|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-396 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 827.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 1 MAKAKFQRTKPHVNIGTIGHVDHGKTTLTAAITKVLHDKFPdlNETKAFDQIDNAPEERQRGITINIAHVEYQTDKRHYA 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGG--AEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 81 HVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVDDEELLELVEMEVRELL 160
Cdd:PRK00049 79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 161 AAQEFD-EDAPVVRVSALKALEG--DAKWVASVEELMNAVDESIPDPVRETDKPFLMPVEDVFTITGRGTVVTGRVERGV 237
Cdd:PRK00049 159 SKYDFPgDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 238 INVNEEVEIVGIRPsTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQVVTKPGTTTPHTEFEGQVYILSKD 317
Cdd:PRK00049 239 IKVGEEVEIVGIRD-TQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489498552 318 EGGRHTPFFNNYRPQFYFRTTDVTGVVTLPEGTEMVMPGDNTNISVKLIQPVAMDEGLRFAIREGGRTVGAGRVTKIIK 396
Cdd:PRK00049 318 EGGRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-396 |
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: 818.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 1 MAKAKFQRTKPHVNIGTIGHVDHGKTTLTAAITKVLHDKFPdlNETKAFDQIDNAPEERQRGITINIAHVEYQTDKRHYA 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGG--AKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 81 HVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVDDEELLELVEMEVRELL 160
Cdd:COG0050 79 HVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 161 AAQEFD-EDAPVVRVSALKALEGD--AKWVASVEELMNAVDESIPDPVRETDKPFLMPVEDVFTITGRGTVVTGRVERGV 237
Cdd:COG0050 159 SKYGFPgDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 238 INVNEEVEIVGIRPsTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQVVTKPGTTTPHTEFEGQVYILSKD 317
Cdd:COG0050 239 IKVGDEVEIVGIRD-TQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489498552 318 EGGRHTPFFNNYRPQFYFRTTDVTGVVTLPEGTEMVMPGDNTNISVKLIQPVAMDEGLRFAIREGGRTVGAGRVTKIIK 396
Cdd:COG0050 318 EGGRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-396 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 776.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 1 MAKAKFQRTKPHVNIGTIGHVDHGKTTLTAAITKVLHDKFpdLNETKAFDQIDNAPEERQRGITINIAHVEYQTDKRHYA 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKG--GGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 81 HVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVDDEELLELVEMEVRELL 160
Cdd:PRK12735 79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 161 AAQEFD-EDAPVVRVSALKALEGD--AKWVASVEELMNAVDESIPDPVRETDKPFLMPVEDVFTITGRGTVVTGRVERGV 237
Cdd:PRK12735 159 SKYDFPgDDTPIIRGSALKALEGDddEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 238 INVNEEVEIVGIRPsTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQVVTKPGTTTPHTEFEGQVYILSKD 317
Cdd:PRK12735 239 VKVGDEVEIVGIKE-TQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489498552 318 EGGRHTPFFNNYRPQFYFRTTDVTGVVTLPEGTEMVMPGDNTNISVKLIQPVAMDEGLRFAIREGGRTVGAGRVTKIIK 396
Cdd:PRK12735 318 EGGRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-396 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 767.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 1 MAKAKFQRTKPHVNIGTIGHVDHGKTTLTAAITKVLHDKfpDLNETKAFDQIDNAPEERQRGITINIAHVEYQTDKRHYA 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAER--GLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 81 HVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVDDEELLELVEMEVRELL 160
Cdd:PRK12736 79 HVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 161 AAQEFD-EDAPVVRVSALKALEGDAKWVASVEELMNAVDESIPDPVRETDKPFLMPVEDVFTITGRGTVVTGRVERGVIN 239
Cdd:PRK12736 159 SEYDFPgDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 240 VNEEVEIVGIRPsTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQVVTKPGTTTPHTEFEGQVYILSKDEG 319
Cdd:PRK12736 239 VGDEVEIVGIKE-TQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEG 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489498552 320 GRHTPFFNNYRPQFYFRTTDVTGVVTLPEGTEMVMPGDNTNISVKLIQPVAMDEGLRFAIREGGRTVGAGRVTKIIK 396
Cdd:PRK12736 318 GRHTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-396 |
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: 673.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 1 MAKAKFQRTKPHVNIGTIGHVDHGKTTLTAAITKVLHDKFpdLNETKAFDQIDNAPEERQRGITINIAHVEYQTDKRHYA 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEG--GAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 81 HVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVDDEELLELVEMEVRELL 160
Cdd:TIGR00485 79 HVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 161 AAQEFD-EDAPVVRVSALKALEGDAKWVASVEELMNAVDESIPDPVRETDKPFLMPVEDVFTITGRGTVVTGRVERGVIN 239
Cdd:TIGR00485 159 SQYDFPgDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 240 VNEEVEIVGIRPsTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQVVTKPGTTTPHTEFEGQVYILSKDEG 319
Cdd:TIGR00485 239 VGEEVEIVGLKD-TRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEG 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489498552 320 GRHTPFFNNYRPQFYFRTTDVTGVVTLPEGTEMVMPGDNTNISVKLIQPVAMDEGLRFAIREGGRTVGAGRVTKIIK 396
Cdd:TIGR00485 318 GRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-396 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 651.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 1 MAKAKFQRTKPHVNIGTIGHVDHGKTTLTAAITKVLHDKfpDLNETKAFDQIDNAPEERQRGITINIAHVEYQTDKRHYA 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAK--GGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 81 HVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVDDEELLELVEMEVRELL 160
Cdd:CHL00071 79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 161 AAQEFDEDA-PVVRVSALKALE----------GDAKWVASVEELMNAVDESIPDPVRETDKPFLMPVEDVFTITGRGTVV 229
Cdd:CHL00071 159 SKYDFPGDDiPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 230 TGRVERGVINVNEEVEIVGIRPSTTkTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQVVTKPGTTTPHTEFEG 309
Cdd:CHL00071 239 TGRIERGTVKVGDTVEIVGLRETKT-TTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 310 QVYILSKDEGGRHTPFFNNYRPQFYFRTTDVTGVVTL-----PEGTEMVMPGDNTNISVKLIQPVAMDEGLRFAIREGGR 384
Cdd:CHL00071 318 QVYILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGR 397
|
410
....*....|..
gi 489498552 385 TVGAGRVTKIIK 396
Cdd:CHL00071 398 TVGAGVVSKILK 409
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
2-395 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 634.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 2 AKAKFQRTKPHVNIGTIGHVDHGKTTLTAAITKVLHDKfpDLNETKAFDQIDNAPEERQRGITINIAHVEYQTDKRHYAH 81
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEE--GKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 82 VDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVDDEELLELVEMEVRELLA 161
Cdd:PLN03127 129 VDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 162 AQEFD-EDAPVVRVSALKALEG--DAKWVASVEELMNAVDESIPDPVRETDKPFLMPVEDVFTITGRGTVVTGRVERGVI 238
Cdd:PLN03127 209 FYKFPgDEIPIIRGSALSALQGtnDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 239 NVNEEVEIVGIRPSTT-KTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQVVTKPGTTTPHTEFEGQVYILSKD 317
Cdd:PLN03127 289 KVGEEVEIVGLRPGGPlKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKD 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489498552 318 EGGRHTPFFNNYRPQFYFRTTDVTGVVTLPEGTEMVMPGDNTNISVKLIQPVAMDEGLRFAIREGGRTVGAGRVTKII 395
Cdd:PLN03127 369 EGGRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVL 446
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-396 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 544.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 2 AKAKFQRTKPHVNIGTIGHVDHGKTTLTAAITKVLHDKfpDLNETKAFDQIDNAPEERQRGITINIAHVEYQTDKRHYAH 81
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASM--GGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 82 VDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVDDEELLELVEMEVRELLA 161
Cdd:PLN03126 149 VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 162 AQEFD-EDAPVVRVSALKALE----------GDAKWVASVEELMNAVDESIPDPVRETDKPFLMPVEDVFTITGRGTVVT 230
Cdd:PLN03126 229 SYEFPgDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVAT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 231 GRVERGVINVNEEVEIVGIRpSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQVVTKPGTTTPHTEFEGQ 310
Cdd:PLN03126 309 GRVERGTVKVGETVDIVGLR-ETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAI 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 311 VYILSKDEGGRHTPFFNNYRPQFYFRTTDVTGVVTL-----PEGTEMVMPGDNTNISVKLIQPVAMDEGLRFAIREGGRT 385
Cdd:PLN03126 388 VYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSimndkDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKT 467
|
410
....*....|.
