|
Name |
Accession |
Description |
Interval |
E-value |
| HflX |
COG2262 |
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
14-444 |
7.98e-158 |
|
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 453.00 E-value: 7.98e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 14 AESVPRERRAVVAKRV-----DSGDADLAEITQLAAAAGYEVVGELTQTR-TEDAAFMFGEGKVAQLRDLVRRTDAGAVI 87
Cdd:COG2262 2 FEREERGERAILVGVDlpgsdEDAEESLEELAELAETAGAEVVGTVTQRRdKPDPATYIGKGKVEELAELVEELEADLVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 88 VDNDVGPYQTFNIGGKLpeGVEVIDRFTLILEIFGQRANTRKAQLQVELAELRYELPRAEAK-ASLAKRDERPGFMGLGE 166
Cdd:COG2262 82 FDDELSPSQQRNLEKAL--GVKVIDRTGLILDIFAQRARTREGKLQVELAQLQYLLPRLVGMwTHLSRQGGGIGTRGPGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 167 YD-ESVERDIKRQISEIRDELESIAEKEEARREQRRDSGFDLVALAGYTNAGKSTLMRRLAaeidvdenadrhpdlDTTA 245
Cdd:COG2262 160 TQlETDRRLIRDRIARLKRELEKVRKQRELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLT---------------GADV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 246 ESQDMLFTTLGTTTRRAEME-KRDVLLTDTVGFIADLPHWLVESFESTLDSVYRADLVLLVVDASEPveDMREKLVTSHD 324
Cdd:COG2262 225 LAEDKLFATLDPTTRRLELPdGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDP--DFEEQIETVNE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 325 TLYER--NEAPVVTVFNKVDRLAPGELAdkrgALSGVAPDPVAVSAKTGAGVAELRDRVEDELPDWERE-RLVLPVSDea 401
Cdd:COG2262 303 VLEELgaDDKPIILVFNKIDLLDDEELE----RLRAGYPDAVFISAKTGEGIDELLEAIEERLPEDRVEvELLLPYSD-- 376
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1233247415 402 MSLVSWIHDHGHVDEESYASDQVTVDFEAKPSIVARARSKAAD 444
Cdd:COG2262 377 GDLVAWLHEHGEVLSEEYDEDGTLLTVRLPPEDLARLEAYLVE 419
|
|
| GTP_HflX |
TIGR03156 |
GTP-binding protein HflX; This protein family is one of a number of homologous small, ... |
23-385 |
1.68e-95 |
|
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: 291.30 E-value: 1.68e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 23 AVVAKRVDSGDADLAEITQLAAAAGYEVVGELTQTRTE-DAAFMFGEGKVAQLRDLVRRTDAGAVIVDNDVGPYQTFNIG 101
Cdd:TIGR03156 6 GVDLGNEDDEEESLEELAELAETAGAEVVGTVTQKRSRpDPATYIGKGKVEEIAELVEELEADLVIFDHELSPSQERNLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 102 GKLpeGVEVIDRFTLILEIFGQRANTRKAQLQVELAELRYELPRaeakasLAKRD---ERP----GFMGLGEYD-ESVER 173
Cdd:TIGR03156 86 KAL--GCRVIDRTGLILDIFAQRARTHEGKLQVELAQLKYLLPR------LVGGWthlSRQgggiGTRGPGETQlETDRR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 174 DIKRQISEIRDELESIAEKEEARREQRRDSGFDLVALAGYTNAGKSTLMRRLAAEidvdenadrhpdlDTTAEsqDMLFT 253
Cdd:TIGR03156 158 LIRERIAQLKKELEKVEKQRERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGA-------------DVYAA--DQLFA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 254 TLGTTTRRAEM-EKRDVLLTDTVGFIADLPHWLVESFESTLDSVYRADLVLLVVDASEPveDMREKLVTSHDTLYE--RN 330
Cdd:TIGR03156 223 TLDPTTRRLDLpDGGEVLLTDTVGFIRDLPHELVAAFRATLEEVREADLLLHVVDASDP--DREEQIEAVEKVLEElgAE 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1233247415 331 EAPVVTVFNKVDRLAPgelaDKRGALSGVAPDPVAVSAKTGAGVAELRDRVEDEL 385
Cdd:TIGR03156 301 DIPQLLVYNKIDLLDE----PRIERLEEGYPEAVFVSAKTGEGLDLLLEAIAERL 351
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
169-385 |
5.23e-72 |
|
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: 225.80 E-value: 5.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 169 ESVERDIKRQISEIRDELESIAEKEEARREQRRDSGFDLVALAGYTNAGKSTLMRRLAAEidvdenadrhpdldtTAESQ 248
Cdd:cd01878 5 ETDRRLIRERIAKLRKELEKVKKQRELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGA---------------DVLAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 249 DMLFTTLGTTTRRAEM-EKRDVLLTDTVGFIADLPHWLVESFESTLDSVYRADLVLLVVDASEPveDMREKLVTSHDTLY 327
Cdd:cd01878 70 DQLFATLDPTTRRIKLpGGREVLLTDTVGFIRDLPHQLVEAFRSTLEEVAEADLLLHVVDASDP--DREEQIETVEEVLK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 328 ERN--EAPVVTVFNKVDRLAPGELADKRGALSgvaPDPVAVSAKTGAGVAELRDRVEDEL 385
Cdd:cd01878 148 ELGadDIPIILVLNKIDLLDDEELEERLRAGR---PDAVFISAKTGEGLDLLKEAIEELL 204
|
|
| PRK11058 |
PRK11058 |
GTPase HflX; Provisional |
35-377 |
1.16e-44 |
|
GTPase HflX; Provisional
Pssm-ID: 182934 [Multi-domain] Cd Length: 426 Bit Score: 161.04 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 35 DLAEITQLAAAAGYEVVGELTQTR-TEDAAFMFGEGKVAQLRDLVRRTDAGAVIVDNDVGPYQTFNIGgKLPEgVEVIDR 113
Cdd:PRK11058 26 DLQEFESLVSSAGVEALQVITGSRkAPHPKYFVGEGKAVEIAEAVKATGASVVLFDHALSPAQERNLE-RLCE-CRVIDR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 114 FTLILEIFGQRANTRKAQLQVELAELRYELPR-AEAKASLAKRDERPGFMGLGEYD-ESVERDIKRQISEIRDELESIAE 191
Cdd:PRK11058 104 TGLILDIFAQRARTHEGKLQVELAQLRHLATRlVRGWTHLERQKGGIGLRGPGETQlETDRRLLRNRIVQILSRLERVEK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 192 KEEARREQRRDSGFDLVALAGYTNAGKSTLMRRLaaeidvdenadrhpdldTTAE--SQDMLFTTLGTTTRRAEMEK-RD 268
Cdd:PRK11058 184 QREQGRRARIKADVPTVSLVGYTNAGKSTLFNRI-----------------TEARvyAADQLFATLDPTLRRIDVADvGE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 269 VLLTDTVGFIADLPHWLVESFESTLDSVYRADLVLLVVDASEpvEDMREKLVTSHDTLYE--RNEAPVVTVFNKVDRL-- 344
Cdd:PRK11058 247 TVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVVDAAD--VRVQENIEAVNTVLEEidAHEIPTLLVMNKIDMLdd 324
|
330 340 350
....*....|....*....|....*....|....
