|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
3-464 |
0e+00 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 923.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 3 INEKDKLAEQNLETLDVTKLTPLSEDVISRQATINLGTIGHVAHGKSTLVHAISGVHTVRFKHEKERNITIKLGYANAKI 82
Cdd:PTZ00327 2 IDTDDGLAKQDLSKLDLDKLTPLTPEVISRQATINIGTIGHVAHGKSTVVKALSGVKTVRFKREKVRNITIKLGYANAKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 83 YKCtnPDCLPPECYKSYESSKEDNPICPrkDCNHEMKLLRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNESCPQP 162
Cdd:PTZ00327 82 YKC--PKCPRPTCYQSYGSSKPDNPPCP--GCGHKMTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 163 QTSEHLAAVEIMRLKHILILQNKVELIKEEQALKQQEEIRNFVSGTAADSAPIIPISAVLKYNIDVVCEYIVTQISIPKR 242
Cdd:PTZ00327 158 QTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 243 DFISSPHMIVIRSFDVNKPGEDIETLQGGVAGGSILHGVLKVGDKIEIRPGIISKDDKGEITCRPIISQILSMFAENNNL 322
Cdd:PTZ00327 238 DLTSPPRMIVIRSFDVNKPGEDIENLKGGVAGGSILQGVLKVGDEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 323 KYAVPGGLIGVGTKIDPILTRADRLVGQVIGHLNKLPDCFAEIEISYYLLRRLLGVKSQDGEKNTKVAKLKNGEFLMINI 402
Cdd:PTZ00327 318 QYAVPGGLIGVGTTIDPTLTRADRLVGQVLGYPGKLPEVYAEIEIQYYLLRRLLGVKSQDGKKATKVAKLKKGESLMINI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124808285 403 GSTSIGCRVTGIKTE-LAKLELTGPVCTKIGDKIALSRRVDKHWRLIGWGQINKGKPLELQEP 464
Cdd:PTZ00327 398 GSTTTGGRVVGIKDDgIAKLELTTPVCTSVGEKIALSRRVDKHWRLIGWGTIRKGVPVKLLNS 460
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
32-453 |
0e+00 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 522.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 32 RQATINLGTIGHVAHGKSTLVHAISGVHTVRFKHEKERNITIKLGYANAKIYKCtnPDCLPPECYKSyesskedNPICPr 111
Cdd:PRK04000 6 VQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATIRKC--PDCEEPEAYTT-------EPKCP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 112 kDCNHEMKLLRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNESCPQPQTSEHLAAVEIMRLKHILILQNKVELIKE 191
Cdd:PRK04000 76 -NCGSETELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 192 EQALKQQEEIRNFVSGTAADSAPIIPISAVLKYNIDVVCEYIVTQISIPKRDFISSPHMIVIRSFDVNKPGEDIETLQGG 271
Cdd:PRK04000 155 ERALENYEQIKEFVKGTVAENAPIIPVSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTPPEKLKGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 272 VAGGSILHGVLKVGDKIEIRPGIISKdDKGEITCRPIISQILSMFAENNNLKYAVPGGLIGVGTKIDPILTRADRLVGQV 351
Cdd:PRK04000 235 VIGGSLIQGVLKVGDEIEIRPGIKVE-EGGKTKWEPITTKIVSLRAGGEKVEEARPGGLVGVGTKLDPSLTKADALAGSV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 352 IGHLNKLPDCFAEIEISYYLLRRLLGVKSqdgekNTKVAKLKNGEFLMINIGS-TSIGCrVTGIKTELAKLELTGPVCTK 430
Cdd:PRK04000 314 AGKPGTLPPVWESLTIEVHLLERVVGTKE-----ELKVEPIKTGEPLMLNVGTaTTVGV-VTSARKDEAEVKLKRPVCAE 387
|
410 420
....*....|....*....|...
gi 124808285 431 IGDKIALSRRVDKHWRLIGWGQI 453
Cdd:PRK04000 388 EGDRVAISRRVGGRWRLIGYGII 410
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
32-453 |
2.32e-178 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 505.14 E-value: 2.32e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 32 RQATINLGTIGHVAHGKSTLVHAISGVHTVRFKHEKERNITIKLGYANAKIYKCtnPDCLPPECYKSyesskedNPICPr 111
Cdd:COG5257 2 KQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATFYKC--PNCEPPEAYTT-------EPKCP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 112 kDCNHEMKLLRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNESCPQPQTSEHLAAVEIMRLKHILILQNKVELIKE 191
Cdd:COG5257 72 -NCGSETELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 192 EQALKQQEEIRNFVSGTAADSAPIIPISAVLKYNIDVVCEYIVTQISIPKRDFISSPHMIVIRSFDVNKPGEDIETLQGG 271
Cdd:COG5257 151 ERALENYEQIKEFVKGTVAENAPIIPVSAQHKVNIDALIEAIEEEIPTPERDLSKPPRMLVARSFDVNKPGTPPKDLKGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 272 VAGGSILHGVLKVGDKIEIRPGiISKDDKGEITCRPIISQILSMFAENNNLKYAVPGGLIGVGTKIDPILTRADRLVGQV 351
Cdd:COG5257 231 VIGGSLIQGVLKVGDEIEIRPG-IKVEKGGKTKYEPITTTVVSLRAGGEEVEEAKPGGLVAVGTKLDPSLTKSDSLVGSV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 352 IGHLNKLPDCFAEIEISYYLLRRLLGVKSqdgekNTKVAKLKNGEFLMINIGS-TSIGCrVTGIKTELAKLELTGPVCTK 430
Cdd:COG5257 310 AGKPGTLPPVLDSLTMEVHLLERVVGTKE-----EVKVEPIKTGEPLMLNVGTaTTVGV-VTSARKDEIEVKLKRPVCAE 383
|
410 420
....*....|....*....|...
