|
Name |
Accession |
Description |
Interval |
E-value |
| tufA |
CHL00071 |
elongation factor Tu |
1-412 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 655.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 1 MIKQIFERTKPHINIGTIGHIDHGKTTLTAVITKILAKYNRAKACNYEDIDSAPEEKLRGITINTAHVEYESTIRHYAHI 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 81 DCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVEDPELLELVELEIRDLLDT 160
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 161 CGYK--DTSIVKGSALKALEALDKLTTVEELEtNKWIKDILNLIYTIDTDIPTPTRILDKPFFMAIEDVFSITGRGTVVT 238
Cdd:CHL00071 161 YDFPgdDIPIVSGSALLALEALTENPKIKRGE-NKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 239 GKITQGKLKVGSTVHLVGYSyIKKSVTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRRGMVVAEKNTLNAFTKFETE 318
Cdd:CHL00071 240 GRIERGTVKVGDTVEIVGLR-ETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 319 LYVLTSEEGGRHKPFFVGYRPQVYVNTTDVTATIESVLSKKGaeeTTNEMILPGDTVSLKLHLLYPIALDKGMHFALREG 398
Cdd:CHL00071 319 VYILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESFTADDG---SKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREG 395
|
410
....*....|....
gi 1833819254 399 NKTIGAGIVTKLLE 412
Cdd:CHL00071 396 GRTVGAGVVSKILK 409
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-412 |
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: 645.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 1 MIKQIFERTKPHINIGTIGHIDHGKTTLTAVITKILAKYNRAKACNYEDIDSAPEEKLRGITINTAHVEYESTIRHYAHI 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 81 DCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVEDPELLELVELEIRDLLDT 160
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 161 CGY--KDTSIVKGSALKALEALDklttveeleTNKWIKDILNLIYTIDTDIPTPTRILDKPFFMAIEDVFSITGRGTVVT 238
Cdd:COG0050 161 YGFpgDDTPIIRGSALKALEGDP---------DPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 239 GKITQGKLKVGSTVHLVGYSYIKKSVtITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRRGMVVAEKNTLNAFTKFETE 318
Cdd:COG0050 232 GRVERGIIKVGDEVEIVGIRDTQKTV-VTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 319 LYVLTSEEGGRHKPFFVGYRPQVYVNTTDVTATIESvlskkgAEETtnEMILPGDTVSLKLHLLYPIALDKGMHFALREG 398
Cdd:COG0050 311 VYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVITL------PEGV--EMVMPGDNVTMTVELITPIAMEEGLRFAIREG 382
|
410
....*....|....
gi 1833819254 399 NKTIGAGIVTKLLE 412
Cdd:COG0050 383 GRTVGAGVVTKIIE 396
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-412 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 632.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 1 MIKQIFERTKPHINIGTIGHIDHGKTTLTAVITKILAKYNRAKACNYEDIDSAPEEKLRGITINTAHVEYESTIRHYAHI 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 81 DCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVEDPELLELVELEIRDLLDT 160
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 161 CGY--KDTSIVKGSALKALEALDKlttveeletNKWIKDILNLIYTIDTDIPTPTRILDKPFFMAIEDVFSITGRGTVVT 238
Cdd:PRK00049 161 YDFpgDDTPIIRGSALKALEGDDD---------EEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 239 GKITQGKLKVGSTVHLVGYSYIKKSvTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRRGMVVAEKNTLNAFTKFETE 318
Cdd:PRK00049 232 GRVERGIIKVGEEVEIVGIRDTQKT-TVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 319 LYVLTSEEGGRHKPFFVGYRPQVYVNTTDVTATIEsvlSKKGAeettnEMILPGDTVSLKLHLLYPIALDKGMHFALREG 398
Cdd:PRK00049 311 VYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIE---LPEGV-----EMVMPGDNVEMTVELIAPIAMEEGLRFAIREG 382
|
410
....*....|....
gi 1833819254 399 NKTIGAGIVTKLLE 412
Cdd:PRK00049 383 GRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-412 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 616.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 1 MIKQIFERTKPHINIGTIGHIDHGKTTLTAVITKILAKYNRAKACNYEDIDSAPEEKLRGITINTAHVEYESTIRHYAHI 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 81 DCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVEDPELLELVELEIRDLLDT 160
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 161 CGYK--DTSIVKGSALKALEALDKlttveeletNKWIKDILNLIYTIDTDIPTPTRILDKPFFMAIEDVFSITGRGTVVT 238
Cdd:PRK12735 161 YDFPgdDTPIIRGSALKALEGDDD---------EEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 239 GKITQGKLKVGSTVHLVGYSYIKKSvTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRRGMVVAEKNTLNAFTKFETE 318
Cdd:PRK12735 232 GRVERGIVKVGDEVEIVGIKETQKT-TVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 319 LYVLTSEEGGRHKPFFVGYRPQVYVNTTDVTATIEsvlskkgAEETTnEMILPGDTVSLKLHLLYPIALDKGMHFALREG 398
Cdd:PRK12735 311 VYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGTIE-------LPEGV-EMVMPGDNVKMTVELIAPIAMEEGLRFAIREG 382
|
410
....*....|....
gi 1833819254 399 NKTIGAGIVTKLLE 412
Cdd:PRK12735 383 GRTVGAGVVAKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-412 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 598.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 1 MIKQIFERTKPHINIGTIGHIDHGKTTLTAVITKILAKYNRAKACNYEDIDSAPEEKLRGITINTAHVEYESTIRHYAHI 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 81 DCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVEDPELLELVELEIRDLLDT 160
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 161 CGY--KDTSIVKGSALKALEALDklttveeletnKWIKDILNLIYTIDTDIPTPTRILDKPFFMAIEDVFSITGRGTVVT 238
Cdd:PRK12736 161 YDFpgDDIPVIRGSALKALEGDP-----------KWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 239 GKITQGKLKVGSTVHLVGYSYIKKSvTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRRGMVVAEKNTLNAFTKFETE 318
Cdd:PRK12736 230 GRVERGTVKVGDEVEIVGIKETQKT-VVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 319 LYVLTSEEGGRHKPFFVGYRPQVYVNTTDVTATIEsvlskkgAEETTnEMILPGDTVSLKLHLLYPIALDKGMHFALREG 398
Cdd:PRK12736 309 VYILTKEEGGRHTPFFNNYRPQFYFRTTDVTGSIE-------LPEGT-EMVMPGDNVTITVELIHPIAMEQGLKFAIREG 380
|
410
....*....|....
gi 1833819254 399 NKTIGAGIVTKLLE 412
Cdd:PRK12736 381 GRTVGAGTVTEILD 394
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-412 |
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: 560.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 1 MIKQIFERTKPHINIGTIGHIDHGKTTLTAVITKILAKYNRAKACNYEDIDSAPEEKLRGITINTAHVEYESTIRHYAHI 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 81 DCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVEDPELLELVELEIRDLLDT 160
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 161 CGY--KDTSIVKGSALKALEAldklttveeleTNKWIKDILNLIYTIDTDIPTPTRILDKPFFMAIEDVFSITGRGTVVT 238
Cdd:TIGR00485 161 YDFpgDDTPIIRGSALKALEG-----------DAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 239 GKITQGKLKVGSTVHLVGYSYIKKSvTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRRGMVVAEKNTLNAFTKFETE 318
Cdd:TIGR00485 230 GRVERGIIKVGEEVEIVGLKDTRKT-TVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 319 LYVLTSEEGGRHKPFFVGYRPQVYVNTTDVTATIEsvlskkgaEETTNEMILPGDTVSLKLHLLYPIALDKGMHFALREG 398
Cdd:TIGR00485 309 VYVLSKEEGGRHTPFFSGYRPQFYFRTTDVTGTIE--------LPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREG 380
|
410
....*....|....