gi 1233247415 345 -APGELADKRGalsgvAPDPVAVSAKTGAGVAEL 377
Cdd:PRK11058 325 fEPRIDRDEEN-----KPIRVWLSAQTGAGIPLL 353
|
|
| GTP-bdg_N |
pfam13167 |
GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. ... |
34-121 |
4.59e-23 |
|
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: 92.41 E-value: 4.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 34 ADLAEITQLAAAAGYEVVGELTQTR-TEDAAFMFGEGKVAQLRDLVRRTDAGAVIVDNDVGPYQTFNIGGKLpeGVEVID 112
Cdd:pfam13167 1 ESLEELEELAETAGAEVVGTVIQKRdKPDPATYIGKGKLEELKELVEALEADLVIFDDELSPSQQRNLEKAL--GVKVID 78
|
....*....
gi 1233247415 113 RFTLILEIF 121
Cdd:pfam13167 79 RTGLILDIF 87
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
208-340 |
9.20e-23 |
|
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: 92.68 E-value: 9.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 208 VALAGYTNAGKSTLMRRLAAEIdvdenadrhpdldttAESQDMLFTTLGTTTRRAEMEKRDVLLTDTVGFI--ADLPHWL 285
Cdd:pfam01926 2 VALVGRPNVGKSTLINALTGAK---------------AIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIegASEGEGL 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1233247415 286 VESFESTLdsvyRADLVLLVVDASEPVEDMREKLVtshdTLYERNEAPVVTVFNK 340
Cdd:pfam01926 67 GRAFLAII----EADLILFVVDSEEGITPLDEELL----ELLRENKKPIILVLNK 113
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
209-385 |
5.55e-22 |
|
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: 91.92 E-value: 5.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 209 ALAGYTNAGKSTLMRRLAaeidvdenadrhpdLDTTAESQDMLFTTLGTTTRRAEM-EKRDVLLTDTVGfIADLPHWLVE 287
Cdd:cd00880 1 AIFGRPNVGKSSLLNALL--------------GQNVGIVSPIPGTTRDPVRKEWELlPLGPVVLIDTPG-LDEEGGLGRE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 288 SFESTLDSVYRADLVLLVVDASEPVEDMREKLvtshDTLYERNeAPVVTVFNKVDRLAPGELA-----DKRGALSGVapD 362
Cdd:cd00880 66 RVEEARQVADRADLVLLVVDSDLTPVEEEAKL----GLLRERG-KPVLLVLNKIDLVPESEEEellreRKLELLPDL--P 138
|
170 180
....*....|....*....|...
gi 1233247415 363 PVAVSAKTGAGVAELRDRVEDEL 385
Cdd:cd00880 139 VIAVSALPGEGIDELRKKIAELL 161
|
|
| GTP-bdg_M |
pfam16360 |
GTP-binding GTPase Middle Region; This family locates between the N-terminal domain and ... |
124-200 |
4.04e-18 |
|
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: 78.64 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 124 RANTRKAQLQVELAELRYELPRAEAKaslAKRDERP----GFMGLGEYD-ESVERDIKRQISEIRDELESIAEKEEARRE 198
Cdd:pfam16360 1 RARTREAKLQVELAQLKYLLPRLRGM---GTHLSRQgggiGTRGPGETKlETDRRLIRRRIAKLKKELEKVRKQRELQRK 77
|
..
gi 1233247415 199 QR 200
Cdd:pfam16360 78 RR 79
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
209-381 |
5.38e-18 |
|
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: 80.96 E-value: 5.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 209 ALAGYTNAGKSTLMRRLAaeidvdenadrhpdLDTTAESQDMLFTTLGTTTRRAEME--KRDVLLTDTVGFIADLPHWlv 286
Cdd:cd00882 1 VVVGRGGVGKSSLLNALL--------------GGEVGEVSDVPGTTRDPDVYVKELDkgKVKLVLVDTPGLDEFGGLG-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 287 eSFESTLDSVYRADLVLLVVDASEPVEDMREKLVtsHDTLYERNEAPVVTVFNKVDRLAPGELADKRGAL---SGVAPDP 363
Cdd:cd00882 65 -REELARLLLRGADLILLVVDSTDRESEEDAKLL--ILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEelaKILGVPV 141
|
170
....*....|....*...
