLVGYTNAGKSTLFNQITAAEVYAAN----------QLFATLDPTLRRIDVPdvG----------ETVLADtvgFIRH 258
Cdd:pfam02421 2 TIALVGNPNVGKTTLFNALTGANQHVGNwpgvtvekkeGKFKYKGYEIEIVDLP--GiyslspyseeERVARD---YLLN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 259 LPHDLVaafkatlqetrqatllLHVIDAADVR------VQenidavntvLAEIeadEIPALLVMNKIDMLDDFEPRIDRD 332
Cdd:pfam02421 77 EKPDVI----------------VNVVDATNLErnlyltLQ---------LLEL---GLPVVLALNMMDEAEKKGIKIDIK 128
|
170 180
....*....|....*....|....*....
gi 490248609 333 DENK----PIrVWLSAQTGVGVPLLFQAL 357
Cdd:pfam02421 129 KLSEllgvPV-VPTSARKGEGIDELLDAI 156
|
|
| FeoB |
cd01879 |
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
202-363 |
2.73e-04 |
|
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: 41.29 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 202 LVGYTNAGKSTLFNQITAAEVYAAN----------QLFATLDPTLRRIDVPdvG----------ETVladTVGFIRHLPH 261
Cdd:cd01879 2 LVGNPNVGKTTLFNALTGARQKVGNwpgvtvekkeGEFKLGGKEIEIVDLP--GtysltpysedEKV---ARDFLLGEEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 262 DLVaafkatlqetrqatllLHVIDAAdvrvqeNIDaVNTVLA-EIEADEIPALLVMNKIDMLDDFEPRIDRDD-ENK--- 336
Cdd:cd01879 77 DLI----------------VNVVDAT------NLE-RNLYLTlQLLELGLPVVVALNMIDEAEKRGIKIDLDKlSELlgv 133
|
170 180
....*....|....*....|....*..
gi 490248609 337 PIrVWLSAQTGVGVPLLFQALTERLSG 363
Cdd:cd01879 134 PV-VPTSARKGEGIDELLDAIAKLAES 159
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
202-361 |
5.00e-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: 40.02 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 202 LVGYTNAGKSTLFNQITAAEVYAANQLFA-TLDPT----------LRRIDVPDVGETVLadtvgfirhlpHDLVAAfKAT 270
Cdd:cd11383 2 LMGKTGAGKSSLCNALFGTEVAAVGDRRPtTRAAQayvwqtggdgLVLLDLPGVGERGR-----------RDREYE-ELY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 271 LQETRQATLLLHVIDAADVRVQENIDavnTVLAEIEADEIPALLVMNKIDmlddfepridrddenkPIrVWLSAQTGVGV 350
Cdd:cd11383 70 RRLLPEADLVLWLLDADDRALAADHD---FYLLPLAGHDAPLLFVLNQVD----------------PV-LAVSARTGWGL 129
|
170
....*....|.
gi 490248609 351 PLLFQALTERL 361
Cdd:cd11383 130 DELAEALITAL 140
|
|
| DRG |
cd01896 |
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ... |
199-234 |
8.21e-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: 8.21e-04
10 20 30
....*....|....*....|....*....|....*.
gi 490248609 199 TVSLVGYTNAGKSTLFNQITAAEVYAANQLFATLDP 234
Cdd:cd01896 2 RVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTC 37
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
197-361 |
1.54e-03 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 40.78 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 197 IPTVSLVGYTNAGKSTLFNQITAaevyaanqlfatldptlRRI----DVPDV------GETVLA-------DTVGFIRHL 259
Cdd:COG1160 2 SPVVAIVGRPNVGKSTLFNRLTG-----------------RRDaivdDTPGVtrdriyGEAEWGgreftliDTGGIEPDD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 260 PHDLVAAFKA-TLQETRQATLLLHVIDAadvrvQENIDAVNTVLAEI--EADeIPALLVMNKIDmlddfepriDRDDEN- 335
Cdd:COG1160 65 DDGLEAEIREqAELAIEEADVILFVVDG-----RAGLTPLDEEIAKLlrRSG-KPVILVVNKVD---------GPKREAd 129
|
170 180 190
....*....|....*....|....*....|....*.
