|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-493 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 830.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 81 DCPGHADYVKNMIarafdqidnapeekargitintshveydtptrhyahvdcpghadyvknmiTGAAQMDGAILVVAATD 160
Cdd:PRK00049 81 DCPGHADYVKNMI--------------------------------------------------TGAAQMDGAILVVSAAD 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 161 GPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEG--DAEWEAK 238
Cdd:PRK00049 111 GPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGddDEEWEKK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 239 IIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTTCTGVEMFRKLLDE 318
Cdd:PRK00049 191 ILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 319 GRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYfrttdvtgtielpegv 398
Cdd:PRK00049 271 GQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFY---------------- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 399 emvmpgdnikmvvtlihpiamddglrfaireggyFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIR 478
Cdd:PRK00049 335 ----------------------------------FRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIR 380
|
490
....*....|....*
gi 821669726 479 EGGRTVGAGVVAKVL 493
Cdd:PRK00049 381 EGGRTVGAGVVTKII 395
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-493 |
0e+00 |
|
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: 809.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 81 DCPGHADYVKNMIarafdqidnapeekargitintshveydtptrhyahvdcpghadyvknmiTGAAQMDGAILVVAATD 160
Cdd:COG0050 81 DCPGHADYVKNMI--------------------------------------------------TGAAQMDGAILVVSATD 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 161 GPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGD--AEWEAK 238
Cdd:COG0050 111 GPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKALEGDpdPEWEKK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 239 IIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTTCTGVEMFRKLLDE 318
Cdd:COG0050 191 ILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRDTQKTVVTGVEMFRKLLDE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 319 GRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYfrttdvtgtielpegv 398
Cdd:COG0050 271 GEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFY---------------- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 399 emvmpgdnikmvvtlihpiamddglrfaireggyFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIR 478
Cdd:COG0050 335 ----------------------------------FRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIR 380
|
490
....*....|....*
gi 821669726 479 EGGRTVGAGVVAKVL 493
Cdd:COG0050 381 EGGRTVGAGVVTKII 395
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-493 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 807.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 81 DCPGHADYVKNMIarafdqidnapeekargitintshveydtptrhyahvdcpghadyvknmiTGAAQMDGAILVVAATD 160
Cdd:PRK12735 81 DCPGHADYVKNMI--------------------------------------------------TGAAQMDGAILVVSAAD 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 161 GPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGD--AEWEAK 238
Cdd:PRK12735 111 GPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGDddEEWEAK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 239 IIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTTCTGVEMFRKLLDE 318
Cdd:PRK12735 191 ILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIVGIKETQKTTVTGVEMFRKLLDE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 319 GRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYfrttdvtgtielpegv 398
Cdd:PRK12735 271 GQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFY---------------- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 399 emvmpgdnikmvvtlihpiamddglrfaireggyFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIR 478
Cdd:PRK12735 335 ----------------------------------FRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIR 380
|
490
....*....|....*
gi 821669726 479 EGGRTVGAGVVAKVL 493
Cdd:PRK12735 381 EGGRTVGAGVVAKII 395
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-435 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 757.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 81 dcpghadyvknmiarafdqidnapeekargitintshveydtptrhyahvDCPGHADYVKNMITGAAQMDGAILVVAATD 160
Cdd:PRK12736 81 --------------------------------------------------DCPGHADYVKNMITGAAQMDGAILVVAATD 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 161 GPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKII 240
Cdd:PRK12736 111 GPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEYDFPGDDIPVIRGSALKALEGDPKWEDAIM 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 241 ELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTTCTGVEMFRKLLDEGR 320
Cdd:PRK12736 191 ELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIKETQKTVVTGVEMFRKLLDEGQ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 321 AGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEM 400
Cdd:PRK12736 271 AGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPEGTEM 350
|
410 420 430
....*....|....*....|....*....|....*
gi 821669726 401 VMPGDNIKMVVTLIHPIAMDDGLRFAIREGGyfRT 435
Cdd:PRK12736 351 VMPGDNVTITVELIHPIAMEQGLKFAIREGG--RT 383
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-431 |
0e+00 |
|
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: 721.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 81 dcpghadyvknmiarafdqidnapeekargitintshveydtptrhyahvDCPGHADYVKNMITGAAQMDGAILVVAATD 160
Cdd:TIGR00485 81 --------------------------------------------------DCPGHADYVKNMITGAAQMDGAILVVSATD 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 161 GPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKII 240
Cdd:TIGR00485 111 GPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEAKIL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 241 ELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTTCTGVEMFRKLLDEGR 320
Cdd:TIGR00485 191 ELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKTTVTGVEMFRKELDEGR 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 321 AGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEM 400
Cdd:TIGR00485 271 AGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEM 350
|
410 420 430
....*....|....*....|....*....|.
gi 821669726 401 VMPGDNIKMVVTLIHPIAMDDGLRFAIREGG 431
Cdd:TIGR00485 351 VMPGDNVKMTVELISPIALEQGMRFAIREGG 381
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-493 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 678.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 81 DCPGHADYVKNMIarafdqidnapeekargitintshveydtptrhyahvdcpghadyvknmiTGAAQMDGAILVVAATD 160
Cdd:CHL00071 81 DCPGHADYVKNMI--------------------------------------------------TGAAQMDGAILVVSAAD 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 161 GPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALE---------- 230
Cdd:CHL00071 111 GPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPGDDIPIVSGSALLALEaltenpkikr 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 231 GDAEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTTCTGVE 310
Cdd:CHL00071 191 GENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLRETKTTTVTGLE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 311 MFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTG 390
Cdd:CHL00071 271 MFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTKEEGGRHTPFFPGYRPQFYVRTTDVTG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 391 TIELpegvemvmpgdnikmvvtlihpiamddglrfaireggyFRTTDVTGTielpegvEMVMPGDNIKMVVTLIHPIAMD 470
Cdd:CHL00071 351 KIES--------------------------------------FTADDGSKT-------EMVMPGDRIKMTVELIYPIAIE 385
|
490 500
....*....|....*....|...
gi 821669726 471 DGLRFAIREGGRTVGAGVVAKVL 493
Cdd:CHL00071 386 KGMRFAIREGGRTVGAGVVSKIL 408
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
2-494 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 636.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 2 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTygGSARAFdqidnapeekargitintshveydtptrhyahvd 81
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEE--GKAKAV---------------------------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 82 cpghadyvknmiarAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG 161
Cdd:PLN03127 95 --------------AFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 162 PMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEG--DAEWEAKI 239
Cdd:PLN03127 161 PMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSALQGtnDEIGKNAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 240 IELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKE--TAKTTCTGVEMFRKLLD 317
Cdd:PLN03127 241 LKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLRPggPLKTTVTGVEMFKKILD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 318 EGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEG 397
Cdd:PLN03127 321 QGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFFSNYRPQFYLRTADVTGKVELPEG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 398 VEMVMPGDNikmvvtlihpiamddglrfaireggyfrttdVTGTIElpegvemvmpgdnikmvvtLIHPIAMDDGLRFAI 477
Cdd:PLN03127 401 VKMVMPGDN-------------------------------VTAVFE-------------------LISPVPLEPGQRFAL 430
|
490
....*....|....*..