gi 1233247415 364 VAVSAKTGAGVAELRDRV 381
Cdd:cd00882 142 FEVSAKTGEGVDELFEKL 159
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
166-383 |
1.81e-15 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 78.23 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 166 EYDESVERDIKRQISEIRDELESIAEkeEARREQRRDSGFdLVALAGYTNAGKSTLMRRLAaeidvdeNADR-----HPd 240
Cdd:PRK05291 179 DIEFLSDEKILEKLEELIAELEALLA--SARQGEILREGL-KVVIAGRPNVGKSSLLNALL-------GEERaivtdIA- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 241 ldttaesqdmlfttlGTTtrraemekRDVL------------LTDTVGfI---ADLphwlVES--FESTLDSVYRADLVL 303
Cdd:PRK05291 248 ---------------GTT--------RDVIeehinldgiplrLIDTAG-IretDDE----VEKigIERSREAIEEADLVL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 304 LVVDASEPVEDMREKLvtshdtLYERNEAPVVTVFNKVDrlapgeLADKRGALSGVAPDPVAVSAKTGAGVAELRDRVED 383
Cdd:PRK05291 300 LVLDASEPLTEEDDEI------LEELKDKPVIVVLNKAD------LTGEIDLEEENGKPVIRISAKTGEGIDELREAIKE 367
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
168-385 |
2.04e-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: 77.79 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 168 DESVERDIKRQISEIRDELESIAEkeEARREQRRDSGFDlVALAGYTNAGKSTLMRRLAAEidvdenaDR-----HPdld 242
Cdd:COG0486 179 EFLDREELLERLEELREELEALLA--SARQGELLREGIK-VVIVGRPNVGKSSLLNALLGE-------ERaivtdIA--- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 243 ttaesqdmlfttlGTTtrraemekRDVL------------LTDTVGfI---ADLphwlVESF--ESTLDSVYRADLVLLV 305
Cdd:COG0486 246 -------------GTT--------RDVIeeriniggipvrLIDTAG-LretEDE----VEKIgiERAREAIEEADLVLLL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 306 VDASEPVEDMREKLvtshdtLYERNEAPVVTVFNKVDRLAPGELADKRGAlsgvAPDPVAVSAKTGAGVAELRDRVEDEL 385
Cdd:COG0486 300 LDASEPLTEEDEEI------LEKLKDKPVIVVLNKIDLPSEADGELKSLP----GEPVIAISAKTGEGIDELKEAILELV 369
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
203-386 |
4.27e-15 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 75.41 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 203 SGFdlVALAGYTNAGKSTLMRRLAAE---IdvdenadrhpdldTTAESQdmlfttlgtTTRRAEM-----EKRDVLLTDT 274
Cdd:COG1159 3 SGF--VAIVGRPNVGKSTLLNALVGQkvsI-------------VSPKPQ---------TTRHRIRgivtrEDAQIVFVDT 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 275 VGFIAdlPH-----WLVESFESTLDSVyraDLVLLVVDASEPV--EDMR--EKLvtshdtlyERNEAPVVTVFNKVDRLA 345
Cdd:COG1159 59 PGIHK--PKrklgrRMNKAAWSALEDV---DVILFVVDATEKIgeGDEFilELL--------KKLKTPVILVINKIDLVK 125
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1233247415 346 PGELADKRGALSGVAP--DPVAVSAKTGAGVAELRDRVEDELP 386
Cdd:COG1159 126 KEELLPLLAEYSELLDfaEIVPISALKGDNVDELLDEIAKLLP 168
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
203-385 |
1.39e-14 |
|
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: 71.34 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 203 SGFdlVALAGYTNAGKSTLMRRLAAE---IdvdenadrhpdldTTAESQdmlfttlgtTTRRAEM-----EKRDVLLTDT 274
Cdd:cd04163 3 SGF--VAIIGRPNVGKSTLLNALVGQkisI-------------VSPKPQ---------TTRNRIRgiytdDDAQIIFVDT 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 275 VGFIAD---LPHWLVESFESTLDSVyraDLVLLVVDASEPVEDMREKLVtshDTLyERNEAPVVTVFNKVDRLAPGE--- 348
Cdd:cd04163 59 PGIHKPkkkLGERMVKAAWSALKDV---DLVLFVVDASEWIGEGDEFIL---ELL-KKSKTPVILVLNKIDLVKDKEdll 131
|
170 180 190
....*....|....*....|....*....|....*...