gi 124808285 431 IGDKIALSRRVDKHWRLIGWGQI 453
Cdd:COG5257 384 KGSRVAISRRIGGRWRLIGWGII 406
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
32-453 |
2.60e-173 |
|
translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Pssm-ID: 274720 [Multi-domain] Cd Length: 406 Bit Score: 492.26 E-value: 2.60e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 32 RQATINLGTIGHVAHGKSTLVHAISGVHTVRFKHEKERNITIKLGYANAKIYKCtnPDCLPPECYKSyesskedNPICPR 111
Cdd:TIGR03680 1 RQPEVNIGMVGHVDHGKTTLTKALTGVWTDTHSEELKRGISIRLGYADAEIYKC--PECDGPECYTT-------EPVCPN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 112 kdCNHEMKLLRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNESCPQPQTSEHLAAVEIMRLKHILILQNKVELIKE 191
Cdd:TIGR03680 72 --CGSETELLRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPCPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 192 EQALKQQEEIRNFVSGTAADSAPIIPISAVLKYNIDVVCEYIVTQISIPKRDFISSPHMIVIRSFDVNKPGEDIETLQGG 271
Cdd:TIGR03680 150 EKALENYEEIKEFVKGTVAENAPIIPVSALHNANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNKPGTPPEKLKGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 272 VAGGSILHGVLKVGDKIEIRPGiISKDDKGEITCRPIISQILSMFAENNNLKYAVPGGLIGVGTKIDPILTRADRLVGQV 351
Cdd:TIGR03680 230 VIGGSLIQGKLKVGDEIEIRPG-IKVEKGGKTKWEPIYTEITSLRAGGYKVEEARPGGLVGVGTKLDPALTKADALAGQV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 352 IGHLNKLPDCFAEIEISYYLLRRLLGVKSQdgeknTKVAKLKNGEFLMINIGS-TSIGCrVTGIKTELAKLELTGPVCTK 430
Cdd:TIGR03680 309 VGKPGTLPPVWESLELEVHLLERVVGTEEE-----LKVEPIKTGEVLMLNVGTaTTVGV-VTSARKDEIEVKLKRPVCAE 382
|
410 420
....*....|....*....|...
gi 124808285 431 IGDKIALSRRVDKHWRLIGWGQI 453
Cdd:TIGR03680 383 EGDRVAISRRVGGRWRLIGYGII 405
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
36-242 |
1.60e-126 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 365.44 E-value: 1.60e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLVHAISGVHTVRFKHEKERNITIKLGYANAKIYKCTNPDClpPECYKSYEsskednPICPRkdCN 115
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWTVRHKEELKRNITIKLGYANAKIYKCPNCGC--PRPYDTPE------CECPG--CG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 116 HEMKLLRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNESCPQPQTSEHLAAVEIMRLKHILILQNKVELIKEEQAL 195
Cdd:cd01888 71 GETKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 124808285 196 KQQEEIRNFVSGTAADSAPIIPISAVLKYNIDVVCEYIVTQISIPKR 242
Cdd:cd01888 151 ENYEQIKEFVKGTIAENAPIIPISAQLKYNIDVLCEYIVKKIPTPPR 197
|
|
| eIF2_gamma_II |
cd03688 |
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily ... |
243-354 |
2.09e-60 |
|
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily represents domain II of the gamma subunit of eukaryotic translation initiation factor 2 (eIF2-gamma) found in eukaryota and archaea. eIF2 is a G protein that delivers the methionyl initiator tRNA to the small ribosomal subunit and releases it upon GTP hydrolysis after the recognition of the initiation codon. eIF2 is composed of three subunits, alpha, beta and gamma. Subunit gamma shows strongest conservation, and it confers both tRNA binding and GTP/GDP binding.
Pssm-ID: 293889 [Multi-domain] Cd Length: 113 Bit Score: 192.78 E-value: 2.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 243 DFISSPHMIVIRSFDVNKPGEDIETLQGGVAGGSILHGVLKVGDKIEIRPGIISKDDkGEITCRPIISQILSMFAENNNL 322
Cdd:cd03688 1 DLDKPPRMIVIRSFDVNKPGTEVDDLKGGVIGGSLIQGVLKVGDEIEIRPGIVVKKG-GKTTCRPIFTKIVSLFAEGNDL 79
|
90 100 110
....*....|....*....|....*....|..
gi 124808285 323 KYAVPGGLIGVGTKIDPILTRADRLVGQVIGH 354
Cdd:cd03688 80 EEAVPGGLIGVGTKLDPTLTKADRLVGQVVGE 111
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
36-453 |
6.91e-49 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 177.03 E-value: 6.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLVHAISGVHTVRFKHEKERNITIKLGYANAKiykctnpdcLPPEcyksyesskednpicprkdcn 115
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGIDTDRLKEEKKRGITIDLGFAYLP---------LPDG--------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 116 hemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKHILILQNKVELIKEEQAL 195
Cdd:COG3276 51 ------RRLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAADEG-VMPQTREHLAILDLLGIKRGIVVLTKADLVDEEWLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 196 KQQEEIRNFVSGTAADSAPIIPISAVLKYNIDVVCEYIVTQI-SIPKRDFISSPHMIVIRSFdvnkpgedieTLQG-G-V 272
Cdd:COG3276 124 LVEEEIRELLAGTFLEDAPIVPVSAVTGEGIDELRAALDALAaAVPARDADGPFRLPIDRVF----------SIKGfGtV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 273 AGGSILHGVLKVGDKIEIRPgiiskddkGEITCRpiisqILSMFAENNNLKYAVPG-----GLIGVGTKidpILTRadrl 347
Cdd:COG3276 194 VTGTLLSGTVRVGDELELLP--------SGKPVR-----VRGIQVHGQPVEEAYAGqrvalNLAGVEKE---EIER---- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 348 vGQVIGHlnklPDCFAEieiSYYLLRRLLGVKSQDgekntkvAKLKNGEFLMINIGSTSIGCRVTGIKTE--------LA 419
Cdd:COG3276 254 -GDVLAA----PGALRP---TDRIDVRLRLLPSAP-------RPLKHWQRVHLHHGTAEVLARVVLLDREelapgeeaLA 318
|
410 420 430
....*....|....*....|....*....|....
