|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-397 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 864.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 1 MAKEKYERTKPHVNIGTLGHVDHGKTTLTAAISTVLAKHGDNKeaAKDYASIDNAPEERERGITINTSHIEYETATRHYA 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAE--AKAYDQIDKAPEEKARGITINTAHVEYETEKRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 81 HIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVDDPELLELVEMEVRDLL 160
Cdd:PRK00049 79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 161 TEYGYPGDEVPVVAGSALLALQG--DEEQEKNVLKLMEEVDAYIPEPERETDKPFMMPVEDVFSITGRGTVATGRVERGQ 238
Cdd:PRK00049 159 SKYDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 239 IKVGDEVEIVGIhEETKKTTVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQRGQVLAAPGTITPHTKFEASVYVLSKE 318
Cdd:PRK00049 239 IKVGEEVEIVGI-RDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092675938 319 EGGRHTPFFTNYRPQFYFRTTDVTGVVELPEGTEMVMPGDNVEMTVELIHPIAIEEGTRFSIREGGRTVGAGTVTSILN 397
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: 861.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 1 MAKEKYERTKPHVNIGTLGHVDHGKTTLTAAISTVLAKHGDNKeaAKDYASIDNAPEERERGITINTSHIEYETATRHYA 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAK--AKAYDQIDKAPEEKERGITINTSHVEYETEKRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 81 HIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVDDPELLELVEMEVRDLL 160
Cdd:COG0050 79 HVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 161 TEYGYPGDEVPVVAGSALLALQGD--EEQEKNVLKLMEEVDAYIPEPERETDKPFMMPVEDVFSITGRGTVATGRVERGQ 238
Cdd:COG0050 159 SKYGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 239 IKVGDEVEIVGIHeETKKTTVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQRGQVLAAPGTITPHTKFEASVYVLSKE 318
Cdd:COG0050 239 IKVGDEVEIVGIR-DTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092675938 319 EGGRHTPFFTNYRPQFYFRTTDVTGVVELPEGTEMVMPGDNVEMTVELIHPIAIEEGTRFSIREGGRTVGAGTVTSIL 396
Cdd:COG0050 318 EGGRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKII 395
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-396 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 831.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 1 MAKEKYERTKPHVNIGTLGHVDHGKTTLTAAISTVLAKHGDNKeaAKDYASIDNAPEERERGITINTSHIEYETATRHYA 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGE--AKAYDQIDNAPEEKARGITINTSHVEYETANRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 81 HIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVDDPELLELVEMEVRDLL 160
Cdd:PRK12735 79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 161 TEYGYPGDEVPVVAGSALLALQGD--EEQEKNVLKLMEEVDAYIPEPERETDKPFMMPVEDVFSITGRGTVATGRVERGQ 238
Cdd:PRK12735 159 SKYDFPGDDTPIIRGSALKALEGDddEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 239 IKVGDEVEIVGIHeETKKTTVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQRGQVLAAPGTITPHTKFEASVYVLSKE 318
Cdd:PRK12735 239 VKVGDEVEIVGIK-ETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092675938 319 EGGRHTPFFTNYRPQFYFRTTDVTGVVELPEGTEMVMPGDNVEMTVELIHPIAIEEGTRFSIREGGRTVGAGTVTSIL 396
Cdd:PRK12735 318 EGGRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKII 395
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-396 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 813.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 1 MAKEKYERTKPHVNIGTLGHVDHGKTTLTAAISTVLAKHGDNKeaAKDYASIDNAPEERERGITINTSHIEYETATRHYA 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQ--AKDYDSIDAAPEEKERGITINTAHVEYETEKRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 81 HIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVDDPELLELVEMEVRDLL 160
Cdd:PRK12736 79 HVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 161 TEYGYPGDEVPVVAGSALLALQGDEEQEKNVLKLMEEVDAYIPEPERETDKPFMMPVEDVFSITGRGTVATGRVERGQIK 240
Cdd:PRK12736 159 SEYDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 241 VGDEVEIVGIHeETKKTTVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQRGQVLAAPGTITPHTKFEASVYVLSKEEG 320
Cdd:PRK12736 239 VGDEVEIVGIK-ETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEG 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092675938 321 GRHTPFFTNYRPQFYFRTTDVTGVVELPEGTEMVMPGDNVEMTVELIHPIAIEEGTRFSIREGGRTVGAGTVTSIL 396
Cdd:PRK12736 318 GRHTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEIL 393
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-397 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 741.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 1 MAKEKYERTKPHVNIGTLGHVDHGKTTLTAAISTVLAKHGDNKeaAKDYASIDNAPEERERGITINTSHIEYETATRHYA 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAK--AKKYDEIDSAPEEKARGITINTAHVEYETENRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 81 HIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVDDPELLELVEMEVRDLL 160
Cdd:CHL00071 79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 161 TEYGYPGDEVPVVAGSALLALQ----------GDEEQEKNVLKLMEEVDAYIPEPERETDKPFMMPVEDVFSITGRGTVA 230
Cdd:CHL00071 159 SKYDFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 231 TGRVERGQIKVGDEVEIVGIhEETKKTTVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQRGQVLAAPGTITPHTKFEA 310
Cdd:CHL00071 239 TGRIERGTVKVGDTVEIVGL-RETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 311 SVYVLSKEEGGRHTPFFTNYRPQFYFRTTDVTGVVEL-----PEGTEMVMPGDNVEMTVELIHPIAIEEGTRFSIREGGR 385
Cdd:CHL00071 318 QVYILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGR 397
|
410
....*....|..