gi 489498552 386 VGAGRVTKIIK 396
Cdd:PLN03126 468 VGAGVIQSIIE 478
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-204 |
2.02e-118 |
|
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: 341.87 E-value: 2.02e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 11 PHVNIGTIGHVDHGKTTLTAAITKVLHDKFPDlnETKAFDQIDNAPEERQRGITINIAHVEYQTDKRHYAHVDAPGHADY 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGA--KAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 91 IKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVDDEELLELVEMEVRELLAAQEFD-EDA 169
Cdd:cd01884 79 IKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDgDDT 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 489498552 170 PVVRVSALKALEGD--AKWVASVEELMNAVDESIPDP 204
Cdd:cd01884 159 PIVRGSALKALEGDdpNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
8-394 |
2.75e-86 |
|
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: 268.34 E-value: 2.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 8 RTKPHVNIGTIGHVDHGKTTL-------TAAITKVLHDKFPDLNETK-------AFdQIDNAPEERQRGITINIAHVEYQ 73
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLvgrllyeTGAIDEHIIEKYEEEAEKKgkesfkfAW-VMDRLKEERERGVTIDLAHKKFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 74 TDKRHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVD-DEELLELV 152
Cdd:COG5256 82 TDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 153 EMEVRELLAAQEFD-EDAPVVRVSALKaleGDAKWVASVE-------ELMNAVDeSIPDPVRETDKPFLMPVEDVFTITG 224
Cdd:COG5256 162 KEEVSKLLKMVGYKvDKIPFIPVSAWK---GDNVVKKSDNmpwyngpTLLEALD-NLKEPEKPVDKPLRIPIQDVYSISG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 225 RGTVVTGRVERGVINVNEEVEIVgirPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQVVTKPgtTTPH 304
Cdd:COG5256 238 IGTVPVGRVETGVLKVGDKVVFM---PAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHP--DNPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 305 T---EFEGQVYILskdeggRH-TPFFNNYRPQFYFRTTDV--------------TGVVtLPEGTEMVMPGDNTNISVKLI 366
Cdd:COG5256 313 TvaeEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVactfvelvskldprTGQV-KEENPQFLKTGDAAIVKIKPT 385
|
410 420 430
....*....|....*....|....*....|....
gi 489498552 367 QPVAMD------EGLRFAIREGGRTVGAGRVTKI 394
Cdd:COG5256 386 KPLVIEkfkefpQLGRFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-394 |
2.27e-82 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 258.32 E-value: 2.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 8 RTKPHVNIGTIGHVDHGKTTL-------TAAITKVLHDKFPDLNETK-----AFDQI-DNAPEERQRGITINIAHVEYQT 74
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLvgrllyeTGAIDEHIIEELREEAKEKgkesfKFAWVmDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 75 DKRHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATD--GPMPQTREHVLLARQVGVPYILVALNKADAVD-DEELLEL 151
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 152 VEMEVRELLAAQEFD-EDAPVVRVSalkALEGD--------AKWVASvEELMNAVDeSIPDPVRETDKPFLMPVEDVFTI 222
Cdd:PRK12317 162 VKEEVSKLLKMVGYKpDDIPFIPVS---AFEGDnvvkksenMPWYNG-PTLLEALD-NLKPPEKPTDKPLRIPIQDVYSI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 223 TGRGTVVTGRVERGVINVNEEVEivgIRPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQVVTKPgtTT 302
Cdd:PRK12317 237 SGVGTVPVGRVETGVLKVGDKVV---FMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHP--DN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 303 PHT---EFEGQVYILskdeggRH-TPFFNNYRPQFYFRTTDV--------------TGVVtLPEGTEMVMPGDNTNISVK 364
Cdd:PRK12317 312 PPTvaeEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVactfeelvkkldprTGQV-AEENPQFIKTGDAAIVKIK 384
|
410 420 430
....*....|....*....|....*....|....*..
gi 489498552 365 LIQPVAMDE-------GlRFAIREGGRTVGAGRVTKI 394
Cdd:PRK12317 385 PTKPLVIEKvkeipqlG-RFAIRDMGQTIAAGMVIDV 420
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-203 |
1.14e-75 |
|
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: 232.80 E-value: 1.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 10 KPHVNIGTIGHVDHGKTTLTAAITKVLHDKFPDLNETKAFD-QIDNAPEERQRGITINIAHVEYQTDKRHYAHVDAPGHA 88
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEaGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 89 DYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPyILVALNKADAVDDEELLELVEMEVRELLAAQEFD-E 167
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDgE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 489498552 168 DAPVVRVSALKALegdakwvaSVEELMNAVDESIPD 203
Cdd:pfam00009 160 FVPVVPGSALKGE--------GVQTLLDALDEYLPS 187
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-391 |
2.48e-75 |
|
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: 245.59 E-value: 2.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 13 VNIGTIGHVDHGKTTLTAAITKVlhdkfpdlnETkafdqiDNAPEERQRGITINI--AHVEyQTDKRHYAHVDAPGHADY 90
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGI---------DT------DRLKEEKKRGITIDLgfAYLP-LPDGRRLGFVDVPGHEKF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 91 IKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADaVDDEELLELVEMEVRELLAAQeFDEDAP 170
Cdd:COG3276 65 IKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKAD-LVDEEWLELVEEEIRELLAGT-FLEDAP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 171 VVRVSalkALEGdakwvASVEELMNAVDESIPD-PVRETDKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEEVEIVgi 249
Cdd:COG3276 143 IVPVS---AVTG-----EGIDELRAALDALAAAvPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELL-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 250 rPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQVVTKPGTTTPHTEFEGQVYILSkdegGRHTPFFNNY 329
Cdd:COG3276 213 -PSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLP----SAPRPLKHWQ 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489498552 330 RPQFYFRTTDVTGVVTLPEGTEMVmPGDNTNISVKLIQPVAMDEGLRFAIREGG--RTVGAGRV 391
Cdd:COG3276 288 RVHLHHGTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
302-391 |
2.64e-61 |
|
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: 192.34 E-value: 2.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 302 TPHTEFEGQVYILSKDEGGRHTPFFNNYRPQFYFRTTDVTGVVTLPEGTEMVMPGDNTNISVKLIQPVAMDEGLRFAIRE 381
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 489498552 382 GGRTVGAGRV 391
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
10-314 |
2.95e-55 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 188.42 E-value: 2.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 10 KPHVNIGTIGHVDHGKTTLTA-------AITKVLHDKFpdlnETKAFDQ----------IDNAPEERQRGITINIAHVEY 72
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGhliykcgGIDKRTIEKF----EKEAAEMgkgsfkyawvLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 73 QTDKRHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMP-------QTREHVLLARQVGVPYILVALNKADAVDD 145
Cdd:PTZ00141 81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 146 EELLELVEMEVREL---LAAQEFD-EDAPVVRVSalkALEGDAKWVASVE-------ELMNAVDESIPdPVRETDKPFLM 214
Cdd:PTZ00141 161 NYSQERYDEIKKEVsayLKKVGYNpEKVPFIPIS---GWQGDNMIEKSDNmpwykgpTLLEALDTLEP-PKRPVDKPLRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 215 PVEDVFTITGRGTVVTGRVERGVINVNeevEIVGIRPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQV 294
Cdd:PTZ00141 237 PLQDVYKIGGIGTVPVGRVETGILKPG---MVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYV 313
|
330 340
....*....|....*....|..