gi 1833819254 399 NKTIGAGIVTKLLE 412
Cdd:TIGR00485 381 GRTVGAGVVSKILE 394
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
5-412 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 540.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 5 IFERTKPHINIGTIGHIDHGKTTLTAVITKILAKYNRAKACNYEDIDSAPEEKLRGITINTAHVEYESTIRHYAHIDCPG 84
Cdd:PLN03127 54 TFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 85 HADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVEDPELLELVELEIRDLLDTcgYK 164
Cdd:PLN03127 134 HADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSF--YK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 165 ----DTSIVKGSALKALEALDklttvEELETNKwikdILNLIYTIDTDIPTPTRILDKPFFMAIEDVFSITGRGTVVTGK 240
Cdd:PLN03127 212 fpgdEIPIIRGSALSALQGTN-----DEIGKNA----ILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 241 ITQGKLKVGSTVHLVGYS-YIKKSVTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRRGMVVAEKNTLNAFTKFETEL 319
Cdd:PLN03127 283 VEQGTIKVGEEVEIVGLRpGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEI 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 320 YVLTSEEGGRHKPFFVGYRPQVYVNTTDVTATIESvlskkgAEETtnEMILPGDTVSLKLHLLYPIALDKGMHFALREGN 399
Cdd:PLN03127 363 YVLTKDEGGRHTPFFSNYRPQFYLRTADVTGKVEL------PEGV--KMVMPGDNVTAVFELISPVPLEPGQRFALREGG 434
|
410
....*....|...
gi 1833819254 400 KTIGAGIVTKLLE 412
Cdd:PLN03127 435 RTVGAGVVSKVLS 447
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
6-412 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 524.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 6 FERTKPHINIGTIGHIDHGKTTLTAVITKILAKYNRAKACNYEDIDSAPEEKLRGITINTAHVEYESTIRHYAHIDCPGH 85
Cdd:PLN03126 75 FERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 86 ADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVEDPELLELVELEIRDLLDTCGY-- 163
Cdd:PLN03126 155 ADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFpg 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 164 KDTSIVKGSALKALEALDKLTTVEELEtNKWIKDILNLIYTIDTDIPTPTRILDKPFFMAIEDVFSITGRGTVVTGKITQ 243
Cdd:PLN03126 235 DDIPIISGSALLALEALMENPNIKRGD-NKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVER 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 244 GKLKVGSTVHLVGYSYiKKSVTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRRGMVVAEKNTLNAFTKFETELYVLT 323
Cdd:PLN03126 314 GTVKVGETVDIVGLRE-TRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLK 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 324 SEEGGRHKPFFVGYRPQVYVNTTDVTATIESVLSKKGAEettNEMILPGDTVSLKLHLLYPIALDKGMHFALREGNKTIG 403
Cdd:PLN03126 393 KEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSIMNDKDEE---SKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVG 469
|
....*....
gi 1833819254 404 AGIVTKLLE 412
Cdd:PLN03126 470 AGVIQSIIE 478
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-212 |
8.04e-114 |
|
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: 330.70 E-value: 8.04e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 11 PHINIGTIGHIDHGKTTLTAVITKILAKYNRAKACNYEDIDSAPEEKLRGITINTAHVEYESTIRHYAHIDCPGHADYIK 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 91 NMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVEDPELLELVELEIRDLLDTCGY--KDTSI 168
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFdgDDTPI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1833819254 169 VKGSALKALEALDKlttveeletNKWIKDILNLIYTIDTDIPTP 212
Cdd:cd01884 161 VRGSALKALEGDDP---------NKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
8-410 |
1.05e-80 |
|
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: 254.47 E-value: 1.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 8 RTKPHINIGTIGHIDHGKTTLT--------AVITKILAKYNR-AKACNYED------IDSAPEEKLRGITINTAHVEYES 72
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLVgrllyetgAIDEHIIEKYEEeAEKKGKESfkfawvMDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 73 TIRHYAHIDCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVE-DPELLELVE 151
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 152 LEIRDLLDTCGYK--DTSIVKGSALKAlealDKLTtvEELETNKWIKDiLNLIYTIDtDIPTPTRILDKPFFMAIEDVFS 229
Cdd:COG5256 163 EEVSKLLKMVGYKvdKIPFIPVSAWKG----DNVV--KKSDNMPWYNG-PTLLEALD-NLKEPEKPVDKPLRIPIQDVYS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 230 ITGRGTVVTGKITQGKLKVGSTV-----HLVGysyikksvTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRRGMVVA 304
Cdd:COG5256 235 ISGIGTVPVGRVETGVLKVGDKVvfmpaGVVG--------EVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 305 EKNTLNAFTK-FETELYVLtseeggrHKP--FFVGYRPQVYVNTTDVTATIESVLSKK----GAEETTN-EMILPGDTVS 376
Cdd:COG5256 307 HPDNPPTVAEeFTAQIVVL-------QHPsaITVGYTPVFHVHTAQVACTFVELVSKLdprtGQVKEENpQFLKTGDAAI 379
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1833819254 377 LKLHLLYPIALDK-------GmHFALREGNKTIGAGIVTKL 410
Cdd:COG5256 380 VKIKPTKPLVIEKfkefpqlG-RFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-410 |
7.05e-75 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 239.44 E-value: 7.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 8 RTKPHINIGTIGHIDHGKTTLT--------AVITKILAKYNR-AKACNYED------IDSAPEEKLRGITINTAHVEYES 72
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVgrllyetgAIDEHIIEELREeAKEKGKESfkfawvMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 73 TIRHYAHIDCPGHADYIKNMITGAAQMEGAILLVSAVD--GPMPQTREHLLLAKQIGVNYLVVFLNKIDQVE-DPELLEL 149
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 150 VELEIRDLLDTCGYK--DTSIVKGSALKAlealDKLttVEELETNKWIKDIlNLIYTIDtDIPTPTRILDKPFFMAIEDV 227
Cdd:PRK12317 162 VKEEVSKLLKMVGYKpdDIPFIPVSAFEG----DNV--VKKSENMPWYNGP-TLLEALD-NLKPPEKPTDKPLRIPIQDV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 228 FSITGRGTVVTGKITQGKLKVGSTVhlvgySYIKKSVT--ITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRRGMVVAE 305
Cdd:PRK12317 234 YSISGVGTVPVGRVETGVLKVGDKV-----VFMPAGVVgeVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGH 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 306 KNtlNAFT---KFETELYVLtseeggrHKP--FFVGYRPQVYVNTTDVTATIESVLSK----KGAEETTN-EMILPGDTV 375
Cdd:PRK12317 309 PD--NPPTvaeEFTAQIVVL-------QHPsaITVGYTPVFHAHTAQVACTFEELVKKldprTGQVAEENpQFIKTGDAA 379
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1833819254 376 SLKLHLLYPIALDK-------GmHFALREGNKTIGAGIVTKL 410
Cdd:PRK12317 380 IVKIKPTKPLVIEKvkeipqlG-RFAIRDMGQTIAAGMVIDV 420
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-407 |
3.14e-69 |
|
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: 230.19 E-value: 3.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 13 INIGTIGHIDHGKTTLTAVITKIlakynrakacnyeDIDSAPEEKLRGITINT--AHVEYESTiRHYAHIDCPGHADYIK 90
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGI-------------DTDRLKEEKKRGITIDLgfAYLPLPDG-RRLGFVDVPGHEKFIK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 91 NMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVeDPELLELVELEIRDLLDTCGYKD----- 165
Cdd:COG3276 67 NMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGTFLEDapivp 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 166 TSIVKGSALKAL-EALDKLTTveeletnkwikdilnliytidtdiPTPTRILDKPFFMAIEDVFSITGRGTVVTGKITQG 244
Cdd:COG3276 146 VSAVTGEGIDELrAALDALAA------------------------AVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 245 KLKVGSTVHLVGysyIKKSVTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRRGMVVAEKNTLNAFTKFETELYVLTS 324
Cdd:COG3276 202 TVRVGDELELLP---SGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 325 EeggrHKPFFVGYRPQVYVNTTDVTATIeSVLSKkgaeettnEMILPGDTVSLKLHLLYPIALDKGMHFALREGN--KTI 402
Cdd:COG3276 279 A----PRPLKHWQRVHLHHGTAEVLARV-VLLDR--------EELAPGEEALAQLRLEEPLVAARGDRFILRDYSprRTI 345
|
....*
gi 1833819254 403 GAGIV 407
Cdd:COG3276 346 GGGRV 350
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-183 |
8.06e-66 |
|