gi 821669726 478 REGGRTVGAGVVAKVLG 494
Cdd:PLN03127 431 REGGRTVGAGVVSKVLS 447
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-431 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 560.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 2 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAkTYGGSArafdqidnapeekargitintshveydtptrhyahvd 81
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALA-SMGGSA------------------------------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 82 cpghadyvknmiARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG 161
Cdd:PLN03126 113 ------------PKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 162 PMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALE----------G 231
Cdd:PLN03126 181 PMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLALEalmenpnikrG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 232 DAEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTTCTGVEM 311
Cdd:PLN03126 261 DNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETRSTTVTGVEM 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 312 FRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGT 391
Cdd:PLN03126 341 FQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGK 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 821669726 392 I-----ELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGG 431
Cdd:PLN03126 421 VtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGG 465
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-253 |
7.61e-120 |
|
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: 349.19 E-value: 7.61e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 11 PHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVdcpghadyvk 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHV---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 91 nmiarafdqidnapeekargitintshveydtptrhyahvDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHI 170
Cdd:cd01884 71 ----------------------------------------DCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 171 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGD--AEWEAKIIELAGHLDT 248
Cdd:cd01884 111 LLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKALEGDdpNKWVDKILELLDALDS 190
|
....*
gi 821669726 249 YIPEP 253
Cdd:cd01884 191 YIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
8-492 |
5.34e-74 |
|
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: 239.84 E-value: 5.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 8 RTKPHVNVGTIGHVDHGKTTLTAAIttvLAKTYGGSARAFDQIDNAPEEKARGitintshveydtpTRHYAHVdcpghad 87
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLVGRL---LYETGAIDEHIIEKYEEEAEKKGKE-------------SFKFAWV------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 88 yvknmiarafdqIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTR 167
Cdd:COG5256 60 ------------MDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 168 EHILLGRQVGVPYIIVFLNKCDMVD-DEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKaleGDaeweaKIIELAGHL 246
Cdd:COG5256 128 EHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWK---GD-----NVVKKSDNM 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 247 DTY-----------IPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV--GIKETAKTtctgVEMFR 313
Cdd:COG5256 200 PWYngptllealdnLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMpaGVVGEVKS----IEMHH 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 314 KLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGtiNPHT---KFESEVYILskdeggRH-TPFFKGYRPQFYFRTTDVT 389
Cdd:COG5256 276 EELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD--NPPTvaeEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 390 GTIElpEGVEMVMPgdnikmvvtlihpiamddglrfaiREGgyfrttdvtGTIElpEGVEMVMPGDNIKMVVTLIHPIAM 469
Cdd:COG5256 348 CTFV--ELVSKLDP------------------------RTG---------QVKE--ENPQFLKTGDAAIVKIKPTKPLVI 390
|
490 500 510
....*....|....*....|....*....|
gi 821669726 470 DD-------GlRFAIREGGRTVGAGVVAKV 492
Cdd:COG5256 391 EKfkefpqlG-RFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-393 |
2.66e-71 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 232.89 E-value: 2.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 8 RTKPHVNVGTIGHVDHGKTTLTAAIttvLAKTYGGSARAFDQIDNAPEEKARGitintshveydtpTRHYAHVdcpghad 87
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRL---LYETGAIDEHIIEELREEAKEKGKE-------------SFKFAWV------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 88 yvknmiarafdqIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATD--GPMPQ 165
Cdd:PRK12317 59 ------------MDRLKEERERGVTIDLAHKKFETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 166 TREHILLGRQVGVPYIIVFLNKCDMVD-DEELLELVEMEVRELLSQYDFPGDDTPIVRGSalkALEGDaeweaKIIELAG 244
Cdd:PRK12317 127 TREHVFLARTLGINQLIVAINKMDAVNyDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVS---AFEGD-----NVVKKSE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 245 HLDTY-----------IPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEV--EIVGIKETAKTtctgVEM 311
Cdd:PRK12317 199 NMPWYngptllealdnLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVvfMPAGVVGEVKS----IEM 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 312 FRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGtiNPHT---KFESEVYILskdeggRH-TPFFKGYRPQFYFRTTD 387
Cdd:PRK12317 275 HHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPD--NPPTvaeEFTAQIVVL------QHpSAITVGYTPVFHAHTAQ 346
|
....*.
gi 821669726 388 VTGTIE 393
Cdd:PRK12317 347 VACTFE 352
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-251 |
2.33e-69 |
|
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: 219.70 E-value: 2.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 10 KPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDqidnapeekargitintshveydtptrhyahvdcpghadyv 89
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 90 knmiarAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREH 169
Cdd:pfam00009 40 ------GEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREH 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 170 ILLGRQVGVPyIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALegdaeweaKIIELAGHLDTY 249
Cdd:pfam00009 114 LRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALKGE--------GVQTLLDALDEY 184
|
..
gi 821669726 250 IP 251
Cdd:pfam00009 185 LP 186
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
350-431 |
1.16e-56 |
|
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.
Pssm-ID: 294006 [Multi-domain] Cd Length: 90 Bit Score: 183.10 E-value: 1.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 350 NPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIRE 429
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
..
gi 821669726 430 GG 431
Cdd:cd03707 81 GG 82
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-435 |
1.20e-56 |
|
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: 198.98 E-value: 1.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 13 VNVGTIGHVDHGKTTLTAAITTVLAktyggsarafdqiDNAPEEKARGITINTShveydtptrhYAHVDCPGhadyvknm 92
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGIDT-------------DRLKEEKKRGITIDLG----------FAYLPLPD-------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 93 iarafdqidnapeekarGITIntshveydtptrhyAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILL 172
Cdd:COG3276 50 -----------------GRRL--------------GFVDVPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAI 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 173 GRQVGVPYIIVFLNKCDMvDDEELLELVEMEVRELLSQYDFPgdDTPIVRGSAlKALEGdaeweakIIELAGHLDTYIPE 252
Cdd:COG3276 99 LDLLGIKRGIVVLTKADL-VDEEWLELVEEEIRELLAGTFLE--DAPIVPVSA-VTGEG-------IDELRAALDALAAA 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 253 -PERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTtcTGVEMFRKLLDEGRAGENVGVLLRG 331
Cdd:COG3276 168 vPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRV--RGIQVHGQPVEEAYAGQRVALNLAG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 332 IKREEIERGQVLAKPGTINPHTKFESEVYILSkdegGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVmPGDniKMVV 411
Cdd:COG3276 246 VEKEEIERGDVLAAPGALRPTDRIDVRLRLLP----SAPRPLKHWQRVHLHHGTAEVLARVVLLDREELA-PGE--EALA 318
|
410 420
....*....|....*....|....*.
gi 821669726 412 TLI--HPIAMDDGLRFAIREGGYFRT 435
Cdd:COG3276 319 QLRleEPLVAARGDRFILRDYSPRRT 344
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
261-347 |
2.63e-51 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 168.85 E-value: 2.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 261 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERG 340
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 821669726 341 QVLAKPG 347
Cdd:cd03697 81 MVLAKPG 87
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-342 |
1.90e-48 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 173.01 E-value: 1.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 1 MSKEKfertkPHVNVGTIGHVDHGKTTLTAAIttvLAKTYGGSARAFDQIDNAPEEKARGitintshveydtpTRHYAHV 80
Cdd:PTZ00141 1 MGKEK-----THINLVVIGHVDSGKSTTTGHL---IYKCGGIDKRTIEKFEKEAAEMGKG-------------SFKYAWV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 81 dcpghadyvknmiarafdqIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATD 160
Cdd:PTZ00141 60 -------------------LDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 161 GPMP-------QTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDa 233
Cdd:PTZ00141 121 GEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGD- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 234 eweaKIIE------------LAGHLDTYIPePERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKET 301
Cdd:PTZ00141 200 ----NMIEksdnmpwykgptLLEALDTLEP-PKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVT 274
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 821669726 302 akTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQV 342
Cdd:PTZ00141 275 --TEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYV 313
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-253 |
3.30e-46 |
|
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: 159.00 E-value: 3.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHAdyvknmi 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHE------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 94 arafdqidnapeekargitintshveydtptrhyahvdcpghaDYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLG 173
Cdd:cd00881 74 -------------------------------------------DFSKETVRGLAQADGALLVVDANEGVEPQTREHLNIA 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 174 RQvGVPYIIVFLNKCDMvDDEELLELVEMEVRELLSQYDF---PGDDTPIVRGSALKALEGDaeweakiiELAGHLDTYI 250
Cdd:cd00881 111 LA-GGLPIIVAVNKIDR-VGEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIE--------ELLDAIVEHL 180
|
...
