|
Name |
Accession |
Description |
Interval |
E-value |
| HflX |
COG2262 |
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
8-340 |
1.03e-68 |
|
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 220.73 E-value: 1.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 8 IGLDIQESVTIRKNS--GRYLISDYKLREIVEKKEKVKAEVILIEPELPPRDKINIIKATKADVIDRTLLLLEVFESNAG 85
Cdd:COG2262 39 AGAEVVGTVTQRRDKpdPATYIGKGKVEELAELVEELEADLVIFDDELSPSQQRNLEKALGVKVIDRTGLILDIFAQRAR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 86 SKEAKLQISLARSGHMLP-LVREVLNNSKRGELPGFLAGGTYAIDKYYRQLRRQVAKTRRELEEIRIRRDILRERRRVSG 164
Cdd:COG2262 119 TREGKLQVELAQLQYLLPrLVGMWTHLSRQGGGIGTRGPGETQLETDRRLIRDRIARLKRELEKVRKQRELQRKRRKRSG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 165 LPLIAIIGYANAGKTTLFNLLTGSNKETSNKPFTTISP---KVSL-SNLGFLVIDTVGFVMNVPPEIIEAFYSTLEEIRE 240
Cdd:COG2262 199 IPTVALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPttrRLELpDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVRE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 241 ADVLLLLLDSTEDLFliEERVKQASVTLSNIESLYKPIVVALNKVEKTGRDDIEEKRAKLYqtcKSVFpmfvglakVSAK 320
Cdd:COG2262 279 ADLLLHVVDASDPDF--EEQIETVNEVLEELGADDKPIILVFNKIDLLDDEELERLRAGYP---DAVF--------ISAK 345
|
330 340
....*....|....*....|
gi 504370862 321 KGLGIDEMVNVIWKALNRKQ 340
Cdd:COG2262 346 TGEGIDELLEAIEERLPEDR 365
|
|
| GTP_HflX |
TIGR03156 |
GTP-binding protein HflX; This protein family is one of a number of homologous small, ... |
1-336 |
2.13e-54 |
|
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: 181.52 E-value: 2.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 1 MKTLSVLIGLDIQESVTIRKNS--GRYLISDYKLREIVEKKEKVKAEVILIEPELPPRDKINIIKATKADVIDRTLLLLE 78
Cdd:TIGR03156 22 LAELAETAGAEVVGTVTQKRSRpdPATYIGKGKVEEIAELVEELEADLVIFDHELSPSQERNLEKALGCRVIDRTGLILD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 79 VFESNAGSKEAKLQISLARSGHMLP-LVR--EVLNNSKRGelpgflaGGTYA-------IDKyyRQLRRQVAKTRRELEE 148
Cdd:TIGR03156 102 IFAQRARTHEGKLQVELAQLKYLLPrLVGgwTHLSRQGGG-------IGTRGpgetqleTDR--RLIRERIAQLKKELEK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 149 IRIRRDILRERRRVSGLPLIAIIGYANAGKTTLFNLLTGSNKETSNKPFTTISP---KVSLSNLG-FLVIDTVGFVMNVP 224
Cdd:TIGR03156 173 VEKQRERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGADVYAADQLFATLDPttrRLDLPDGGeVLLTDTVGFIRDLP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 225 PEIIEAFYSTLEEIREADVLLLLLDSTEDLFliEERVKQASVTLSNIESLYKPIVVALNKVEKTGRDDIEEKRAKLYQTc 304
Cdd:TIGR03156 253 HELVAAFRATLEEVREADLLLHVVDASDPDR--EEQIEAVEKVLEELGAEDIPQLLVYNKIDLLDEPRIERLEEGYPEA- 329
|
330 340 350
....*....|....*....|....*....|..
gi 504370862 305 ksVFpmfvglakVSAKKGLGIDEMVNVIWKAL 336
Cdd:TIGR03156 330 --VF--------VSAKTGEGLDLLLEAIAERL 351
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
126-336 |
8.38e-48 |
|
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: 159.93 E-value: 8.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 126 YAIDKYYRQLRRQVAKTRRELEEIRIRRDILRERRRVSGLPLIAIIGYANAGKTTLFNLLTGSNKETSNKPFTTISPKVS 205
Cdd:cd01878 2 TQLETDRRLIRERIAKLRKELEKVKKQRELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 206 LSNLG----FLVIDTVGFVMNVPPEIIEAFYSTLEEIREADVLLLLLDSTEDLFliEERVKQASVTLSNIESLYKPIVVA 281
Cdd:cd01878 82 RIKLPggreVLLTDTVGFIRDLPHQLVEAFRSTLEEVAEADLLLHVVDASDPDR--EEQIETVEEVLKELGADDIPIILV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504370862 282 LNKVEKTGRDDIEEKRAKLYQtcKSVFpmfvglakVSAKKGLGIDEMVNVIWKAL 336
Cdd:cd01878 160 LNKIDLLDDEELEERLRAGRP--DAVF--------ISAKTGEGLDLLKEAIEELL 204
|
|
| PRK11058 |
PRK11058 |
GTPase HflX; Provisional |
24-336 |
6.56e-30 |
|
GTPase HflX; Provisional
Pssm-ID: 182934 [Multi-domain] Cd Length: 426 Bit Score: 118.28 E-value: 6.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 24 RYLISDYKLREIVEKKEKVKAEVILIEPELPPRDKINIIKATKADVIDRTLLLLEVFESNAGSKEAKLQISLARSGHMLP 103
Cdd:PRK11058 55 KYFVGEGKAVEIAEAVKATGASVVLFDHALSPAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLAT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 104 -LVR--EVLNNSKRGelPGFLAGGTYAIDKYYRQLRRQVAKTRRELEEIRIRRDILRERRRVSGLPLIAIIGYANAGKTT 180
Cdd:PRK11058 135 rLVRgwTHLERQKGG--IGLRGPGETQLETDRRLLRNRIVQILSRLERVEKQREQGRRARIKADVPTVSLVGYTNAGKST 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 181 LFNLLTGSNKETSNKPFTTISP---KVSLSNLGFLVI-DTVGFVMNVPPEIIEAFYSTLEEIREADVLLLLLDSTEDLFl 256
Cdd:PRK11058 213 LFNRITEARVYAADQLFATLDPtlrRIDVADVGETVLaDTVGFIRHLPHDLVAAFKATLQETRQATLLLHVVDAADVRV- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 257 iEERVKQASVTLSNIESLYKPIVVALNKVektgrDDIEEKRAKLYQTCKSVfPMFVGLakvSAKKGLGIDemvnVIWKAL 336
Cdd:PRK11058 292 -QENIEAVNTVLEEIDAHEIPTLLVMNKI-----DMLDDFEPRIDRDEENK-PIRVWL---SAQTGAGIP----LLFQAL 357
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
168-284 |
3.89e-24 |
|
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: 94.99 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKETSNKPFTTISP---KVSLSNLGFLVIDTVGFVMNVPPE--IIEAFystlEEIREAD 242
Cdd:pfam01926 2 VALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPnegRLELKGKQIILVDTPGLIEGASEGegLGRAF----LAIIEAD 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 504370862 243 VLLLLLDSTEDLFLIEERVkqasvtLSNIESLYKPIVVALNK 284
Cdd:pfam01926 78 LILFVVDSEEGITPLDEEL------LELLRENKKPIILVLNK 113
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
169-327 |
8.91e-21 |
|
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: 87.30 E-value: 8.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 169 AIIGYANAGKTTLFNLLTGSN-KETSNKPFTTISPK----VSLSNLGFLVIDTVGFVMnVPPEIIEAFYSTLEEIREADV 243
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLGQNvGIVSPIPGTTRDPVrkewELLPLGPVVLIDTPGLDE-EGGLGRERVEEARQVADRADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 244 LLLLLDSTEDLFLIEERvkqasvtLSNIESLYKPIVVALNKVEKTGRDdieEKRAKLYQTCKSVFPmFVGLAKVSAKKGL 323
Cdd:cd00880 80 VLLVVDSDLTPVEEEAK-------LGLLRERGKPVLLVLNKIDLVPES---EEEELLRERKLELLP-DLPVIAVSALPGE 148
|
....