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: 208.15 E-value: 8.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 10 KPHINIGTIGHIDHGKTTLTAVITKILAKYNRAKACNYED---IDSAPEEKLRGITINTAHVEYESTIRHYAHIDCPGHA 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 87 DYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNyLVVFLNKIDQVEDPELLELVELEIRDLLDTCGYK-- 164
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDge 159
|
170 180
....*....|....*....|....*
gi 1833819254 165 DTSIVKGSALKA------LEALDKL 183
Cdd:pfam00009 160 FVPVVPGSALKGegvqtlLDALDEY 184
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-318 |
2.89e-47 |
|
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: 170.44 E-value: 2.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 13 INIGTIGHIDHGKTTLTAVITKIlakynrakacnyeDIDSAPEEKLRGITINTAHVEYESTIRHYAHIDCPGHADYIKNM 92
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGI-------------AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 93 ITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVEDPELLELVELEIRDLLDTCGYKDTSIVKGS 172
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIKRTEMFMKQILNSYIFLKNAKIFKTS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 173 AlKALEALDKLTtveeletnkwiKDILNLIYTIDtdiptpTRILDKPFFMAIEDVFSITGRGTVVTGKITQGKLKVGSTV 252
Cdd:TIGR00475 148 A-KTGQGIGELK-----------KELKNLLESLD------IKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNL 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833819254 253 HLVGysyIKKSVTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRRGMV--VAEKNTLNAFTKFETE 318
Cdd:TIGR00475 210 RLLP---INHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLilTPEDPKLRVVVKFIAE 274
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-190 |
1.41e-45 |
|
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: 155.53 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLTAVITKILAKYNRAKACNYEDIDSAPEEKLRGITINTAHVEYESTIRHYAHIDCPGHADYIKNMI 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 94 TGAAQMEGAILLVSAVDGPMPQTREHLLLAKQiGVNYLVVFLNKIDQVeDPELLELVELEIRDLL-----DTCGYKDTSI 168
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLkligfTFLKGKDVPI 158
|
170 180
....*....|....*....|..
gi 1833819254 169 VKGSALKALEALDKLTTVEELE 190
Cdd:cd00881 159 IPISALTGEGIEELLDAIVEHL 180
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
10-407 |
2.53e-45 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 162.22 E-value: 2.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 10 KPHINIGTIGHIDHGKTTLTAVITKILAKYNRAKACNYED---------------IDSAPEEKLRGITINTAHVEYESTI 74
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaaemgkgsfkyawvLDKLKAERERGITIDIALWKFETPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 75 RHYAHIDCPGHADYIKNMITGAAQMEGAILLVSAVDGPMP-------QTREHLLLAKQIGVNYLVVFLNKIDQVE---DP 144
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTvnySQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 145 ELLELVELEIRDLLDTCGYKDTSI--VKGSALKALEALDKLTTVEeletnkWIKDiLNLIYTIDTDIPtPTRILDKPFFM 222
Cdd:PTZ00141 165 ERYDEIKKEVSAYLKKVGYNPEKVpfIPISGWQGDNMIEKSDNMP------WYKG-PTLLEALDTLEP-PKRPVDKPLRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 223 AIEDVFSITGRGTVVTGKITQGKLKVGSTVHL--VGYSYIKKSVtitgiEMFQKTLAEGYAGDNIGILLRGIQKTEVRRG 300
Cdd:PTZ00141 237 PLQDVYKIGGIGTVPVGRVETGILKPGMVVTFapSGVTTEVKSV-----EMHHEQLAEAVPGDNVGFNVKNVSVKDIKRG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 301 MVVAE-KNT-LNAFTKFETELYVLTSEegGRHKPffvGYRPQVYVNTTDVTATIESVLSK------KGAEETTnEMILPG 372
Cdd:PTZ00141 312 YVASDsKNDpAKECADFTAQVIVLNHP--GQIKN---GYTPVLDCHTAHIACKFAEIESKidrrsgKVLEENP-KAIKSG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1833819254 373 DTVSLKLHLLYPIALDKGM------HFALREGNKTIGAGIV 407
Cdd:PTZ00141 386 DAAIVKMVPTKPMCVEVFNeypplgRFAVRDMKQTVAVGVI 426
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
220-304 |
1.62e-40 |
|
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: 138.81 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 220 FFMAIEDVFSITGRGTVVTGKITQGKLKVGSTVHLVGYSYIKKSvTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRR 299
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKT-TVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVER 79
|
....*
gi 1833819254 300 GMVVA 304
Cdd:cd03697 80 GMVLA 84
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
310-407 |
1.03e-38 |
|
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: 134.18 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 310 NAFTKFETELYVLTSEEGGRHKPFFVGYRPQVYVNTTDVTATIESvlskkgaeETTNEMILPGDTVSLKLHLLYPIALDK 389
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIEL--------PEGVEMVMPGDNVKMTVELIHPIALEE 72
|
90
....*....|....*...
gi 1833819254 390 GMHFALREGNKTIGAGIV 407
Cdd:cd03707 73 GLRFAIREGGRTVGAGVV 90
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-169 |
1.72e-38 |
|
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: 138.01 E-value: 1.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLT--------AVITKILAKYNR-AKACNYED------IDSAPEEKLRGITINTAHVEYESTIRHYA 78
Cdd:cd01883 1 NLVVIGHVDAGKSTLTghllyklgGVDKRTIEKYEKeAKEMGKESfkyawvLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 79 HIDCPGHADYIKNMITGAAQMEGAILLVSAVDG-------PMPQTREHLLLAKQIGVNYLVVFLNKIDQVEDPELLE--- 148
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQEryd 160
|
170 180
....*....|....*....|.
gi 1833819254 149 LVELEIRDLLDTCGYKDTSIV 169
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVP 181
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-300 |
8.88e-36 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 138.65 E-value: 8.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 15 IGTIGHIDHGKTTLTAVITKIlakynrakacnyeDIDSAPEEKLRGITINTAHVEY-ESTIRHYAHIDCPGHADYIKNMI 93
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGV-------------NADRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 94 TGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVEDPeLLELVELEIRDLLDTCGYKDTSIVKGSA 173
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEA-RIAEVRRQVKAVLREYGFAEAKLFVTAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 174 LKAlealdklTTVEELETNkwikdILNLiytidtdiPTPTRILDKPFFMAIEDVFSITGRGTVVTGKITQGKLKVGSTVH 253
Cdd:PRK10512 149 TEG-------RGIDALREH-----LLQL--------PEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLW 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1833819254 254 LVGysyIKKSVTITGIEMfQKTLAE-GYAGDNIGILLRG-IQKTEVRRG 300
Cdd:PRK10512 209 LTG---VNKPMRVRGLHA-QNQPTEqAQAGQRIALNIAGdAEKEQINRG 253
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
8-407 |
2.08e-35 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 135.60 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 8 RTKPHINIGTIGHIDHGKTTLTAVITKILAKYNRAKACNYED---------------IDSAPEEKLRGITINTAHVEYES 72
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKeaaemnkrsfkyawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 73 TIRHYAHIDCPGHADYIKNMITGAAQMEGAILLVSAVDGPMP-------QTREHLLLAKQIGVNYLVVFLNKIDQVEDPE 145
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTPKY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 146 LLELVELEIRDL---LDTCGYKDTSI--VKGSALKALEALDKLTTVEeletnkWIKDIlNLIYTIDtDIPTPTRILDKPF 220
Cdd:PLN00043 163 SKARYDEIVKEVssyLKKVGYNPDKIpfVPISGFEGDNMIERSTNLD------WYKGP-TLLEALD-QINEPKRPSDKPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 221 FMAIEDVFSITGRGTVVTGKITQGKLKVGStvhLVGYSYIKKSVTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRRG 300
Cdd:PLN00043 235 RLPLQDVYKIGGIGTVPVGRVETGVIKPGM---VVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 301 MVVAEKNTLNAFTKFETELYVLTSEEGGRhkpFFVGYRPQVYVNTTDVTATIESVLSK----KGAE-ETTNEMILPGDTV 375
Cdd:PLN00043 312 YVASNSKDDPAKEAANFTSQVIIMNHPGQ---IGNGYAPVLDCHTSHIAVKFAEILTKidrrSGKElEKEPKFLKNGDAG 388
|
410 420 430
....*....|....*....|....*....|....*...