gi 821669726 251 PEP 253
Cdd:cd00881 181 PPP 183
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
348-492 |
9.53e-43 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 147.03 E-value: 9.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 348 TINPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIelpegvemvmpgdnikmvVTLIHPIamddglrfai 427
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKF------------------VELLHKL---------- 52
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 821669726 428 reggyfrttDVTGTIELPegvEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKV 492
Cdd:pfam03143 53 ---------DPGGVSENP---EFVMPGDNVIVTVELIKPIALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
84-397 |
1.17e-41 |
|
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: 156.96 E-value: 1.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 84 GHADYVKNMIARAFDQIDNA--PEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG 161
Cdd:TIGR00475 7 GHVDHGKTTLLKALTGIAADrlPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDADEG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 162 PMPQTREHILLGRQVGVPYIIVFLNKCDmVDDEELLELVEMEVRELLSQYDFpGDDTPIVRGSAlKALEGDAEWEAKIIE 241
Cdd:TIGR00475 87 VMTQTGEHLAVLDLLGIPHTIVVITKAD-RVNEEEIKRTEMFMKQILNSYIF-LKNAKIFKTSA-KTGQGIGELKKELKN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 242 LAGHLDTyipepeRAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTtcTGVEMFRKLLDEGRA 321
Cdd:TIGR00475 164 LLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRV--KAIQAQNQDVEIAYA 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 821669726 322 GENVGVLLRGIKREEIERGQVLAKPgtinPHTKFESEVYILSkdeggrHTPFFKGYRPQFYFRTTDVTGTIELPEG 397
Cdd:TIGR00475 236 GQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLLELQPYHIAHGMSVTTGKISLLDK 301
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
11-364 |
1.03e-40 |
|
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: 150.97 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 11 PHVNVGTIGHVDHGKTTLTAAITTVLAKTYGgsarafdqidnapEEKARGITINTSHVE---YDTPTrhyahvdCPGHAD 87
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVWTDTHS-------------EELKRGISIRLGYADaeiYKCPE-------CDGPEC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 88 YVknmiarafdqidnaPEEKARGITINTSHVeydtptRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQT 166
Cdd:TIGR03680 63 YT--------------TEPVCPNCGSETELL------RRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 167 REHILLGRQVGVPYIIVFLNKCDMvddeellelveMEVRELLSQYD--------FPGDDTPIVRGSALKALEGDAEWEAk 238
Cdd:TIGR03680 123 KEHLMALEIIGIKNIVIVQNKIDL-----------VSKEKALENYEeikefvkgTVAENAPIIPVSALHNANIDALLEA- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 239 iielaghLDTYIPEPERAIDKPFLLPIEDVFSISGRGT--------VVTGRVERGIIKVGEEVEIV-GIK---------E 300
Cdd:TIGR03680 191 -------IEKFIPTPERDLDKPPLMYVARSFDVNKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKvekggktkwE 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 821669726 301 TAKTTCTGVEMFRKLLDEGRAGENVGV---LLRGIKREEIERGQVLAKPGTINP-HTKFESEVYILSK 364
Cdd:TIGR03680 264 PIYTEITSLRAGGYKVEEARPGGLVGVgtkLDPALTKADALAGQVVGKPGTLPPvWESLELEVHLLER 331
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
7-364 |
4.92e-36 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 138.06 E-value: 4.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 7 ERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGgsarafdqidnapEEKARGITINTSHVeyDTPTRhyahvDCPGHa 86
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHS-------------EELKRGITIRLGYA--DATIR-----KCPDC- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 87 dyvknmiarafdqidNAPEekarGITINTSHVEYDTPT---RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-P 162
Cdd:PRK04000 63 ---------------EEPE----AYTTEPKCPNCGSETellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 163 MPQTREHILLGRQVGVPYIIVFLNKCDMvddeellelveMEVRELLSQY----DFP----GDDTPIVRGSALKALEGDAe 234
Cdd:PRK04000 124 QPQTKEHLMALDIIGIKNIVIVQNKIDL-----------VSKERALENYeqikEFVkgtvAENAPIIPVSALHKVNIDA- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 235 weakiieLAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGT--------VVTGRVERGIIKVGEEVEIV-GIKETAK-- 303
Cdd:PRK04000 192 -------LIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKVEEGgk 264
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 821669726 304 -------TTCTGVEMFRKLLDEGRAGENVGV---LLRGIKREEIERGQVLAKPGTINP-HTKFESEVYILSK 364
Cdd:PRK04000 265 tkwepitTKIVSLRAGGEKVEEARPGGLVGVgtkLDPSLTKADALAGSVAGKPGTLPPvWESLTIEVHLLER 336
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-189 |
5.19e-36 |
|
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: 133.00 E-value: 5.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLTAAIttvLAKTYGGSARAFDQIDNAPEEKARGitintshveydtpTRHYAHVdcpghadyvknmi 93
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHL---LYKLGGVDKRTIEKYEKEAKEMGKE-------------SFKYAWV------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 94 arafdqIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-------PMPQT 166
Cdd:cd01883 52 ------LDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQT 125
|
170 180
....*....|....*....|...
gi 821669726 167 REHILLGRQVGVPYIIVFLNKCD 189
Cdd:cd01883 126 REHALLARTLGVKQLIVAVNKMD 148
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-363 |
2.01e-35 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 137.14 E-value: 2.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 1 MSKEKFertkpHVNVGTIGHVDHGKTTLTAAIttvLAKTYGGSARAFDQIDnapEEKArgitintshvEYDTPTRHYAHV 80
Cdd:PLN00043 1 MGKEKV-----HINIVVIGHVDSGKSTTTGHL---IYKLGGIDKRVIERFE---KEAA----------EMNKRSFKYAWV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 81 dcpghadyvknmiarafdqIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATD 160
Cdd:PLN00043 60 -------------------LDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 161 GPMP-------QTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVREL---LSQYDFPGDDTPIVrgsALKALE 230
Cdd:PLN00043 121 GGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVssyLKKVGYNPDKIPFV---PISGFE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 231 GDaeweaKIIELAGHLDTY-----------IPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIK 299
Cdd:PLN00043 198 GD-----NMIERSTNLDWYkgptllealdqINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPG---MVVTFG 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 821669726 300 ETAKTT-CTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVL--AKPGTINPHTKFESEVYILS 363
Cdd:PLN00043 270 PTGLTTeVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAsnSKDDPAKEAANFTSQVIIMN 336
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-362 |
5.49e-35 |
|
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: 134.96 E-value: 5.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 8 RTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGgsarafdqidnapEEKARGITINTshveydtptrhyahvdcpGHAD 87
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHS-------------EELKRGITIRL------------------GYAD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 88 yvknmiaRAFDQIDNAPEEKARGITINTSHVEYDT-PTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQ 165
Cdd:COG5257 50 -------ATFYKCPNCEPPEAYTTEPKCPNCGSETeLLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 166 TREHILLGRQVGVPYIIVFLNKCDMvddeellelveMEVRELLSQY----DF----PGDDTPIVRGSALKALEGDAewea 237
Cdd:COG5257 123 TKEHLMALDIIGIKNIVIVQNKIDL-----------VSKERALENYeqikEFvkgtVAENAPIIPVSAQHKVNIDA---- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 238 kiieLAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGT--------VVTGRVERGIIKVGEEVEIV-GIKETAK----- 303