gi 1233247415 349 -LADKRGALSGVApDPVAVSAKTGAGVAELRDRVEDEL 385
Cdd:cd04163 132 pLLEKLKELHPFA-EIFPISALKGENVDELLEYIVEYL 168
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
166-383 |
2.03e-14 |
|
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: 74.05 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 166 EYDESVERDIKRQISEIRDELESIAEKeeARREQRRDSGFDlVALAGYTNAGKSTLMRRLAAEidvdenaDR-----HPd 240
Cdd:pfam12631 58 DIEELTEEELLERLEELLAELEKLLAT--ADRGRILREGIK-VVIVGKPNVGKSSLLNALLGE-------ERaivtdIP- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 241 ldttaesqdmlfttlGTTtrraemekRDVL------------LTDTVGfI---ADLphwlVESF--ESTLDSVYRADLVL 303
Cdd:pfam12631 127 ---------------GTT--------RDVIeetiniggiplrLIDTAG-IretDDE----VEKIgiERAREAIEEADLVL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 304 LVVDASEPVEDMREKLVTSHdtlyeRNEAPVVTVFNKVDRLAPGELADKRGalsgvAPDPVAVSAKTGAGVAELRDRVED 383
Cdd:pfam12631 179 LVLDASRPLDEEDLEILELL-----KDKKPIIVVLNKSDLLGEIDELEELK-----GKPVLAISAKTGEGLDELEEAIKE 248
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
203-386 |
5.47e-14 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 72.00 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 203 SGFdlVALAGYTNAGKSTLMRRLAAE---IdvdenadrhpdldTTAESQdmlfttlgtTTRRAEM-----EKRDVLLTDT 274
Cdd:PRK00089 5 SGF--VAIVGRPNVGKSTLLNALVGQkisI-------------VSPKPQ---------TTRHRIRgivteDDAQIIFVDT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 275 VGFIAdlPH-----WLVESFESTLDSVyraDLVLLVVDASEPVEDMREKLVTshdtLYERNEAPVVTVFNKVDRLAP-GE 348
Cdd:PRK00089 61 PGIHK--PKralnrAMNKAAWSSLKDV---DLVLFVVDADEKIGPGDEFILE----KLKKVKTPVILVLNKIDLVKDkEE 131
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1233247415 349 LADKRGALSGVAP--DPVAVSAKTGAGVAELRDRVEDELP 386
Cdd:PRK00089 132 LLPLLEELSELMDfaEIVPISALKGDNVDELLDVIAKYLP 171
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
208-385 |
1.21e-12 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 66.16 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 208 VALAGYTNAGKSTLMRRLAAEIDVDENADrhpdldttaesqdmlfTTLGTTTRRAEME----KRDVLLTDTVG--FIADL 281
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYL----------------STNGVTIDKKELKldglDVDLVIWDTPGqdEFRET 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 282 PhwlvESFESTLDSvyrADLVLLVVDASepVEDMREKLVTSHDTLYERN-EAPVVTVFNKVDRLAPGELADK---RGALS 357
Cdd:COG1100 70 R----QFYARQLTG---ASLYLFVVDGT--REETLQSLYELLESLRRLGkKSPIILVLNKIDLYDEEEIEDEerlKEALS 140
|
170 180
....*....|....*....|....*....
gi 1233247415 358 GVAPDP-VAVSAKTGAGVAELRDRVEDEL 385
Cdd:COG1100 141 EDNIVEvVATSAKTGEGVEELFAALAEIL 169
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
208-385 |
1.25e-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: 65.59 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 208 VALAGYTNAGKSTLMRRLAAEidvdenaDR-----HPdldttaesqdmlfttlGTTtrraemekRDVL------------ 270
Cdd:cd04164 6 VVIAGKPNVGKSSLLNALAGR-------DRaivsdIA----------------GTT--------RDVIeeeidlggipvr 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 271 LTDTVGfI---ADLphwlVES--FESTLDSVYRADLVLLVVDASEPVedmreklvTSHDT--LYERNEAPVVTVFNKVDr 343
Cdd:cd04164 55 LIDTAG-LretEDE----IEKigIERAREAIEEADLVLLVVDASEGL--------DEEDLeiLELPAKKPVIVVLNKSD- 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1233247415 344 lapgeLADKRGALSGVAPDP-VAVSAKTGAGVAELRDRVEDEL 385
Cdd:cd04164 121 -----LLSDAEGISELNGKPiIAISAKTGEGIDELKEALLELA 158
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
175-394 |
2.15e-11 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 64.79 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 175 IKRQISEIRDELESIAEKEEARREQRRdsgfdlVALAGYTNAGKSTLMRRL----AAEIDVdenadrhpDLDTTAESQDM 250
Cdd:COG3596 15 LKRLPQVLRELLAEALERLLVELPPPV------IALVGKTGAGKSSLINALfgaeVAEVGV--------GRPCTREIQRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 251 LFTTLGTTTrraemekrdVLLTDTVGF-IADLPHWLVesfESTLDSVYRADLVLLVVDASEPVEDMREKLVTSHDTLYER 329
Cdd:COG3596 81 RLESDGLPG---------LVLLDTPGLgEVNERDREY---RELRELLPEADLILWVVKADDRALATDEEFLQALRAQYPD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 330 NeaPVVTVFNKVDRLAPGE--------------------LADKRGALSGVAPDPVAVSAK---TGAGVAELRDRVEDELP 386
Cdd:COG3596 149 P--PVLVVLTQVDRLEPERewdppynwpsppkeqnirraLEAIAEQLGVPIDRVIPVSAAedrTGYGLEELVDALAEALP 226
|
....*...
gi 1233247415 387 DWERERLV 394
Cdd:COG3596 227 EAKRSRLA 234
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
208-386 |
1.93e-10 |
|
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: 59.62 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 208 VALAGYTNAGKSTLMRRLaaeidVDENADRHPDLDTTAESQDMLF------TTLGTTTRRAEMEKRDVLLTDTVGfiadl 281
Cdd:cd00881 2 VGVIGHVDHGKTTLTGSL-----LYQTGAIDRRGTRKETFLDTLKeerergITIKTGVVEFEWPKRRINFIDTPG----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 282 pHwlVESFESTLDSVYRADLVLLVVDASEPVEDMREKLVTshdTLYERNEaPVVTVFNKVDRLAPGELAD---------K 352
Cdd:cd00881 72 -H--EDFSKETVRGLAQADGALLVVDANEGVEPQTREHLN---IALAGGL-PIIVAVNKIDRVGEEDFDEvlreikellK 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 1233247415 353 RGALSGVAPDPVAV---SAKTGAGVAELRDRVEDELP 386
Cdd:cd00881 145 LIGFTFLKGKDVPIipiSALTGEGIEELLDAIVEHLP 181
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
208-383 |
4.73e-10 |
|
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: 58.21 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 208 VALAGYTNAGKSTLMRRLAAE---IdVDENADrhpdldTTAESQDMLFttlgtttrraEMEKRDVLLTDTVGF-----IA 279
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLGEervI-VSDIAG------TTRDSIDVPF----------EYDGQKYTLIDTAGIrkkgkVT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 280 DLPHWLveSFESTLDSVYRADLVLLVVDASEPVEDMREKLVtshDTLYERNEAPVVtVFNKVDRLAP---------GELA 350
Cdd:cd01895 68 EGIEKY--SVLRTLKAIERADVVLLVLDASEGITEQDLRIA---GLILEEGKALII-VVNKWDLVEKdektmkefeKELR 141
|
170 180 190
....*....|....*....|....*....|....