gi 489498552 295 VTKPGTTTPH--TEFEGQVYIL 314
Cdd:PTZ00141 314 ASDSKNDPAKecADFTAQVIVL 335
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-349 |
4.08e-51 |
|
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: 180.07 E-value: 4.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 13 VNIGTIGHVDHGKTTLTAAITKVlhdkfpdlnetkafdQIDNAPEERQRGITINIAHVEYQTDKRHYAHVDAPGHADYIK 92
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGI---------------AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFIS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 93 NMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADaVDDEELLELVEMEVRELLAAQEFDEDAPVV 172
Cdd:TIGR00475 66 NAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKAD-RVNEEEIKRTEMFMKQILNSYIFLKNAKIF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 173 RVSAlKALEGDAKWVASVEELMNAVDESipdpvrETDKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEEVEIVGIrps 252
Cdd:TIGR00475 145 KTSA-KTGQGIGELKKELKNLLESLDIK------RIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPI--- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 253 TTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQVVTKPgtttPHTEFEGQVYILSkdeggrHTPFFNNYRPQ 332
Cdd:TIGR00475 215 NHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLLELQPYH 284
|
330
....*....|....*..
gi 489498552 333 FYFRTTDVTGVVTLPEG 349
Cdd:TIGR00475 285 IAHGMSVTTGKISLLDK 301
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
212-299 |
7.80e-51 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 165.38 E-value: 7.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 212 FLMPVEDVFTITGRGTVVTGRVERGVINVNEEVEIVGIRPsTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVER 291
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKE-TLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVER 79
|
....*...
gi 489498552 292 GQVVTKPG 299
Cdd:cd03697 80 GMVLAKPG 87
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-204 |
2.21e-50 |
|
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: 167.47 E-value: 2.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLTAAITKVLHDKFPDlnETKAFDQIDNAPEERQRGITINIAHVEYQTDKRHYAHVDAPGHADYIKN 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRR--GTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 94 MITGAAQMDGAILVVAATDGPMPQTREHVLLARQvGVPYILVALNKADAVDDEELLELVEMEVREL---LAAQEFDEDAP 170
Cdd:cd00881 79 TVRGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRVGEEDFDEVLREIKELLkliGFTFLKGKDVP 157
|
170 180 190
....*....|....*....|....*....|....
gi 489498552 171 VVRVSALKALegdakwvaSVEELMNAVDESIPDP 204
Cdd:cd00881 158 IIPISALTGE--------GIEELLDAIVEHLPPP 183
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
11-384 |
3.61e-48 |
|
translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Pssm-ID: 274720 [Multi-domain] Cd Length: 406 Bit Score: 168.69 E-value: 3.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 11 PHVNIGTIGHVDHGKTTLTAAITKVLHDKFpdlnetkafdqidnaPEERQRGITINIAHVE--------------YQTDK 76
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVWTDTH---------------SEELKRGISIRLGYADaeiykcpecdgpecYTTEP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 77 ------------RHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDG-PMPQTREHVLLARQVGVPYILVALNKADaV 143
Cdd:TIGR03680 68 vcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKID-L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 144 DDEELLELVEMEVRELLAAqEFDEDAPVVRVSALKALEGDAkwvasveeLMNAVDESIPDPVRETDKPFLMPVEDVFTIT 223
Cdd:TIGR03680 147 VSKEKALENYEEIKEFVKG-TVAENAPIIPVSALHNANIDA--------LLEAIEKFIPTPERDLDKPPLMYVARSFDVN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 224 GRGT--------VVTGRVERGVINVNEEVEIV-GIR---PSTTK-----TTVTGVEMFRKLLDQGQAGdnvGLLLRGVK- 285
Cdd:TIGR03680 218 KPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKvekGGKTKwepiyTEITSLRAGGYKVEEARPG---GLVGVGTKl 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 286 -----REDVERGQVVTKPGTTTP-HTEFEGQVYILSK----DEGGRHTPFFNNYRPQFYFRTTDVTGVVTLPEGTEmvmp 355
Cdd:TIGR03680 295 dpaltKADALAGQVVGKPGTLPPvWESLELEVHLLERvvgtEEELKVEPIKTGEVLMLNVGTATTVGVVTSARKDE---- 370
|
410 420 430
....*....|....*....|....*....|.
gi 489498552 356 gdntnISVKLIQPVAMDEGLRFAI--REGGR 384
Cdd:TIGR03680 371 -----IEVKLKRPVCAEEGDRVAIsrRVGGR 396
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
1-384 |
4.18e-47 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 165.80 E-value: 4.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 1 MAKAKFQrtkPHVNIGTIGHVDHGKTTLTAAITKVLHDKFPdlnetkafdqidnapEERQRGITINIAHVE--------- 71
Cdd:PRK04000 1 MMWEKVQ---PEVNIGMVGHVDHGKTTLVQALTGVWTDRHS---------------EELKRGITIRLGYADatirkcpdc 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 72 -----YQTDK------------RHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDG-PMPQTREHVLLARQVGVPYI 133
Cdd:PRK04000 63 eepeaYTTEPkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 134 LVALNKADavddeellelveMEVREllAA-------QEF-----DEDAPVVRVSALKALEGDAkwvasveeLMNAVDESI 201
Cdd:PRK04000 143 VIVQNKID------------LVSKE--RAlenyeqiKEFvkgtvAENAPIIPVSALHKVNIDA--------LIEAIEEEI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 202 PDPVRETDKPFLMPVEDVFTITGRGT--------VVTGRVERGVINVNEEVEIV-GIR----------PSTTKttVTGVE 262
Cdd:PRK04000 201 PTPERDLDKPPRMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKveeggktkwePITTK--IVSLR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 263 MFRKLLDQGQAGdnvGLLLRGVK------REDVERGQVVTKPGTTTP-HTEFEGQVYILSK----DEGGRHTPFFNNYRP 331
Cdd:PRK04000 279 AGGEKVEEARPG---GLVGVGTKldpsltKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPL 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 489498552 332 QFYFRTTDVTGVVTLPEGTEMvmpgdntniSVKLIQPVAMDEGLRFAI--REGGR 384
Cdd:PRK04000 356 MLNVGTATTVGVVTSARKDEA---------EVKLKRPVCAEEGDRVAIsrRVGGR 401
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
300-394 |
1.40e-44 |
|