Cdd:COG5257 188 ----LIEAIEEEIPTPERDLSKPPRMLVARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKGgktky 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 821669726 304 ----TTCTGVEMFRKLLDEGRAGENVGV---LLRGIKREEIERGQVLAKPGTINP-HTKFESEVYIL 362
Cdd:COG5257 264 epitTTVVSLRAGGEEVEEAKPGGLVAVgtkLDPSLTKSDSLVGSVAGKPGTLPPvLDSLTMEVHLL 330
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
4-440 |
3.99e-34 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 134.68 E-value: 3.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFdqIDNAPEEKARGITINTSHVEY----DTPTRhyah 79
Cdd:COG5258 114 EGKEKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLSADLSYAVYgfddDGPVR---- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 80 vdcpghadyVKNMIARAfdqidnapeEKARgITINTSHVEYdtptrhyaHVDCPGHADYVKNMITG--AAQMDGAILVVA 157
Cdd:COG5258 188 ---------MKNPLRKT---------DRAR-VVEESDKLVS--------FVDTVGHEPWLRTTIRGlvGQKLDYGLLVVA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 158 ATDGPMPQTREHILLGRQVGVPYIIVfLNKCDMvDDEELLELVEMEVRELLSQYD---FPGDD---------------TP 219
Cdd:COG5258 241 ADDGPTHTTREHLGILLAMDLPVIVA-ITKIDK-VDDERVEEVEREIENLLRIVGrtpLEVESrhdvdaaieeingrvVP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 220 IVRGSALkALEGdaeweakiIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIK 299
Cdd:COG5258 319 ILKTSAV-TGEG--------LDLLDELFERLPKRATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 300 ETA--KTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTI-NPHTKFESEVYILSkdeggrH-TPFFK 375
Cdd:COG5258 390 DGSfrEVEVKSIEMHYHRVDKAEAGRIVGIALKGVEEEELERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKE 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821669726 376 GYRPQFYFRTTDVTGTIElPEGVEMVMPGDNIKMVVT-LIHPIAMDDGLRFAIREG---GYFRTTDVTG 440
Cdd:COG5258 464 GYEPVVHLETISEAVRFE-PIDKGYLLPGDSGRVRLRfKYRPYYVEEGQRFVFREGrskGVGTVTDILD 531
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
17-340 |
1.88e-30 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 124.78 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 17 TIGHVDHGKTTLTAAITTVLAktyggsarafdqiDNAPEEKARGITINTShveydtptrhYAHVdcpghadyvknmiara 96
Cdd:PRK10512 5 TAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLG----------YAYW---------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 97 fdqidnaPEEKARGItintshveydtptrhyAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQV 176
Cdd:PRK10512 46 -------PQPDGRVL----------------GFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVMAQTREHLAILQLT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 177 GVPYIIVFLNKCDMVDDEELLELVEMEVrELLSQYDFPgdDTPIVRGSALKALegdaeweaKIIELAGHLDTyIPEPERA 256
Cdd:PRK10512 103 GNPMLTVALTKADRVDEARIAEVRRQVK-AVLREYGFA--EAKLFVTAATEGR--------GIDALREHLLQ-LPEREHA 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 257 IDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTtcTGVEMFRKLLDEGRAGENVGVLLRG-IKRE 335
Cdd:PRK10512 171 AQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRV--RGLHAQNQPTEQAQAGQRIALNIAGdAEKE 248
|
....*
gi 821669726 336 EIERG 340
Cdd:PRK10512 249 QINRG 253
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-243 |
2.65e-29 |
|
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: 113.08 E-value: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 15 VGTIGHVDHGKTTLTAAITTVlaktyggsarafdQIDNAPEEKARGITINTShveydtptrhYAHVDCPGHadyvknmia 94
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLG----------FAYLDLPDG--------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 95 rafdqidnapeekargitintshveydtptRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGR 174
Cdd:cd04171 50 ------------------------------KRLGFIDVPGHEKFVKNMLAGAGGIDAVLLVVAADEGIMPQTREHLEILE 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821669726 175 QVGVPYIIVFLNKCDMvDDEELLELVEMEVRELLSQYDFPgdDTPIVRGSALKAlEGDAEWEAKIIELA 243
Cdd:cd04171 100 LLGIKKGLVVLTKADL-VDEDRLELVEEEILELLAGTFLA--DAPIFPVSSVTG-EGIEELKNYLDELA 164
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
351-442 |
5.51e-29 |
|
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.
Pssm-ID: 294005 [Multi-domain] Cd Length: 93 Bit Score: 109.63 E-value: 5.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 351 PHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREG 430
Cdd:cd03706 2 MHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLREG 81
|
90
....*....|..
gi 821669726 431 GYfrtTDVTGTI 442
Cdd:cd03706 82 GR---TIGTGVV 90
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-307 |
1.18e-27 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 115.10 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 13 VNVGTIGHVDHGKTTLTAAITTVLAKTYggsarafdqidnaPEEKARGITIntsHVEYDTpTRHYAHVDCPGHADYvknm 92
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKTVRF-------------KREKVRNITI---KLGYAN-AKIYKCPKCPRPTCY---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 93 iaRAF--DQIDNAPEEkargitiNTSHVEydTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREH 169
Cdd:PTZ00327 94 --QSYgsSKPDNPPCP-------GCGHKM--TLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 170 ILLGRQVGVPYIIVFLNKCDMVDDEellelvemevrELLSQY----DF----PGDDTPIVRGSALKALEGDAeweakiie 241
Cdd:PTZ00327 163 LAAVEIMKLKHIIILQNKIDLVKEA-----------QAQDQYeeirNFvkgtIADNAPIIPISAQLKYNIDV-------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 242 LAGHLDTYIPEPERAIDKPFLL----------PIEDVFSIsgRGTVVTGRVERGIIKVGEEVEI----VGIKETAKTTCT 307
Cdd:PTZ00327 224 VLEYICTQIPIPKRDLTSPPRMivirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEIrpgiISKDSGGEFTCR 301
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-347 |
3.03e-27 |
|
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 442140 [Multi-domain] Cd Length: 430 Bit Score: 113.64 E-value: 3.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 1 MSKEKFERTKPHVNVG-----TIGHVDHGKTTL-------TAAITTvlaktyggsarafDQIDNAPEEKARgitintshv 68
Cdd:COG2895 1 MSTDIEAYLAQHENKDllrfiTCGSVDDGKSTLigrllydTKSIFE-------------DQLAALERDSKK--------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 69 eydtptrhyahvdcpghadyvknmiaRAFDQIDNAP------EEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNM 142
Cdd:COG2895 59 --------------------------RGTQEIDLALltdglqAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNM 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 143 ITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCD---------------MvddeellelvemevREL 207
Cdd:COG2895 113 VTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDlvdyseevfeeivadY--------------RAF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 208 LSQYDFPgDDTPIvrgsALKALEGDaeweaKIIE------------LAGHLDTyIPEPERAIDKPFLLPIEDV--FSISG 273
Cdd:COG2895 179 AAKLGLE-DITFI----PISALKGD-----NVVErsenmpwydgptLLEHLET-VEVAEDRNDAPFRFPVQYVnrPNLDF 247
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 821669726 274 RGtvVTGRVERGIIKVGEEVEIVGIKETakTTCTGVEMFRKLLDEGRAGENVGVLLrgiKRE-EIERGQVLAKPG 347
Cdd:COG2895 248 RG--YAGTIASGTVRVGDEVVVLPSGKT--STVKSIVTFDGDLEEAFAGQSVTLTL---EDEiDISRGDVIVAAD 315
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-255 |
8.04e-27 |
|
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: 106.97 E-value: 8.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 13 VNVGTIGHVDHGKTTLTAAITTVlaktyggsarafdQIDNAPEEKARGITIntsHVEYdTPTRHYAHVDCPGHADYVKnm 92
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGV-------------WTVRHKEELKRNITI---KLGY-ANAKIYKCPNCGCPRPYDT-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 93 iarafdqidnaPEEKARGITINTSHVeydtptRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHIL 171
Cdd:cd01888 62 -----------PECECPGCGGETKLV------RHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 172 LGRQVGVPYIIVFLNKCDMVDDEellelvemevrELLSQYDF--------PGDDTPIVRGSALKalegdaewEAKIIELA 243
Cdd:cd01888 125 ALEIMGLKHIIILQNKIDLVKEE-----------QALENYEQikefvkgtIAENAPIIPISAQL--------KYNIDVLC 185
|
250
....*....|..