gi 1833819254 376 SLKLHLLYPIALDKGMH------FALREGNKTIGAGIV 407
Cdd:PLN00043 389 FVKMIPTKPMVVETFSEypplgrFAVRDMRQTVAVGVI 426
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-183 |
1.68e-34 |
|
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: 125.80 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 15 IGTIGHIDHGKTTLTAVITKIlakynrakacnyeDIDSAPEEKLRGITINT--AHVEYESTiRHYAHIDCPGHADYIKNM 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLgfAYLDLPDG-KRLGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 93 ITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVeDPELLELVELEIRDLLDTCGYKD-----TS 167
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFLADapifpVS 146
|
170
....*....|....*..
gi 1833819254 168 IVKGSALKAL-EALDKL 183
Cdd:cd04171 147 SVTGEGIEELkNYLDEL 163
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
7-249 |
8.05e-34 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 130.36 E-value: 8.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 7 ERTKPHINIGTIGHIDHGKTTLTAVITKILAkynrakacnyediDSAPEEKLRGITI-------------NTAHVEYEST 73
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIrlgyadatirkcpDCEEPEAYTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 74 -------------IRHYAHIDCPGHADYIKNMITGAAQMEGAILLVSAVDG-PMPQTREHLLLAKQIGVNYLVVFLNKID 139
Cdd:PRK04000 71 epkcpncgsetelLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 140 QVeDPELLELVELEIRDLLDTCGYKDTSIVKGSALKalealdklttveelETNKWIkdilnLIYTIDTDIPTPTRILDKP 219
Cdd:PRK04000 151 LV-SKERALENYEQIKEFVKGTVAENAPIIPVSALH--------------KVNIDA-----LIEAIEEEIPTPERDLDKP 210
|
250 260 270
....*....|....*....|....*....|....*...
gi 1833819254 220 FFMAIEDVFSITGRGT--------VVTGKITQGKLKVG 249
Cdd:PRK04000 211 PRMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVG 248
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
313-410 |
1.25e-33 |
|
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: 121.22 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 313 TKFETELYVLTSEEGGRHKPFFVGYRPQVYVNTTDVTATIESVLSKKGAEETT--NEMILPGDTVSLKLHLLYPIALDKG 390
Cdd:pfam03143 6 TKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVELLHKLDPGGVSenPEFVMPGDNVIVTVELIKPIALEKG 85
|
90 100
....*....|....*....|
gi 1833819254 391 MHFALREGNKTIGAGIVTKL 410
Cdd:pfam03143 86 QRFAIREGGRTVAAGVVTEI 105
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-412 |
4.24e-29 |
|
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: 117.50 E-value: 4.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 1 MIKQIFERTKPHINIG-----TIGHIDHGKTTL-------TAVIT--KILAKYNRAKACNYEDIDSAP------EEKLRG 60
Cdd:COG2895 1 MSTDIEAYLAQHENKDllrfiTCGSVDDGKSTLigrllydTKSIFedQLAALERDSKKRGTQEIDLALltdglqAEREQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 61 ITINTAHVeYEST-IRHYAHIDCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKID 139
Cdd:COG2895 81 ITIDVAYR-YFSTpKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 140 QVE-DPELLELVELEIRDLLDTCGYKDTSIVKGSALKAlealDKLTT-------------VEELETnkwikdilnliyti 205
Cdd:COG2895 160 LVDySEEVFEEIVADYRAFAAKLGLEDITFIPISALKG----DNVVErsenmpwydgptlLEHLET-------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 206 dtdIPTPTRILDKPFFMAIEDV--FSITGRGtvVTGKITQGKLKVGSTVhLVGYSyiKKSVTITGIEMFQKTLAEGYAGD 283
Cdd:COG2895 222 ---VEVAEDRNDAPFRFPVQYVnrPNLDFRG--YAGTIASGTVRVGDEV-VVLPS--GKTSTVKSIVTFDGDLEEAFAGQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 284 NIGILLrgiqKTE--VRRG-MVVAEKNTLNAFTKFETELYVLTSEeggrhkPFFVGYRPQVYVNTTDVTATIESVLSKKG 360
Cdd:COG2895 294 SVTLTL----EDEidISRGdVIVAADAPPEVADQFEATLVWMDEE------PLLPGRKYLLKHGTRTVRATVTAIKYRID 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833819254 361 AEETTNEmilPGDTVSL------KLHLLYPIALDKGMH------FAL--REGNKTIGAGIVTKLLE 412
Cdd:COG2895 364 VNTLEHE---AADSLELndigrvTLRLAEPIAFDPYADnratgsFILidRLTNATVGAGMIRGALR 426
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
314-410 |
2.47e-28 |
|
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: 106.93 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 314 KFETELYVLTSEEGGRHKPFFVGYRPQVYVNTTDVTATIESVLSKkgaeettnEMILPGDTVSLKLHLLYPIALDKGMHF 393
Cdd:cd03706 5 HFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGK--------EMVMPGEDTSVKLTLLKPMVLEKGQRF 76
|
90
....*....|....*..