gi 124808285 420 KLELTGPVCTKIGDKIALsRRVDKHwRLIGWGQI 453
Cdd:COG3276 319 QLRLEEPLVAARGDRFIL-RDYSPR-RTIGGGRV 350
|
|
| eIF2_gamma_III |
cd15490 |
Domain III of eukaryotic initiation factor eIF2 gamma; This family represents the C-terminal ... |
359-453 |
1.86e-43 |
|
Domain III of eukaryotic initiation factor eIF2 gamma; This family represents the C-terminal domain of the gamma subunit of eukaryotic translation initiation factor 2 (eIF2-gamma) found in eukaryotes and archaea. eIF2 is a G protein that delivers the methionyl initiator tRNA to the small ribosomal subunit and releases it upon GTP hydrolysis after the recognition of the initiation codon. eIF2 is composed three subunits, alpha, beta and gamma. Subunit gamma shows strongest conservation, and it confers both tRNA binding and GTP/GDP binding.
Pssm-ID: 294011 [Multi-domain] Cd Length: 90 Bit Score: 147.66 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 359 PDCFAEIEISYYLLRRLLGVKSQdgeknTKVAKLKNGEFLMINIGSTSIGCRVTGIKTELAKLELTGPVCTKIGDKIALS 438
Cdd:cd15490 1 PPVYTELEIEYHLLERVVGVKEE-----IKVEKIKKGEVLMLNIGSATTGGVVTSVKKDEAEVELKRPVCAEIGERVAIS 75
|
90
....*....|....*
gi 124808285 439 RRVDKHWRLIGWGQI 453
Cdd:cd15490 76 RRIDGRWRLIGWGII 90
|
|
| eIF2_C |
pfam09173 |
Initiation factor eIF2 gamma, C terminal; Members of this family, which are found in the ... |
364-453 |
1.40e-39 |
|
Initiation factor eIF2 gamma, C terminal; Members of this family, which are found in the initiation factors eIF2 and EF-Tu, adopt a structure consisting of a beta barrel with Greek key topology. They are required for formation of the ternary complex with GTP and initiator tRNA.
Pssm-ID: 462703 [Multi-domain] Cd Length: 86 Bit Score: 137.25 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 364 EIEISYYLLRRLLGVKSQdgeknTKVAKLKNGEFLMINIGSTSIGCRVTGIKTELAKLELTGPVCTKIGDKIALSRRVDK 443
Cdd:pfam09173 2 ELEIEYHLLERVVGVKEE-----KKVEPIKKGEVLMLNVGTATTGGVVTSVKKDEAEVELKKPVCAEKGERVAISRRIGG 76
|
90
....*....|
gi 124808285 444 HWRLIGWGQI 453
Cdd:pfam09173 77 RWRLIGWGII 86
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
38-233 |
3.43e-38 |
|
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: 136.58 E-value: 3.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 38 LGTIGHVAHGKSTLVHAISGVHTVRFKHEKERNITIKLGYANAKiykctnpdcLPPEcyksyesskednpicprkdcnhe 117
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGIETDRLPEEKKRGITIDLGFAYLD---------LPDG----------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 118 mkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNESCpQPQTSEHLAAVEIMRLKHILILQNKVELIKEEQALKQ 197
Cdd:cd04171 50 ----KRLGFIDVPGHEKFVKNMLAGAGGIDAVLLVVAADEGI-MPQTREHLEILELLGIKKGLVVLTKADLVDEDRLELV 124
|
170 180 190
....*....|....*....|....*....|....*.
gi 124808285 198 QEEIRNFVSGTAADSAPIIPISAVLKYNIDVVCEYI 233
Cdd:cd04171 125 EEEILELLAGTFLADAPIFPVSSVTGEGIEELKNYL 160
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
36-290 |
4.83e-28 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 115.04 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLVHAISGV----HTVRFK---------HEKERNITIKLGYAnakiykctnpdclppecykSYESS 102
Cdd:PRK12736 13 VNIGTIGHVDHGKTTLTAAITKVlaerGLNQAKdydsidaapEEKERGITINTAHV-------------------EYETE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 103 KednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKHILIL 182
Cdd:PRK12736 74 K------------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVPYLVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 183 QNKVELIKEEQALKQQE-EIRNFVS--GTAADSAPIIPISAVLKYN------------IDVVCEYIVTqisiPKRDfISS 247
Cdd:PRK12736 135 LNKVDLVDDEELLELVEmEVRELLSeyDFPGDDIPVIRGSALKALEgdpkwedaimelMDAVDEYIPT----PERD-TDK 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 124808285 248 PHMIvirsfdvnkPGEDIETL--QGGVAGGSILHGVLKVGDKIEI 290
Cdd:PRK12736 210 PFLM---------PVEDVFTItgRGTVVTGRVERGTVKVGDEVEI 245
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
36-290 |
1.18e-27 |
|
translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]
Pssm-ID: 129576 [Multi-domain] Cd Length: 394 Bit Score: 113.72 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLVHAISGVHTVRFK-------------HEKERNITIKLGYAnakiykctnpdclppecykSYESS 102
Cdd:TIGR00485 13 VNVGTIGHVDHGKTTLTAAITTVLAKEGGaaaraydqidnapEEKARGITINTAHV-------------------EYETE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 103 KednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKHILIL 182
Cdd:TIGR00485 74 T------------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 183 QNKVELIKEEQALKQQE-EIRNFVS--GTAADSAPIIPISAVLKYNIDVVCEYIVTQISIPKRDFISSPHMIVIRSFDVn 259
Cdd:TIGR00485 135 LNKCDMVDDEELLELVEmEVRELLSqyDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLL- 213
|
250 260 270
....*....|....*....|....*....|...