gi 821669726 244 GHLDTYIPEPER 255
Cdd:cd01888 186 EYIVKKIPTPPR 197
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-189 |
3.00e-26 |
|
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: 105.53 E-value: 3.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 13 VNVGTIGHVDHGKTTLTAAITTVLaktyggSARAFDQidnAPEEKARGITINT--SHVEYDTPtrhyahvdcpghaDYVK 90
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIA------STAAFDK---NPQSQERGITLDLgfSSFEVDKP-------------KHLE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 91 NMIARAFDQIDnapeekargITIntshveydtptrhyahVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHI 170
Cdd:cd01889 59 DNENPQIENYQ---------ITL----------------VDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECL 113
|
170
....*....|....*....
gi 821669726 171 LLGRQVGVPYIIVfLNKCD 189
Cdd:cd01889 114 VIGELLCKPLIVV-LNKID 131
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-190 |
3.01e-21 |
|
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: 91.86 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 17 TIGHVDHGKTTLtaaITTVLAKTyggsarafDQIdnaPEEKARGITINTSHveydtptrhyahvdcpghadyvknmiARA 96
Cdd:cd04166 4 TCGSVDDGKSTL---IGRLLYDS--------KSI---FEDQLAALERSKSS--------------------------GTQ 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 97 FDQIDNA------PEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHI 170
Cdd:cd04166 44 GEKLDLAllvdglQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHS 123
|
170 180
....*....|....*....|
gi 821669726 171 LLGRQVGVPYIIVFLNKCDM 190
Cdd:cd04166 124 YIASLLGIRHVVVAVNKMDL 143
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-351 |
1.03e-20 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 95.47 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLTAAIttvL--AKTYGGSARAFDQI-DNAPEEKARGITI---NTShVEYdtptrhyahvdcpghad 87
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDAL---LkqSGTFRENQEVAERVmDSNDLERERGITIlakNTA-VRY----------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 88 yvknmiarafdqidnapeekaRGITINTshveydtptrhyahVDCPGHADY------VKNMItgaaqmDGAILVVAATDG 161
Cdd:COG1217 67 ---------------------KGVKINI--------------VDTPGHADFggeverVLSMV------DGVLLLVDAFEG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 162 PMPQTRehILLGR--QVGVPyIIVFLNKCDmvddeellelvemevR-------------ELL-------SQYDFpgddtP 219
Cdd:COG1217 106 PMPQTR--FVLKKalELGLK-PIVVINKID---------------RpdarpdevvdevfDLFielgatdEQLDF-----P 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 220 IVRGSalkALEGDA--EWEAK----------IIElaghldtYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGII 287
Cdd:COG1217 163 VVYAS---ARNGWAslDLDDPgedltplfdtILE-------HVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTI 232
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 821669726 288 KVGEEVEIV---GIKETAKttCTGVEMFRKL----LDEGRAGENVGVLlrGIkrEEIERGQVLAKPGTINP 351
Cdd:COG1217 233 KKGQQVALIkrdGKVEKGK--ITKLFGFEGLerveVEEAEAGDIVAIA--GI--EDINIGDTICDPENPEA 297
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
261-345 |
1.62e-20 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. 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' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 85.66 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 261 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTtcTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERG 340
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRV--RSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
gi 821669726 341 QVLAK 345
Cdd:cd03696 79 FVLSE 83
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
257-342 |
5.84e-20 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 84.16 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 257 IDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIvgiketAKTTCTG----VEMFRKLLDEGRAGENVGVLLRGI 332
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTF------APAGVTGevksVEMHHEPLEEAIPGDNVGFNVKGV 74
|
90
....*....|
gi 821669726 333 KREEIERGQV 342
Cdd:cd03693 75 SVKDIKRGDV 84
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
100-346 |
3.88e-19 |
|
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 213679 [Multi-domain] Cd Length: 406 Bit Score: 89.35 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 100 IDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVP 179
Cdd:TIGR02034 55 VDGLQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 180 YIIVFLNKCDMVDDEELL-ELVEMEVRELLSQYDFPgDDTPIvrgsALKALEGD--------AEWEAKIIeLAGHLDTYI 250
Cdd:TIGR02034 135 HVVLAVNKMDLVDYDEEVfENIKKDYLAFAEQLGFR-DVTFI----PLSALKGDnvvsrsesMPWYSGPT-LLEILETVE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 251 PEPERAiDKPFLLPIEDVF--SISGRGtvVTGRVERGIIKVGEEVEIVgiKETAKTTCTGVEMFRKLLDEGRAGENVGVL 328
Cdd:TIGR02034 209 VERDAQ-DLPLRFPVQYVNrpNLDFRG--YAGTIASGSVHVGDEVVVL--PSGRSSRVARIVTFDGDLEQARAGQAVTLT 283
|
250
....*....|....*....
gi 821669726 329 LrgiKRE-EIERGQVLAKP 346
Cdd:TIGR02034 284 L---DDEiDISRGDLLAAA 299
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-346 |
3.10e-18 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 87.74 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLTAAI---TTVLAKTYGGSARAFDQIDnapEEKARGITI---NTShVEYDtptrhyahvdcpghad 87
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALlkqSGTFRANEAVAERVMDSND---LERERGITIlakNTA-IRYN---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 88 yvknmiarafdqidnapeekarGITINTshveydtptrhyahVDCPGHADY------VKNMItgaaqmDGAILVVAATDG 161
Cdd:TIGR01394 63 ----------------------GTKINI--------------VDTPGHADFggeverVLGMV------DGVLLLVDASEG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 162 PMPQTREHILLGRQVGVPyIIVFLNKCDMVDDEELLELVEMEvrELL-------SQYDFpgddtPIVRGSALKALEG-DA 233
Cdd:TIGR01394 101 PMPQTRFVLKKALELGLK-PIVVINKIDRPSARPDEVVDEVF--DLFaelgaddEQLDF-----PIVYASGRAGWASlDL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 234 EWEAKiiELAGHLDT---YIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV---GIKETAKTtcT 307
Cdd:TIGR01394 173 DDPSD--NMAPLFDAivrHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMkrdGTIENGRI--S 248
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 821669726 308 GVEMFRKL----LDEGRAGENVGVLlrGIkrEEIERGQVLAKP 346
Cdd:TIGR01394 249 KLLGFEGLerveIDEAGAGDIVAVA--GL--EDINIGETIADP 287
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
275-344 |
4.08e-18 |
|
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: 78.46 E-value: 4.08e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 821669726 275 GTVVTGRVERGIIKVGEEVEIVG---IKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLA 344
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPngtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
106-347 |
1.08e-16 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 83.05 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 106 EKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFL 185
Cdd:PRK05506 85 EREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 186 NKCDMVDDEELL-ELVEMEVRELLSQYDFPgDDTPIvrgsALKALEGD--------AEWEAKIIeLAGHLDTYIPEPERA 256
Cdd:PRK05506 165 NKMDLVDYDQEVfDEIVADYRAFAAKLGLH-DVTFI----PISALKGDnvvtrsarMPWYEGPS-LLEHLETVEIASDRN 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 257 iDKPFLLPIEDV------FsisgRGtvVTGRVERGIIKVGEEVEIVGIKETakTTCTGVEMFRKLLDEGRAGENVGVLLr 330
Cdd:PRK05506 239 -LKDFRFPVQYVnrpnldF----RG--FAGTVASGVVRPGDEVVVLPSGKT--SRVKRIVTPDGDLDEAFAGQAVTLTL- 308
|
250
....*....|....*....