gi 1833819254 394 ALREGNKTIGAGIVTKL 410
Cdd:cd03706 77 TLREGGRTIGTGVVTKL 93
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-287 |
1.87e-26 |
|
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: 111.62 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLtavITKIL--AKYNRAKACNYEDI-DSAPEEKLRGITI---NTAhVEYESTirHYAHIDCPGHAD 87
Cdd:TIGR01394 3 NIAIIAHVDHGKTTL---VDALLkqSGTFRANEAVAERVmDSNDLERERGITIlakNTA-IRYNGT--KINIVDTPGHAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 88 Y------IKNMItgaaqmEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVfLNKID-------QVEDpellelvelEI 154
Cdd:TIGR01394 77 FggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDrpsarpdEVVD---------EV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 155 RDLLDTCGYKDTS----IVKGSalkALEALDKLTTVEELETnkwIKDILNliyTIDTDIPTPTRILDKPFFMAIE--DVF 228
Cdd:TIGR01394 141 FDLFAELGADDEQldfpIVYAS---GRAGWASLDLDDPSDN---MAPLFD---AIVRHVPAPKGDLDEPLQMLVTnlDYD 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1833819254 229 SITGRgtVVTGKITQGKLKVGSTVHLVGYSYIKKSVTITGIEMFQ----KTLAEGYAGDNIGI 287
Cdd:TIGR01394 212 EYLGR--IAIGRVHRGTVKKGQQVALMKRDGTIENGRISKLLGFEglerVEIDEAGAGDIVAV 272
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-214 |
5.47e-25 |
|
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: 101.19 E-value: 5.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 13 INIGTIGHIDHGKTTLTAVITKILAKYNRakacnyedidsapEEKLRGITI-----------------NTAHVEYEST-- 73
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWTVRHK-------------EELKRNITIklgyanakiykcpncgcPRPYDTPECEcp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 74 --------IRHYAHIDCPGHADYIKNMITGAAQMEGAILLVSAVDG-PMPQTREHLLLAKQIGVNYLVVFLNKIDQVeDP 144
Cdd:cd01888 68 gcggetklVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLV-KE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 145 ELLELVELEIRDLLDTCGYKDTSIVKGSALkalealdklttveeLETNkwikdILNLIYTIDTDIPTPTR 214
Cdd:cd01888 147 EQALENYEQIKEFVKGTIAENAPIIPISAQ--------------LKYN-----IDVLCEYIVKKIPTPPR 197
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-287 |
4.83e-24 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 104.33 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLtavITKIL--AKYNRAKACNYEDI-DSAPEEKLRGITI---NTAhVEYEST---IrhyahIDCPG 84
Cdd:COG1217 8 NIAIIAHVDHGKTTL---VDALLkqSGTFRENQEVAERVmDSNDLERERGITIlakNTA-VRYKGVkinI-----VDTPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 85 HADY------IKNMItgaaqmEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVfLNKID-------QVEDpellelve 151
Cdd:COG1217 79 HADFggeverVLSMV------DGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVV-INKIDrpdarpdEVVD-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 152 lEIRDLLDTCGYKDT----SIVKGSALKALEALDklttVEELETNkwIKDILNLIytIDTdIPTPTRILDKPFFMAiedV 227
Cdd:COG1217 144 -EVFDLFIELGATDEqldfPVVYASARNGWASLD----LDDPGED--LTPLFDTI--LEH-VPAPEVDPDGPLQML---V 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1833819254 228 FSI-----TGRgtVVTGKITQGKLKVGSTVHLVGYSYIKKSVTITGIEMFQ----KTLAEGYAGDNIGI 287
Cdd:COG1217 211 TNLdysdyVGR--IAIGRIFRGTIKKGQQVALIKRDGKVEKGKITKLFGFEglerVEVEEAEAGDIVAI 277
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-252 |
1.02e-23 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 102.39 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 13 INIGTIGHIDHGKTTLTAVITKILA-KYNRakacnyedidsapeEKLRGITIN-----------------TAHVEYEST- 73
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKTvRFKR--------------EKVRNITIKlgyanakiykcpkcprpTCYQSYGSSk 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 74 ---------------IRHYAHIDCPGHADYIKNMITGAAQMEGAILLVSAVDG-PMPQTREHLLLAKQIGVNYLVVFLNK 137
Cdd:PTZ00327 101 pdnppcpgcghkmtlKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 138 IDQVEDpELLELVELEIRDLLDTCGYKDTSIVKGSALkalealdklttveeletnkwikdilnLIYTID-------TDIP 210
Cdd:PTZ00327 181 IDLVKE-AQAQDQYEEIRNFVKGTIADNAPIIPISAQ--------------------------LKYNIDvvleyicTQIP 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1833819254 211 TPTRILDKPFFMAI----------EDVFSItgRGTVVTGKITQGKLKVGSTV 252
Cdd:PTZ00327 234 IPKRDLTSPPRMIVirsfdvnkpgEDIENL--KGGVAGGSILQGVLKVGDEI 283
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-142 |
1.25e-22 |
|
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: 94.94 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 17 TIGHIDHGKTTLT--------AVITKILAKYNRAKAC--NYEDIDSA------PEEKLRGITINTAHVEYESTIRHYAHI 80
Cdd:cd04166 4 TCGSVDDGKSTLIgrllydskSIFEDQLAALERSKSSgtQGEKLDLAllvdglQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1833819254 81 DCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVE 142
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVD 145
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-174 |
2.60e-21 |
|
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: 90.89 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 13 INIGTIGHIDHGKTTLTAVITKILAKynrakacnyEDIDSAPEEKLRGITI-------------------NTAHVEYEST 73
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAST---------AAFDKNPQSQERGITLdlgfssfevdkpkhledneNPQIENYQIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 74 IrhyahIDCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAkQIGVNYLVVFLNKIDQVEDPELLELVELE 153
Cdd:cd01889 72 L-----VDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIG-ELLCKPLIVVLNKIDLIPEEERKRKIEKM 145
|
170 180
....*....|....*....|....
gi 1833819254 154 IRDLLDT---CGYKDTSIVKGSAL 174
Cdd:cd01889 146 KKRLQKTlekTRLKDSPIIPVSAK 169
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-139 |
8.90e-21 |
|
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: 89.19 E-value: 8.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLtavITKILAKYN--RAKACNYEDI-DSAPEEKLRGITI---NTAhVEYESTIRHYahIDCPGHAD 87
Cdd:cd01891 4 NIAIIAHVDHGKTTL---VDALLKQSGtfRENEEVGERVmDSNDLERERGITIlakNTA-ITYKDTKINI--IDTPGHAD 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1833819254 88 Y------IKNMItgaaqmEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVfLNKID 139
Cdd:cd01891 78 FggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKID 128
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
17-407 |
1.76e-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: 89.74 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 17 TIGHIDHGKTTLTAVI---TKI--------LAKYNRAKACNYEDIDSA------PEEKLRGITINTAHVEYESTIRHYAH 79
Cdd:TIGR02034 5 TCGSVDDGKSTLIGRLlhdTKQiyedqlaaLERDSKKHGTQGGEIDLAllvdglQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 80 IDCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQVE-DPELLELVELEIRDLL 158
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDyDEEVFENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 159 DTCGYKDTSIVKGSALKALEALDK---------LTTVEELETnkwikdilnliytidtdIPTPTRILDKPFFMAIEDVF- 228
Cdd:TIGR02034 165 EQLGFRDVTFIPLSALKGDNVVSRsesmpwysgPTLLEILET-----------------VEVERDAQDLPLRFPVQYVNr 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 229 -SITGRGtvVTGKITQGKLKVGSTVHLVGYSyikKSVTITGIEMFQKTLAEGYAGDNIGILLRgiQKTEVRRG-MVVAEK 306
Cdd:TIGR02034 228 pNLDFRG--YAGTIASGSVHVGDEVVVLPSG---RSSRVARIVTFDGDLEQARAGQAVTLTLD--DEIDISRGdLLAAAD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 307 NTLNAFTKFETELYVLTSEeggrhkPFFVGYRPQVYVNTTDVTATIESVLSK---KGAEETTNEMILPGDTVSLKLHLLY 383
Cdd:TIGR02034 301 SAPEVADQFAATLVWMAEE------PLLPGRSYDLKLGTRKVRASVAAIKHKvdvNTLEKGAAKSLELNEIGRVNLSLDE 374
|
410 420 430
....*....|....*....|....*....|..
gi 1833819254 384 PIALDK--------GMHFALREGNKTIGAGIV 407
Cdd:TIGR02034 375 PIAFDPyaenrttgAFILIDRLSNRTVGAGMI 406
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-287 |
3.81e-19 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 89.38 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLTAVITKILAKYNRAKACNYEDIDSAPEEKLRGITINTAHVEYESTIRHYAHIDCPGHADYIKNMI 93
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 94 TGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVfLNKIDQV-EDPELLELVELEIRDLLDTCGYK-DTSIVKG 171
Cdd:PRK10218 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPgARPDWVVDQVFDLFVNLDATDEQlDFPIVYA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 172 SALKALEALDKLTTVEeletnkwikDILNLIYTIDTDIPTPTRILDKPFFMAIEDVFSITGRGTVVTGKITQGKLKVGST 251
Cdd:PRK10218 166 SALNGIAGLDHEDMAE---------DMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1833819254 252 VHLVGYS------YIKKSVTITGIEMFQKTLAEgyAGDNIGI 287
Cdd:PRK10218 237 VTIIDSEgktrnaKVGKVLGHLGLERIETDLAE--AGDIVAI 276
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-139 |
2.62e-18 |
|
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: 83.05 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLT-AVITK--ILAKYNRAKACnYedIDSAPEEKLRGITINTAHV----EYESTIRHYAH-----ID 81
Cdd:cd01885 2 NICIIAHVDHGKTTLSdSLLASagIISEKLAGKAR-Y--LDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinlID 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 82 CPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLllaKQIGVNYL--VVFLNKID 139
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVL---RQALEERVkpVLVINKID 135
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
220-305 |
2.74e-18 |
|
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: 79.11 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 220 FFMAIEDVFSITGRGTVVTGKITQGKLKVGSTVHLVGysyIKKSVTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRR 299
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPP---LGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77
|
....*.