gi 504370862 324 GIDE 327
Cdd:cd00880 149 GIDE 152
|
|
| Obg_CgtA |
TIGR02729 |
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ... |
165-336 |
3.45e-16 |
|
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: 78.23 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 165 LPLIA---IIGYANAGKTTLFNLLTGSNKETSNKPFTTISPkvslsNLGFLVIDTV-GFVMNVPPEIIEA---------- 230
Cdd:TIGR02729 154 LKLLAdvgLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVP-----NLGVVRVDDGrSFVIADIPGLIEGasegaglghr 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 231 FystLEEIREADVLLLLLDST--------EDLFLIEERVKQASVTLSNieslyKPIVVALNKVEKTGRDDIEEKRAKLYQ 302
Cdd:TIGR02729 229 F---LKHIERTRVLLHLIDISpedgsdpvEDYEIIRNELKKYSPELAE-----KPRIVVLNKIDLLDEEELEELLKELKK 300
|
170 180 190
....*....|....*....|....*....|....*
gi 504370862 303 TC-KSVFPmfvglakVSAKKGLGIDEMVNVIWKAL 336
Cdd:TIGR02729 301 ELgKPVFP-------ISALTGEGLDELLDALAELL 328
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
169-332 |
9.70e-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: 73.64 E-value: 9.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 169 AIIGYANAGKTTLFNLLTGSN-KETSNKPFTTISPK-----VSLSNLGFLVIDTVGFVMNvppEIIEAFYSTLEEIREAD 242
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEvGEVSDVPGTTRDPDvyvkeLDKGKVKLVLVDTPGLDEF---GGLGREELARLLLRGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 243 VLLLLLDSTEDLFLIEERVKQasvtLSNIESLYKPIVVALNKVEKTGRDDIEEKRAKLYQTCKSVFPMFvglaKVSAKKG 322
Cdd:cd00882 78 LILLVVDSTDRESEEDAKLLI----LRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVF----EVSAKTG 149
|
170
....*....|
gi 504370862 323 LGIDEMVNVI 332
Cdd:cd00882 150 EGVDELFEKL 159
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
168-336 |
1.44e-15 |
|
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: 73.23 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKETSNKPFTTISPkvslsNLGFLVI-DTVGFVMNVPPEIIE----------AFystLE 236
Cdd:cd01898 3 VGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVP-----NLGVVRVdDGRSFVIADIPGLIEgasegkglghRF---LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 237 EIREADVLLLLLDST------EDLFLIEERVKQASVTLSNieslyKPIVVALNKVEKTGRDDIEEKRAKLYQTCKS--VF 308
Cdd:cd01898 75 HIERTRVLLHVIDLSgeddpvEDYETIRNELEAYNPGLAE-----KPRIVVLNKIDLLDAEERFEKLKELLKELKGkkVF 149
|
170 180
....*....|....*....|....*...
gi 504370862 309 PmfvglakVSAKKGLGIDEMVNVIWKAL 336
Cdd:cd01898 150 P-------ISALTGEGLDELLKKLAKLL 170
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
169-336 |
2.16e-15 |
|
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: 72.47 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 169 AIIGYANAGKTTLFNLLTGSNKE-TSNKPFTT---ISPKVSLSNLGFLVIDTVGFVMNVPPEIIEAFYSTLEEIREADVL 244
Cdd:cd01894 1 AIVGRPNVGKSTLFNRLTGRRDAiVSDTPGVTrdrKYGEAEWGGREFILIDTGGIEPDDEGISKEIREQAEIAIEEADVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 245 LLLLDSTEDLFLIEERVkqasvtlsnIESLY---KPIVVALNKVEKTGRDDIEEKRAKLYqtcksvfpmFVGLAKVSAKK 321
Cdd:cd01894 81 LFVVDGREGLTPADEEI---------AKYLRkskKPVILVVNKIDNIKEEEEAAEFYSLG---------FGEPIPISAEH 142
|
170
....*....|....*
gi 504370862 322 GLGIDEMVNVIWKAL 336
Cdd:cd01894 143 GRGIGDLLDAILELL 157
|
|
| Rbg1 |
COG1163 |
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; |
134-337 |
2.13e-14 |
|
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440777 [Multi-domain] Cd Length: 368 Bit Score: 73.29 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 134 QLRRQVAKTRRELEEIRIRRDILRERRRV--SGLPLIAIIGYANAGKTTLFNLLTGSNKETSNKPFTTISPkvslsNLGF 211
Cdd:COG1163 30 RLKAKLAELKEELEKRKKKSGGGGEGFAVkkSGDATVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDV-----VPGM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 212 LVIDTVGF-VMNVPPEIIEAFYST------LEEIREADVLLLLLD----------------------------------- 249
Cdd:COG1163 105 LEYKGAKIqILDVPGLIEGAASGKgrgkevLSVVRNADLILIVLDvfeleqydvlkeelydagirlnkpppdvtiekkgk 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 250 ------STEDLFLIEERVKQ---------ASVTLS---NIESL---------YKPIVVALNKVEKTGRDDIEEKRAKLYQ 302
Cdd:COG1163 185 ggirvnSTGKLDLDEEDIKKilreygivnADVLIRedvTLDDLidalmgnrvYKPAIVVVNKIDLADEEYVEELKSKLPD 264
|
250 260 270
....*....|....*....|....*....|....*
gi 504370862 303 TCKSVFpmfvglakVSAKKGLGIDEMVNVIWKALN 337
Cdd:COG1163 265 GVPVIF--------ISAEKGIGLEELKEEIFEELG 291
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
165-336 |
3.89e-14 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 72.78 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 165 LPLIAIIGYANAGKTTLFNLLTGSNKE-TSNKPFTT---ISPKVSLSNLGFLVIDTVGFVMN---VPPEIIEafySTLEE 237
Cdd:PRK00093 1 KPVVAIVGRPNVGKSTLFNRLTGKRDAiVADTPGVTrdrIYGEAEWLGREFILIDTGGIEPDddgFEKQIRE---QAELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 238 IREADVLLLLLD-----STEDLFLIeERVKQASvtlsnieslyKPIVVALNKVEKtgrDDIEEKRAKLYQT-CKSVFPmf 311
Cdd:PRK00093 78 IEEADVILFVVDgraglTPADEEIA-KILRKSN----------KPVILVVNKVDG---PDEEADAYEFYSLgLGEPYP-- 141
|
170 180
....*....|....*....|....*
gi 504370862 312 vglakVSAKKGLGIDEMVNVIWKAL 336
Cdd:PRK00093 142 -----ISAEHGRGIGDLLDAILEEL 161
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
168-335 |
6.01e-14 |
|
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: 69.00 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKE-TSNKPFTT---ISPKVSLSNLGFLVIDTVGFVMNVP-PEIIEaFYS---TLEEIR 239
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLGEERViVSDIAGTTrdsIDVPFEYDGQKYTLIDTAGIRKKGKvTEGIE-KYSvlrTLKAIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 240 EADVLLLLLDSTE-----DLFLIEErvkqasvtlsnIESLYKPIVVALNK---VEKTgRDDIEEKRAKLYQtcKSVFPMF 311
Cdd:cd01895 84 RADVVLLVLDASEgiteqDLRIAGL-----------ILEEGKALIIVVNKwdlVEKD-EKTMKEFEKELRR--KLPFLDY 149
|
170 180
....*....|....*....|....