gi 821669726 331 gikREEIE--RGQVLAKPG 347
Cdd:PRK05506 309 ---ADEIDisRGDMLARAD 324
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-243 |
1.31e-15 |
|
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: 74.43 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 19 GHVDHGKTTLTAAITtvlaKTyggsarafdqidNAPEEKARGIT--INTSHVEYDTPTRHYAHVDCPGHADYvKNMIARa 96
Cdd:cd01887 7 GHVDHGKTTLLDKIR----KT------------NVAAGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRAR- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 97 fdqidnapeekargitintshveydtptrhyahvdcpghadyvknmitGAAQMDGAILVVAATDGPMPQTREHILLGRQV 176
Cdd:cd01887 69 ------------------------------------------------GASVTDIAILVVAADDGVMPQTIEAINHAKAA 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 821669726 177 GVPyIIVFLNKCDmvdDEELLELVEMEVRELLSQYDFPGDD----TPIVRGSALKAlEGDAEWEAKIIELA 243
Cdd:cd01887 101 NVP-IIVAINKID---KPYGTEADPERVKNELSELGLVGEEwggdVSIVPISAKTG-EGIDDLLEAILLLA 166
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-189 |
9.49e-15 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 72.63 E-value: 9.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLTAAITTvlaktYGGSARAFDQI-----DNAPEEKARGITI---NTShVEYDtptrhyahvdcpgh 85
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLK-----QSGTFRENEEVgervmDSNDLERERGITIlakNTA-ITYK-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 86 adyvknmiarafdqidnapeekarGITINTshveydtptrhyahVDCPGHADY------VKNMItgaaqmDGAILVVAAT 159
Cdd:cd01891 64 ------------------------DTKINI--------------IDTPGHADFggeverVLSMV------DGVLLLVDAS 99
|
170 180 190
....*....|....*....|....*....|..
gi 821669726 160 DGPMPQTRehILLGR--QVGVPyIIVFLNKCD 189
Cdd:cd01891 100 EGPMPQTR--FVLKKalEAGLK-PIVVINKID 128
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-189 |
4.28e-14 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 71.49 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLT---AAITTVLAKTYGGSARAfdqIDNAPEEKARGITINTSHV----EYDTPTrhyahvdcPGHA 86
Cdd:cd01885 2 NICIIAHVDHGKTTLSdslLASAGIISEKLAGKARY---LDTREDEQERGITIKSSAIslyfEYEEEK--------MDGN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 87 DYVKNMIarafdqidnapeekargitintshveydtptrhyahvDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQT 166
Cdd:cd01885 71 DYLINLI-------------------------------------DSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT 113
|
170 180
....*....|....*....|....*
gi 821669726 167 reHILLgRQVGVPYI--IVFLNKCD 189
Cdd:cd01885 114 --ETVL-RQALEERVkpVLVINKID 135
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
261-344 |
7.30e-14 |
|
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: 66.52 E-value: 7.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 261 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTtcTGVEMFRKLLDEGRAGENVGVLLRGIKreEIERG 340
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRV--TSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76
|
....
gi 821669726 341 QVLA 344
Cdd:cd01342 77 DTLT 80
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
84-293 |
5.43e-13 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 71.34 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 84 GHADYVKNMIARAFDQIDNAPEEkARGIT--INTSHVEYDTpTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG 161
Cdd:TIGR00487 94 GHVDHGKTSLLDSIRKTKVAQGE-AGGITqhIGAYHVENED-GKMITFLDTPGHEAFTSMRARGAKVTDIVVLVVAADDG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 162 PMPQTREHILLGRQVGVPyIIVFLNKCDmvddeeLLELVEMEVRELLSQYDFP----GDDTPIVRGSALKALEGDAEWEA 237
Cdd:TIGR00487 172 VMPQTIEAISHAKAANVP-IIVAINKID------KPEANPDRVKQELSEYGLVpedwGGDTIFVPVSALTGDGIDELLDM 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 821669726 238 kiIELAGHLDTYIPEPERAIDKPFLlpieDVFSISGRGTVVTGRVERGIIKVGEEV 293
Cdd:TIGR00487 245 --ILLQSEVEELKANPNGQASGVVI----EAQLDKGRGPVATVLVQSGTLRVGDIV 294
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-189 |
6.07e-13 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 71.05 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLT-----AA--ITTVLAktygGSARAFDQIDnapEEKARGITINTSHV----EYDTptrhyahvdc 82
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA----GEQLALDFDE---EEQARGITIKAANVsmvhEYEG---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 83 pghADYVKNMIarafdqidnapeekargitintshveyDTPtrhyAHVDCPGHadyvknmITGAAQ-MDGAILVVAATDG 161
Cdd:PRK07560 85 ---KEYLINLI---------------------------DTP----GHVDFGGD-------VTRAMRaVDGAIVVVDAVEG 123
|
170 180 190
....*....|....*....|....*....|..
gi 821669726 162 PMPQTrEHILlgRQV---GV-PyiIVFLNKCD 189
Cdd:PRK07560 124 VMPQT-ETVL--RQAlreRVkP--VLFINKVD 150
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-189 |
7.19e-13 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 68.03 E-value: 7.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLTAAIttvLAKTygGSARAFDQIDNApeekargitintshveyDTPTrhyahvdcpghadyvknmi 93
Cdd:cd04168 1 NIGILAHVDAGKTTLTESL---LYTS--GAIRELGSVDKG-----------------TTRT------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 94 arafdqiDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLG 173
Cdd:cd04168 40 -------DSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLL 112
|
170
....*....|....*.
gi 821669726 174 RQVGVPYIIvFLNKCD 189
Cdd:cd04168 113 RKLNIPTII-FVNKID 127
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
106-348 |
1.56e-12 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 69.56 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 106 EKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFL 185
Cdd:PRK05124 88 EREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 186 NKCD-MVDDEELLELVEMEVRELLSQydFPGDdtPIVRGSALKALEGDaeweaKIIELAGHLDTY-----------IPEP 253
Cdd:PRK05124 168 NKMDlVDYSEEVFERIREDYLTFAEQ--LPGN--LDIRFVPLSALEGD-----NVVSQSESMPWYsgptllevletVDIQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 254 ERAIDKPFLLPIEDVF--SISGRGtvVTGRVERGIIKVGEEVEIV--GIKETAKTTCTgvemFRKLLDEGRAGENVGVLL 329
Cdd:PRK05124 239 RVVDAQPFRFPVQYVNrpNLDFRG--YAGTLASGVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGEAITLVL 312
|
250 260
....*....|....*....|
gi 821669726 330 rgiKRE-EIERGQVLAKPGT 348
Cdd:PRK05124 313 ---EDEiDISRGDLLVAADE 329
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-189 |
4.13e-12 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 68.53 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 1 MSKEKFERTKphvNVGTIGHVDHGKTTLTAAI------TTVLAKTYGGSArafdQIDNAPEEKARGITINTS--HVEYdt 72
Cdd:COG0480 1 MAEYPLEKIR---NIGIVAHIDAGKTTLTERIlfytgaIHRIGEVHDGNT----VMDWMPEEQERGITITSAatTCEW-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 73 ptrhyahvdcpghadyvknmiarafdqidnapeekaRGITINTshveydtptrhyahVDCPGHADYVKNMITGAAQMDGA 152
Cdd:COG0480 72 ------------------------------------KGHKINI--------------IDTPGHVDFTGEVERSLRVLDGA 101
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 821669726 153 ILVVAATDGPMPQTrehILLGRQV---GVPyIIVFLNKCD 189
Cdd:COG0480 102 VVVFDAVAGVEPQT---ETVWRQAdkyGVP-RIVFVNKMD 137
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-296 |
7.75e-12 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 67.43 E-value: 7.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLtaaITTVLAKTYGGSARAFDQ---IDNAPEEKARGITI--NTSHVEYDtptrhyahvdcpghaDY 88
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDSRAETQervMDSNDLEKERGITIlaKNTAIKWN---------------DY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 89 VKNMiarafdqidnapeekargitintshveydtptrhyahVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTRE 168
Cdd:PRK10218 69 RINI-------------------------------------VDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRF 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 169 HILLGRQVGVPYIIVfLNKCDMVDDEELLELVEMEvrELLSQYDFPGD--DTPIVRGSALKALEG-DAEWEAK-IIELAG 244
Cdd:PRK10218 112 VTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVF--DLFVNLDATDEqlDFPIVYASALNGIAGlDHEDMAEdMTPLYQ 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 821669726 245 HLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV 296
Cdd:PRK10218 189 AIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-189 |
1.29e-11 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 66.58 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 17 TI-GHVDHGKTTLTAAI--TTVLAKtyggsarafdqidnapeEkARGIT--INTSHVEydTPTRHYAHVDCPGHAdyvkn 91
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNVAAG-----------------E-AGGITqhIGAYQVE--TNGGKITFLDTPGHE----- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 92 miarAFDQIdnapeeKARGitintshveydtptrhyahvdcpghadyvknmitgaAQM-DGAILVVAATDGPMPQTREHI 170
Cdd:COG0532 63 ----AFTAM------RARG------------------------------------AQVtDIVILVVAADDGVMPQTIEAI 96
|
170
....*....|....*....