gi 1092675938 386 TVGAGTVTSILN 397
Cdd:CHL00071 398 TVGAGVVSKILK 409
|
|
| 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: 735.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 1 MAKEKYERTKPHVNIGTLGHVDHGKTTLTAAISTVLAKHGdnKEAAKDYASIDNAPEERERGITINTSHIEYETATRHYA 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEG--GAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 81 HIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVDDPELLELVEMEVRDLL 160
Cdd:TIGR00485 79 HVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 161 TEYGYPGDEVPVVAGSALLALQGDEEQEKNVLKLMEEVDAYIPEPERETDKPFMMPVEDVFSITGRGTVATGRVERGQIK 240
Cdd:TIGR00485 159 SQYDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 241 VGDEVEIVGIhEETKKTTVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQRGQVLAAPGTITPHTKFEASVYVLSKEEG 320
Cdd:TIGR00485 239 VGEEVEIVGL-KDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEG 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092675938 321 GRHTPFFTNYRPQFYFRTTDVTGVVELPEGTEMVMPGDNVEMTVELIHPIAIEEGTRFSIREGGRTVGAGTVTSIL 396
Cdd:TIGR00485 318 GRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKIL 393
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
2-396 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 682.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 2 AKEKYERTKPHVNIGTLGHVDHGKTTLTAAISTVLAKHGDNKEAAkdYASIDNAPEERERGITINTSHIEYETATRHYAH 81
Cdd:PLN03127 51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVA--FDEIDKAPEEKARGITIATAHVEYETAKRHYAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 82 IDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVDDPELLELVEMEVRDLLT 161
Cdd:PLN03127 129 VDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 162 EYGYPGDEVPVVAGSALLALQG--DEEQEKNVLKLMEEVDAYIPEPERETDKPFMMPVEDVFSITGRGTVATGRVERGQI 239
Cdd:PLN03127 209 FYKFPGDEIPIIRGSALSALQGtnDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 240 KVGDEVEIVGI-HEETKKTTVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQRGQVLAAPGTITPHTKFEASVYVLSKE 318
Cdd:PLN03127 289 KVGEEVEIVGLrPGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKD 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092675938 319 EGGRHTPFFTNYRPQFYFRTTDVTGVVELPEGTEMVMPGDNVEMTVELIHPIAIEEGTRFSIREGGRTVGAGTVTSIL 396
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: 615.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 2 AKEKYERTKPHVNIGTLGHVDHGKTTLTAAISTVLAKHGDNkeAAKDYASIDNAPEERERGITINTSHIEYETATRHYAH 81
Cdd:PLN03126 71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGS--APKKYDEIDAAPEERARGITINTATVEYETENRHYAH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 82 IDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVDDPELLELVEMEVRDLLT 161
Cdd:PLN03126 149 VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 162 EYGYPGDEVPVVAGSALLALQ----------GDEEQEKNVLKLMEEVDAYIPEPERETDKPFMMPVEDVFSITGRGTVAT 231
Cdd:PLN03126 229 SYEFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVAT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 232 GRVERGQIKVGDEVEIVGIhEETKKTTVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQRGQVLAAPGTITPHTKFEAS 311
Cdd:PLN03126 309 GRVERGTVKVGETVDIVGL-RETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAI 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 312 VYVLSKEEGGRHTPFFTNYRPQFYFRTTDVTGVV-----ELPEGTEMVMPGDNVEMTVELIHPIAIEEGTRFSIREGGRT 386
Cdd:PLN03126 388 VYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKT 467
|
410
....*....|
gi 1092675938 387 VGAGTVTSIL 396
Cdd:PLN03126 468 VGAGVIQSII 477
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-205 |
2.53e-134 |
|
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: 382.32 E-value: 2.53e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 11 PHVNIGTLGHVDHGKTTLTAAISTVLAKHGdnKEAAKDYASIDNAPEERERGITINTSHIEYETATRHYAHIDAPGHADY 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKG--GAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 91 VKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVDDPELLELVEMEVRDLLTEYGYPGDEV 170
Cdd:cd01884 79 IKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDT 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1092675938 171 PVVAGSALLALQGDEEQE--KNVLKLMEEVDAYIPEP 205
Cdd:cd01884 159 PIVRGSALKALEGDDPNKwvDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-395 |
4.35e-93 |
|
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: 285.67 E-value: 4.35e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 1 MAKEKyertkPHVNIGTLGHVDHGKTTLTAAIstvLAKHG--------DNKEAAKD-------YASI-DNAPEERERGIT 64
Cdd:COG5256 1 MASEK-----PHLNLVVIGHVDHGKSTLVGRL---LYETGaidehiieKYEEEAEKkgkesfkFAWVmDRLKEERERGVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 65 INTSHIEYETATRHYAHIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVD 144