gi 504370862 312 VGLAKVSAKKGLGIDEMVNVIWKA 335
Cdd:cd01895 150 APIVFISALTGQGVDKLFDAIKEV 173
|
|
| Obg_like |
cd01881 |
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
169-336 |
7.40e-14 |
|
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: 68.57 E-value: 7.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 169 AIIGYANAGKTTLFNLLTGSNKETSNKPFTTISPKVSLSNLG----FLVIDTVGFVMNVPPE--IIEAFystLEEIREAD 242
Cdd:cd01881 1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGdgvdIQIIDLPGLLDGASEGrgLGEQI---LAHLYRSD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 243 VLLLLLDSTED---------LFLIEErvkqasVTLSNIESLYKPIVVALNKVEKTGRD----DIEEKRAKLYQTCksvfp 309
Cdd:cd01881 78 LILHVIDASEDcvgdpledqKTLNEE------VSGSFLFLKNKPEMIVANKIDMASENnlkrLKLDKLKRGIPVV----- 146
|
170 180
....*....|....*....|....*..
gi 504370862 310 mfvglaKVSAKKGLGIDEMVNVIWKAL 336
Cdd:cd01881 147 ------PTSALTRLGLDRVIRTIRKLL 167
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
168-339 |
8.88e-14 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 71.62 E-value: 8.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKE-TSNKPFTT---ISPKVSLSNLGFLVIDTVGfvMNVPPEIIEA--FYS---TLEEI 238
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLGEERViVSDIAGTTrdsIDTPFERDGQKYTLIDTAG--IRRKGKVTEGveKYSvirTLKAI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 239 READVLLLLLDSTEDlflIEERVKQasvTLSNIESLYKPIVVALNK---VEKTGRDDIEEK-RAKLYqtcksvfpmFVGL 314
Cdd:PRK00093 254 ERADVVLLVIDATEG---ITEQDLR---IAGLALEAGRALVIVVNKwdlVDEKTMEEFKKElRRRLP---------FLDY 318
|
170 180 190
....*....|....*....|....*....|.
gi 504370862 315 AK---VSAKKGLGID---EMVNVIWKALNRK 339
Cdd:PRK00093 319 APivfISALTGQGVDkllEAIDEAYENANRR 349
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
165-336 |
9.54e-14 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 71.59 E-value: 9.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 165 LPLIAIIGYANAGKTTLFNLLTGSNKE-TSNKPFTT---ISPKVSLSNLGFLVIDTVGFVMNvPPEIIEA--FYSTLEEI 238
Cdd:COG1160 2 SPVVAIVGRPNVGKSTLFNRLTGRRDAiVDDTPGVTrdrIYGEAEWGGREFTLIDTGGIEPD-DDDGLEAeiREQAELAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 239 READVLLLLLDSTEDLFLIEERVkqASVtlsniesLY---KPIVVALNKVEKtgrDDIEEKRAKLYQtcksvfpmfVGLA 315
Cdd:COG1160 81 EEADVILFVVDGRAGLTPLDEEI--AKL-------LRrsgKPVILVVNKVDG---PKREADAAEFYS---------LGLG 139
|
170 180
....*....|....*....|....
gi 504370862 316 K---VSAKKGLGIDEMVNVIWKAL 336
Cdd:COG1160 140 EpipISAEHGRGVGDLLDAVLELL 163
|
|
| obgE |
PRK12299 |
GTPase CgtA; Reviewed |
165-341 |
1.32e-13 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 70.48 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 165 LPLIA---IIGYANAGKTTLFNLLTGSNKETSNKPFTTISPkvslsNLGFLVIDTV-GFVMNVPPEIIE----------A 230
Cdd:PRK12299 155 LKLLAdvgLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHP-----NLGVVRVDDYkSFVIADIPGLIEgasegaglghR 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 231 FYSTLEEIReadVLLLLLDST-----EDLFLIEERVKQASVTLSNieslyKPIVVALNKVEKTGRDDIEEKRAKLYQTCK 305
Cdd:PRK12299 230 FLKHIERTR---LLLHLVDIEavdpvEDYKTIRNELEKYSPELAD-----KPRILVLNKIDLLDEEEEREKRAALELAAL 301
|
170 180 190
....*....|....*....|....*....|....*.
gi 504370862 306 SVFPMFvglakVSAKKGLGIDEMVNVIWKALNRKQA 341
Cdd:PRK12299 302 GGPVFL-----ISAVTGEGLDELLRALWELLEEARR 332
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
168-332 |
3.75e-13 |
|
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: 66.77 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKE--TSNKPFTTISPKVSLSNLGFLVIDTVGF-VMNVPPEIIEAFYSTLEE-IREADV 243
Cdd:cd01876 2 VAFAGRSNVGKSSLINALTNRKKLarTSKTPGRTQLINFFNVGDKFRLVDLPGYgYAKVSKEVREKWGKLIEEyLENREN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 244 L---LLLLDST-----EDL----FLIEERVkqasvtlsnieslykPIVVALNKVEKTGRDDIeEKRAKLYQTCKSVFPMF 311
Cdd:cd01876 82 LkgvVLLIDARhgptpIDLemleFLEELGI---------------PFLIVLTKADKLKKSEL-AKVLKKIKEELNLFNIL 145
|
170 180
....*....|....*....|.
gi 504370862 312 VGLAKVSAKKGLGIDEMVNVI 332
Cdd:cd01876 146 PPVILFSSKKGTGIDELRALI 166
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
168-339 |
3.91e-13 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 69.67 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGsnKE---TSNKPFTT---ISPKVSLSNLGFLVIDTVGfvM----NVpPEIIEaFYS---T 234
Cdd:COG1160 178 IAIVGRPNVGKSSLINALLG--EErviVSDIAGTTrdsIDTPFERDGKKYTLIDTAG--IrrkgKV-DEGIE-KYSvlrT 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 235 LEEIREADVLLLLLDSTE-----DLFLIEErvkqasvtlsnIESLYKPIVVALNK---VEK--TGRDDIEEK-RAKLYQT 303
Cdd:COG1160 252 LRAIERADVVLLVIDATEgiteqDLKIAGL-----------ALEAGKALVIVVNKwdlVEKdrKTREELEKEiRRRLPFL 320
|
170 180 190
....*....|....*....|....*....|....*....