gi 124808285 260 kPGEDIETLQ--GGVAGGSILHGVLKVGDKIEI 290
Cdd:TIGR00485 214 -PIEDVFSITgrGTVVTGRVERGIIKVGEEVEI 245
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
37-240 |
4.21e-27 |
|
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: 107.00 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 37 NLGTIGHVAHGKSTLV-------HAISGVHTVRF------KHEKERNITIKLGYANAKIYKctnpdclppecyksyessk 103
Cdd:cd00881 1 NVGVIGHVDHGKTTLTgsllyqtGAIDRRGTRKEtfldtlKEERERGITIKTGVVEFEWPK------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 104 ednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKhILILQ 183
Cdd:cd00881 62 ------------------RRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEG-VEPQTREHLNIALAGGLP-IIVAV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124808285 184 NKVELIKEEQALKQQEEIRNFVSGTAADS-----APIIPISAVLKYNIDVVCEYIVTQISIP 240
Cdd:cd00881 122 NKIDRVGEEDFDEVLREIKELLKLIGFTFlkgkdVPIIPISALTGEGIEELLDAIVEHLPPP 183
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
36-333 |
1.17e-26 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 113.04 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLVHAISGVHTVRFKHEKERNITIKLGYANakiykCTNPDclppecyksyesskednpicprkdcn 115
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAADRLPEEKKRGMTIDLGFAY-----FPLPD-------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 116 hemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKHILILQNKVELIKEEQAL 195
Cdd:TIGR00475 50 ------YRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDADEG-VMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 196 KQQEEIRNFVSGTA-ADSAPIIPISAVLKYNIDVVCEYIVTQISIPKRDFISSPHMIVI-RSFDVNKPGEdietlqggVA 273
Cdd:TIGR00475 123 RTEMFMKQILNSYIfLKNAKIFKTSAKTGQGIGELKKELKNLLESLDIKRIQKPLRMAIdRAFKVKGAGT--------VV 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 274 GGSILHGVLKVGDKIEIRPgiISKddkgeitcrpiISQILSMFAENNNLKYAVPGGLIGV 333
Cdd:TIGR00475 195 TGTAFSGEVKVGDNLRLLP--INH-----------EVRVKAIQAQNQDVEIAYAGQRIAL 241
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
36-290 |
1.79e-26 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 110.28 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLVHAISGVHTVRFK-------------HEKERNITIklgyANAKIykctnpdclppecykSYESS 102
Cdd:PRK00049 13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGaeakaydqidkapEEKARGITI----NTAHV---------------EYETE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 103 KednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKHILIL 182
Cdd:PRK00049 74 K------------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 183 QNKVELIKEEQALKQQE-EIRNFVS--GTAADSAPIIPISAVLKYN--------------IDVVCEYIVTqisiPKRDfI 245
Cdd:PRK00049 135 LNKCDMVDDEELLELVEmEVRELLSkyDFPGDDTPIIRGSALKALEgdddeewekkilelMDAVDSYIPT----PERA-I 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 124808285 246 SSPHMIvirsfdvnkPGEDIETLQG--GVAGGSILHGVLKVGDKIEI 290
Cdd:PRK00049 210 DKPFLM---------PIEDVFSISGrgTVVTGRVERGIIKVGEEVEI 247
|
|
| tufA |
CHL00071 |
elongation factor Tu |
36-290 |
4.41e-26 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 109.66 E-value: 4.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLVHAISGVHTVRFK-------------HEKERNITIKLGYAnakiykctnpdclppecykSYESS 102
Cdd:CHL00071 13 VNIGTIGHVDHGKTTLTAAITMTLAAKGGakakkydeidsapEEKARGITINTAHV-------------------EYETE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 103 KednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKHILIL 182
Cdd:CHL00071 74 N------------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTKEHILLAKQVGVPNIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 183 QNKVELIKEEQALK-QQEEIRNFVS--GTAADSAPIIPISAVLK---------------------YN-IDVVCEYIVTqi 237
Cdd:CHL00071 135 LNKEDQVDDEELLElVELEVRELLSkyDFPGDDIPIVSGSALLAlealtenpkikrgenkwvdkiYNlMDAVDSYIPT-- 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 124808285 238 siPKRDfISSPHMIVIrsfdvnkpgEDIE--TLQGGVAGGSILHGVLKVGDKIEI 290
Cdd:CHL00071 213 --PERD-TDKPFLMAI---------EDVFsiTGRGTVATGRIERGTVKVGDTVEI 255
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
36-237 |
4.64e-26 |
|
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: 104.53 E-value: 4.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLV-------HAISGVHTVRF---------KHEKERNITIKLGYAnakiykctnpdclppecykSY 99