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: 149.72 E-value: 1.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 300 TTTPHTEFEGQVYILSKDEGGRHTPFFNNYRPQFYFRTTDVTG-VVTL-----PEGT----EMVMPGDNTNISVKLIQPV 369
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGkFVELlhkldPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 489498552 370 AMDEGLRFAIREGGRTVGAGRVTKI 394
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-392 |
9.62e-44 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 156.92 E-value: 9.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 8 RTKPHVNIGTIGHVDHGKTTLTAAITKVLHDKFPdlnetkafdqidnapEERQRGITINIAHVE--------------YQ 73
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHS---------------EELKRGITIRLGYADatfykcpnceppeaYT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 74 TDK------------RHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDG-PMPQTREHVLLARQVGVPYILVALNKA 140
Cdd:COG5257 66 TEPkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 141 DavddEELLELVEMEVRELlaaQEF-----DEDAPVVRVSALKALEGDAkwvasveeLMNAVDESIPDPVRETDKPFLMP 215
Cdd:COG5257 146 D----LVSKERALENYEQI---KEFvkgtvAENAPIIPVSAQHKVNIDA--------LIEAIEEEIPTPERDLSKPPRML 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 216 VEDVFTITGRGT--------VVTGRVERGVINVNEEVEIV-GIR-PSTTK-------TTVTGVEMFRKLLDQGQAGdnvG 278
Cdd:COG5257 211 VARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKvEKGGKtkyepitTTVVSLRAGGEEVEEAKPG---G 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 279 LLLRGVK------REDVERGQVVTKPGTTTP-HTEFEGQVYILSK----DEGGRHTPFFNNYRPQFYFRTTDVTGVVTLP 347
Cdd:COG5257 288 LVAVGTKldpsltKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLERvvgtKEEVKVEPIKTGEPLMLNVGTATTVGVVTSA 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 489498552 348 EGTEmvmpgdntnISVKLIQPVAMDEGLRFAI--REGG--RTVGAGRVT 392
Cdd:COG5257 368 RKDE---------IEVKLKRPVCAEKGSRVAIsrRIGGrwRLIGWGIIK 407
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-396 |
1.82e-43 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 157.17 E-value: 1.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 1 MAKAKFqrtkpHVNIGTIGHVDHGKTTLTA-------AITKVLHDKF----PDLNEtKAFDQ---IDNAPEERQRGITIN 66
Cdd:PLN00043 1 MGKEKV-----HINIVVIGHVDSGKSTTTGhliyklgGIDKRVIERFekeaAEMNK-RSFKYawvLDKLKAERERGITID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 67 IAHVEYQTDKRHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMP-------QTREHVLLARQVGVPYILVALNK 139
Cdd:PLN00043 75 IALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 140 ADAVDDEELLELVEMEVREL---LAAQEFDEDA-PVVRVSalkALEGDAKWVASVE-------ELMNAVDEsIPDPVRET 208
Cdd:PLN00043 155 MDATTPKYSKARYDEIVKEVssyLKKVGYNPDKiPFVPIS---GFEGDNMIERSTNldwykgpTLLEALDQ-INEPKRPS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 209 DKPFLMPVEDVFTITGRGTVVTGRVERGVINVNeevEIVGIRPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKRED 288
Cdd:PLN00043 231 DKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPG---MVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 289 VERGQVV--TKPGTTTPHTEFEGQVYILSK--DEGGRHTPFFNNYRPQFYFRTTDVTGVVTLPEGTEM------VMPGDN 358
Cdd:PLN00043 308 LKRGYVAsnSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 489498552 359 TNISVKLIQPVAMDEGL------RFAIREGGRTVGAGRVTKIIK 396
Cdd:PLN00043 388 GFVKMIPTKPMVVETFSeypplgRFAVRDMRQTVAVGVIKSVEK 431
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-142 |
1.26e-41 |
|
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: 145.71 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLTA-------AITKVLHDKFpdlnETKAFDQ----------IDNAPEERQRGITINIAHVEYQTDK 76
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGhllyklgGVDKRTIEKY----EKEAKEMgkesfkyawvLDKLKEERERGVTIDVGLAKFETEK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489498552 77 RHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDG-------PMPQTREHVLLARQVGVPYILVALNKADA 142
Cdd:cd01883 77 YRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDD 149
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-207 |
2.86e-40 |
|
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: 140.82 E-value: 2.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 15 IGTIGHVDHGKTTLTAAITKVlhdkfpdlnETkafdqiDNAPEERQRGITINI--AHVEYQTDKRhYAHVDAPGHADYIK 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI---------ET------DRLPEEKKRGITIDLgfAYLDLPDGKR-LGFIDVPGHEKFVK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 93 NMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADaVDDEELLELVEMEVRELLAAQEFdEDAPVV 172
Cdd:cd04171 66 NMLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKAD-LVDEDRLELVEEEILELLAGTFL-ADAPIF 143
|
170 180 190
....*....|....*....|....*....|....*
gi 489498552 173 RVSalkALEGDakwvaSVEELMNAVDEsIPDPVRE 207
Cdd:cd04171 144 PVS---SVTGE-----GIEELKNYLDE-LAEPQSK 169
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
7-299 |
3.58e-40 |
|
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: 147.54 E-value: 3.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 7 QRTKPHVNIGTIGHVDHGKTTLtaaITKVLHD-K--FPD----LNET---KAFDQIDNAP------EERQRGITINIAHV 70
Cdd:COG2895 12 HENKDLLRFITCGSVDDGKSTL---IGRLLYDtKsiFEDqlaaLERDskkRGTQEIDLALltdglqAEREQGITIDVAYR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 71 EYQTDKRHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVddeelle 150
Cdd:COG2895 89 YFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLV------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 151 lvemevrellaaqEFDEDA-----------------PVVRVSALKALEGDAkwVASVEE---------LMNAVdESIPDP 204
Cdd:COG2895 162 -------------DYSEEVfeeivadyrafaaklglEDITFIPISALKGDN--VVERSEnmpwydgptLLEHL-ETVEVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 205 VRETDKPFLMPVEDV--FTITGRGtvVTGRVERGVINVNEEVEIVgirPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLr 282
Cdd:COG2895 226 EDRNDAPFRFPVQYVnrPNLDFRG--YAGTIASGTVRVGDEVVVL---PSGKTSTVKSIVTFDGDLEEAFAGQSVTLTL- 299
|
330
....*....|....*...