gi 490248609 336 ----------KPIRVwlSAQTGVGVPLLFQALTERL 361
Cdd:COG1160 130 aaefyslglgEPIPI--SAEHGRGVGDLLDAVLELL 163
|
|
| feoB |
PRK09554 |
Fe(2+) transporter permease subunit FeoB; |
199-352 |
2.30e-03 |
|
Fe(2+) transporter permease subunit FeoB;
Pssm-ID: 236563 [Multi-domain] Cd Length: 772 Bit Score: 40.47 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 199 TVSLVGYTNAGKSTLFNQITAAEVYAAN----------QLFATLDPTLRRIDVPDVGE--TVLADTvgfirhlphdlvaa 266
Cdd:PRK09554 5 TIGLIGNPNSGKTTLFNQLTGARQRVGNwagvtverkeGQFSTTDHQVTLVDLPGTYSltTISSQT-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 267 fkaTLQE--------TRQATLLLHVIDAADvrVQENIdAVNTVLAEIeadEIPALLVMNKIDMLDDFEPRIDRDDenkpi 338
Cdd:PRK09554 71 ---SLDEqiachyilSGDADLLINVVDASN--LERNL-YLTLQLLEL---GIPCIVALNMLDIAEKQNIRIDIDA----- 136
|
170
....*....|....*
gi 490248609 339 rvwLSAQTGVGV-PL 352
Cdd:PRK09554 137 ---LSARLGCPViPL 148
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
197-218 |
4.09e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 39.26 E-value: 4.09e-03
|
| FeoB |
COG0370 |
Fe2+ transporter FeoB [Inorganic ion transport and metabolism]; |
198-226 |
4.56e-03 |
|
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
Pssm-ID: 440139 [Multi-domain] Cd Length: 662 Bit Score: 39.33 E-value: 4.56e-03
10 20
....*....|....*....|....*....
gi 490248609 198 PTVSLVGYTNAGKSTLFNQITAAEVYAAN 226
Cdd:COG0370 4 ITIALVGNPNVGKTTLFNALTGSRQKVGN 32
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
310-361 |
4.81e-03 |
|
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: 37.89 E-value: 4.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490248609 310 IPALLVMNKIDMLDDFEPR-------------IDRDDENKPIrVWLSAQTGVGVPLLFQALTERL 361
Cdd:pfam00009 122 VPIIVFINKMDRVDGAELEevveevsrellekYGEDGEFVPV-VPGSALKGEGVQTLLDALDEYL 185
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
200-363 |
4.95e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 39.18 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 200 VSLVGYTNAGKSTLFNQITAAE-VYAANQLFATLDPTLRRIDVPdvGET-VLADTVGFIRHLPHDLVAAFKATLQeTRQA 277
Cdd:PRK03003 214 VALVGKPNVGKSSLLNKLAGEErSVVDDVAGTTVDPVDSLIELG--GKTwRFVDTAGLRRRVKQASGHEYYASLR-THAA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248609 278 tlllhvIDAADVRVQEnIDAvNTVLAE---------IEADEipAL-LVMNKIDMLDD-----FEPRIDRDDENKP--IRV 340
Cdd:PRK03003 291 ------IEAAEVAVVL-IDA-SEPISEqdqrvlsmvIEAGR--ALvLAFNKWDLVDEdrryyLEREIDRELAQVPwaPRV 360
|
170 180
....*....|....*....|...
gi 490248609 341 WLSAQTGVGVPLLFQALTERLSG 363
Cdd:PRK03003 361 NISAKTGRAVDKLVPALETALES 383
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
294-365 |
9.64e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 37.88 E-value: 9.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490248609 294 NIDAVNTVLAEIEADEIPALLVMNKIDMLDDFEpriDRDDENKPIR------VWLSAQTGVGVPllfqALTERLSGEV 365
Cdd:PRK00098 96 STDLLDRFLVLAEANGIKPIIVLNKIDLLDDLE---EARELLALYRaigydvLELSAKEGEGLD----ELKPLLAGKV 166
|
|
| |