gi 504370862 304 cksvfpMFVGLAKVSAKKGLGID---EMVNVIWKALNRK 339
Cdd:COG1160 321 ------DYAPIVFISALTGQGVDkllEAVDEVYESANKR 353
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
168-336 |
1.00e-12 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 67.38 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGsnkE----TSNKPFTT---ISPKVSLSNLGFLVIDTVGF---------VMNvppeiiEAF 231
Cdd:PRK00089 8 VAIVGRPNVGKSTLLNALVG---QkisiVSPKPQTTrhrIRGIVTEDDAQIIFVDTPGIhkpkralnrAMN------KAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 232 YSTLEeirEADVLLLLLDSTEDLFLIEERVkqasvtLSNIESLYKPIVVALNKVEKTG-RDDIEEKRAKLYQTC--KSVF 308
Cdd:PRK00089 79 WSSLK---DVDLVLFVVDADEKIGPGDEFI------LEKLKKVKTPVILVLNKIDLVKdKEELLPLLEELSELMdfAEIV 149
|
170 180
....*....|....*....|....*...
gi 504370862 309 PmfvglakVSAKKGLGIDEMVNVIWKAL 336
Cdd:PRK00089 150 P-------ISALKGDNVDELLDVIAKYL 170
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
168-332 |
3.12e-12 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 64.02 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSnK--ETSNKPFTT------IspkVSLSNLGFLVIDTVGFV---------MNvppeiiEA 230
Cdd:cd04163 6 VAIIGRPNVGKSTLLNALVGQ-KisIVSPKPQTTrnrirgI---YTDDDAQIIFVDTPGIHkpkkklgerMV------KA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 231 FYSTLEeirEADVLLLLLDSTEDLFLIEERVkqasvtLSNIESLYKPIVVALNKVEKTG-RDDIEEKRAKLYQTC--KSV 307
Cdd:cd04163 76 AWSALK---DVDLVLFVVDASEWIGEGDEFI------LELLKKSKTPVILVLNKIDLVKdKEDLLPLLEKLKELHpfAEI 146
|
170 180
....*....|....*....|....*
gi 504370862 308 FPmfvglakVSAKKGLGIDEMVNVI 332
Cdd:cd04163 147 FP-------ISALKGENVDELLEYI 164
|
|
| GTP-bdg_M |
pfam16360 |
GTP-binding GTPase Middle Region; This family locates between the N-terminal domain and ... |
84-148 |
7.33e-12 |
|
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: 60.53 E-value: 7.33e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504370862 84 AGSKEAKLQISLARSGHMLP-LVREVLNNSKRGELPGFLAGGTYAIDKYYRQLRRQVAKTRRELEE 148
Cdd:pfam16360 2 ARTREAKLQVELAQLKYLLPrLRGMGTHLSRQGGGIGTRGPGETKLETDRRLIRRRIAKLKKELEK 67
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
168-336 |
9.67e-12 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 64.62 E-value: 9.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGsnkE----TSNKPFTT------IspkVSLSNLGFLVIDTVGF---------VMNvppeii 228
Cdd:COG1159 6 VAIVGRPNVGKSTLLNALVG---QkvsiVSPKPQTTrhrirgI---VTREDAQIVFVDTPGIhkpkrklgrRMN------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 229 EAFYSTLEeirEADVLLLLLDST-----EDLFLIeERVKQASvtlsnieslyKPIVVALNKVEKTGRDDIEEKRAKLYQT 303
Cdd:COG1159 74 KAAWSALE---DVDVILFVVDATekigeGDEFIL-ELLKKLK----------TPVILVINKIDLVKKEELLPLLAEYSEL 139
|
170 180 190
....*....|....*....|....*....|...
gi 504370862 304 CKsvfpmFVGLAKVSAKKGLGIDEMVNVIWKAL 336
Cdd:COG1159 140 LD-----FAEIVPISALKGDNVDELLDEIAKLL 167
|
|
| FeoB |
COG0370 |
Fe2+ transporter FeoB [Inorganic ion transport and metabolism]; |
168-339 |
3.88e-11 |
|
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
Pssm-ID: 440139 [Multi-domain] Cd Length: 662 Bit Score: 63.99 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKETSNKPFTTISPK---VSLSNLGFLVIDTvgfvmnvpPEIieafYS----TLEEI-- 238
Cdd:COG0370 6 IALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKegkFKLKGKEIELVDL--------PGT----YSlsaySPDEKva 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 239 ------READVLLLLLDSTedlflieervkqasvtlsNIE-SLY---------KPIVVALNKVektgrdDIEEKR----- 297
Cdd:COG0370 74 rdflleEKPDVVVNVVDAT------------------NLErNLYltlqllelgIPVVLALNMM------DEAEKKgikid 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504370862 298 -AKLYQT--CKsVFPmfvglakVSAKKGLGIDEMVNVIWKALNRK 339
Cdd:COG0370 130 vEKLSKLlgVP-VVP-------TSARKGKGIDELKEAIIEAAEGK 166
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
168-332 |
7.05e-11 |
|
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: 62.77 E-value: 7.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKE-TSNKPFTT---ISPKVSLSNLGFLVIDTVGfvMNVPPEIIEAfy--sTLEEIREA 241
Cdd:COG0486 216 VVIVGRPNVGKSSLLNALLGEERAiVTDIAGTTrdvIEERINIGGIPVRLIDTAG--LRETEDEVEKigierAREAIEEA 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 242 DVLLLLLDSTEDLFLIEERVkqasvtLSNIESlyKPIVVALNKVEKTGRDDIEEKRAKLYQTCksvfpmfvglaKVSAKK 321
Cdd:COG0486 294 DLVLLLLDASEPLTEEDEEI------LEKLKD--KPVIVVLNKIDLPSEADGELKSLPGEPVI-----------AISAKT 354
|
170
....*....|.
gi 504370862 322 GLGIDEMVNVI 332
Cdd:COG0486 355 GEGIDELKEAI 365
|
|
| obgE |
PRK12297 |
GTPase CgtA; Reviewed |
165-336 |
1.22e-10 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237046 [Multi-domain] Cd Length: 424 Bit Score: 62.04 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 165 LPLIA---IIGYANAGKTTLFNLLTGSNKETSNKPFTTISPkvslsNLGflVIDTVG---FVMNVPPEIIEA-------- 230
Cdd:PRK12297 155 LKLLAdvgLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVP-----NLG--VVETDDgrsFVMADIPGLIEGasegvglg 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 231 --FystLEEIREADVLLLLLDST--------EDLFLIEERVKQASVTLSNieslyKPIVVALNKVEKTGRDD-IEEKRAK 299
Cdd:PRK12297 228 hqF---LRHIERTRVIVHVIDMSgsegrdpiEDYEKINKELKLYNPRLLE-----RPQIVVANKMDLPEAEEnLEEFKEK 299
|
170 180 190
....*....|....*....|....*....|....*..