Cdd:COG5256 73 IDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 145 -DPELLELVEMEVRDLLTEYGYPGDEVPVVAGSALLalqGDeeqekNVLK------------LMEEVDAyIPEPERETDK 211
Cdd:COG5256 153 ySEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWK---GD-----NVVKksdnmpwyngptLLEALDN-LKEPEKPVDK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 212 PFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIVGIHeetKKTTVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQ 291
Cdd:COG5256 224 PLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAG---VVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 292 RGQVLAAPGT-ITPHTKFEASVYVLskeeggRHTPFFT-NYRPQFYFRTTDV--------------TG-VVElpEGTEMV 354
Cdd:COG5256 301 RGDVAGHPDNpPTVAEEFTAQIVVL------QHPSAITvGYTPVFHVHTAQVactfvelvskldprTGqVKE--ENPQFL 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1092675938 355 MPGDNVEMTVELIHPIAIE------EGTRFSIREGGRTVGAGTVTSI 395
Cdd:COG5256 373 KTGDAAIVKIKPTKPLVIEkfkefpQLGRFAIRDMGQTVAAGVVLDV 419
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-203 |
5.76e-89 |
|
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: 266.70 E-value: 5.76e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 10 KPHVNIGTLGHVDHGKTTLTAAISTVLAK-HGDNKEAAKDYASIDNAPEERERGITINTSHIEYETATRHYAHIDAPGHA 88
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAiSKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 89 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPyFVVFLNKVDQVDDPELLELVEMEVRDLLTEYGYPGD 168
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1092675938 169 EVPVVAGSALLALqgdeeqekNVLKLMEEVDAYIP 203
Cdd:pfam00009 160 FVPVVPGSALKGE--------GVQTLLDALDEYLP 186
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-395 |
6.68e-88 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 272.57 E-value: 6.68e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 8 RTKPHVNIGTLGHVDHGKTTL-------TAAI-STVLAKHgdnKEAAKD-------YASI-DNAPEERERGITINTSHIE 71
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLvgrllyeTGAIdEHIIEEL---REEAKEkgkesfkFAWVmDRLKEERERGVTIDLAHKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 72 YETATRHYAHIDAPGHADYVKNMITGAAQMDGAILVVSAAD--GPMPQTREHILLAHQVGVPYFVVFLNKVDQVD-DPEL 148
Cdd:PRK12317 79 FETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 149 LELVEMEVRDLLTEYGYPGDEVPVVAGSallALQGDeeqekNVLK------------LMEEVDAyIPEPERETDKPFMMP 216
Cdd:PRK12317 159 YEEVKEEVSKLLKMVGYKPDDIPFIPVS---AFEGD-----NVVKksenmpwyngptLLEALDN-LKPPEKPTDKPLRIP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 217 VEDVFSITGRGTVATGRVERGQIKVGDEVeivgIHEETKKT-TVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQRGQV 295
Cdd:PRK12317 230 IQDVYSISGVGTVPVGRVETGVLKVGDKV----VFMPAGVVgEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 296 LAAPGTI-TPHTKFEASVYVLskeeggRHTPFFT-NYRPQFYFRTTDV--------------TG-VVElpEGTEMVMPGD 358
Cdd:PRK12317 306 CGHPDNPpTVAEEFTAQIVVL------QHPSAITvGYTPVFHAHTAQVactfeelvkkldprTGqVAE--ENPQFIKTGD 377
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1092675938 359 NVEMTVELIHPIAIEEGT------RFSIREGGRTVGAGTVTSI 395
Cdd:PRK12317 378 AAIVKIKPTKPLVIEKVKeipqlgRFAIRDMGQTIAAGMVIDV 420
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-392 |
2.60e-74 |
|
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: 242.90 E-value: 2.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 13 VNIGTLGHVDHGKTTLTAA---ISTvlakhgdnkeaakdyasiDNAPEERERGITINTShieyetatrhYAH-------- 81
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKAltgIDT------------------DRLKEEKKRGITIDLG----------FAYlplpdgrr 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 82 ---IDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVdDPELLELVEMEVRD 158
Cdd:COG3276 53 lgfVDVPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 159 LLTEYGYPGdeVPVVAGSAlLALQGDEEqeknvlkLMEEVDAYIPE-PERETDKPFMMPVEDVFSITGRGTVATGRVERG 237
Cdd:COG3276 132 LLAGTFLED--APIVPVSA-VTGEGIDE-------LRAALDALAAAvPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 238 QIKVGDEVEIVGIHEETKkttVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQRGQVLAAPGTITPHTKFEASVYVLSK 317
Cdd:COG3276 202 TVRVGDELELLPSGKPVR---VRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPS 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092675938 318 EeggrHTPFFTNYRPQFYFRTTDVTGVVELPEGTEMVmPGDnvEMTVELI--HPIAIEEGTRFSIREGG--RTVGAGTV 392
Cdd:COG3276 279 A----PRPLKHWQRVHLHHGTAEVLARVVLLDREELA-PGE--EALAQLRleEPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
303-392 |
7.66e-65 |
|
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: 201.59 E-value: 7.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 303 TPHTKFEASVYVLSKEEGGRHTPFFTNYRPQFYFRTTDVTGVVELPEGTEMVMPGDNVEMTVELIHPIAIEEGTRFSIRE 382
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 1092675938 383 GGRTVGAGTV 392
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-395 |