gi 821669726 171 LLGRQVGVPyIIVFLNKCD 189
Cdd:COG0532 97 NHAKAAGVP-IIVAINKID 114
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
27-247 |
3.44e-11 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 65.62 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 27 TLTAAITTVLAKTYGGSArafdQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMIARAFDQIDNAPEE 106
Cdd:CHL00189 198 IIDISIISQVADDFGINI----ISEEKNNINEKTSNLDNTSAFTENSINRPPIVTILGHVDHGKTTLLDKIRKTQIAQKE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 107 kARGIT--INTSHVEYD--TPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyII 182
Cdd:CHL00189 274 -AGGITqkIGAYEVEFEykDENQKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-II 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 183 VFLNKCDmvddeeLLELVEMEVRELLSQYDFP----GDDTPIVRGSALKA------------------LEGDAEWEAKII 240
Cdd:CHL00189 352 VAINKID------KANANTERIKQQLAKYNLIpekwGGDTPMIPISASQGtnidklletilllaeiedLKADPTQLAQGI 425
|
....*..
gi 821669726 241 ELAGHLD 247
Cdd:CHL00189 426 ILEAHLD 432
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-189 |
5.88e-11 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 64.76 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 18 IGHVDHGKTTLTAAI------TTVLAKTYGGSARAfdqiDNAPEEKARGITINTS--HVEYDtptrhyahvdcpghadyv 89
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfytgaIHRIGEVEDGTTTM----DFMPEERERGISITSAatTCEWK------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 90 knmiarafdqidnapeekarGITINTshveydtptrhyahVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREH 169
Cdd:PRK12740 59 --------------------GHKINL--------------IDTPGHVDFTGEVERALRVLDGAVVVVCAVGGVEPQTETV 104
|
170 180
....*....|....*....|
gi 821669726 170 ILLGRQVGVPyIIVFLNKCD 189
Cdd:PRK12740 105 WRQAEKYGVP-RIIFVNKMD 123
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
351-489 |
6.84e-11 |
|
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).
Pssm-ID: 275447 [Multi-domain] Cd Length: 102 Bit Score: 58.94 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 351 PHTKFESEVYILSKDEggrhtPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKmvvtlihpiamddglrfaireg 430
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEKKP---------------------- 54
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 821669726 431 gyfrttdvtgtielpegVEMVMPGDNIKMVVTLIHPIAMDDG------LRFAIREGGRTVGAGVV 489
Cdd:cd01513 55 -----------------PDSLQPGENGTVEVELQKPVVLERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
101-189 |
1.34e-10 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 61.84 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 101 DNAPEEKARGITINTS--HVEYDTpTRHYAhVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGV 178
Cdd:cd04170 40 DYDPEEKKRKMSIETSvaPLEWNG-HKINL-IDTPGYADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKL 117
|
90
....*....|.
gi 821669726 179 PyIIVFLNKCD 189
Cdd:cd04170 118 P-RIIFINKMD 127
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
260-344 |
2.65e-10 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation 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: 293899 [Multi-domain] Cd Length: 84 Bit Score: 56.74 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 260 PFLLPIEDVFSiSGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTTCTGVEMFRKlLDEGRAGENVGVLLRGIKREEIER 339
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQP 78
|
....*
gi 821669726 340 GQVLA 344
Cdd:cd03698 79 GDILS 83
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-189 |
4.18e-10 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 62.28 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLTAAITTvlaktYGGSARAFDQIDnapeekaRGITintshveydtptrhyahvdcpgHADYVknmi 93
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILF-----YTGKIHKMGEVE-------DGTT----------------------VTDWM---- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 94 arafdqidnaPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLG 173
Cdd:PRK13351 52 ----------PQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQA 121
|
170
....*....|....*.
gi 821669726 174 RQVGVPyIIVFLNKCD 189
Cdd:PRK13351 122 DRYGIP-RLIFINKMD 136
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
261-344 |
4.36e-10 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 56.07 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 261 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEI----VGikETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREE 336
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLgpdaDG--KFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRES 78
|
....*...
gi 821669726 337 IERGQVLA 344
Cdd:cd03694 79 LRKGMVLV 86
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
3-189 |
1.22e-09 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 60.68 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 3 KEKFERTKPHVNVGTIGHVDHGKTTLT---AAITTVLAKTYGGSARAFDqIDNapEEKARGITINTSHVeydtptrhyAH 79
Cdd:TIGR00490 10 KELMWKPKFIRNIGIVAHIDHGKTTLSdnlLAGAGMISEELAGQQLYLD-FDE--QEQERGITINAANV---------SM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 80 VDCPGHADYVKNMIarafdqidnapeekargitintshveydtptrhyahvDCPGHADYVKNMITGAAQMDGAILVVAAT 159
Cdd:TIGR00490 78 VHEYEGNEYLINLI-------------------------------------DTPGHVDFGGDVTRAMRAVDGAIVVVCAV 120
|
170 180 190
....*....|....*....|....*....|..
gi 821669726 160 DGPMPQTrEHILlgRQVGVPYI--IVFLNKCD 189
Cdd:TIGR00490 121 EGVMPQT-ETVL--RQALKENVkpVLFINKVD 149
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
260-343 |
3.05e-09 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 53.64 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 260 PFLLPIEDVFSisGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTT---CTGVEMfrkllDEGRAGENVGVLLRGIKREE 336
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTgiyIDEEEV-----DSAKPGENVKLKLKGVEEED 73
|
....*..
gi 821669726 337 IERGQVL 343
Cdd:cd04089 74 ISPGFVL 80
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
14-189 |
4.14e-09 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 59.29 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLTAAITT---VLAKTYGGSARAfdqIDNAPEEKARGITINTS----HVEYDTPtrhyahvDCPGHA 86
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTDSLVCkagIISSKNAGDARF---TDTRADEQERGITIKSTgislYYEHDLE-------DGDDKQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 87 DYVKNMIarafdqidnapeekargitintshveydtptrhyahvDCPGHADYvKNMITGAAQM-DGAILVVAATDGPMPQ 165
Cdd:PTZ00416 91 PFLINLI-------------------------------------DSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQ 132
|
170 180
....*....|....*....|....*.
gi 821669726 166 TrEHILlgRQVGVPYI--IVFLNKCD 189
Cdd:PTZ00416 133 T-ETVL--RQALQERIrpVLFINKVD 155
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
260-343 |
6.12e-09 |
|
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.