gi 1833819254 300 GMVVAE 305
Cdd:cd03696 78 GFVLSE 83
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
1-139 |
6.13e-18 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 86.07 E-value: 6.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 1 MIKQIFE--RTKPHI-NIGTIGHIDHGKTTLT-------AVITKILAKYNRAkacnyedIDSAPEEKLRGITINTAHV-- 68
Cdd:PRK07560 6 MVEKILElmKNPEQIrNIGIIAHIDHGKTTLSdnllagaGMISEELAGEQLA-------LDFDEEEQARGITIKAANVsm 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1833819254 69 --EYESTIRHYAHIDCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNyLVVFLNKID 139
Cdd:PRK07560 79 vhEYEGKEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVK-PVLFINKVD 150
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
2-141 |
7.60e-18 |
|
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: 85.72 E-value: 7.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 2 IKQIFERTKPHINIGTIGHIDHGKTTLT-------AVITKILAKYNRAkacnyedIDSAPEEKLRGITINTAHV----EY 70
Cdd:TIGR00490 9 IKELMWKPKFIRNIGIVAHIDHGKTTLSdnllagaGMISEELAGQQLY-------LDFDEQEQERGITINAANVsmvhEY 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1833819254 71 ESTIRHYAHIDCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNyLVVFLNKIDQV 141
Cdd:TIGR00490 82 EGNEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVK-PVLFINKVDRL 151
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
217-306 |
7.81e-17 |
|
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: 75.30 E-value: 7.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 217 DKPFFMAIEDVFSITGRGTVVTGKITQGKLKVGSTV-----HLVGysyikksvTITGIEMFQKTLAEGYAGDNIGILLRG 291
Cdd:cd03693 2 DKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVtfapaGVTG--------EVKSVEMHHEPLEEAIPGDNVGFNVKG 73
|
90
....*....|....*
gi 1833819254 292 IQKTEVRRGMVVAEK 306
Cdd:cd03693 74 VSVKDIKRGDVAGDS 88
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-141 |
1.48e-15 |
|
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: 75.74 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLTAVI---TKILAKYNRAKACNYEdIDSAPEEKLRGITINTAHVEYESTIRHYAHIDCPGHADYIK 90
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytSGAIRELGSVDKGTTR-TDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1833819254 91 NMITGAAQMEGAILLVSAVDGPMPQTRE--HLLLAKQIGVnylVVFLNKIDQV 141
Cdd:cd04168 80 EVERSLSVLDGAILVISAVEGVQAQTRIlfRLLRKLNIPT---IIFVNKIDRA 129
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
234-304 |
2.40e-15 |
|
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: 70.37 E-value: 2.40e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1833819254 234 GTVVTGKITQGKLKVGSTVHLVGYSYIKK--SVTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVRRGMVVA 304
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKKkiVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
14-141 |
3.09e-15 |
|
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: 77.78 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTL-------TAVITKIlakynrakaCNYED----IDSAPEEKLRGITINTA--HVEYES---TIrhy 77
Cdd:COG0480 11 NIGIVAHIDAGKTTLterilfyTGAIHRI---------GEVHDgntvMDWMPEEQERGITITSAatTCEWKGhkiNI--- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1833819254 78 ahIDCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLvVFLNKIDQV 141
Cdd:COG0480 79 --IDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRI-VFVNKMDRE 139
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
56-412 |
6.47e-15 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 76.11 E-value: 6.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 56 EKLRGITINTAHvEYEST-IRHYAHIDCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVF 134
Cdd:PRK05124 88 EREQGITIDVAY-RYFSTeKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 135 LNKIDQVE-DPELLELVELEIRDLLDTCGY-KDTSIVKGSALKAlealDKLttVEELETNKWIKD--ILNLIYTIDTDip 210
Cdd:PRK05124 167 VNKMDLVDySEEVFERIREDYLTFAEQLPGnLDIRFVPLSALEG----DNV--VSQSESMPWYSGptLLEVLETVDIQ-- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 211 tpTRILDKPFFMAIEDV---------FSitgrGTVVTGKITQG-KLKV---GSTvhlvgySYIKKSVTitgiemFQKTLA 277
Cdd:PRK05124 239 --RVVDAQPFRFPVQYVnrpnldfrgYA----GTLASGVVKVGdRVKVlpsGKE------SNVARIVT------FDGDLE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 278 EGYAGDNIGILLRgiQKTEVRRG-MVVAEKNTLNAFTKFETELyVLTSEEG------------GRHKPFFV-GYRPQVYV 343
Cdd:PRK05124 301 EAFAGEAITLVLE--DEIDISRGdLLVAADEALQAVQHASADV-VWMAEQPlqpgqsydikiaGKKTRARVdAIRYQVDI 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833819254 344 NTtdvtatiesvLSKKGAEEttnemiLPGDTVSL-KLHLLYPIALDK--------GMHFALREGNKTIGAGIVTKLLE 412
Cdd:PRK05124 378 NT----------LTQREAEN------LPLNGIGLvELTFDEPLVLDPyqqnrvtgGFIFIDRLTNVTVGAGMVREPLA 439
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
17-259 |
9.20e-15 |
|
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: 75.96 E-value: 9.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 17 TI-GHIDHGKTTLTAVITKIlaKYNRAKAcnyedidsapeeklRGIT--INTAHVEYESTiRHYAHIDCPGHADYIKNMI 93
Cdd:TIGR00487 91 TImGHVDHGKTSLLDSIRKT--KVAQGEA--------------GGITqhIGAYHVENEDG-KMITFLDTPGHEAFTSMRA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 94 TGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNyLVVFLNKIDQVEDPELLELVELEIRDLLDTCGYKDTSIVKGSA 173
Cdd:TIGR00487 154 RGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEANPDRVKQELSEYGLVPEDWGGDTIFVPVSA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 174 LKAL---EALDKLTTVEELETNKWIKDILNLIYTIDTDiptptriLDKpffmaiedvfsitGRGTVVTGKITQGKLKVGS 250
Cdd:TIGR00487 233 LTGDgidELLDMILLQSEVEELKANPNGQASGVVIEAQ-------LDK-------------GRGPVATVLVQSGTLRVGD 292
|
....*....
gi 1833819254 251 TVhLVGYSY 259
Cdd:TIGR00487 293 IV-VVGAAY 300
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-187 |
1.87e-14 |
|
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: 70.96 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 19 GHIDHGKTTLTAVITKIlakyNRAkacnyedidsapEEKLRGIT--INTAHVEYESTIRHYAHIDCPGHADYiKNMITGA 96
Cdd:cd01887 7 GHVDHGKTTLLDKIRKT----NVA------------AGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 97 AQM-EGAILLVSAVDGPMPQTREHLLLAKQIGVnYLVVFLNKIDqvEDPELLELVELEIRDLLDTCGY-----KDTSIVK 170
Cdd:cd01887 70 ASVtDIAILVVAADDGVMPQTIEAINHAKAANV-PIIVAINKID--KPYGTEADPERVKNELSELGLVgeewgGDVSIVP 146
|
170 180
....*....|....*....|...