1.27e-64 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 213.07 E-value: 1.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 1 MAKEKyertkPHVNIGTLGHVDHGKTTLTAAIstvLAKHGD---------NKEAAK------DYA-SIDNAPEERERGIT 64
Cdd:PTZ00141 1 MGKEK-----THINLVVIGHVDSGKSTTTGHL---IYKCGGidkrtiekfEKEAAEmgkgsfKYAwVLDKLKAERERGIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 65 INTSHIEYETATRHYAHIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLAHQVGVPYFVVFL 137
Cdd:PTZ00141 73 IDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 138 NKVD--QVD-DPELLELVEMEVRDLLTEYGYPGDEVPVVAGSallALQGDEEQEKNV-------LKLMEEVDAYIPePER 207
Cdd:PTZ00141 153 NKMDdkTVNySQERYDEIKKEVSAYLKKVGYNPEKVPFIPIS---GWQGDNMIEKSDnmpwykgPTLLEALDTLEP-PKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 208 ETDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEI--VGIHEETKKttvtgVEMFRKMLDYAEAGDNIGALLRGI 285
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFapSGVTTEVKS-----VEMHHEQLAEAVPGDNVGFNVKNV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 286 TREDIQRGQVlAAPGTITPH---TKFEASVYVLS--KEEGGRHTPF-----------FTNYRPQFYFRTTDVtgvveLPE 349
Cdd:PTZ00141 304 SVKDIKRGYV-ASDSKNDPAkecADFTAQVIVLNhpGQIKNGYTPVldchtahiackFAEIESKIDRRSGKV-----LEE 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1092675938 350 GTEMVMPGDNVEMTVELIHPIAIEEGT------RFSIREGGRTVGAGTVTSI 395
Cdd:PTZ00141 378 NPKAIKSGDAAIVKMVPTKPMCVEVFNeypplgRFAVRDMKQTVAVGVIKSV 429
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-205 |
1.36e-56 |
|
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: 183.65 E-value: 1.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTAAISTVLakHGDNKEAAKDYASIDNAPEERERGITINTSHIEYETATRHYAHIDAPGHADYVKN 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQT--GAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 94 MITGAAQMDGAILVVSAADGPMPQTREHILLAhQVGVPYFVVFLNKVDQVdDPELLELVEMEVRDLLTEYGY---PGDEV 170
Cdd:cd00881 79 TVRGLAQADGALLVVDANEGVEPQTREHLNIA-LAGGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDV 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1092675938 171 PVVAGSALLALQGDEeqeknvlkLMEEVDAYIPEP 205
Cdd:cd00881 157 PIIPISALTGEGIEE--------LLDAIVEHLPPP 183
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-390 |
2.33e-54 |
|
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: 188.93 E-value: 2.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 13 VNIGTLGHVDHGKTTLTAAISTVlakhgdnkeaakdyaSIDNAPEERERGITINTSHIEYETATRHYAHIDAPGHADYVK 92
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGI---------------AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFIS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 93 NMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVDDpELLELVEMEVRDLLTEYGYpGDEVPV 172
Cdd:TIGR00475 66 NAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNE-EEIKRTEMFMKQILNSYIF-LKNAKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 173 VAGSALLAlQGDEEQEKNVLKLMEEVDAyipepeRETDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIVGIHE 252
Cdd:TIGR00475 144 FKTSAKTG-QGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 253 ETKkttVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQRGQVLAAPgtitPHTKFEASVYVLSkeeggrHTPFFTNYRP 332
Cdd:TIGR00475 217 EVR---VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLLELQPY 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 333 QFYFRTTDVTGVVELPEGT--EMVMPGdnvemtvelihPIAIEEGTRFSIREGGRTVGAG 390
Cdd:TIGR00475 284 HIAHGMSVTTGKISLLDKGiaLLTLDA-----------PLILAKGDKLVLRDSSGNFLAG 332
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
11-392 |
6.92e-50 |
|
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: 173.31 E-value: 6.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 11 PHVNIGTLGHVDHGKTTLTAAISTVLakhgdnkeaakdyasIDNAPEERERGITINTSHI-----------EYETAT--- 76
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVW---------------TDTHSEELKRGISIRLGYAdaeiykcpecdGPECYTtep 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 77 ------------RHYAHIDAPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLAHQVGVPYFVVFLNKVDQV 143
Cdd:TIGR03680 68 vcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 144 DDPELLELVEmEVRDLLTeyGYPGDEVPVVAGSALlalqgdeeQEKNVLKLMEEVDAYIPEPERETDKPFMMPVEDVFSI 223
Cdd:TIGR03680 148 SKEKALENYE-EIKEFVK--GTVAENAPIIPVSAL--------HNANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 224 TGRGT--------VATGRVERGQIKVGDEVEIV-GI-HEETKK-------TTVTGVEMFRKMLDYAEAGD--NIGALLR- 283
Cdd:TIGR03680 217 NKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIkVEKGGKtkwepiyTEITSLRAGGYKVEEARPGGlvGVGTKLDp 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 284 GITREDIQRGQVLAAPGTITP-HTKFEASVYVLSK----EEGGRHTPFFTNYRPQFYFRTTDVTGVVELPEGTemvmpgd 358
Cdd:TIGR03680 297 ALTKADALAGQVVGKPGTLPPvWESLELEVHLLERvvgtEEELKVEPIKTGEVLMLNVGTATTVGVVTSARKD------- 369
|
410 420 430
....*....|....*....|....*....|....*...