gi 1233247415 351 DKRGALSGVapdP-VAVSAKTGAGVAELRDRVED 383
Cdd:cd01895 142 RKLPFLDYA---PiVFISALTGQGVDKLFDAIKE 172
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
208-385 |
1.62e-09 |
|
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: 56.66 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 208 VALAGYTNAGKSTLMRRLAA---EIdvdenADRHpdldttaesqdmlFTTL----GTttrraemekrdVLLTDTVGF-IA 279
Cdd:cd01898 3 VGLVGLPNAGKSTLLSAISNakpKI-----ADYP-------------FTTLvpnlGV-----------VRVDDGRSFvIA 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 280 DLPHwLVE----------SFestLDSVYRADLVLLVVDAS---EPVEDM---REKLVTSHDTLYERneaPVVTVFNKVDR 343
Cdd:cd01898 54 DIPG-LIEgasegkglghRF---LRHIERTRVLLHVIDLSgedDPVEDYetiRNELEAYNPGLAEK---PRIVVLNKIDL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1233247415 344 LAPGELADK-RGALSGVAPDPV-AVSAKTGAGVAELRDRVEDEL 385
Cdd:cd01898 127 LDAEERFEKlKELLKELKGKKVfPISALTGEGLDELLKKLAKLL 170
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
207-387 |
3.83e-09 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 58.52 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 207 LVALAGYTNAGKSTLMRRLAAEID--VDENA----DRHPdldttaesqdmlfttlgtttRRAEMEKRDVLLTDTVGFIAD 280
Cdd:PRK00093 3 VVAIVGRPNVGKSTLFNRLTGKRDaiVADTPgvtrDRIY--------------------GEAEWLGREFILIDTGGIEPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 281 LPHWLVESFESTLDSVYRADLVLLVVDASEPVEDMREKLVtshDTLYeRNEAPVVTVFNKVDRLAPGELADKRGALsGVa 360
Cdd:PRK00093 63 DDGFEKQIREQAELAIEEADVILFVVDGRAGLTPADEEIA---KILR-KSNKPVILVVNKVDGPDEEADAYEFYSL-GL- 136
|
170 180
....*....|....*....|....*..
gi 1233247415 361 PDPVAVSAKTGAGVAELRDRVEDELPD 387
Cdd:PRK00093 137 GEPYPISAEHGRGIGDLLDAILEELPE 163
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
208-391 |
6.00e-09 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 57.73 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 208 VALAGYTNAGKSTLMRRLAAEID--VDENA----DRHpdldttaesqdmlfttlgttTRRAEMEKRDVLLTDTVGF-IAD 280
Cdd:COG1160 5 VAIVGRPNVGKSTLFNRLTGRRDaiVDDTPgvtrDRI--------------------YGEAEWGGREFTLIDTGGIePDD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 281 LPHWLVESFESTLDSVYRADLVLLVVDASEPVEDMREKLVtshDTLYeRNEAPVVTVFNKVDRLAPGELADKRGALsGVa 360
Cdd:COG1160 65 DDGLEAEIREQAELAIEEADVILFVVDGRAGLTPLDEEIA---KLLR-RSGKPVILVVNKVDGPKREADAAEFYSL-GL- 138
|
170 180 190
....*....|....*....|....*....|.
gi 1233247415 361 PDPVAVSAKTGAGVAELRDRVEDELPDWERE 391
Cdd:COG1160 139 GEPIPISAEHGRGVGDLLDAVLELLPEEEEE 169
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
209-385 |
7.41e-09 |
|
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: 54.36 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 209 ALAGYTNAGKSTLMRRLAAEID--VDENA----DRHpdldttaesqdmlfttlgttTRRAEMEKRDVLLTDTVGFIADLP 282
Cdd:cd01894 1 AIVGRPNVGKSTLFNRLTGRRDaiVSDTPgvtrDRK--------------------YGEAEWGGREFILIDTGGIEPDDE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 283 HWLVESFESTLDSVYRADLVLLVVDASEPVEDMREKLVtshDTLYERNEaPVVTVFNKVDRLAPGELADKRGALsGVaPD 362
Cdd:cd01894 61 GISKEIREQAEIAIEEADVILFVVDGREGLTPADEEIA---KYLRKSKK-PVILVVNKIDNIKEEEEAAEFYSL-GF-GE 134
|
170 180
....*....|....*....|...