gi 1833819254 171 GSALKA------LEALDKLTTVE 187
Cdd:cd01887 147 ISAKTGegiddlLEAILLLAEVL 169
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
17-141 |
2.07e-14 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 74.97 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 17 TIGHIDHGKTTL--------TAVITKILAKYNR---AKACNYEDIDSA------PEEKLRGITINTAHVEYESTIRHYAH 79
Cdd:PRK05506 29 TCGSVDDGKSTLigrllydsKMIFEDQLAALERdskKVGTQGDEIDLAllvdglAAEREQGITIDVAYRYFATPKRKFIV 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1833819254 80 IDCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVFLNKIDQV 141
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLV 170
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-143 |
3.61e-14 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 74.22 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLTAVI---TKILAKYNRAKACNYEdIDSAPEEKLRGITINTA--HVEYESTirHYAHIDCPGHADY 88
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIlfyTGKIHKMGEVEDGTTV-TDWMPQEQERGITIESAatSCDWDNH--RINLIDTPGHIDF 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1833819254 89 IKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLvVFLNKIDQVED 143
Cdd:PRK13351 87 TGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRL-IFINKMDRVGA 140
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-139 |
2.38e-13 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 71.70 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 18 IGHIDHGKTTLTAVI---TKILAKYNRAkacnyED----IDSAPEEKLRGITINTA--HVEYESTirHYAHIDCPGHADY 88
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfyTGAIHRIGEV-----EDgtttMDFMPEERERGISITSAatTCEWKGH--KINLIDTPGHVDF 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1833819254 89 IKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLvVFLNKID 139
Cdd:PRK12740 74 TGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNKMD 123
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
311-407 |
2.54e-13 |
|
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: 65.49 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 311 AFTKFETELYVLTSEeggrhKPFFVGYRPQVYVNTTDVTATIESVLSK---KGAEETTNEMILPGDTVSLKLHLLYPIAL 387
Cdd:cd01513 2 AVWKFDAKVIVLEHP-----KPIRPGYKPVMDVGTAHVPGRIAKLLSKedgKTKEKKPPDSLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 1833819254 388 DKGMH------FALREGNKTIGAGIV 407
Cdd:cd01513 77 ERGKEfptlgrFALRDGGRTVGAGLI 102
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-139 |
5.61e-13 |
|
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: 68.77 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLTAVI---TKILAKYNRAKACNyEDIDSAPEEKLRGITINT--AHVEYESTiRHYAhIDCPGHADY 88
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALlyaTGAIDRLGRVEDGN-TVSDYDPEEKKRKMSIETsvAPLEWNGH-KINL-IDTPGYADF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1833819254 89 IKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLvVFLNKID 139
Cdd:cd04170 78 VGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMD 127
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
2-141 |
6.14e-13 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 70.46 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 2 IKQIFERTKPHINIGTIGHIDHGKTTLT-AVITK--ILAKYNRAKACNyedIDSAPEEKLRGITINTAHVE--YESTIRH 76
Cdd:PTZ00416 9 IREIMDNPDQIRNMSVIAHVDHGKSTLTdSLVCKagIISSKNAGDARF---TDTRADEQERGITIKSTGISlyYEHDLED 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1833819254 77 YAH--------IDCPGHADYiKNMITGAAQM-EGAILLVSAVDGPMPQTREHLLLAKQIGVNyLVVFLNKIDQV 141
Cdd:PTZ00416 86 GDDkqpflinlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQTETVLRQALQERIR-PVLFINKVDRA 157
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
14-294 |
7.04e-13 |
|
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a GTP-binding membrane protein related to EF-G and EF-Tu. Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including GUF1 of yeast) originated within the bacterial LepA family. The function is unknown. [Unknown function, General]
Pssm-ID: 130460 [Multi-domain] Cd Length: 595 Bit Score: 70.04 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLTAVI---TKILAKynRAKACNYedIDSAPEEKLRGITI--NTAHVEY-----ESTIRHYahIDCP 83
Cdd:TIGR01393 5 NFSIIAHIDHGKSTLADRLleyTGAISE--REMREQV--LDSMDLERERGITIkaQAVRLNYkakdgETYVLNL--IDTP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 84 GHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQigvNYLVVF--LNKID----QVEdpelleLVELEIRDL 157
Cdd:TIGR01393 79 GHVDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALE---NDLEIIpvINKIDlpsaDPE------RVKKEIEEV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 158 LdtcGYKDTSIVKGSAlkalealdklttveelETNKWIKDILNliyTIDTDIPTPTRILDKPFFMAIEDVFSITGRGTVV 237
Cdd:TIGR01393 150 I---GLDASEAILASA----------------KTGIGIEEILE---AIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVA 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1833819254 238 TGKITQGKLKVGSTVHL--VGYSYIKKSVTITGIEMFQKTLAEgyAGDnIGILLRGIQK 294
Cdd:TIGR01393 208 LVRVFEGTIKPGDKIRFmsTGKEYEVDEVGVFTPKLTKTDELS--AGE-VGYIIAGIKD 263
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-139 |
5.75e-12 |
|
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: 63.71 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLTAVI---TKILAKynRAKACNYedIDSAPEEKLRGITI--NTAHVEYES---TIRHYAHIDCPGH 85
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSE--REMKEQV--LDSMDLERERGITIkaQAVRLFYKAkdgEEYLLNLIDTPGH 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1833819254 86 ADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVfLNKID 139
Cdd:cd01890 78 VDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPV-INKID 130
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
222-304 |
6.14e-12 |
|
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: 61.13 E-value: 6.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 222 MAIEDVFSITGRGTVVTGKITQGKLKVGSTVHLVGYSYIKKsvtITGIEMFQKTLAEGYAGDNIGILLRGIQktEVRRGM 301
Cdd:cd01342 3 MQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGR---VTSIERFHEEVDEAKAGDIVGIGILGVK--DILTGD 77
|
...
gi 1833819254 302 VVA 304
Cdd:cd01342 78 TLT 80
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
220-305 |
1.04e-11 |
|
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: 60.70 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 220 FFMAIEDVFSITGRGTVVTGKITQGKLKVGSTVHLVGYSYIK-KSVTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVR 298
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80
|
....*..
gi 1833819254 299 RGMVVAE 305
Cdd:cd03694 81 KGMVLVS 87
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-139 |
4.70e-10 |
|
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: 59.20 E-value: 4.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLtaviTKILAKYNRAKACNYEDI-------DSAPEEKLRGITI----------NTAHVEYESTIrh 76
Cdd:cd04167 2 NVCIAGHLHHGKTSL----LDMLIEQTHKRTPSVKLGwkplrytDTRKDEQERGISIksnpislvleDSKGKSYLINI-- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1833819254 77 yahIDCPGHADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNyLVVFLNKID 139
Cdd:cd04167 76 ---IDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLP-MVLVINKID 134
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-139 |
3.65e-09 |
|
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: 57.12 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLTAvitKILAKYNRAKACNYED-----IDSAPEEKLRGITINTAHVEYESTIRHYAHIDCPGHADY 88
Cdd:cd01886 1 NIGIIAHIDAGKTTTTE---RILYYTGRIHKIGEVHgggatMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1833819254 89 IKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYlVVFLNKID 139
Cdd:cd01886 78 TIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPR-IAFVNKMD 127
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
219-302 |
2.62e-08 |
|
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: 50.56 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 219 PFFMAIEDVFSitGRGTVVTGKITQGKLKVGSTVHLVGysyIKKSVTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVR 298
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMP---NKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDIS 75
|
....