gi 489498552 283 gvKRE-DVERGQVVTKPG 299
Cdd:COG2895 300 --EDEiDISRGDVIVAAD 315
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-292 |
7.15e-38 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 144.04 E-value: 7.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 15 IGTIGHVDHGKTTLTAAITKVLHDKFPdlnetkafdqidnapEERQRGITINIAHVEY-QTDKRHYAHVDAPGHADYIKN 93
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNADRLP---------------EEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 94 MITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADaVDDEELLELVEMEVRELLAAQEFDeDAPVVR 173
Cdd:PRK10512 68 MLAGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKAD-RVDEARIAEVRRQVKAVLREYGFA-EAKLFV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 174 VSALKALegdakwvaSVEELMNAVdESIPDPVRETDKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEEVEIVGIrpsT 253
Cdd:PRK10512 146 TAATEGR--------GIDALREHL-LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGV---N 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489498552 254 TKTTVTGVEMFRKLLDQGQAGDNVGLLLRG-VKREDVERG 292
Cdd:PRK10512 214 KPMRVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
12-395 |
7.44e-37 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 140.45 E-value: 7.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 12 HVNIGTIGHVDHGKTTLTAA-ITKVLHDkfpDLNETKAFdqIDNAPEERQRGITINIAHVEY---------------QTD 75
Cdd:COG5258 122 HIVVGVAGHVDHGKSTLVGTlVTGKLDD---GNGGTRSF--LDVQPHEVERGLSADLSYAVYgfdddgpvrmknplrKTD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 76 K--------RHYAHVDAPGHADYIKNMITG--AAQMDGAILVVAATDGPMPQTREH--VLLArqVGVPyILVALNKADAV 143
Cdd:COG5258 197 RarvveesdKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLA--MDLP-VIVAITKIDKV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 144 DDEELLELVEMEVREL-----------------LAAQEFDED-APVVRVSALkALEGdakwVASVEELMNavdeSIPDPV 205
Cdd:COG5258 274 DDERVEEVEREIENLLrivgrtplevesrhdvdAAIEEINGRvVPILKTSAV-TGEG----LDLLDELFE----RLPKRA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 206 RETDKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEEVeIVGIRP--STTKTTVTGVEMFRKLLDQGQAGDNVGLLLRG 283
Cdd:COG5258 345 TDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDEL-LIGPTKdgSFREVEVKSIEMHYHRVDKAEAGRIVGIALKG 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 284 VKREDVERGQVVTKPGT-TTPHTEFEGQVYILSkdeggrH-TPFFNNYRPQFYFRTTDVTgVVTLPEGTEMVMPGDNTNI 361
Cdd:COG5258 424 VEEEELERGMVLLPRDAdPKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEA-VRFEPIDKGYLLPGDSGRV 496
|
410 420 430
....*....|....*....|....*....|....*
gi 489498552 362 SVK-LIQPVAMDEGLRFAIREgGRTVGAGRVTKII 395
Cdd:COG5258 497 RLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDIL 530
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
302-394 |
2.88e-36 |
|
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: 127.73 E-value: 2.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 302 TPHTEFEGQVYILSKDEGGRHTPFFNNYRPQFYFRTTDVTGVVTLPEGTEMVMPGDNTNISVKLIQPVAMDEGLRFAIRE 381
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 489498552 382 GGRTVGAGRVTKI 394
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-141 |
1.21e-29 |
|
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: 113.82 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 17 TIGHVDHGKTTLtaaITKVLHDK---FPDLNET--------KAFDQIDNA------PEERQRGITINIAHVEYQTDKRHY 79
Cdd:cd04166 4 TCGSVDDGKSTL---IGRLLYDSksiFEDQLAAlerskssgTQGEKLDLAllvdglQAEREQGITIDVAYRYFSTPKRKF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489498552 80 AHVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKAD 141
Cdd:cd04166 81 IIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMD 142
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-177 |
1.27e-28 |
|
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: 110.53 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 13 VNIGTIGHVDHGKTTLTAAITKVLhdkfpdlnETKAFDQidnAPEERQRGITINIAHVEYQTDKRHYAH----------- 81
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIA--------STAAFDK---NPQSQERGITLDLGFSSFEVDKPKHLEdnenpqienyq 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 82 ---VDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPyILVALNKADAVDDEELLELVEMEVRE 158
Cdd:cd01889 70 itlVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKP-LIVVLNKIDLIPEEERKRKIEKMKKR 148
|
170 180
....*....|....*....|.
gi 489498552 159 LLAAQE--FDEDAPVVRVSAL 177
Cdd:cd01889 149 LQKTLEktRLKDSPIIPVSAK 169
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-206 |
4.56e-28 |
|
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: 109.28 E-value: 4.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 13 VNIGTIGHVDHGKTTLTAAITKVLHDKFPdlnetkafdqidnapEERQRGITINIAHVE--------------YQTDK-- 76
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWTVRHK---------------EELKRNITIKLGYANakiykcpncgcprpYDTPEce 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 77 -----------RHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDG-PMPQTREHVLLARQVGVPYILVALNKADavd 144
Cdd:cd01888 66 cpgcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKID--- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489498552 145 deelLELVEMEVRELLAAQEF-----DEDAPVVRVSALKALEGDAkwvasveeLMNAVDESIPDPVR 206
Cdd:cd01888 143 ----LVKEEQALENYEQIKEFvkgtiAENAPIIPISAQLKYNIDV--------LCEYIVKKIPTPPR 197
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-275 |
8.21e-28 |
|
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: 115.09 E-value: 8.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLTAAI---TKVLHDKfpDLNETKAFDQIDnapEERQRGITI---NIAhVEYQTDKRHYahVDAPGH 87
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALlkqSGTFRAN--EAVAERVMDSND---LERERGITIlakNTA-IRYNGTKINI--VDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 88 ADY------IKNMItgaaqmDGAILVVAATDGPMPQTREHVLLARQVGVPYILVaLNKADAVDDEELLELVEMEvrELLA 161
Cdd:TIGR01394 75 ADFggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPSARPDEVVDEVF--DLFA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 162 AQEFDEDA---PVVRVSalkALEGDAKWVA-----SVEELMNAVDESIPDPVRETDKPFLMPVE--DVFTITGRgtVVTG 231
Cdd:TIGR01394 146 ELGADDEQldfPIVYAS---GRAGWASLDLddpsdNMAPLFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLGR--IAIG 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489498552 232 RVERGVINVNEEVEIVGIRPSTTKTTVTGVEMFRKL----LDQGQAGD 275
Cdd:TIGR01394 221 RVHRGTVKKGQQVALMKRDGTIENGRISKLLGFEGLerveIDEAGAGD 268
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-303 |
1.37e-27 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 114.35 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLTAAItkvlhdkfpdLNETKAFDQIDNAPE--------ERQRGITI---NIAhVEYQTDKRHYahV 82
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDAL----------LKQSGTFRENQEVAErvmdsndlERERGITIlakNTA-VRYKGVKINI--V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 83 DAPGHADY------IKNMItgaaqmDGAILVVAATDGPMPQTReHVL---LARqvGVPYILVaLNKADavddeellelve 153
Cdd:COG1217 75 DTPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR-FVLkkaLEL--GLKPIVV-INKID------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 154 mevR-------------EL---LAAQEFDEDAPVVRVSalkALEGDAKWVASVEE-----LMNAVDESIPDPVRETDKPF 212
Cdd:COG1217 133 ---RpdarpdevvdevfDLfieLGATDEQLDFPVVYAS---ARNGWASLDLDDPGedltpLFDTILEHVPAPEVDPDGPL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 213 LMpveDVFTI-----TGRgtVVTGRVERGVINVNEEVEIVGIRPSTTKTTVTGVEMFRKL----LDQGQAGDNV---GLl 280
Cdd:COG1217 207 QM---LVTNLdysdyVGR--IAIGRIFRGTIKKGQQVALIKRDGKVEKGKITKLFGFEGLerveVEEAEAGDIVaiaGI- 280
|
330 340
....*....|....*....|...
gi 489498552 281 lrgvkrEDVERGQVVTKPGTTTP 303
Cdd:COG1217 281 ------EDINIGDTICDPENPEA 297
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-316 |
8.76e-27 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 111.25 E-value: 8.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 13 VNIGTIGHVDHGKTTLTAAITKVLHDKFPDlnetkafdqidnapeERQRGITINIAHVE--------------YQ----- 73
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKTVRFKR---------------EKVRNITIKLGYANakiykcpkcprptcYQsygss 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 74 --------------TDKRHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDG-PMPQTREHVLLARQVGVPYILVALN 138
Cdd:PTZ00327 100 kpdnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 139 KADavddeellelvemEVRELLAAQEFDE-----------DAPVVRVSA-LKalegdakwvASVEELMNAVDESIPDPVR 206
Cdd:PTZ00327 180 KID-------------LVKEAQAQDQYEEirnfvkgtiadNAPIIPISAqLK---------YNIDVVLEYICTQIPIPKR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 207 ETDKPFLM----------PVEDVFTItgRGTVVTGRVERGVINVNEEVEIV-GIRPSTTKTTVTGVEMFRKLLDQgQAGD 275
Cdd:PTZ00327 238 DLTSPPRMivirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEIRpGIISKDSGGEFTCRPIRTRIVSL-FAEN 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489498552 276 NV-------GLLLRGVK------REDVERGQVVTKPGTTTP-HTEFEGQVYILSK 316
Cdd:PTZ00327 315 NElqyavpgGLIGVGTTidptltRADRLVGQVLGYPGKLPEvYAEIEIQYYLLRR 369
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
17-298 |
5.21e-26 |
|
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: 108.23 E-value: 5.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 17 TIGHVDHGKTTLtaaITKVLHDkfpdlneTKAF--DQ-----------------------IDNAPEERQRGITINIAHVE 71
Cdd:TIGR02034 5 TCGSVDDGKSTL---IGRLLHD-------TKQIyeDQlaalerdskkhgtqggeidlallVDGLQAEREQGITIDVAYRY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 72 YQTDKRHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVDDEELLEL 151
Cdd:TIGR02034 75 FSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 152 VEMEVRELLAAQEFDEDAPVVRVSALKaleGDAkwVASVEELMN--------AVDESIPDPVRETDKPFLMPVEDV---- 219
Cdd:TIGR02034 155 NIKKDYLAFAEQLGFRDVTFIPLSALK---GDN--VVSRSESMPwysgptllEILETVEVERDAQDLPLRFPVQYVnrpn 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 220 FTITG-RGTVVTGRVERGvinvnEEVEIVgirPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLrgvKRE-DVERGQVVTK 297
Cdd:TIGR02034 230 LDFRGyAGTIASGSVHVG-----DEVVVL---PSGRSSRVARIVTFDGDLEQARAGQAVTLTL---DDEiDISRGDLLAA 298
|
.