Cdd:pfam00009 4 RNIGIIGHVDHGKTTLTdrllyytGAISKRGEVKGegeagldnlPEERERGITIKSAAV-------------------SF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 100 ESSKednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKHI 179
Cdd:pfam00009 65 ETKD------------------YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-VMPQTREHLRLARQLGVPII 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124808285 180 LILqNKVELIKEEQALKQQEEIRN---FVSGTAADSAPIIPISAVLKYNIDVVCEYIVTQI 237
Cdd:pfam00009 126 VFI-NKMDRVDGAELEEVVEEVSRellEKYGEDGEFVPVVPGSALKGEGVQTLLDALDEYL 185
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
36-290 |
5.11e-26 |
|
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439820 [Multi-domain] Cd Length: 396 Bit Score: 109.08 E-value: 5.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLVHAISGV----HTVRFK---------HEKERNITIklgyANAKIykctnpdclppecykSYESS 102
Cdd:COG0050 13 VNIGTIGHVDHGKTTLTAAITKVlakkGGAKAKaydqidkapEEKERGITI----NTSHV---------------EYETE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 103 KednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKHILIL 182
Cdd:COG0050 74 K------------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 183 QNKVELIKEEQALKQQE-EIRNFVS--GTAADSAPIIPISAVLKYNIDVVCEY---IV-------TQISIPKRDfISSPH 249
Cdd:COG0050 135 LNKCDMVDDEELLELVEmEVRELLSkyGFPGDDTPIIRGSALKALEGDPDPEWekkILelmdavdSYIPEPERD-TDKPF 213
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 124808285 250 MIvirsfdvnkPGEDIETLQG-G-VAGGSILHGVLKVGDKIEI 290
Cdd:COG0050 214 LM---------PVEDVFSITGrGtVVTGRVERGIIKVGDEVEI 247
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
36-290 |
1.96e-25 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 107.62 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLVHAISGVHTVRFK-------------HEKERNITIklgyANAKIykctnpdclppecykSYESS 102
Cdd:PRK12735 13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGgeakaydqidnapEEKARGITI----NTSHV---------------EYETA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 103 KednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKHILIL 182
Cdd:PRK12735 74 N------------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 183 QNKVELIKEEQALKQQE-EIRNFVS--GTAADSAPIIPISAVLKYN--------------IDVVCEYIVTqisiPKRDfI 245
Cdd:PRK12735 135 LNKCDMVDDEELLELVEmEVRELLSkyDFPGDDTPIIRGSALKALEgdddeeweakilelMDAVDSYIPE----PERA-I 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 124808285 246 SSPHMIvirsfdvnkPGEDIETLQ--GGVAGGSILHGVLKVGDKIEI 290
Cdd:PRK12735 210 DKPFLM---------PIEDVFSISgrGTVVTGRVERGIVKVGDEVEI 247
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
19-290 |
2.28e-25 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 107.99 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 19 VTKLTPLSEDVISR-QATINLGTIGHVAHGKSTLVHAISGV-------HTVRFKH------EKERNITIklgyANAKIyk 84
Cdd:PLN03127 44 SPSPWWRSMATFTRtKPHVNVGTIGHVDHGKTTLTAAITKVlaeegkaKAVAFDEidkapeEKARGITI----ATAHV-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 85 ctnpdclppecykSYESSKednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQT 164
Cdd:PLN03127 118 -------------EYETAK------------------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDG-PMPQT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 165 SEHLAAVEIMRLKHILILQNKVELIKEEQALKQQE-EIRNFVS--GTAADSAPIIPISAV--LKYNIDVVCEYIVTQISI 239
Cdd:PLN03127 166 KEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEmELRELLSfyKFPGDEIPIIRGSALsaLQGTNDEIGKNAILKLMD 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 124808285 240 PKRDFISSPHMIVIRSFDVnkPGEDIETLQ--GGVAGGSILHGVLKVGDKIEI 290
Cdd:PLN03127 246 AVDEYIPEPVRVLDKPFLM--PIEDVFSIQgrGTVATGRVEQGTIKVGEEVEI 296
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
36-220 |
3.22e-22 |
|
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 eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 93.97 E-value: 3.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLVHAISGV-HTVRF-KH--EKERNITIKLGYAnakiykctnpdclppecykSYESSKEDNPICPR 111
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIaSTAAFdKNpqSQERGITLDLGFS-------------------SFEVDKPKHLEDNE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 112 kdcNHEMKLLRhVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKHILILqNKVELIKE 191
Cdd:cd01889 62 ---NPQIENYQ-ITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-IQTQTAECLVIGELLCKPLIVVL-NKIDLIPE 135
|
170 180 190
....*....|....*....|....*....|...