gi 1092675938 359 nvEMTVELIHPIAIEEGTRFSI--REGGR--TVGAGTV 392
Cdd:TIGR03680 370 --EIEVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 405
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
213-300 |
1.06e-49 |
|
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: 162.30 E-value: 1.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 213 FMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIVGIhEETKKTTVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQR 292
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGF-KETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVER 79
|
....*...
gi 1092675938 293 GQVLAAPG 300
Cdd:cd03697 80 GMVLAKPG 87
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
301-395 |
3.18e-49 |
|
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: 161.66 E-value: 3.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 301 TITPHTKFEASVYVLSKEEGGRHTPFFTNYRPQFYFRTTDVTG-VVEL-----PEGT----EMVMPGDNVEMTVELIHPI 370
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGkFVELlhkldPGGVsenpEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 1092675938 371 AIEEGTRFSIREGGRTVGAGTVTSI 395
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
4-392 |
2.25e-48 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 169.26 E-value: 2.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 4 EKYERTKPHVNIGTLGHVDHGKTTLTAAISTV-LAKHGdnkeaakdyasidnapEERERGITI-------------NTSH 69
Cdd:PRK04000 1 MMWEKVQPEVNIGMVGHVDHGKTTLVQALTGVwTDRHS----------------EELKRGITIrlgyadatirkcpDCEE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 70 IEYETAT-------------RHYAHIDAPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLAHQVGVPYFVV 135
Cdd:PRK04000 65 PEAYTTEpkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 136 FLNKVDQVDDPELLELVEmEVRDLLTeyGYPGDEVPVVAGSALlalqgdeeQEKNVLKLMEEVDAYIPEPERETDKPFMM 215
Cdd:PRK04000 145 VQNKIDLVSKERALENYE-QIKEFVK--GTVAENAPIIPVSAL--------HKVNIDALIEAIEEEIPTPERDLDKPPRM 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 216 PVEDVFSITGRGT--------VATGRVERGQIKVGDEVEIV-GI-HEETKK-------TTVTGVEMFRKMLDYAEAGD-- 276
Cdd:PRK04000 214 YVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIkVEEGGKtkwepitTKIVSLRAGGEKVEEARPGGlv 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 277 NIGALLR-GITREDIQRGQVLAAPGTITP-HTKFEASVYVLSK----EEGGRHTPFFTNYRPQFYFRTTDVTGVVelpeg 350
Cdd:PRK04000 294 GVGTKLDpSLTKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLNVGTATTVGVV----- 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1092675938 351 TEMvmpGDNvEMTVELIHPIAIEEGTRFSI--REGGR--TVGAGTV 392
Cdd:PRK04000 369 TSA---RKD-EAEVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 410
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
4-396 |
4.27e-48 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 171.27 E-value: 4.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 4 EKYERTKPHVNIGTLGHVDHGKTTLTAAISTVLAKHGDNKEAAKdyasIDNAPEERERGITINTSHIEY----------- 72
Cdd:COG5258 114 EGKEKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF----LDVQPHEVERGLSADLSYAVYgfdddgpvrmk 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 73 ------------ETATRHYAHIDAPGHADYVKNMITG--AAQMDGAILVVSAADGPMPQTREH--ILLAhqVGVPYFVVf 136
Cdd:COG5258 190 nplrktdrarvvEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLA--MDLPVIVA- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 137 LNKVDQVDDpELLELVEMEVRDLLTEYGypgdEVPVVAGSALLALQGDEEQEKNV-------------LKLMEEVDAYIP 203
Cdd:COG5258 267 ITKIDKVDD-ERVEEVEREIENLLRIVG----RTPLEVESRHDVDAAIEEINGRVvpilktsavtgegLDLLDELFERLP 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 204 EPERETDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIVGIHE-ETKKTTVTGVEMFRKMLDYAEAGDNIGALL 282
Cdd:COG5258 342 KRATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDgSFREVEVKSIEMHYHRVDKAEAGRIVGIAL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 283 RGITREDIQRGQVLAAPGTI-TPHTKFEASVYVLSkeeggrH-TPFFTNYRPQFYFRTTDVTGVVElPEGTEMVMPGDNV 360
Cdd:COG5258 422 KGVEEEELERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAVRFE-PIDKGYLLPGDSG 494
|
410 420 430
....*....|....*....|....*....|....*..