gi 489498552 298 P 298
Cdd:TIGR02034 299 A 299
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
17-303 |
2.10e-23 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 101.53 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 17 TIGHVDHGKTTLtaaITKVLHDkfpdlneTKAF--DQ-----------------------IDNAPEERQRGITINIAHVE 71
Cdd:PRK05124 32 TCGSVDDGKSTL---IGRLLHD-------TKQIyeDQlaslhndskrhgtqgekldlallVDGLQAEREQGITIDVAYRY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 72 YQTDKRHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVDDEELLEl 151
Cdd:PRK05124 102 FSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVF- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 152 vemevrELLAAQ--EFDEDAPV---VRVSALKALEGDAkwVASVEELMN--------AVDESIpDPVRETD-KPFLMPVE 217
Cdd:PRK05124 181 ------ERIREDylTFAEQLPGnldIRFVPLSALEGDN--VVSQSESMPwysgptllEVLETV-DIQRVVDaQPFRFPVQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 218 DV------FtitgRGtvVTGRVERGVINVNEEVEIVgirPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLrgvKRE-DVE 290
Cdd:PRK05124 252 YVnrpnldF----RG--YAGTLASGVVKVGDRVKVL---PSGKESNVARIVTFDGDLEEAFAGEAITLVL---EDEiDIS 319
|
330
....*....|...
gi 489498552 291 RGQVVTKPGTTTP 303
Cdd:PRK05124 320 RGDLLVAADEALQ 332
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
7-299 |
1.24e-21 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 96.92 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 7 QRTKPHVNIGTIGHVDHGKTTLtaaITKVLHDK---FPDL-----NETKAF----DQIDNA------PEERQRGITINIA 68
Cdd:PRK05506 19 HERKSLLRFITCGSVDDGKSTL---IGRLLYDSkmiFEDQlaaleRDSKKVgtqgDEIDLAllvdglAAEREQGITIDVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 69 HVEYQTDKRHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKADAVDDEEL 148
Cdd:PRK05506 96 YRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 149 LELVEMEVRELLAAQEFDEDAPVVRVSALKaleGDAKWVASVE-------ELMNAVDESIPDPVREtDKPFLMPVEDV-- 219
Cdd:PRK05506 176 VFDEIVADYRAFAAKLGLHDVTFIPISALK---GDNVVTRSARmpwyegpSLLEHLETVEIASDRN-LKDFRFPVQYVnr 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 220 ----FtitgRGtvVTGRVERGVINVNEEVEIVgirPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRgvKREDVERGQVV 295
Cdd:PRK05506 252 pnldF----RG--FAGTVASGVVRPGDEVVVL---PSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLA--DEIDISRGDML 320
|
....
gi 489498552 296 TKPG 299
Cdd:PRK05506 321 ARAD 324
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
208-294 |
6.16e-21 |
|
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: 86.47 E-value: 6.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 208 TDKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEEVEIVgirPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKRE 287
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFA---PAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVK 77
|
....*..
gi 489498552 288 DVERGQV 294
Cdd:cd03693 78 DIKRGDV 84
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
212-297 |
2.51e-19 |
|
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: 81.80 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 212 FLMPVEDVFTITGRGTVVTGRVERGVINVNEEVEIVgirPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVER 291
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIP---PLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77
|
....*.
gi 489498552 292 GQVVTK 297
Cdd:cd03696 78 GFVLSE 83
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-141 |
2.96e-19 |
|
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: 84.95 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLTAAITKVLHDkFPDlNETKAFDQIDNAPEERQRGITI---NIAhVEYQTDKRHYahVDAPGHADY 90
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGT-FRE-NEEVGERVMDSNDLERERGITIlakNTA-ITYKDTKINI--IDTPGHADF 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489498552 91 ------IKNMItgaaqmDGAILVVAATDGPMPQTReHVLL-ARQVGVPYILVaLNKAD 141
Cdd:cd01891 79 ggeverVLSMV------DGVLLLVDASEGPMPQTR-FVLKkALEAGLKPIVV-INKID 128
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-279 |
2.24e-18 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 87.07 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLtaaITKVLHDK--FPDLNETKAfDQIDNAPEERQRGITINIAHVEYQTDKRHYAHVDAPGHADYI 91
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSgtFDSRAETQE-RVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 92 KNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVaLNKADAVDDEELLELVEMEVREL-LAAQEFDEDAP 170
Cdd:PRK10218 83 GEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVFDLFVnLDATDEQLDFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 171 VVRVSALKALEG-DAKWVAS-VEELMNAVDESIPDPVRETDKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEEVEIVG 248
Cdd:PRK10218 162 IVYASALNGIAGlDHEDMAEdMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIID 241
|
250 260 270
....*....|....*....|....*....|....*
gi 489498552 249 ----IRPSTTKTTVTGVEMFRKLLDQGQAGDNVGL 279
Cdd:PRK10218 242 segkTRNAKVGKVLGHLGLERIETDLAEAGDIVAI 276
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-142 |
2.83e-18 |
|
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: 83.05 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLTAAItkvlhdkfpdLNETKAFDQI----------DNAPEERQRGITINIAHVEYQTDKRHYAHVD 83
Cdd:cd04168 1 NIGILAHVDAGKTTLTESL----------LYTSGAIRELgsvdkgttrtDSMELERQRGITIFSAVASFQWEDTKVNIID 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489498552 84 APGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVaLNKADA 142
Cdd:cd04168 71 TPGHMDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIF-VNKIDR 128
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
19-178 |
8.44e-18 |
|
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: 80.21 E-value: 8.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 19 GHVDHGKTTLTAAITKVlhdkfpdlnetkafdqidNAPEERQRGITINIA--HVEYQTDKRHYAHVDAPGHADYiKNMIT 96
Cdd:cd01887 7 GHVDHGKTTLLDKIRKT------------------NVAAGEAGGITQHIGayQVPIDVKIPGITFIDTPGHEAF-TNMRA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 97 GAAQM-DGAILVVAATDGPMPQTREHVLLARQVGVPyILVALNKADavDDEELLELVEMEVREL----LAAQEFDEDAPV 171
Cdd:cd01887 68 RGASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKID--KPYGTEADPERVKNELselgLVGEEWGGDVSI 144
|
....*..