gi 124808285 192 EQALKQQEEIRNFVSGTAAD----SAPIIPISA 220
Cdd:cd01889 136 EERKRKIEKMKKRLQKTLEKtrlkDSPIIPVSA 168
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
36-227 |
4.33e-22 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 93.42 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLVHAISGVHTVRF-------------KHEKERNITIklgyaNAkiykctnpdclppeCYKSYESS 102
Cdd:cd01884 3 VNVGTIGHVDHGKTTLTAAITKVLAKKGgakakkydeidkaPEEKARGITI-----NT--------------AHVEYETA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 103 KednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKHILIL 182
Cdd:cd01884 64 N------------------RHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDG-PMPQTREHLLLARQVGVPYIVVF 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 124808285 183 QNKVELIKEEQALKQQE-EIRNFVS--GTAADSAPIIPISAVLKYNID 227
Cdd:cd01884 125 LNKADMVDDEELLELVEmEVRELLSkyGFDGDDTPIVRGSALKALEGD 172
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
36-290 |
9.08e-21 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 94.68 E-value: 9.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLVHAISGV-----HTVRFKH--------EKERNITIklgyanakiykctNPDCLppecykSYESS 102
Cdd:PLN03126 82 VNIGTIGHVDHGKTTLTAALTMAlasmgGSAPKKYdeidaapeERARGITI-------------NTATV------EYETE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 103 KednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKHILIL 182
Cdd:PLN03126 143 N------------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPNMVVF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 183 QNKVELIKEEQALKQQE-EIRNFVSGTA--ADSAPIIPISAVLK---------------------YNI-DVVCEYivtqI 237
Cdd:PLN03126 204 LNKQDQVDDEELLELVElEVRELLSSYEfpGDDIPIISGSALLAlealmenpnikrgdnkwvdkiYELmDAVDSY----I 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 124808285 238 SIPKRDfISSPHMIVIrsfdvnkpgEDIETL--QGGVAGGSILHGVLKVGDKIEI 290
Cdd:PLN03126 280 PIPQRQ-TDLPFLLAV---------EDVFSItgRGTVATGRVERGTVKVGETVDI 324
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
36-359 |
5.98e-19 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 88.84 E-value: 5.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLV-------HAISGvHTV----------------------RFKHEKERNITIKLGYanakiykct 86
Cdd:COG5256 8 LNLVVIGHVDHGKSTLVgrllyetGAIDE-HIIekyeeeaekkgkesfkfawvmdRLKEERERGVTIDLAH--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 87 npdclppecyKSYESSKednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNEScPQPQTSE 166
Cdd:COG5256 78 ----------KKFETDK------------------YYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDG-VMGQTRE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 167 HLAAVEIMRLKHILILQNKVELIKEEQalKQQEEIRNFVS------GTAADSAPIIPISAVLKYNidvvceyiVTQISiP 240
Cdd:COG5256 129 HAFLARTLGINQLIVAVNKMDAVNYSE--KRYEEVKEEVSkllkmvGYKVDKIPFIPVSAWKGDN--------VVKKS-D 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 241 KRDFISSPhmIVIRSFD--------VNK----PGEDIETLQ--GGVAGGSILHGVLKVGDKIEIRPGIISkddkGEItcR 306
Cdd:COG5256 198 NMPWYNGP--TLLEALDnlkepekpVDKplriPIQDVYSISgiGTVPVGRVETGVLKVGDKVVFMPAGVV----GEV--K 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 124808285 307 PIisqilSMFAEnnNLKYAVPGGLIGVGTKidpILTRADRLVGQVIGHLNKLP 359
Cdd:COG5256 270 SI-----EMHHE--ELEQAEPGDNIGFNVR---GVEKNDIKRGDVAGHPDNPP 312
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
36-292 |
7.13e-19 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 88.44 E-value: 7.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLVHAI---SGV---HTV----------------------RFKHEKERNITIKLGYanakiykctn 87
Cdd:PRK12317 7 LNLAVIGHVDHGKSTLVGRLlyeTGAideHIIeelreeakekgkesfkfawvmdRLKEERERGVTIDLAH---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 88 pdclppecyKSYESSKednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNES-CPQPQTSE 166
Cdd:PRK12317 77 ---------KKFETDK------------------YYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAgGVMPQTRE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 167 HLAAVEIMRLKHILILQNKVELIKEEQalKQQEEIRNFVS------GTAADSAPIIPISAVLKYNIdvvceyivtqisip 240
Cdd:PRK12317 130 HVFLARTLGINQLIVAINKMDAVNYDE--KRYEEVKEEVSkllkmvGYKPDDIPFIPVSAFEGDNV-------------- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124808285 241 krdFISSPHM------IVIRSFD--------VNK----PGEDIETLQ--GGVAGGSILHGVLKVGDKIEIRP 292
Cdd:PRK12317 194 ---VKKSENMpwyngpTLLEALDnlkppekpTDKplriPIQDVYSISgvGTVPVGRVETGVLKVGDKVVFMP 262
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
40-288 |
1.94e-18 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 88.18 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 40 TIGHVAHGKSTLVHAISGVHTVRFKHEKERNITIKLGYAnakiYkctnpdclppecyksyesskednpiCPRKDCnhemk 119
Cdd:PRK10512 5 TAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYA----Y-------------------------WPQPDG----- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 120 llRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNESCpQPQTSEHLAaveIMRL---KHILILQNKVELIKEEQALK 196
Cdd:PRK10512 51 --RVLGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGV-MAQTREHLA---ILQLtgnPMLTVALTKADRVDEARIAE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 197 QQEEIRNFVSGTAADSAPIIPISAVLKYNIDVVCEYIVT---QISIPKRDFisspHMIVIRSFDVNKPGEdietlqggVA 273
Cdd:PRK10512 125 VRRQVKAVLREYGFAEAKLFVTAATEGRGIDALREHLLQlpeREHAAQHRF----RLAIDRAFTVKGAGL--------VV 192
|
250
....*....|....*
gi 124808285 274 GGSILHGVLKVGDKI 288
Cdd:PRK10512 193 TGTALSGEVKVGDTL 207
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
36-292 |
2.57e-13 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 71.89 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKSTLVHA-ISG----------VHTVRFKHEKERNITIKLGYA-----NAKIYKCTNPDCLPPECyKSY 99