gi 504370862 300 LYQTcksVFPmfvglakVSAKKGLGIDEMVNVIWKAL 336
Cdd:PRK12297 300 LGPK---VFP-------ISALTGQGLDELLYAVAELL 326
|
|
| FeoB_N |
pfam02421 |
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ... |
168-332 |
2.39e-10 |
|
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: 58.23 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKETSNKPFTTISPKV---SLSNLGFLVIDTVGfvmnvppeiieaFYS----TLEEI-- 238
Cdd:pfam02421 3 IALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEgkfKYKGYEIEIVDLPG------------IYSlspySEEERva 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 239 ------READVLLLLLDST---EDLFLieervkqasvTLSNIEsLYKPIVVALNK---VEKTGRD-DIEEKRAKLyqTCK 305
Cdd:pfam02421 71 rdyllnEKPDVIVNVVDATnleRNLYL----------TLQLLE-LGLPVVLALNMmdeAEKKGIKiDIKKLSELL--GVP 137
|
170 180
....*....|....*....|....*..
gi 504370862 306 SVfpmfvglaKVSAKKGLGIDEMVNVI 332
Cdd:pfam02421 138 VV--------PTSARKGEGIDELLDAI 156
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
168-338 |
2.48e-10 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 58.84 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTG-----SNKETSNKP-FTTISPKVSLSNLGFLVIDTVGfvmnvppeiIEAFYST----LEE 237
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLVGdifslEKYLSTNGVtIDKKELKLDGLDVDLVIWDTPG---------QDEFRETrqfyARQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 238 IREADVLLLLLDSTedlflIEERVKQASVTLSNIESLYK--PIVVALNKVEKTGRDDIEEKrAKLYQTCKSVfpMFVGLA 315
Cdd:COG1100 77 LTGASLYLFVVDGT-----REETLQSLYELLESLRRLGKksPIILVLNKIDLYDEEEIEDE-ERLKEALSED--NIVEVV 148
|
170 180
....*....|....*....|...
gi 504370862 316 KVSAKKGLGIDEMVNVIWKALNR 338
Cdd:COG1100 149 ATSAKTGEGVEELFAALAEILRG 171
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
168-332 |
7.04e-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: 57.12 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKE-TSNKPFTT---ISPKVSLSNLGFLVIDTVGfvMNVPPEIIE------AFystlEE 237
Cdd:cd04164 6 VVIAGKPNVGKSSLLNALAGRDRAiVSDIAGTTrdvIEEEIDLGGIPVRLIDTAG--LRETEDEIEkigierAR----EA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 238 IREADVLLLLLDSTEDL----FLIEERVKQasvtlsnieslyKPIVVALNKVEKTGRDDIEEKRAKLYQTcksvfpmfvg 313
Cdd:cd04164 80 IEEADLVLLVVDASEGLdeedLEILELPAK------------KPVIVVLNKSDLLSDAEGISELNGKPII---------- 137
|
170
....*....|....*....
gi 504370862 314 laKVSAKKGLGIDEMVNVI 332
Cdd:cd04164 138 --AISAKTGEGIDELKEAL 154
|
|
| FeoB |
cd01879 |
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
169-332 |
1.06e-09 |
|
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: 56.70 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 169 AIIGYANAGKTTLFNLLTGSNKETSNKPFTTISPKV---SLSNLGFLVIDTVGfvmnvppeiieaFYS----TLEEI--- 238
Cdd:cd01879 1 ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEgefKLGGKEIEIVDLPG------------TYSltpySEDEKvar 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 239 -----READVLLLLLDSTedlflieervkqasvtlsNIE-SLY---------KPIVVALNKVEKTGRDDIEEKRAKLYQT 303
Cdd:cd01879 69 dfllgEEPDLIVNVVDAT------------------NLErNLYltlqllelgLPVVVALNMIDEAEKRGIKIDLDKLSEL 130
|
170 180 190
....*....|....*....|....*....|.
gi 504370862 304 --CKSVfpmfvglaKVSAKKGLGIDEMVNVI 332
Cdd:cd01879 131 lgVPVV--------PTSARKGEGIDELLDAI 153
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
168-332 |
1.07e-09 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 59.35 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKE-TSNKPFTT---ISPKVSLSNLGFLVIDTVGFVMnvPPEIIEAfy--sTLEEIREA 241
Cdd:PRK05291 218 VVIAGRPNVGKSSLLNALLGEERAiVTDIAGTTrdvIEEHINLDGIPLRLIDTAGIRE--TDDEVEKigierSREAIEEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 242 DVLLLLLDST-----EDLFLIEERVKqasvtlsnieslyKPIVVALNKVektgrdDIEEKRAKLYQTCKSVFpmfvglaK 316
Cdd:PRK05291 296 DLVLLVLDASeplteEDDEILEELKD-------------KPVIVVLNKA------DLTGEIDLEEENGKPVI-------R 349
|
170
....*....|....*.
gi 504370862 317 VSAKKGLGIDEMVNVI 332
Cdd:PRK05291 350 ISAKTGEGIDELREAI 365
|
|
| NOG |
cd01897 |
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ... |
166-327 |
4.32e-09 |
|
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: 54.87 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 166 PLIAIIGYANAGKTTLFNLLTGSNKETSNKPFTTISPKVSLSNLGFL---VIDTVGFV------MNvppeIIEAFYST-L 235
Cdd:cd01897 1 RTLVIAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLrwqVIDTPGILdrpleeRN----TIEMQAITaL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 236 EEIReaDVLLLLLDSTED-LFLIEERVKqasvTLSNIESLY-KPIVVALNKVEKTGRDDIEEKRAKLYqtcKSVFPMFvg 313
Cdd:cd01897 77 AHLR--AAVLFFIDPSETcGYSIEEQLS----LFKEIKPLFnKPVIVVLNKIDLLTEEDLSEIEKELE---KEGEEVI-- 145
|
170
....*....|....
gi 504370862 314 laKVSAKKGLGIDE 327
Cdd:cd01897 146 --KISTLTEEGVDE 157
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
163-336 |
3.92e-08 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 54.80 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 163 SGLPLIAIIGYANAGKTTLFNLLTGSNKETSNK-PFTTISPKVSLSNLG---FLVIDTVGFVMNVPPEIIEAFYSTLEE- 237
Cdd:PRK09518 448 SGLRRVALVGRPNVGKSSLLNQLTHEERAVVNDlAGTTRDPVDEIVEIDgedWLFIDTAGIKRRQHKLTGAEYYSSLRTq 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 238 --IREADVLLLLLDSTEDLFLIEERVkqasvtLSNIESLYKPIVVALNKVEKTGrddiEEKRAKLYQTCKSVFPMFVGLA 315
Cdd:PRK09518 528 aaIERSELALFLFDASQPISEQDLKV------MSMAVDAGRALVLVFNKWDLMD----EFRRQRLERLWKTEFDRVTWAR 597
|
170 180
....*....|....*....|...