gi 1092675938 361 EMTVE-LIHPIAIEEGTRFSIREgGRTVGAGTVTSIL 396
Cdd:COG5258 495 RVRLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDIL 530
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-318 |
2.23e-47 |
|
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: 167.19 E-value: 2.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 1 MAKEKYERTKPHVNIGTL-----GHVDHGKTTLT---------------AAISTVLAKHGDNKeaakdyasIDNAP---- 56
Cdd:COG2895 1 MSTDIEAYLAQHENKDLLrfitcGSVDDGKSTLIgrllydtksifedqlAALERDSKKRGTQE--------IDLALltdg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 57 --EERERGITINTSHIEYETATRHYAHIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFV 134
Cdd:COG2895 73 lqAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 135 VFLNKVDQVD-DPELLELVEMEVRDLLTEYGYPGDE-VPVvagSallALQGDeeqekNV---------------LKLMEE 197
Cdd:COG2895 153 VAVNKMDLVDySEEVFEEIVADYRAFAAKLGLEDITfIPI---S---ALKGD-----NVversenmpwydgptlLEHLET 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 198 VDAyipePERETDKPFMMPVEDV--FSITGRGtVAtGRVERGQIKVGDEVEIV--GiheetKKTTVTGVEMFRKMLDYAE 273
Cdd:COG2895 222 VEV----AEDRNDAPFRFPVQYVnrPNLDFRG-YA-GTIASGTVRVGDEVVVLpsG-----KTSTVKSIVTFDGDLEEAF 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1092675938 274 AGDNIGALLrgiTRE-DIQRGQVLAAPG-TITPHTKFEASVYVLSKE 318
Cdd:COG2895 291 AGQSVTLTL---EDEiDISRGDVIVAADaPPEVADQFEATLVWMDEE 334
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-395 |
5.20e-45 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 161.03 E-value: 5.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 1 MAKEKYertkpHVNIGTLGHVDHGKTTLTAAISTVLAKHGD------NKEAAK------DYA-SIDNAPEERERGITINT 67
Cdd:PLN00043 1 MGKEKV-----HINIVVIGHVDSGKSTTTGHLIYKLGGIDKrvierfEKEAAEmnkrsfKYAwVLDKLKAERERGITIDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 68 SHIEYETATRHYAHIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLAHQVGVPYFVVFLNKV 140
Cdd:PLN00043 76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 141 DQVD---DPELLELVEMEVRDLLTEYGYPGDEVPVVAGSallALQGDEEQEKNV-------LKLMEEVDAyIPEPERETD 210
Cdd:PLN00043 156 DATTpkySKARYDEIVKEVSSYLKKVGYNPDKIPFVPIS---GFEGDNMIERSTnldwykgPTLLEALDQ-INEPKRPSD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 211 KPFMMPVEDVFSITGRGTVATGRVERGQIKVGdevEIVGIHEETKKTTVTGVEMFRKMLDYAEAGDNIGALLRGITREDI 290
Cdd:PLN00043 232 KPLRLPLQDVYKIGGIGTVPVGRVETGVIKPG---MVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 291 QRGQVlAAPGTITP---HTKFEASVYVLSK--EEGGRHTPFFTNYRPQFYFRTTDVTGVVELPEGTEM------VMPGDN 359
Cdd:PLN00043 309 KRGYV-ASNSKDDPakeAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1092675938 360 VEMTVELIHPIAIEEGT------RFSIREGGRTVGAGTVTSI 395
Cdd:PLN00043 388 GFVKMIPTKPMVVETFSeypplgRFAVRDMRQTVAVGVIKSV 429
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-178 |
2.86e-44 |
|
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: 153.03 E-value: 2.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTAAI--------STVLAKHGdnKEAAK------DYASI-DNAPEERERGITINTSHIEYETATRH 78
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLlyklggvdKRTIEKYE--KEAKEmgkesfKYAWVlDKLKEERERGVTIDVGLAKFETEKYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 79 YAHIDAPGHADYVKNMITGAAQMDGAILVVSAADG-------PMPQTREHILLAHQVGVPYFVVFLNKVDQVDDP---EL 148
Cdd:cd01883 79 FTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNwsqER 158
|
170 180 190
....*....|....*....|....*....|
gi 1092675938 149 LELVEMEVRDLLTEYGYPGDEVPVVAGSAL 178
Cdd:cd01883 159 YDEIKKKVSPFLKKVGYNPKDVPFIPISGF 188
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-394 |
8.68e-43 |
|
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: 154.22 E-value: 8.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 8 RTKPHVNIGTLGHVDHGKTTLTAAISTV-LAKHGdnkeaakdyasidnapEERERGITINtshIEYETAT---------- 76
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVwTDRHS----------------EELKRGITIR---LGYADATfykcpncepp 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 77 -------------------RHYAHIDAPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLAHQVGVPYFVVF 136
Cdd:COG5257 62 eayttepkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 137 LNKVDQVDDPELLELVEmEVRDLLTeyGYPGDEVPVVAGSALlalqgdeeQEKNVLKLMEEVDAYIPEPERETDKPFMMP 216
Cdd:COG5257 142 QNKIDLVSKERALENYE-QIKEFVK--GTVAENAPIIPVSAQ--------HKVNIDALIEAIEEEIPTPERDLSKPPRML 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 217 VEDVFSITGRGT--------VATGRVERGQIKVGDEVEI---VGIHEETKK------TTVTGVEMFRKMLDYAEAGD--N 277
Cdd:COG5257 211 VARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIrpgIKVEKGGKTkyepitTTVVSLRAGGEEVEEAKPGGlvA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 278 IGALLR-GITREDIQRGQVLAAPGTITP-HTKFEASVYVLSKEEGgrhtpfftnyrpqfyfrTTDVTGVVELPEGtEMVM 355
Cdd:COG5257 291 VGTKLDpSLTKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLERVVG-----------------TKEEVKVEPIKTG-EPLM 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092675938 356 PgdNV---------------EMTVELIHPIAIEEGTRFSI--REGG--RTVGAGTVTS 394