gi 1233247415 363 PVAVSAKTGAGVAELRDRVEDEL 385
Cdd:cd01894 135 PIPISAEHGRGIGDLLDAILELL 157
|
|
| NOG |
cd01897 |
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ... |
208-385 |
3.91e-08 |
|
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: 52.56 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 208 VALAGYTNAGKSTLMRRLaaeidvdenadrhpdldTTA--ESQDMLFTT----LGTTTRRAEmekrDVLLTDTVGfIADL 281
Cdd:cd01897 3 LVIAGYPNVGKSSLVNKL-----------------TRAkpEVAPYPFTTkslfVGHFDYKYL----RWQVIDTPG-ILDR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 282 PhwLVESFESTLDSV----YRADLVLLVVDASE----PVEDMREKLvtshDTLYERNEAPVVTVFNKVDRLAPGELADKR 353
Cdd:cd01897 61 P--LEERNTIEMQAItalaHLRAAVLFFIDPSEtcgySIEEQLSLF----KEIKPLFNKPVIVVLNKIDLLTEEDLSEIE 134
|
170 180 190
....*....|....*....|....*....|..
gi 1233247415 354 GALSGVAPDPVAVSAKTGAGVAELRDRVEDEL 385
Cdd:cd01897 135 KELEKEGEEVIKISTLTEEGVDELKNKACELL 166
|
|
| Obg_like |
cd01881 |
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
209-385 |
6.43e-08 |
|
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: 52.01 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 209 ALAGYTNAGKSTLMRRLaaeidvdenadrhpdldTTA--ESQDMLFTTLGTTTRRAEM-EKRDVLLTDTVGFIaDLPHWL 285
Cdd:cd01881 1 GLVGLPNVGKSTLLSAL-----------------TSAkvEIASYPFTTLEPNVGVFEFgDGVDIQIIDLPGLL-DGASEG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 286 VESFESTLDSVYRADLVLLVVDASE-----PVEDMREKLVTSHDTLYERNEAPVVTVFNKVDrlAPGELADKRGALSGVA 360
Cdd:cd01881 63 RGLGEQILAHLYRSDLILHVIDASEdcvgdPLEDQKTLNEEVSGSFLFLKNKPEMIVANKID--MASENNLKRLKLDKLK 140
|
170 180
....*....|....*....|....*..
gi 1233247415 361 PDP--VAVSAKTGAGVAELRDRVEDEL 385
Cdd:cd01881 141 RGIpvVPTSALTRLGLDRVIRTIRKLL 167
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
208-383 |
9.59e-08 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 51.74 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 208 VALAGYTNAGKSTLMRRLAaeidvdenadrhpdldttaeSQDMLFTTLGT--TTRRA---EMEKrDVLLTDTVGFI-ADL 281
Cdd:cd01876 2 VAFAGRSNVGKSSLINALT--------------------NRKKLARTSKTpgRTQLInffNVGD-KFRLVDLPGYGyAKV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 282 PHWLVESFESTLDS--VYRADL--VLLVVDASEPVedmreklvTSHD----TLYERNEAPVVTVFNKVDRLAPGELADK- 352
Cdd:cd01876 61 SKEVREKWGKLIEEylENRENLkgVVLLIDARHGP--------TPIDlemlEFLEELGIPFLIVLTKADKLKKSELAKVl 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 1233247415 353 ---RGALSGVAPDP--VAVSAKTGAGVAELRDRVED 383
Cdd:cd01876 133 kkiKEELNLFNILPpvILFSSKKGTGIDELRALIAE 168
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
181-383 |
2.31e-07 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 52.72 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 181 EIRDELESIAEKEEARREQRrdsgfdlVALAGYTNAGKSTLMRRLAAE---IdVDENAdrhpdlDTTAESQDMLFttlgt 257
Cdd:COG1160 158 AVLELLPEEEEEEEEDDPIK-------IAIVGRPNVGKSSLINALLGEervI-VSDIA------GTTRDSIDTPF----- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 258 ttrraEMEKRDVLLTDTVGF-----IADlphwLVE--SFESTLDSVYRADLVLLVVDASEPVEDMREKLVtshDTLYERN 330
Cdd:COG1160 219 -----ERDGKKYTLIDTAGIrrkgkVDE----GIEkySVLRTLRAIERADVVLLVIDATEGITEQDLKIA---GLALEAG 286
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1233247415 331 EAPVVtVFNKVDRLAPG---------ELADKRGALSGvAPdPVAVSAKTGAGVAELRDRVED 383
Cdd:COG1160 287 KALVI-VVNKWDLVEKDrktreelekEIRRRLPFLDY-AP-IVFISALTGQGVDKLLEAVDE 345
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
181-383 |
4.64e-07 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 51.97 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 181 EIRDELESIAEKEEARREQRrdsgfdlVALAGYTNAGKSTLMRRLAAEidvdenaDRHPDLD---TTAESQDMLFttlgt 257
Cdd:PRK00093 156 AILEELPEEEEEDEEDEPIK-------IAIIGRPNVGKSSLINALLGE-------ERVIVSDiagTTRDSIDTPF----- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 258 ttrraEMEKRDVLLTDTVGF-----IADLphwlVE--SFESTLDSVYRADLVLLVVDASEPVEDMREKLVtshDTLYERN 330
Cdd:PRK00093 217 -----ERDGQKYTLIDTAGIrrkgkVTEG----VEkySVIRTLKAIERADVVLLVIDATEGITEQDLRIA---GLALEAG 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1233247415 331 EAPVVtVFNKVDRLAPG-------ELADKRGALSGVapdP-VAVSAKTGAGVAELRDRVED 383
Cdd:PRK00093 285 RALVI-VVNKWDLVDEKtmeefkkELRRRLPFLDYA---PiVFISALTGQGVDKLLEAIDE 341
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
300-383 |
7.81e-07 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 49.70 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 300 DLVLLVVDASEPVEDMR--EKLVTshdtLYERNEAPVVTVFNKVDRLAPGELADKRGALSGVAPDPVAVSAKTGAGVAEL 377
Cdd:cd01854 4 DQVLIVFSLKEPFFNLRllDRYLV----AAEASGIEPVIVLNKADLVDDEELEELLEIYEKLGYPVLAVSAKTGEGLDEL 79
|
....*.