gi 504370862 316 KV--SAKKGLGIDEMVNVIWKAL 336
Cdd:PRK09518 598 RVnlSAKTGWHTNRLAPAMQEAL 620
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
168-332 |
5.79e-08 |
|
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: 53.64 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKE-TSNKPFTT---ISPKVSLSNLGFLVIDTVGfvMNVPPEIIE------AfystLEE 237
Cdd:pfam12631 97 VVIVGKPNVGKSSLLNALLGEERAiVTDIPGTTrdvIEETINIGGIPLRLIDTAG--IRETDDEVEkigierA----REA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 238 IREADVLLLLLDST-----EDLFLIEERVKQasvtlsnieslyKPIVVALNKVEKTGRDDIEEKRAklyqtcksvfpmFV 312
Cdd:pfam12631 171 IEEADLVLLVLDASrpldeEDLEILELLKDK------------KPIIVVLNKSDLLGEIDELEELK------------GK 226
|
170 180
....*....|....*....|
gi 504370862 313 GLAKVSAKKGLGIDEMVNVI 332
Cdd:pfam12631 227 PVLAISAKTGEGLDELEEAI 246
|
|
| Ygr210 |
cd01899 |
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ... |
168-249 |
2.47e-07 |
|
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: 51.46 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKETSNKPFTTISPKVSlsnLGFLVID------------TVGFVMN----VPPEIIEA- 230
Cdd:cd01899 1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVG---VGYVRVEcpckelgvscnpRYGKCIDgkryVPVELIDVa 77
|
90 100 110
....*....|....*....|....*....|....
gi 504370862 231 ---------------FystLEEIREADVLLLLLD 249
Cdd:cd01899 78 glvpgahegkglgnqF---LDDLRDADVLIHVVD 108
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
168-332 |
3.33e-07 |
|
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: 49.99 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKETSNKPFT----------------TISPK-VSLSNLGFLV--IDTVG---FVMNvpp 225
Cdd:cd00881 2 VGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRketfldtlkeerergiTIKTGvVEFEWPKRRInfIDTPGhedFSKE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 226 eiieafysTLEEIREADVLLLLLDSTEDlflieerVKQASVTLSNIESLY-KPIVVALNKVEKTGRDDIEEKRAKLYQTC 304
Cdd:cd00881 79 --------TVRGLAQADGALLVVDANEG-------VEPQTREHLNIALAGgLPIIVAVNKIDRVGEEDFDEVLREIKELL 143
|
170 180 190
....*....|....*....|....*....|...
gi 504370862 305 KSVFPMFVGLAKV-----SAKKGLGIDEMVNVI 332
Cdd:cd00881 144 KLIGFTFLKGKDVpiipiSALTGEGIEELLDAI 176
|
|
| GTP-bdg_N |
pfam13167 |
GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. ... |
8-80 |
5.84e-07 |
|
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: 46.96 E-value: 5.84e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504370862 8 IGLDIQESVTIRKNS--GRYLISDYKLREIVEKKEKVKAEVILIEPELPPRDKINIIKATKADVIDRTLLLLEVF 80
Cdd:pfam13167 13 AGAEVVGTVIQKRDKpdPATYIGKGKLEELKELVEALEADLVIFDDELSPSQQRNLEKALGVKVIDRTGLILDIF 87
|
|
| PRK09602 |
PRK09602 |
translation-associated GTPase; Reviewed |
167-249 |
7.87e-07 |
|
translation-associated GTPase; Reviewed
Pssm-ID: 236584 [Multi-domain] Cd Length: 396 Bit Score: 50.19 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 167 LIAIIGYANAGKTTLFNLLTGSNKETSNKPFTTISPKVSLS-----------------NLGFlVIDTVGFvmnVPPEIIE 229
Cdd:PRK09602 3 TIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVAyvrvecpckelgvkcnpRNGK-CIDGTRF---IPVELID 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 504370862 230 ----------------AFystLEEIREADVLLLLLD 249
Cdd:PRK09602 79 vaglvpgahegrglgnQF---LDDLRQADALIHVVD 111
|
|
| feoB |
TIGR00437 |
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ... |
172-339 |
8.90e-07 |
|
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: 50.51 E-value: 8.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 172 GYANAGKTTLFNLLTGSNKETSNKPFTTISPKVSLSNLG---FLVIDTVG---FVMNVPPEIIEAFYSTLEeirEADVLL 245
Cdd:TIGR00437 1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQgedIEIVDLPGiysLTTFSLEEEVARDYLLNE---KPDLVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 246 LLLDSTEdlflIEervKQASVTLSNIEsLYKPIVVALNKVEKTGRDDIEEKRAKLYQTcksvfpMFVGLAKVSAKKGLGI 325
Cdd:TIGR00437 78 NVVDASN----LE---RNLYLTLQLLE-LGIPMILALNLVDEAEKKGIRIDEEKLEER------LGVPVVPTSATEGRGI 143
|
170
....*....|....
gi 504370862 326 DEMVNVIWKALNRK 339
Cdd:TIGR00437 144 ERLKDAIRKAIGLK 157
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
166-332 |
1.02e-06 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 48.24 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 166 PLIAIIGYANAGKTTLFNLLTGSN---KE----TSNKPFTTISpkVSLSNLGFLVIDTvgfvmnvPPEiiEAFystlEEI 238
Cdd:cd01887 1 PVVTVMGHVDHGKTTLLDKIRKTNvaaGEaggiTQHIGAYQVP--IDVKIPGITFIDT-------PGH--EAF----TNM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 239 RE-----ADVLLLLLDstedlflIEERVK-QASVTLSNIESLYKPIVVALNKVEKT-GRDDIEEK-RAKLYQTCKSVFPM 310
Cdd:cd01887 66 RArgasvTDIAILVVA-------ADDGVMpQTIEAINHAKAANVPIIVAINKIDKPyGTEADPERvKNELSELGLVGEEW 138
|
170 180
....*....|....*....|....
gi 504370862 311 --FVGLAKVSAKKGLGIDEMVNVI 332
Cdd:cd01887 139 ggDVSIVPISAKTGEGIDDLLEAI 162
|
|
| PTZ00258 |
PTZ00258 |
GTP-binding protein; Provisional |
168-205 |
5.32e-06 |
|
GTP-binding protein; Provisional
Pssm-ID: 240334 [Multi-domain] Cd Length: 390 Bit Score: 47.63 E-value: 5.32e-06
10 20 30
....*....|....*....|....*....|....*...