gi 489498552 172 VRVSALK 178
Cdd:cd01887 145 VPISAKT 151
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
226-296 |
2.53e-17 |
|
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: 75.76 E-value: 2.53e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489498552 226 GTVVTGRVERGVINVNEEVEIVGIR--PSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVERGQVVT 296
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGtgKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-141 |
1.94e-16 |
|
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: 77.66 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLTAAitkvLHDKFPDLNETKAFDQ--IDNAPEERQRGITINIAHV--EYQTDKRHYAH-------V 82
Cdd:cd01885 2 NICIIAHVDHGKTTLSDS----LLASAGIISEKLAGKAryLDTREDEQERGITIKSSAIslYFEYEEEKMDGndylinlI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489498552 83 DAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTrEHVLlaRQV---GVPYILVaLNKAD 141
Cdd:cd01885 78 DSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT-ETVL--RQAleeRVKPVLV-INKID 135
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
4-141 |
6.38e-16 |
|
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: 79.43 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 4 AKFQRTKPHVNIgtIGHVDHGKTTLTAAITKVlhdkfpDLNETKAfdqidnapeerqRGITINIA--HVEYQtDKRHYAH 81
Cdd:TIGR00487 81 DLLVERPPVVTI--MGHVDHGKTSLLDSIRKT------KVAQGEA------------GGITQHIGayHVENE-DGKMITF 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 82 VDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPyILVALNKAD 141
Cdd:TIGR00487 140 LDTPGHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKID 198
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-127 |
7.42e-16 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 79.52 E-value: 7.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLT------AAItkvlhdkfpdLNETKAFDQ--IDNAPEERQRGITINIAHV----EYQtDKRHYAH 81
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllagAGM----------ISEELAGEQlaLDFDEEEQARGITIKAANVsmvhEYE-GKEYLIN 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489498552 82 -VDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTrEHVLlaRQ 127
Cdd:PRK07560 91 lIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQ 134
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
11-178 |
5.49e-15 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 76.79 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 11 PHVNIgtIGHVDHGKTTLTAAITKvlhdkfpdlnetkafdqiDNAPEERQRGITINIA----HVEYQTDKRHYAHVDAPG 86
Cdd:CHL00189 245 PIVTI--LGHVDHGKTTLLDKIRK------------------TQIAQKEAGGITQKIGayevEFEYKDENQKIVFLDTPG 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 87 HADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYIlVALNKADAVDDEELLELVEMEVRELLaAQEFD 166
Cdd:CHL00189 305 HEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPII-VAINKIDKANANTERIKQQLAKYNLI-PEKWG 382
|
170
....*....|..
gi 489498552 167 EDAPVVRVSALK 178
Cdd:CHL00189 383 GDTPMIPISASQ 394
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-141 |
1.01e-14 |
|
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: 75.85 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 1 MAKAKFQRTKphvNIGTIGHVDHGKTTLTAAI---TKVLHdKFPDLNETKAfdQIDNAPEERQRGITIN--IAHVEYQtD 75
Cdd:COG0480 1 MAEYPLEKIR---NIGIVAHIDAGKTTLTERIlfyTGAIH-RIGEVHDGNT--VMDWMPEEQERGITITsaATTCEWK-G 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489498552 76 KRHYAhVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTrEHVL-LARQVGVPYIlVALNKAD 141
Cdd:COG0480 74 HKINI-IDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQT-ETVWrQADKYGVPRI-VFVNKMD 137
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
212-296 |
1.43e-14 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 68.45 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 212 FLMPVEDVFTITGRGTVVTGRVERGVINVNEEVEIVgirPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKreDVER 291
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRIL---PKGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILT 75
|
....*
gi 489498552 292 GQVVT 296
Cdd:cd01342 76 GDTLT 80
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-142 |
3.34e-14 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 74.39 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 18 IGHVDHGKTTLTAAItkvlhdkfpdLNETKAFDQI----------DNAPEERQRGITIN--IAHVEYQtDKRHYAhVDAP 85
Cdd:PRK12740 1 VGHSGAGKTTLTEAI----------LFYTGAIHRIgevedgtttmDFMPEERERGISITsaATTCEWK-GHKINL-IDTP 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489498552 86 GHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVaLNKADA 142
Cdd:PRK12740 69 GHVDFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIF-VNKMDR 124
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-123 |
1.29e-13 |
|
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: 72.62 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 1 MAKAKFQRtkphvNIGTIGHVDHGKTTLT-------AAITKVL--HDKFPDLNEtkafdqidnapEERQRGITINIAHV- 70
Cdd:TIGR00490 13 MWKPKFIR-----NIGIVAHIDHGKTTLSdnllagaGMISEELagQQLYLDFDE-----------QEQERGITINAANVs 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 489498552 71 ---EYQTDKRHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTrEHVL 123
Cdd:TIGR00490 77 mvhEYEGNEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVL 131
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
17-141 |
1.95e-13 |
|
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: 71.58 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 17 TI-GHVDHGKTTLTAAI--TKVlhdkfpdlNETKAfdqidnapeerqRGITINIA--HVEyqTDKRHYAHVDAPGHADYI 91
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNV--------AAGEA------------GGITQHIGayQVE--TNGGKITFLDTPGHEAFT 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489498552 92 KNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPyILVALNKAD 141
Cdd:COG0532 66 AMRARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKID 114
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-141 |
2.23e-13 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 71.52 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLTAAItkvlhdkfpdLNETKAFDQI----------DNAPEERQRGITINIAHVEYQTDKRHYAHVD 83
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERI----------LFYTGKIHKMgevedgttvtDWMPQEQERGITIESAATSCDWDNHRINLID 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489498552 84 APGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPyILVALNKAD 141
Cdd:PRK13351 80 TPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIP-RLIFINKMD 136
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-142 |
2.24e-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: 69.54 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLTAAItkvlhdkfpdLNETKAFDQ----------IDNAPEERQRGITIN--IAHVEYQtDKRHYAh 81
Cdd:cd04170 1 NIALVGHSGSGKTTLAEAL----------LYATGAIDRlgrvedgntvSDYDPEEKKRKMSIEtsVAPLEWN-GHKINL- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489498552 82 VDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVaLNKADA 142
Cdd:cd04170 69 IDTPGYADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIF-INKMDR 128
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-141 |
6.42e-13 |
|
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: 67.29 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLTAAITKVLHDKFPDLNET-KAFDQIDNAPEERQRGITINIAHV-EYQTDKRHYAHV----DAPGH 87
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQTHKRTPSVKLGwKPLRYTDTRKDEQERGISIKSNPIsLVLEDSKGKSYLiniiDTPGH 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489498552 88 ADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYILVaLNKAD 141
Cdd:cd04167 82 VNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLV-INKID 134
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
303-391 |
7.24e-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: 64.34 E-value: 7.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 303 PHTEFEGQVYILSKDEggrhtPFFNNYRPQFYFRTTDVTGVVTLPEGTEM-----------VMPGDNTNISVKLIQPVAM 371
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekkppdsLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 489498552 372 DEG------LRFAIREGGRTVGAGRV 391
Cdd:cd01513 77 ERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-204 |
8.16e-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: 63.32 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLTAAI---TKVLHDKfpDLNEtkafdQI-DNAPEERQRGITI--NIAHVEYQ-TDKRHYAH--VDA 84
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSER--EMKE-----QVlDSMDLERERGITIkaQAVRLFYKaKDGEEYLLnlIDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 85 PGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPyILVALNKADAVDDEELLelvemevrellAAQE 164
Cdd:cd01890 75 PGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLE-IIPVINKIDLPAADPDR-----------VKQE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489498552 165 FDED-----APVVRVSAlKALEGdakwvasVEELMNAVDESIPDP 204
Cdd:cd01890 143 IEDVlgldaSEAILVSA-KTGLG-------VEDLLEAIVERIPPP 179
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
212-295 |
2.04e-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: 59.54 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 212 FLMPVEDVFTITGRGTVVTGRVERGVINVNEEVEI----VGirpSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKRE 287
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLgpdaDG---KFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRE 77
|
....*...