Cdd:COG5257 353 L--NVgtattvgvvtsarkdEIEVKLKRPVCAEKGSRVAIsrRIGGrwRLIGWGIIKE 408
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-298 |
3.92e-41 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 153.28 E-value: 3.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 15 IGTLGHVDHGKTTLTAAISTVLAkhgdnkeaakdyasiDNAPEERERGITINTSHIEY-ETATRHYAHIDAPGHADYVKN 93
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNA---------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 94 MITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVDDPELLElVEMEVRDLLTEYGYPGDEVPVV 173
Cdd:PRK10512 68 MLAGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGFAEAKLFVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 174 AGSallALQGDEEQEKNVLKLmeevdayiPEPERETDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIVGIHee 253
Cdd:PRK10512 147 AAT---EGRGIDALREHLLQL--------PEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVN-- 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1092675938 254 tKKTTVTGVEMFRKMLDYAEAGDNIGALLRG-ITREDIQRGQVLAA 298
Cdd:PRK10512 214 -KPMRVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRGDWLLA 258
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-304 |
7.65e-38 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 144.01 E-value: 7.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTAAI---STVLAKHGDNKEAAKDyaSIDnapEERERGITI---NTShIEYETAtrhyaHI---DA 84
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALlkqSGTFRENQEVAERVMD--SND---LERERGITIlakNTA-VRYKGV-----KInivDT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 85 PGHADY------VKNMItgaaqmDGAILVVSAADGPMPQTRehillahqvgvpyFV------------VFLNKVDQVD-D 145
Cdd:COG1217 77 PGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR-------------FVlkkalelglkpiVVINKIDRPDaR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 146 PEllELVEmEVRDLLTEYGYPGD--EVPVVAGSallALQG-----DEEQEKNVLKLMEEVDAYIPEPERETDKPFMMPVE 218
Cdd:COG1217 138 PD--EVVD-EVFDLFIELGATDEqlDFPVVYAS---ARNGwasldLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 219 DVFSITGRGTVATGRVERGQIKVGDEVEIVGIHEETKKTTVTGVEMF----RKMLDYAEAGDnIGALLrGItrEDIQRGQ 294
Cdd:COG1217 212 NLDYSDYVGRIAIGRIFRGTIKKGQQVALIKRDGKVEKGKITKLFGFegleRVEVEEAEAGD-IVAIA-GI--EDINIGD 287
|
330
....*....|
gi 1092675938 295 VLAAPGTITP 304
Cdd:COG1217 288 TICDPENPEA 297
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-200 |
7.10e-37 |
|
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: 131.96 E-value: 7.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 15 IGTLGHVDHGKTTLTAAISTVlakhgdnkeaakdyaSIDNAPEERERGITINT--SHIEYETATRhYAHIDAPGHADYVK 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI---------------ETDRLPEEKKRGITIDLgfAYLDLPDGKR-LGFIDVPGHEKFVK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 93 NMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVdDPELLELVEMEVRDLLTEYGYPGdeVPV 172
Cdd:cd04171 66 NMLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFLAD--API 142
|
170 180
....*....|....*....|....*...
gi 1092675938 173 VAGSALLAlQGDEEQEKNVLKLMEEVDA 200
Cdd:cd04171 143 FPVSSVTG-EGIEELKNYLDELAEPQSK 169
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
303-395 |
4.71e-35 |
|
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: 124.27 E-value: 4.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 303 TPHTKFEASVYVLSKEEGGRHTPFFTNYRPQFYFRTTDVTGVVELPEGTEMVMPGDNVEMTVELIHPIAIEEGTRFSIRE 382
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 1092675938 383 GGRTVGAGTVTSI 395
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-299 |
2.59e-34 |
|
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: 133.97 E-value: 2.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTAAI---STVLAKHGDNKEAAKDyaSIDnapEERERGITI---NTShIEYETATRHYahIDAPGH 87
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALlkqSGTFRANEAVAERVMD--SND---LERERGITIlakNTA-IRYNGTKINI--VDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 88 ADY------VKNMItgaaqmDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVfLNKVDQVD-DPEllELVEmEVRDLL 160
Cdd:TIGR01394 75 ADFggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPSaRPD--EVVD-EVFDLF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 161 TEYGYPGDEV--PVVAGSAL--LALQGDEEQEKNVLKLMEEVDAYIPEPERETDKPFMMPVE--DVFSITGRgtVATGRV 234
Cdd:TIGR01394 145 AELGADDEQLdfPIVYASGRagWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLGR--IAIGRV 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092675938 235 ERGQIKVGDEVEIVGIHEETKKTTVTGVEMF----RKMLDYAEAGDnIGALLrGItrEDIQRGQVLAAP 299
Cdd:TIGR01394 223 HRGTVKKGQQVALMKRDGTIENGRISKLLGFegleRVEIDEAGAGD-IVAVA-GL--EDINIGETIADP 287
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-317 |
1.06e-31 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 125.12 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 13 VNIGTLGHVDHGKTTLTAAIS---TVLAKHgdnkeaakdyasidnapeERERGITIntsHIEYETA-------------- 75