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKETSNKPFTTISPKVS 205
Cdd:PTZ00258 24 MGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTA 61
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
166-341 |
5.93e-06 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 47.45 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 166 PLIAIIGYANAGKTTLFNLLTGSNK-ETSN-KPfTTISPKV---SLSNLGFLVI-DTVGF--VMNVPPEIIEAfystLEE 237
Cdd:COG3596 40 PVIALVGKTGAGKSSLINALFGAEVaEVGVgRP-CTREIQRyrlESDGLPGLVLlDTPGLgeVNERDREYREL----REL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 238 IREADVLLLLLDSTEDLFLIEERVKQAsvtlsnIESLY--KPIVVALNKVEK----------------TGRDDIEEK--- 296
Cdd:COG3596 115 LPEADLILWVVKADDRALATDEEFLQA------LRAQYpdPPVLVVLTQVDRleperewdppynwpspPKEQNIRRAlea 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504370862 297 -RAKLYQTCKSVFPmfvglakVSAKK---GLGIDEMVNVIWKALNRKQA 341
Cdd:COG3596 189 iAEQLGVPIDRVIP-------VSAAEdrtGYGLEELVDALAEALPEAKR 230
|
|
| EngB |
COG0218 |
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ... |
164-336 |
7.67e-06 |
|
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 439988 [Multi-domain] Cd Length: 194 Bit Score: 45.83 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 164 GLPLIAIIGYANAGKTTLFNLLTGSNK--ETSNKP-FT-TIspkvslsNLgFLVIDTVGFV-------MNVPPEIIEAFY 232
Cdd:COG0218 22 DLPEIAFAGRSNVGKSSLINALTNRKKlaRTSKTPgKTqLI-------NF-FLINDKFYLVdlpgygyAKVSKAEKEKWQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 233 STLEE-IREADVL---LLLLDS----TE-DLFLIEErvkqasvtlsnIESLYKPIVVALNKVEKTGRddieEKRAKLYQT 303
Cdd:COG0218 94 KLIEDyLEGRENLkgvVLLIDIrhppKElDLEMLEW-----------LDEAGIPFLIVLTKADKLKK----SELAKQLKA 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 504370862 304 CKSVFPMFVGLAKV---SAKKGLGIDEMVNVIWKAL 336
Cdd:COG0218 159 IKKALGKDPAAPEVilfSSLKKEGIDELRAAIEEWL 194
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
168-332 |
8.21e-06 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 45.18 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKETSNKPFTTISPKvslsnlgflVIDTvgfvmnvPPEIIE--AFYSTLeeI---READ 242
Cdd:COG4917 4 IMLIGRSGAGKTTLTQALNGEELEYRKTQAVEYYDN---------IIDT-------PGEYIEnpRFYKAL--IataQDAD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 243 VLLLLLDSTEDlflieervkqasvtlsniESLYKPIVV-ALNK-----VEKTGRDDIEEKRAK--LYQT-CKSVFPmfvg 313
Cdd:COG4917 66 VIVLVQDATEP------------------RSVFPPGFAkAFNKpvigvITKIDLPEADVERARkwLKSAgVEPIFI---- 123
|
170
....*....|....*....
gi 504370862 314 lakVSAKKGLGIDEMVNVI 332
Cdd:COG4917 124 ---VSSVTGEGIEELKEYL 139
|
|
| Arf_Arl |
cd00878 |
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
168-327 |
2.24e-05 |
|
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.
Pssm-ID: 206644 [Multi-domain] Cd Length: 158 Bit Score: 44.10 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLtgsnketSNKPFTTISP-------KVSLSNLGFLVIDTVGfvmnvpPEIIEAFYSTLEEirE 240
Cdd:cd00878 2 ILMLGLDGAGKTTILYKL-------KLGEVVTTIPtigfnveTVEYKNVKFTVWDVGG------QDKIRPLWKHYYE--N 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 241 ADVLLLLLDSTEdlfliEERVKQASVTLSNI----ESLYKPIVVALNKVEKTGRDDIEE--KRAKLYQTCKSVFPMFvgl 314
Cdd:cd00878 67 TDGLIFVVDSSD-----RERIEEAKNELHKLlneeELKGAPLLILANKQDLPGALTESEliELLGLESIKGRRWHIQ--- 138
|
170
....*....|...
gi 504370862 315 aKVSAKKGLGIDE 327
Cdd:cd00878 139 -PCSAVTGDGLDE 150
|
|
| DRG |
cd01896 |
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ... |
168-342 |
8.82e-05 |
|
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: 43.30 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKETSNKPFTTispkvslsnlgflvIDTVGFVMNVP---------PEIIEAFYST---- 234
Cdd:cd01896 3 VALVGFPSVGKSTLLSKLTNTKSEVAAYEFTT--------------LTCVPGVMEYKgakiqlldlPGIIEGASDGkgrg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 235 ---LEEIREADVLLLLLDSTEDLF----------------------------------------------------LIEE 259
Cdd:cd01896 69 rqvIAVARTADLILIVLDATKPEGqreilerelegvgirlnkkppnvtikkkkkgginitstvpltkldektvkaiLREY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 260 RVKQASVTL---SNIESL---------YKPIVVALNKVEKTGRDDIEekraKLYQTCKSVFpmfvglakVSAKKGLGIDE 327
Cdd:cd01896 149 KIHNADVLIredITVDDLidviegnrvYIPCLYVYNKIDLISIEELD----RLARIPNSVV--------ISAEKDLNLDE 216
|
250
....*....|....*
gi 504370862 328 MVNVIWKALNRKQAY 342
Cdd:cd01896 217 LLERIWDYLGLIRIY 231
|
|
| feoB |
PRK09554 |
Fe(2+) transporter permease subunit FeoB; |
168-332 |
1.35e-04 |
|
Fe(2+) transporter permease subunit FeoB;
Pssm-ID: 236563 [Multi-domain] Cd Length: 772 Bit Score: 43.55 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKETSN----------KPFTTISPKVSLSNL-GFLVIDTvgfvmnvppeiIEAFYSTLE 236
Cdd:PRK09554 6 IGLIGNPNSGKTTLFNQLTGARQRVGNwagvtverkeGQFSTTDHQVTLVDLpGTYSLTT-----------ISSQTSLDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 237 EIR-------EADVLLLLLDST---EDLFLieervkqasvTLSNIEsLYKPIVVALNKVE----KTGRDDIEEKRAKLyq 302
Cdd:PRK09554 75 QIAchyilsgDADLLINVVDASnleRNLYL----------TLQLLE-LGIPCIVALNMLDiaekQNIRIDIDALSARL-- 141
|
170 180 190
....*....|....*....|....*....|
gi 504370862 303 TCkSVFPMfvglakVSAkKGLGIDEMVNVI 332
Cdd:PRK09554 142 GC-PVIPL------VST-RGRGIEALKLAI 163
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
162-284 |
1.50e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 43.42 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 162 VSGLPLIAIIGYANAGKTTLFNLLTGSNKE-TSNKPFTTISPKVSLSNLG---FLVIDTVGFVMNVPPEIIEAFYSTLEE 237
Cdd:PRK03003 208 SGGPRRVALVGKPNVGKSSLLNKLAGEERSvVDDVAGTTVDPVDSLIELGgktWRFVDTAGLRRRVKQASGHEYYASLRT 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 504370862 238 ---IREADVLLLLLDSTEDLFLIEERVkqasvtLSNIESLYKPIVVALNK 284
Cdd:PRK03003 288 haaIEAAEVAVVLIDASEPISEQDQRV------LSMVIEAGRALVLAFNK 331
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
168-332 |
3.19e-04 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 40.97 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLF-NLLTGSNKE-------------------------TSNKPFTTISPKvslsNLGFLVIDTVG--- 218
Cdd:pfam00009 6 IGIIGHVDHGKTTLTdRLLYYTGAIskrgevkgegeagldnlpeerergiTIKSAAVSFETK----DYLINLIDTPGhvd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 219 FVMNVppeiieafYSTLeeiREADVLLLLLDSTEDLFL-IEERVKQASvtlsnieSLYKPIVVALNKVEKTGRDDIEEKR 297
Cdd:pfam00009 82 FVKEV--------IRGL---AQADGAILVVDAVEGVMPqTREHLRLAR-------QLGVPIIVFINKMDRVDGAELEEVV 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 504370862 298 AKLYQTCKSVFPM---FVGLAKVSAKKGLGIDEMVNVI 332
Cdd:pfam00009 144 EEVSRELLEKYGEdgeFVPVVPGSALKGEGVQTLLDAL 181
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
168-332 |
5.01e-04 |
|
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: 40.05 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGsNK--ETSNKPFTT---ISPKVSLSNLGFLV--IDTVGfVMNVPPEIIEAFYSTLEEIRE 240
Cdd:TIGR00231 4 IVIVGHPNVGKSTLLNSLLG-NKgsITEYYPGTTrnyVTTVIEEDGKTYKFnlLDTAG-QEDYDAIRRLYYPQVERSLRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 241 ADVLLLLLDS----TEDLFLIeERVKQASVtlsnieslykPIVVALNKVEKTGRDDIEE---KRAKLYQtcKSVFPmfvg 313
Cdd:TIGR00231 82 FDIVILVLDVeeilEKQTKEI-IHHADSGV----------PIILVGNKIDLKDADLKTHvasEFAKLNG--EPIIP---- 144
|
170
....*....|....*....