gi 1233247415 378 RDRVED 383
Cdd:cd01854 80 RELLKG 85
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
208-387 |
1.27e-06 |
|
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: 48.68 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 208 VALAGYTNAGKSTLMRRL-AAEIDVDENADRHPD----LDTTAE------SQDMLFTTLGTttrraemEKRDVLLTDTVG 276
Cdd:pfam00009 6 IGIIGHVDHGKTTLTDRLlYYTGAISKRGEVKGEgeagLDNLPEerergiTIKSAAVSFET-------KDYLINLIDTPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 277 ---FIADlphwlvesfestldsVYR----ADLVLLVVDASEPVEDMREKlvtsHDTLYERNEAPVVTVFNKVDRL----- 344
Cdd:pfam00009 79 hvdFVKE---------------VIRglaqADGAILVVDAVEGVMPQTRE----HLRLARQLGVPIIVFINKMDRVdgael 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1233247415 345 --APGELADKRGALSGVAPDPVAV---SAKTGAGVAELRDRVEDELPD 387
Cdd:pfam00009 140 eeVVEEVSRELLEKYGEDGEFVPVvpgSALKGEGVQTLLDALDEYLPS 187
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
208-398 |
4.28e-06 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 49.02 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 208 VALAGYTNAGKSTLMRR-LAAEIDVDENadrhpdldttaesqdmlftTLGTTTRR----AEMEKRDVLLTDTVGFIADlp 282
Cdd:PRK09518 278 VAIVGRPNVGKSTLVNRiLGRREAVVED-------------------TPGVTRDRvsydAEWAGTDFKLVDTGGWEAD-- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 283 hwlVESFESTLDS-----VYRADLVLLVVDASEPVEDMREKLVTshdtLYERNEAPVVTVFNKVDRLAPGELADKRGALS 357
Cdd:PRK09518 337 ---VEGIDSAIASqaqiaVSLADAVVFVVDGQVGLTSTDERIVR----MLRRAGKPVVLAVNKIDDQASEYDAAEFWKLG 409
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1233247415 358 gvAPDPVAVSAKTGAGVAELRDRVEDELPDWERERLVLPVS 398
Cdd:PRK09518 410 --LGEPYPISAMHGRGVGDLLDEALDSLKVAEKTSGFLTPS 448
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
209-380 |
1.33e-05 |
|
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: 44.64 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 209 ALAGYTNAGKSTLMRRLAAeIDVDENADRHPdldttaesqdmlFTTLGTTTRRAEMEKRDVLLtDTVGFiadlPHWLV-- 286
Cdd:cd11383 1 GLMGKTGAGKSSLCNALFG-TEVAAVGDRRP------------TTRAAQAYVWQTGGDGLVLL-DLPGV----GERGRrd 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 287 -ESFESTLDSVYRADLVLLVVDASEP----VEDMREKLVTSHDtlyerneAPVVTVFNKVDRLapgeladkrgalsgvap 361
Cdd:cd11383 63 rEYEELYRRLLPEADLVLWLLDADDRalaaDHDFYLLPLAGHD-------APLLFVLNQVDPV----------------- 118
|
170
....*....|....*....
gi 1233247415 362 dpVAVSAKTGAGVAELRDR 380
Cdd:cd11383 119 --LAVSARTGWGLDELAEA 135
|
|
| obgE |
PRK12299 |
GTPase CgtA; Reviewed |
208-391 |
1.52e-05 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 46.60 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 208 VALAGYTNAGKSTLMRRLAA---EIdvdenADrHPdldttaesqdmlFTTL----GTTtrRAEMEKRDVlltdtvgfIAD 280
Cdd:PRK12299 161 VGLVGLPNAGKSTLISAVSAakpKI-----AD-YP------------FTTLhpnlGVV--RVDDYKSFV--------IAD 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 281 LPHwLVE----------SFestLDSVYRADLVLLVVDASE--PVED---MREKLVTSHDTLYERneaPVVTVFNKVDRLA 345
Cdd:PRK12299 213 IPG-LIEgasegaglghRF---LKHIERTRLLLHLVDIEAvdPVEDyktIRNELEKYSPELADK---PRILVLNKIDLLD 285
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1233247415 346 PGELADKRGAL-SGVAPDPV-AVSAKTGAGVAELRDRVEDELPDWERE 391
Cdd:PRK12299 286 EEEEREKRAALeLAALGGPVfLISAVTGEGLDELLRALWELLEEARRE 333
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
299-383 |
5.42e-05 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 43.68 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 299 ADLVLLVVDASEPveDMREKLVTSHDTLYERNEAPVVTVFNKVDRLAPGELADKRGA-LSGVAPDPVAVSAKTGAGVAEL 377
Cdd:pfam03193 23 VDQAVIVFSLKEP--DFNLNLLDRFLVLAEASGIEPVIVLNKIDLLDEEEELEELLKiYRAIGYPVLFVSAKTGEGIEAL 100
|
....*.