Cdd:COG5258 123 IVVGVAGHVDHGKSTLVGTlVTGklddgnggtrSFLDVQPHEVERGLSADLSYAvygfdDDGPVRMKNPLRKTDRA-RVV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 100 ESSKednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNG--AAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLK 177
Cdd:COG5258 202 EESD------------------KLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDG-PTHTTREHLGILLAMDLP 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 178 hILILQNKVELIKEEQALKQQEEIRNFV-----------SGTAADSA---------PIIPISAVLKYNIDVVCEYIvtqI 237
Cdd:COG5258 263 -VIVAITKIDKVDDERVEEVEREIENLLrivgrtpleveSRHDVDAAieeingrvvPILKTSAVTGEGLDLLDELF---E 338
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124808285 238 SIPKR--DFISSPHMIVIRSFDVnkpgedieTLQGGVAGGSILHGVLKVGDKIEIRP 292
Cdd:COG5258 339 RLPKRatDEDEPFLMYIDRIYNV--------TGVGTVVSGTVKSGKVEAGDELLIGP 387
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
2-290 |
6.90e-11 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 64.47 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 2 NINEKD-KLAEQNLETLDVTKLTPLsedvisrqATInlgtIGHVAHGKSTLVHAISGVHTVrfkhEKERN-ITIKLGyan 79
Cdd:CHL00189 222 NINEKTsNLDNTSAFTENSINRPPI--------VTI----LGHVDHGKTTLLDKIRKTQIA----QKEAGgITQKIG--- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 80 akiykctnpdclppecykSYESskednpICPRKDCNhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNESC 159
Cdd:CHL00189 283 ------------------AYEV------EFEYKDEN------QKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGV 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 160 pQPQTSEHLAAVEIMRLKhILILQNKVE-----LIKEEQALKQQeeirNFVSGTAADSAPIIPISAVLKYNIDVVCEYI- 233
Cdd:CHL00189 333 -KPQTIEAINYIQAANVP-IIVAINKIDkananTERIKQQLAKY----NLIPEKWGGDTPMIPISASQGTNIDKLLETIl 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 124808285 234 -VTQISIPKRDFISSPHMIVIRSFdvnkpgedIETLQGGVAGGSILHGVLKVGDKIEI 290
Cdd:CHL00189 407 lLAEIEDLKADPTQLAQGIILEAH--------LDKTKGPVATILVQNGTLHIGDIIVI 456
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
40-226 |
2.70e-09 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 56.81 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 40 TIGHVAHGKSTLV---------------HAISGVHTVR--------------FKHEKERNITIKLGYanakiykctnpdc 90
Cdd:cd04166 4 TCGSVDDGKSTLIgrllydsksifedqlAALERSKSSGtqgekldlallvdgLQAEREQGITIDVAY------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 91 lppecykSYESSKEdnpicpRKdcnhemkllrhvsFV--DCPGHDILMATMLNGAAVMDAALLLVAGNESCpQPQTSEHL 168
Cdd:cd04166 71 -------RYFSTPK------RK-------------FIiaDTPGHEQYTRNMVTGASTADLAILLVDARKGV-LEQTRRHS 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 169 AAVEIMRLKHILILQNKVELI--KEEQALKQQEEIRNFVSGTAADSAPIIPISAVLKYNI 226
Cdd:cd04166 124 YIASLLGIRHVVVAVNKMDLVdyDEEVFEEIKADYLAFAASLGIEDITFIPISALEGDNV 183
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
270-353 |
3.64e-09 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 53.04 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 270 GGVAGGSILHGVLKVGDKIEIRPGIISKDdkgeitcrPIISQILSMFAENNNLKYAVPGGLIGVGTKIDPILtraDRLVG 349
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKK--------KIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLE---DIRVG 69
|
....
gi 124808285 350 QVIG 353
Cdd:pfam03144 70 DTLT 73
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
37-220 |
3.66e-09 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 56.73 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 37 NLGTIGHVAHGKSTLV-HAI--SGV---HTV----------------------RFKHEKERNITIKLGYANakiykctnp 88
Cdd:cd01883 1 NLVVIGHVDAGKSTLTgHLLykLGGvdkRTIekyekeakemgkesfkyawvldKLKEERERGVTIDVGLAK--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 89 dclppecyksYESSKednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNESC------PQP 162
Cdd:cd01883 72 ----------FETEK------------------YRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEfeagfeKGG 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124808285 163 QTSEHLAAVEIMRLKHILILQNKVELIKEEQALKQQEEIRNFVS------GTAADSAPIIPISA 220
Cdd:cd01883 124 QTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSpflkkvGYNPKDVPFIPISG 187
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
36-336 |
2.88e-06 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 49.36 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 36 INLGTIGHVAHGKST----LVHAISGV--HTV----------------------RFKHEKERNITIklgyaNAKIYKctn 87
Cdd:PTZ00141 8 INLVVIGHVDSGKSTttghLIYKCGGIdkRTIekfekeaaemgkgsfkyawvldKLKAERERGITI-----DIALWK--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 88 pdclppecyksYESSKednpicprkdcnhemkllRHVSFVDCPGHDILMATMLNGAAVMDAALLLVAGNES------CPQ 161
Cdd:PTZ00141 80 -----------FETPK------------------YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGefeagiSKD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 162 PQTSEHLAAVEIMRLKHILILQNKVELIKEEQALKQQEEIRNFVS------GTAADSAPIIPISAVLKYNI----DVVCE 231
Cdd:PTZ00141 131 GQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSaylkkvGYNPEKVPFIPISGWQGDNMieksDNMPW 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 232 Y-------IVTQISIPKRDfISSPHMIVIRsfDVNKPGEdietlQGGVAGGSILHGVLKVGDKIEIRPGiiskddkgeit 304
Cdd:PTZ00141 211 YkgptlleALDTLEPPKRP-VDKPLRLPLQ--DVYKIGG-----IGTVPVGRVETGILKPGMVVTFAPS----------- 271
|
330 340 350
....*....|....*....|....*....|..
gi 124808285 305 crPIISQILSMFAENNNLKYAVPGGLIGVGTK 336
Cdd:PTZ00141 272 --GVTTEVKSVEMHHEQLAEAVPGDNVGFNVK 301
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
126-234 |
1.03e-05 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 47.29 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 126 FVDCPG--------HDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKHILILqNKVELIKEEQALKQ 197
Cdd:COG1159 55 FVDTPGihkpkrklGRRMNKAAWSALEDVDVILFVVDATEK-IGEGDEFILELLKKLKTPVILVI-NKIDLVKKEELLPL 132
|
90 100 110
....*....|....*....|....*....|....*..