gi 504370862 314 lakVSAKKGLGIDEMVNVI 332
Cdd:TIGR00231 145 ---LSAETGKNIDSAFKIV 160
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
166-332 |
5.28e-04 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 41.74 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 166 PLIAIIGYANAGKTTLFNLLTGSNkeTSNKPFTTISPKVSL---------SNLGFLVIDTVGFvmnvppeiiEAFYST-L 235
Cdd:CHL00189 245 PIVTILGHVDHGKTTLLDKIRKTQ--IAQKEAGGITQKIGAyevefeykdENQKIVFLDTPGH---------EAFSSMrS 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 236 EEIREADVLLLLLdstedlfLIEERVKQASV-TLSNIESLYKPIVVALNKVEKTGrDDIEEKRAKLYQtcKSVFPMFVG- 313
Cdd:CHL00189 314 RGANVTDIAILII-------AADDGVKPQTIeAINYIQAANVPIIVAINKIDKAN-ANTERIKQQLAK--YNLIPEKWGg 383
|
170 180
....*....|....*....|..
gi 504370862 314 ---LAKVSAKKGLGIDEMVNVI 332
Cdd:CHL00189 384 dtpMIPISASQGTNIDKLLETI 405
|
|
| MMR_HSR1_Xtn |
pfam16897 |
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ... |
275-337 |
2.61e-03 |
|
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: 37.02 E-value: 2.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504370862 275 YKPIVVALNKVektgrDDI-EEKRAKLYQTCKSVFpmfvglakVSAKKGLGIDEMVNVIWKALN 337
Cdd:pfam16897 54 YIPCLYVYNKI-----DLIsIEELDRLAREPDSVP--------ISAEKGLNLDELKERIWEYLG 104
|
|
| Rab7 |
cd01862 |
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ... |
230-341 |
3.67e-03 |
|
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates vesicular traffic from early to late endosomal stages of the endocytic pathway. The yeast Ypt7 and mammalian Rab7 are both involved in transport to the vacuole/lysosome, whereas Ypt7 is also required for homotypic vacuole fusion. Mammalian Rab7 is an essential participant in the autophagic pathway for sequestration and targeting of cytoplasmic components to the lytic compartment. Mammalian Rab7 is also proposed to function as a tumor suppressor. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
Pssm-ID: 206655 [Multi-domain] Cd Length: 172 Bit Score: 37.64 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 230 AFYstleeiREADVLLLL-----------LDSTEDLFLIeervkQASVtlSNIESLykPIVVALNKVEKTGRDDIEEKRA 298
Cdd:cd01862 68 AFY------RGADCCVLVydvtnpksfesLDSWRDEFLI-----QASP--RDPENF--PFVVLGNKIDLEEKRQVSTKKA 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 504370862 299 KlyQTCKSVF--PMFvglaKVSAKKGLGIDEMVNVIWK-ALNRKQA 341
Cdd:cd01862 133 Q--QWCKSKGniPYF----ETSAKEAINVDQAFETIARlALEQEKE 172
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
168-286 |
4.04e-03 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 39.01 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 168 IAIIGYANAGKTTLFNLLTGSNKE-TSNKPFTT---ISPKVSLSNLGFLVIDTVGFVMNVppEIIEAFYSTLEEI--REA 241
Cdd:PRK09518 278 VAIVGRPNVGKSTLVNRILGRREAvVEDTPGVTrdrVSYDAEWAGTDFKLVDTGGWEADV--EGIDSAIASQAQIavSLA 355
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 504370862 242 DVLLLLLDSTEDLFLIEERVkqasvtLSNIESLYKPIVVALNKVE 286
Cdd:PRK09518 356 DAVVFVVDGQVGLTSTDERI------VRMLRRAGKPVVLAVNKID 394
|
|
| PRK04213 |
PRK04213 |
GTP-binding protein EngB; |
166-230 |
4.23e-03 |
|
GTP-binding protein EngB;
Pssm-ID: 179790 [Multi-domain] Cd Length: 201 Bit Score: 37.97 E-value: 4.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504370862 166 PLIAIIGYANAGKTTLFNLLTGSNKETSNKPFTTISP-KVSLSNlgFLVIDT--VGFVMNVPPEIIEA 230
Cdd:PRK04213 10 PEIVFVGRSNVGKSTLVRELTGKKVRVGKRPGVTRKPnHYDWGD--FILTDLpgFGFMSGVPKEVQEK 75
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
167-187 |
9.19e-03 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 37.33 E-value: 9.19e-03
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
170-338 |
9.74e-03 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 36.43 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 170 IIGYA---NAGKTTLFNLLTGSN----KETSNKPFTTispkvslsNLGFLVID-----TVGFVmNVPPEiiEAFYST-LE 236
Cdd:cd04171 1 IIGTAghiDHGKTTLIKALTGIEtdrlPEEKKRGITI--------DLGFAYLDlpdgkRLGFI-DVPGH--EKFVKNmLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504370862 237 EIREADVLLLLLDstedlflIEERVK-QASVTLSNIESL-YKPIVVALNKVEKTGRDDIEEKRAKLYQTCKSVFPMFVGL 314
Cdd:cd04171 70 GAGGIDAVLLVVA-------ADEGIMpQTREHLEILELLgIKKGLVVLTKADLVDEDRLELVEEEILELLAGTFLADAPI 142
|
170 180
....*....|....*....|....
gi 504370862 315 AKVSAKKGLGIDEMVNVIWKALNR 338
Cdd:cd04171 143 FPVSSVTGEGIEELKNYLDELAEP 166
|
|
| |