gi 489498552 288 DVERGQVV 295
Cdd:cd03694 78 SLRKGMVL 85
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-141 |
2.28e-11 |
|
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: 63.66 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLTAAI---TKVLHdKFPDLNETKAfdQIDNAPEERQRGITINIAHVEYQTDKRHYAHVDAPGHADY 90
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyyTGRIH-KIGEVHGGGA--TMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 489498552 91 IKNMITGAAQMDGAILVVAATDGPMPQTrEHVL-LARQVGVPYIlVALNKAD 141
Cdd:cd01886 78 TIEVERSLRVLDGAVAVFDAVAGVQPQT-ETVWrQADRYGVPRI-AFVNKMD 127
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
211-295 |
2.19e-10 |
|
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: 56.75 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 211 PFLMPVEDVFTITGRGTVVTGRVERGVINVNEEVEIVgirPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLRGVKREDVE 290
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVM---PSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77
|
....*
gi 489498552 291 RGQVV 295
Cdd:cd16267 78 VGSIL 82
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
14-141 |
2.50e-09 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 59.29 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLT------AAItkvlhdkfpdLNETKAFDQ--IDNAPEERQRGITINIAHV--------EYQTDKR 77
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTdslvckAGI----------ISSKNAGDArfTDTRADEQERGITIKSTGIslyyehdlEDGDDKQ 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489498552 78 HYA--HVDAPGHADYiKNMITGAAQM-DGAILVVAATDGPMPQTrEHVLlaRQVGVPYI--LVALNKAD 141
Cdd:PTZ00416 91 PFLinLIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVD 155
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
211-296 |
1.34e-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: 51.33 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 211 PFLMPVEDVFTitGRGTVVTGRVERGVINVNEEVEIVgirPSTTKTTVTGV-----EMfrkllDQGQAGDNVGLLLRGVK 285
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLM---PNKTKVEVTGIyideeEV-----DSAKPGENVKLKLKGVE 70
|
90
....*....|.
gi 489498552 286 REDVERGQVVT 296
Cdd:cd04089 71 EEDISPGFVLC 81
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
216-294 |
2.79e-08 |
|
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: 50.76 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 216 VEDVFTITGRgTVVTGRVERGVINVNEEV---EIVGIrpsttkttVTGVEMFRKLLDQGQAGDNVGLLLRGVKRedVERG 292
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKVkgdKGVAL--------IRAIEREHRKVDFAVAGDEVALILEGKIK--VKEG 73
|
..
gi 489498552 293 QV 294
Cdd:cd16265 74 DV 75
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-141 |
2.96e-08 |
|
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: 52.76 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 13 VNIGTIGHVDHGKTTLTAAITKVlhdkfpdlnetkafdqiDNAPEERQRGITINIA--HVEYQTDKRHYAHVDAPGHADY 90
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGN-----------------KGSITEYYPGTTRNYVttVIEEDGKTYKFNLLDTAGQEDY 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489498552 91 IK------NMITGAAQM-DGAILVVAATDGPMPQTREHVLLARQvGVPyILVALNKAD 141
Cdd:TIGR00231 65 DAirrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHHADS-GVP-IILVGNKID 120
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
211-296 |
9.80e-08 |
|
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: 49.04 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 211 PFLMPVEDVFTiTGRGTVVTGRVERGVINVNEEVEIVgirPSTTKTTVTGVEM-FRKLLDQGQAGDNVGLLLRGVKREDV 289
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDM---PSQQDAEVKNIIRnSDEETDWAIAGDTVTLRLRGIEVEDI 76
|
....*..
gi 489498552 290 ERGQVVT 296
Cdd:cd03698 77 QPGDILS 83
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
14-127 |
1.38e-07 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 53.57 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLT----AAITKVLHDKFPDLNETkafdqiDNAPEERQRGITI--------------NIAHVEYQTD 75
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTdslvAAAGIIAQEVAGDVRMT------DTRADEAERGITIkstgislyyemtdeSLKDFKGERD 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489498552 76 KRHYA--HVDAPGHADYiKNMITGAAQM-DGAILVVAATDGPMPQTrEHVLlaRQ 127
Cdd:PLN00116 95 GNEYLinLIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQ 145
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
18-178 |
3.66e-07 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 49.38 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 18 IGHVDHGKTTLtaaITKVLHDKFPDLnetkafdqidnaPEERQRGITINIAHVEYQTDKRHYAHVDAPGHADYIKNMITG 97
Cdd:cd00882 3 VGRGGVGKSSL---LNALLGGEVGEV------------SDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 98 AAQM-----DGAILVVAATDGPMPQTREHVLLARQV--GVPYILVaLNKADavddeellELVEMEVRELLAAQE--FDED 168
Cdd:cd00882 68 LARLllrgaDLILLVVDSTDRESEEDAKLLILRRLRkeGIPIILV-GNKID--------LLEEREVEELLRLEElaKILG 138
|
170
....*....|
gi 489498552 169 APVVRVSALK 178
Cdd:cd00882 139 VPVFEVSAKT 148
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
212-297 |
4.56e-07 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 47.18 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 212 FLMPVEDVFTITG--RGtvVTGRVERGVINVNEEVEIVgirPSTTKTTVTGVEMFRKLLDQGQAGDNVGLLLrgvKRE-D 288
Cdd:cd03695 1 FRFPVQYVNRPNLdfRG--YAGTIASGSIRVGDEVTVL---PSGKTSRVKSIVTFDGELDSAGAGEAVTLTL---EDEiD 72
|
....*....
gi 489498552 289 VERGQVVTK 297
Cdd:cd03695 73 VSRGDLIVR 81
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
18-141 |
9.71e-06 |
|
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: 47.50 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 18 IGHVDHGKTTLTAAI--TKVLHDKFPDLNETKAFDQIDNAPEERQRGITINIAHVEYQTDKRHYahVDAPGHADYIKNMI 95
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIrgTAVVKKEAGGITQHIGASEVPTDVIEKICGDLLKSFKIKLKIPGLLF--IDTPGHEAFTNLRK 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489498552 96 TGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYIlVALNKAD 141
Cdd:TIGR00491 88 RGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFV-VAANKID 132
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
19-141 |
9.90e-05 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 44.40 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 19 GHVDHGKTTL------TA-------AITKVLHDKFPDLN--ETKAFDQIDNAPEErqrgitINIAHVEYqtdkrhyahVD 83
Cdd:PRK04004 13 GHVDHGKTTLldkirgTAvaakeagGITQHIGATEVPIDviEKIAGPLKKPLPIK------LKIPGLLF---------ID 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489498552 84 APGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYIlVALNKAD 141
Cdd:PRK04004 78 TPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFV-VAANKID 134
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
14-186 |
6.48e-04 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 40.22 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 14 NIGTIGHVDHGKTTLTAAItkvLHDKF-PdlnetkafdqIDNAPEerqrgiTINIAHVEYQTdKRHYAHVDAPG------ 86
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNAL---LGEEVlP----------TGVTPT------TAVITVLRYGL-LKGVVLVDTPGlnstie 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 87 -HADYIKNMItgaAQMDGAILVVAAtDGPMPQT-REHVLLARQVGVPYILVALNKADAVDDEELLELVEMEVRELLAAQE 164
Cdd:cd09912 62 hHTEITESFL---PRADAVIFVLSA-DQPLTESeREFLKEILKWSGKKIFFVLNKIDLLSEEELEEVLEYSREELGVLEL 137
|
170 180
....*....|....*....|..
gi 489498552 165 FDEDAPVVRVSALKALEGDAKW 186
Cdd:cd09912 138 GGGEPRIFPVSAKEALEARLQG 159
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
82-141 |
8.14e-04 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 41.79 E-value: 8.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489498552 82 VDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYIlVALNKAD 141
Cdd:PRK14845 531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTPFV-VAANKID 589
|
|
| |