gi 124808285 198 QEEIRNFvsgtaADSAPIIPISAVLKYNIDVVCEYIV 234
Cdd:COG1159 133 LAEYSEL-----LDFAEIVPISALKGDNVDELLDEIA 164
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
37-240 |
1.61e-05 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 45.22 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 37 NLGTIGHVAHGKSTLVHAI---SGVHTVRFKH---------EKERNITIKLgyANAKI-YKCTNPdclppecyKSYEssk 103
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSEREMKeqvldsmdlERERGITIKA--QAVRLfYKAKDG--------EEYL--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 104 ednpicprkdcnhemkllrhVSFVDCPGH-DI-------LMATmlngaavmDAALLLVAGNESCpQPQTSEHL-AAVEiM 174
Cdd:cd01890 69 --------------------LNLIDTPGHvDFsyevsrsLAAC--------EGALLVVDATQGV-EAQTLANFyLALE-N 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124808285 175 RLKHILILqNKVELIKE--EQALKQQEEIrnfvsgTAADSAPIIPISAVLKYNIDVVCEYIVTQISIP 240
Cdd:cd01890 119 NLEIIPVI-NKIDLPAAdpDRVKQEIEDV------LGLDASEAILVSAKTGLGVEDLLEAIVERIPPP 179
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
42-236 |
1.06e-04 |
|
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: 42.84 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 42 GHVAHGKSTLVHAISGVHTVrfkhEKE-RNITIKLGyANAKIYKCTNPDCLppecyksyesskednpicprkdcnhemkl 120
Cdd:cd01887 7 GHVDHGKTTLLDKIRKTNVA----AGEaGGITQHIG-AYQVPIDVKIPGIT----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 121 lrhvsFVDCPGHDILMATMLNGAAVMDAALLLVAGNESCpQPQTSEhlaAVEIMRLKH--ILILQNKVELI----KEEQA 194
Cdd:cd01887 53 -----FIDTPGHEAFTNMRARGASVTDIAILVVAADDGV-MPQTIE---AINHAKAANvpIIVAINKIDKPygteADPER 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 124808285 195 LKQQ--------EEIRNFVsgtaadsaPIIPISAVLKYNIDVVCEYIVTQ 236
Cdd:cd01887 124 VKNElselglvgEEWGGDV--------SIVPISAKTGEGIDDLLEAILLL 165
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
267-338 |
1.27e-04 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 40.33 E-value: 1.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124808285 267 TLQGGVAGGSILHGVLKVGDKIEIRPGIISKddkgeitcrpIISQILSMFAEnnnLKYAVPGGLIGVGTKID 338
Cdd:cd01342 12 PGRGRVAGGRVESGTLKVGDEIRILPKGITG----------RVTSIERFHEE---VDEAKAGDIVGIGILGV 70
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
128-292 |
5.62e-04 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 42.22 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 128 DCPGHDILMATMLNGAAVMDAALLLVAGNESCpQPQTSEHLAAVEIMRLKHILILQNKVELIKEEQAL--KQQEEIRNFV 205
Cdd:PRK05506 110 DTPGHEQYTRNMVTGASTADLAIILVDARKGV-LTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVfdEIVADYRAFA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 206 SGTAADSAPIIPISAVLKYNidvvceyiVTQISiPKRDFISSPHMIVI---------RSFD--------VNKPGEDIETL 268
Cdd:PRK05506 189 AKLGLHDVTFIPISALKGDN--------VVTRS-ARMPWYEGPSLLEHletveiasdRNLKdfrfpvqyVNRPNLDFRGF 259
|
170 180
....*....|....*....|....
gi 124808285 269 QGGVAGGSIlhgvlKVGDKIEIRP 292
Cdd:PRK05506 260 AGTVASGVV-----RPGDEVVVLP 278
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
126-236 |
7.62e-04 |
|
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: 40.14 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 126 FVDCPG----HDILMaTMLNGAAVM-----DAALLLVAGNESCPqPQTSEHLAAVEIMRLKHILILqNKVELIKEEQALK 196
Cdd:cd04163 55 FVDTPGihkpKKKLG-ERMVKAAWSalkdvDLVLFVVDASEWIG-EGDEFILELLKKSKTPVILVL-NKIDLVKDKEDLL 131
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 124808285 197 QQEEIRNFVSgtaaDSAPIIPISAVLKYNIDVVCEYIVTQ 236
Cdd:cd04163 132 PLLEKLKELH----PFAEIFPISALKGENVDELLEYIVEY 167
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
126-234 |
1.20e-03 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 40.80 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 126 FVDCPG--------HDILMATMLNGAAVMDAALLLVAGNEScPQPQTSEHLAAVEIMRLKHILILqNKVELIKE-EQALK 196
Cdd:PRK00089 57 FVDTPGihkpkralNRAMNKAAWSSLKDVDLVLFVVDADEK-IGPGDEFILEKLKKVKTPVILVL-NKIDLVKDkEELLP 134
|
90 100 110
....*....|....*....|....*....|....*...
gi 124808285 197 QQEEIRNFVsgtaaDSAPIIPISAVLKYNIDVVCEYIV 234
Cdd:PRK00089 135 LLEELSELM-----DFAEIVPISALKGDNVDELLDVIA 167
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
126-204 |
9.62e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 38.71 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124808285 126 FVDCPGHDILMATMLNGAAVMDAALLLVAGNESCpQPQTSEhlaAVEIMRLKH--ILILQNKVELIKEEQALKQQEEIRN 203
Cdd:PRK14845 530 FIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGF-KPQTIE---AINILRQYKtpFVVAANKIDLIPGWNISEDEPFLLN 605
|
.
gi 124808285 204 F 204
Cdd:PRK14845 606 F 606
|
|
| |