gi 1833819254 299 RGMV 302
Cdd:cd04089 76 PGFV 79
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
18-261 |
4.88e-08 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 55.22 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 18 IGHIDHGKTTLtavitkiLAKYNRAKACNYEdidsapeekLRGITINTA----HVEYESTIRHYAHIDCPGHADYIKNMI 93
Cdd:CHL00189 250 LGHVDHGKTTL-------LDKIRKTQIAQKE---------AGGITQKIGayevEFEYKDENQKIVFLDTPGHEAFSSMRS 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 94 TGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYlVVFLNKIDQVEDPELLELVELEIRDLLDTCGYKDTSIVKGSA 173
Cdd:CHL00189 314 RGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPI-IVAINKIDKANANTERIKQQLAKYNLIPEKWGGDTPMIPISA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 174 LKAlEALDKLttveeLETNKWIKDILNLiYTIDTDIPTPTRI---LDKPffmaiedvfsitgRGTVVTGKITQGKLKVGS 250
Cdd:CHL00189 393 SQG-TNIDKL-----LETILLLAEIEDL-KADPTQLAQGIILeahLDKT-------------KGPVATILVQNGTLHIGD 452
|
250
....*....|.
gi 1833819254 251 TVhLVGYSYIK 261
Cdd:CHL00189 453 II-VIGTSYAK 462
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-139 |
7.82e-07 |
|
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: 51.17 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 17 TI-GHIDHGKTTLTAVI--TKILAKynrakacnyedidsapEEklRGIT--INTAHVEYEStiRHYAHIDCPGHAdyikn 91
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNVAAG----------------EA--GGITqhIGAYQVETNG--GKITFLDTPGHE----- 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1833819254 92 mitgaA--QME--GA------ILLVSAVDGPMPQTREHLLLAKQIGVNyLVVFLNKID 139
Cdd:COG0532 63 -----AftAMRarGAqvtdivILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKID 114
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-141 |
8.57e-07 |
|
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: 48.52 E-value: 8.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 13 INIGTIGHIDHGKTTLTAVITKilakynrakacNYEDIDSAPEeklrGIT--INTAHVEYESTIRHYAHIDCPGHADYIK 90
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLG-----------NKGSITEYYP----GTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1833819254 91 ------NMITGAAQM-EGAILLVSAVDGPMPQTREHLLLAKQiGVNyLVVFLNKIDQV 141
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHHADS-GVP-IILVGNKIDLK 122
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
223-304 |
1.35e-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: 45.75 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 223 AIEDVFSITGRgTVVTGKITQGKLKVGSTVHLVgysyiKKSVTITGIEMFQKTLAEGYAGDNIGILLRGiqKTEVRRGMV 302
Cdd:cd16265 4 RVEKVFKILGR-QVLTGEVESGVIYVGYKVKGD-----KGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDV 75
|
..
gi 1833819254 303 VA 304
Cdd:cd16265 76 LE 77
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
14-140 |
2.01e-06 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 50.11 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 14 NIGTIGHIDHGKTTLTAVITK---ILAKYNrakACNYEDIDSAPEEKLRGITINTAHVE--YEST---IRHYAH------ 79
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTDSLVAaagIIAQEV---AGDVRMTDTRADEAERGITIKSTGISlyYEMTdesLKDFKGerdgne 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 80 -----IDCPGHADYiKNMITGAAQM-EGAILLVSAVDGPMPQTrEHLL---LAKQIGVnylVVFLNKIDQ 140
Cdd:PLN00116 98 ylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVLrqaLGERIRP---VLTVNKMDR 162
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
219-303 |
2.22e-06 |
|
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: 45.20 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 219 PFFMAIEDVFSITGRGTVVTGKITQGKLKVGSTVHLVGysyIKKSVTITGIEMFQKTLAEGYAGDNIGILLRGIQKTEVR 298
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMP---SNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77
|
....*
gi 1833819254 299 RGMVV 303
Cdd:cd16267 78 VGSIL 82
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
12-139 |
1.01e-05 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 47.71 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 12 HI-NIGTIGHIDHGKTTL-------TAVITK------ILakynrakacnyediDSAPEEKLRGITINtAHveyesTIR-H 76
Cdd:COG0481 5 NIrNFSIIAHIDHGKSTLadrllelTGTLSEremkeqVL--------------DSMDLERERGITIK-AQ-----AVRlN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 77 YAH----------IDCPGHADY-------IknmitgAAqMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVfLNKID 139
Cdd:COG0481 65 YKAkdgetyqlnlIDTPGHVDFsyevsrsL------AA-CEGALLVVDASQGVEAQTLANVYLALENDLEIIPV-INKID 136
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
315-410 |
1.25e-05 |
|
Domain III of the GP-1 family of GTPases; This family 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 the 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: 294007 [Multi-domain] Cd Length: 87 Bit Score: 43.28 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 315 FETELYVLtseeggrHKP--FFVGYRPQVYVNTTDVTATIESVLSkkgaeettnEMILPGDTVSLKLHLLY-PIALDKGM 391
Cdd:cd03708 6 FEAEVLVL-------HHPttISPGYQPVVHCGTIRQTARIISIDK---------EVLRTGDRALVRFRFLYrPEYLREGQ 69
|
90
....*....|....*....
gi 1833819254 392 HFALREGnKTIGAGIVTKL 410
Cdd:cd03708 70 RLIFREG-RTKGIGTVTKV 87
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
219-304 |
5.85e-05 |
|
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: 41.33 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 219 PFFMAIEDVFSiTGRGTVVTGKITQGKLKVGSTVHLVGysyIKKSVTITGIEM-FQKTLAEGYAGDNIGILLRGIQKTEV 297
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMP---SQQDAEVKNIIRnSDEETDWAIAGDTVTLRLRGIEVEDI 76
|
....*..
gi 1833819254 298 RRGMVVA 304
Cdd:cd03698 77 QPGDILS 83
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
18-141 |
6.85e-05 |
|
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: 45.19 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 18 IGHIDHGKTTLTAVITKI-LAKYNRAKACNYEDIDSAPEEKLRGITINT-AHVEYESTIRHYAHIDCPGHADYIKNMITG 95
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIRGTaVVKKEAGGITQHIGASEVPTDVIEKICGDLlKSFKIKLKIPGLLFIDTPGHEAFTNLRKRG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1833819254 96 AAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYlVVFLNKIDQV 141
Cdd:TIGR00491 90 GALADIAILVVDINEGFKPQTLEALNILRSRKTPF-VVAANKIDRI 134
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
313-410 |
6.20e-04 |
|
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.
Pssm-ID: 294008 [Multi-domain] Cd Length: 109 Bit Score: 39.07 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 313 TKFETELYVLTSEeggrhKPFFVGYRPQVYVNTTDVTATIESVLS--KKGAEETTNEM---ILPGDTVSLKLHLLYPIAL 387
Cdd:cd04093 6 SKFEARIVTFDLQ-----VPILKGTPVVLHRHSLSEPATISKLVStlDKSTGEVIKKKprcLGKNQSAVVEIELERPIPL 80
|
90 100
....*....|....*....|....*....
gi 1833819254 388 DKGMH------FALREGNKTIGAGIVTKL 410
Cdd:cd04093 81 ETFKDnkelgrFVLRRGGETIAAGIVTEI 109
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
19-141 |
8.85e-03 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 38.24 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819254 19 GHIDHGKTTL------TAVITK--------ILAkynrakacNYEDIDSApeEKLRGITINTAHVEYEstIRHYAHIDCPG 84
Cdd:PRK04004 13 GHVDHGKTTLldkirgTAVAAKeaggitqhIGA--------TEVPIDVI--EKIAGPLKKPLPIKLK--IPGLLFIDTPG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1833819254 85 HADYIKNMITGAAQMEGAILLVSAVDGPMPQTREHLLLAKQIGVNYLVVfLNKIDQV 141
Cdd:PRK04004 81 HEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANKIDRI 136
|
|
| |