gi 1233247415 378 RDRVED 383
Cdd:pfam03193 101 KELLKG 106
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
208-382 |
6.23e-05 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 43.13 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 208 VALAGYTNAGKSTLMRRLAaeidvdenadrhpdLDTTAESQDMLFTTLGTTTRRAEM--EKRDVLLTDTVGFIADLPHWL 285
Cdd:TIGR00231 4 IVIVGHPNVGKSTLLNSLL--------------GNKGSITEYYPGTTRNYVTTVIEEdgKTYKFNLLDTAGQEDYDAIRR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 286 VeSFESTLDSVYRADLVLLVVDASEPVEDMREKLVTSHDTlyernEAPVVTVFNKVD---RLAPGELADKRGALSGvaPD 362
Cdd:TIGR00231 70 L-YYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHADS-----GVPIILVGNKIDlkdADLKTHVASEFAKLNG--EP 141
|
170 180
....*....|....*....|
gi 1233247415 363 PVAVSAKTGAGVAELRDRVE 382
Cdd:TIGR00231 142 IIPLSAETGKNIDSAFKIVE 161
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
208-391 |
9.52e-05 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 44.58 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 208 VALAGYTNAGKSTLMRRLaaeIDVDEnadrhpdldttAESQDmlftTLGTTTRR----AEMEKRDVLLTDTVGFIAD--- 280
Cdd:PRK03003 41 VAVVGRPNVGKSTLVNRI---LGRRE-----------AVVED----VPGVTRDRvsydAEWNGRRFTVVDTGGWEPDakg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 281 LPHWLVESFESTLDSvyrADLVLLVVDASEPVEDMREKLVTshdtLYERNEAPVVTVFNKVDrlAPGELADKRGALSGVA 360
Cdd:PRK03003 103 LQASVAEQAEVAMRT---ADAVLFVVDATVGATATDEAVAR----VLRRSGKPVILAANKVD--DERGEADAAALWSLGL 173
|
170 180 190
....*....|....*....|....*....|.
gi 1233247415 361 PDPVAVSAKTGAGVAELRDRVEDELPDWERE 391
Cdd:PRK03003 174 GEPHPVSALHGRGVGDLLDAVLAALPEVPRV 204
|
|
| MJ1464 |
cd01859 |
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ... |
298-387 |
1.17e-04 |
|
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.
Pssm-ID: 206752 [Multi-domain] Cd Length: 157 Bit Score: 42.31 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 298 RADLVLLVVDASEPVE---DMREKLVtshdtlyERNEAPVVTVFNKVDrLAPGELADK-RGALSGVAPDPVAVSAKTGAG 373
Cdd:cd01859 11 EADVVLEVVDARDPELtrsRKLERMA-------LELGKKLIIVLNKAD-LVPREVLEKwKEVFESEGLPVVYVSARERLG 82
|
90
....*....|....
gi 1233247415 374 VAELRDRVEDELPD 387
Cdd:cd01859 83 TRILRRTIKELAID 96
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
162-390 |
3.86e-04 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 42.86 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 162 MGLGE-YDESVERDikRQISEIRDELESIAEKEEARREQRRDSGFDLVALAGYTNAGKSTLMRRLAAEidvdenaDRhpd 240
Cdd:PRK09518 408 LGLGEpYPISAMHG--RGVGDLLDEALDSLKVAEKTSGFLTPSGLRRVALVGRPNVGKSSLLNQLTHE-------ER--- 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 241 ldttAESQDMLFTTLGTTTRRAEMEKRDVLLTDTVGfIADLPHWLV--ESFES--TLDSVYRADLVLLVVDASEPVEDMR 316
Cdd:PRK09518 476 ----AVVNDLAGTTRDPVDEIVEIDGEDWLFIDTAG-IKRRQHKLTgaEYYSSlrTQAAIERSELALFLFDASQPISEQD 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 317 EKLVTshdTLYERNEApVVTVFNKVDRLApgelADKRGAL--------SGVAPDP-VAVSAKTGAGVAELRDRVEDELPD 387
Cdd:PRK09518 551 LKVMS---MAVDAGRA-LVLVFNKWDLMD----EFRRQRLerlwktefDRVTWARrVNLSAKTGWHTNRLAPAMQEALES 622
|
...
gi 1233247415 388 WER 390
Cdd:PRK09518 623 WDQ 625
|
|
| HflX_C |
pfam19275 |
HflX C-terminal domain; This entry represents the C-terminal domain of the HflX protein. HflX ... |
364-416 |
1.82e-03 |
|
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: 37.68 E-value: 1.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1233247415 364 VAVSAKTGAGVAELRDRVEDELPDWERER-LVLPVsdEAMSLVSWIHDHGHVDE 416
Cdd:pfam19275 13 IAVSAITGEGVDALMDEISRRLSGVLTETtVVLPA--DKLALLSWVYENAIVDG 64
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
300-383 |
8.29e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 38.26 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 300 DLVLLVVDASEPveDMREKLVTSHDTLYERNEAPVVTVFNKVDRLAPGELADKRGAL-SGVAPDPVAVSAKTGAGVAELR 378
Cdd:PRK00098 82 DQAVLVFAAKEP--DFSTDLLDRFLVLAEANGIKPIIVLNKIDLLDDLEEARELLALyRAIGYDVLELSAKEGEGLDELK 159
|
....*
gi 1233247415 379 DRVED 383
Cdd:PRK00098 160 PLLAG 164
|
|
| YqeH |
cd01855 |
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
287-387 |
9.31e-03 |
|
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.
Pssm-ID: 206748 [Multi-domain] Cd Length: 191 Bit Score: 37.24 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233247415 287 ESFESTLDSV-YRADLVLLVVDASEPvedmreklvtsHDTLYER-----NEAPVVTVFNKVDRLAPGE--------LADK 352
Cdd:cd01855 21 EDFLEILSTLlNDNALVVHVVDIFDF-----------PGSLIPGlaeliGAKPVILVGNKIDLLPKDVkpnrlkqwVKKR 89
|
90 100 110
....*....|....*....|....*....|....*
gi 1233247415 353 RGALSGVAPDPVAVSAKTGAGVAELRDRVEDELPD 387
Cdd:cd01855 90 LKIGGLKIKDVILVSAKKGWGVEELIEEIKKLAKY 124
|
|
| |