Pssm-ID: 293912 [Multi-domain] Cd Length: 84 Bit Score: 52.90 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 260 PFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAktTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIER 339
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETA--TVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
|
....
gi 821669726 340 GQVL 343
Cdd:cd16267 79 GSIL 82
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-189 |
1.21e-07 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 52.27 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLtaaITTVLAKTYggsarafdqidnapeekargiTINTSHVEYDTPTRHYahvdcpghadyvknmi 93
Cdd:cd04167 2 NVCIAGHLHHGKTSL---LDMLIEQTH---------------------KRTPSVKLGWKPLRYT---------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 94 arafdqiDNAPEEKARGITINTSHVEYDTP-TRHYAHV----DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTRE 168
Cdd:cd04167 42 -------DTRKDEQERGISIKSNPISLVLEdSKGKSYLiniiDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTER 114
|
170 180
....*....|....*....|.
gi 821669726 169 HILLGRQVGVPYIIVfLNKCD 189
Cdd:cd04167 115 LIRHAIQEGLPMVLV-INKID 134
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-190 |
2.15e-07 |
|
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: 51.00 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLTAAIttvLAKTYGGSARAF-DQI-DNAPEEKARGITINTSHVEYDtptrhYAHVDcpGHaDYVKN 91
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRL---LELTGTVSEREMkEQVlDSMDLERERGITIKAQAVRLF-----YKAKD--GE-EYLLN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 92 MIarafdqidnapeekargitintshveydtptrhyahvDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHIL 171
Cdd:cd01890 71 LI-------------------------------------DTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFY 113
|
170
....*....|....*....
gi 821669726 172 LGRQVGVPyIIVFLNKCDM 190
Cdd:cd01890 114 LALENNLE-IIPVINKIDL 131
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
265-344 |
2.42e-06 |
|
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.
Pssm-ID: 293910 [Multi-domain] Cd Length: 80 Bit Score: 45.36 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 265 IEDVFSISGRgTVVTGRVERGIIKVGEEVeivgIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGikREEIERGQVLA 344
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKV----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVLE 77
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
14-175 |
5.85e-06 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 48.95 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLT---AAITTVLAKTYGGSARAfdqIDNAPEEKARGITINTSHVE--YDTPTRHYAHV--DCPGHa 86
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTdslVAAAGIIAQEVAGDVRM---TDTRADEAERGITIKSTGISlyYEMTDESLKDFkgERDGN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 87 DYVKNMIarafdqidnapeekargitintshveydtptrhyahvDCPGHADYvKNMITGAAQM-DGAILVVAATDGPMPQ 165
Cdd:PLN00116 97 EYLINLI-------------------------------------DSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQ 138
|
170
....*....|
gi 821669726 166 TrEHILlgRQ 175
Cdd:PLN00116 139 T-ETVL--RQ 145
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-189 |
1.21e-05 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 46.72 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 14 NVGTIGHVDHGKTTLTAAI------TTVLAKTYGGSArafdQIDNAPEEKARGITInTShveydtptrhyAHVDCPGHaD 87
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyytgrIHKIGEVHGGGA----TMDWMEQERERGITI-QS-----------AATTCFWK-D 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 88 YVKNMIarafdqidnapeekargitintshveydtptrhyahvDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTr 167
Cdd:cd01886 64 HRINII-------------------------------------DTPGHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQT- 105
|
170 180
....*....|....*....|....*
gi 821669726 168 ehILLGRQV---GVPYIIvFLNKCD 189
Cdd:cd01886 106 --ETVWRQAdryGVPRIA-FVNKMD 127
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
18-190 |
1.42e-05 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 46.82 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 18 IGHVDHGKTTLTAAITtvlakTYGGSarafdqIDNAPEEKARGITINTShveydtptrhyahvdcpghADYVKnMiaraf 97
Cdd:cd04169 8 ISHPDAGKTTLTEKLL-----LFGGA------IQEAGAVKARKSRKHAT-------------------SDWME-I----- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 98 dqidnapeEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVG 177
Cdd:cd04169 52 --------EKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRG 123
|
170
....*....|...
gi 821669726 178 VPyIIVFLNKCDM 190
Cdd:cd04169 124 IP-IITFINKLDR 135
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
111-241 |
4.52e-05 |
|
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: 43.98 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 111 ITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQM-----DGAILVVAATDGPMPQTREHILLGRQV--GVPyIIV 183
Cdd:cd00882 33 RDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELARLllrgaDLILLVVDSTDRESEEDAKLLILRRLRkeGIP-IIL 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 821669726 184 FLNKCDMVDDEELLELVEMEVRELLSqydfpgdDTPIVRGSALKaLEGDAEWEAKIIE 241
Cdd:cd00882 112 VGNKIDLLEEREVEELLRLEELAKIL-------GVPVFEVSAKT-GEGVDELFEKLIE 161
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
19-189 |
5.78e-05 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 45.56 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 19 GHVDHGKTTLTAAI--TTVLAKTYGGsarafdqidnapeekargIT--INTSHVEYDTptrhyahvdcpghadyVKNMIA 94
Cdd:PRK04004 13 GHVDHGKTTLLDKIrgTAVAAKEAGG------------------ITqhIGATEVPIDV----------------IEKIAG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 95 RAFDQIDNapEEKARGITIntshveydtptrhyahVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGR 174
Cdd:PRK04004 59 PLKKPLPI--KLKIPGLLF----------------IDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILK 120
|
170
....*....|....*
gi 821669726 175 QVGVPYIIVfLNKCD 189
Cdd:PRK04004 121 RRKTPFVVA-ANKID 134
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
261-345 |
6.94e-05 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 41.40 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 261 FLLPIEDV--FSISGRGtvVTGRVERGIIKVGEEVEIvgIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLrgiKRE-EI 337
Cdd:cd03695 1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTV--LPSGKTSRVKSIVTFDGELDSAGAGEAVTLTL---EDEiDV 73
|
....*...
gi 821669726 338 ERGQVLAK 345
Cdd:cd03695 74 SRGDLIVR 81
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-189 |
1.40e-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: 42.36 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 13 VNVGTIGHVDHGKTTLTaaitTVLAKTYGgsarafdqidnAPEEKARGIT--INTSHVEYDTPTRHYAHVDCPGHADYvk 90
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLL----NSLLGNKG-----------SITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDY-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 91 NMIARAfdqidnapeekargitintshveydtptrhyahvdcpghadYVKNMITGAAQMDGAILVVAATDGPMPQTREHI 170
Cdd:TIGR00231 65 DAIRRL-----------------------------------------YYPQVERSLRVFDIVILVLDVEEILEKQTKEII 103
|
170
....*....|....*....
gi 821669726 171 LLgRQVGVPyIIVFLNKCD 189
Cdd:TIGR00231 104 HH-ADSGVP-IILVGNKID 120
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
146-243 |
3.13e-03 |
|
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: 38.38 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 146 AAQMDGAILVVAATDGPMPQTREHILLgRQVGVPYIIVFlNKCDMVDDEELLELVEMEVRELLSQYdfpgddtPIVRGSA 225
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVL-NKIDLVPESEEEELLRERKLELLPDL-------PVIAVSA 144
|
90
....*....|....*...
gi 821669726 226 LKaLEGDAEWEAKIIELA 243
Cdd:cd00880 145 LP-GEGIDELRKKIAELL 161
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
15-189 |
4.32e-03 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 39.80 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 15 VGTIGHVDHGKTTLTAAI--TTVLAKTYGGSarafdqidnapeekargitintshveydtpTRHYAHVDCPghadyvknm 92
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIrgTAVVKKEAGGI------------------------------TQHIGASEVP--------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821669726 93 iaraFDQIdnapeEKARGITINTSHVEYDTPTRHYahVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILL 172
Cdd:TIGR00491 48 ----TDVI-----EKICGDLLKSFKIKLKIPGLLF--IDTPGHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEALNI 116
|
170
....*....|....*..
gi 821669726 173 GRQVGVPYiIVFLNKCD 189
Cdd:TIGR00491 117 LRSRKTPF-VVAANKID 132
|
|
| |