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSgvkTVRFKR------------------EKVRNITI---KLGYANAkiykcpkcprptcy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 76 ----------------------TRHYAHIDAPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLAHQVGVPY 132
Cdd:PTZ00327 94 qsygsskpdnppcpgcghkmtlKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 133 FVVFLNKVDQVDDPELLELVEmEVRDLLTeyGYPGDEVPVVAGSALLalqgdeeqEKNVLKLMEEVDAYIPEPERE-TDK 211
Cdd:PTZ00327 174 IIILQNKIDLVKEAQAQDQYE-EIRNFVK--GTIADNAPIIPISAQL--------KYNIDVVLEYICTQIPIPKRDlTSP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 212 PFMM---------PVEDVFSItgRGTVATGRVERGQIKVGDEVEIV-GIHEETKKTTVTGVEMFRKM---------LDYA 272
Cdd:PTZ00327 243 PRMIvirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEIRpGIISKDSGGEFTCRPIRTRIvslfaenneLQYA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1092675938 273 EAGDNIGA---LLRGITREDIQRGQVLAAPGTITP-HTKFEASVYVLSK 317
Cdd:PTZ00327 321 VPGGLIGVgttIDPTLTRADRLVGQVLGYPGKLPEvYAEIEIQYYLLRR 369
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-184 |
1.63e-30 |
|
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: 116.13 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 17 TLGHVDHGKTTL-------TAAI----------STVLAKHGDNKeaakDYAS-IDNAPEERERGITINTSHIEYETATRH 78
Cdd:cd04166 4 TCGSVDDGKSTLigrllydSKSIfedqlaalerSKSSGTQGEKL----DLALlVDGLQAEREQGITIDVAYRYFSTPKRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 79 YAHIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVD-DPELLELVEMEVR 157
Cdd:cd04166 80 FIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDyDEEVFEEIKADYL 159
|
170 180
....*....|....*....|....*..
gi 1092675938 158 DLLTEYGypgdeVPVVAGSALLALQGD 184
Cdd:cd04166 160 AFAASLG-----IEDITFIPISALEGD 181
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
17-304 |
7.07e-29 |
|
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: 116.32 E-value: 7.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 17 TLGHVDHGKTTLT---------------AAISTVLAKHGDNKEAAkDYA-SIDNAPEERERGITINTSHIEYETATRHYA 80
Cdd:TIGR02034 5 TCGSVDDGKSTLIgrllhdtkqiyedqlAALERDSKKHGTQGGEI-DLAlLVDGLQAEREQGITIDVAYRYFSTDKRKFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 81 HIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVD-DPELLELVEMEVRDL 159
Cdd:TIGR02034 84 VADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDyDEEVFENIKKDYLAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 160 LTEYGyPGDEVPVvagsALLALQGDEEQEKN----------VLKLMEEVDAyipePERETDKPFMMPVEDV--------- 220
Cdd:TIGR02034 164 AEQLG-FRDVTFI----PLSALKGDNVVSRSesmpwysgptLLEILETVEV----ERDAQDLPLRFPVQYVnrpnldfrg 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 221 FSitgrGTVATGRVergqiKVGDEVEIVgihEETKKTTVTGVEMFRKMLDYAEAGDNIGALLRgitRE-DIQRGQVLAAP 299
Cdd:TIGR02034 235 YA----GTIASGSV-----HVGDEVVVL---PSGRSSRVARIVTFDGDLEQARAGQAVTLTLD---DEiDISRGDLLAAA 299
|
....*
gi 1092675938 300 GTITP 304
Cdd:TIGR02034 300 DSAPE 304
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-207 |
3.43e-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: 109.66 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 13 VNIGTLGHVDHGKTTLTAAISTVlakhgdnkeaakdyaSIDNAPEERERGITI-----------------NTSHIEYE-- 73
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGV---------------WTVRHKEELKRNITIklgyanakiykcpncgcPRPYDTPEce 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 74 --------TATRHYAHIDAPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLAHQVGVPYFVVFLNKVDQVD 144
Cdd:cd01888 66 cpgcggetKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092675938 145 DPELLELVEmEVRDLLTeyGYPGDEVPVVAGSALLalqgdeeqEKNVLKLMEEVDAYIPEPER 207
Cdd:cd01888 146 EEQALENYE-QIKEFVK--GTIAENAPIIPISAQL--------KYNIDVLCEYIVKKIPTPPR 197
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-178 |
2.29e-27 |
|
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: 107.07 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 13 VNIGTLGHVDHGKTTLTAAISTVLAKhgdnkeaakdyASIDNAPEERERGITIN----------TSHIEYETATRH---- 78
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAST-----------AAFDKNPQSQERGITLDlgfssfevdkPKHLEDNENPQIenyq 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 79 YAHIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVfLNKVDQVDDPELLELVE-MEVR 157
Cdd:cd01889 70 ITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEERKRKIEkMKKR 148
|
170 180
....*....|....*....|.
gi 1092675938 158 DLLTEYGYPGDEVPVVAGSAL 178
Cdd:cd01889 149 LQKTLEKTRLKDSPIIPVSAK 169
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
17-300 |
3.26e-27 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 113.49 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 17 TLGHVDHGKTTLT---------------AAISTVLAKHGDNKEAAkDYA-SIDNAPEERERGITINTSHIEYETATRHYA 80
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVGTQGDEI-DLAlLVDGLAAEREQGITIDVAYRYFATPKRKFI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 81 HIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVD-DPELLELVEMEVRDL 159
Cdd:PRK05506 108 VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDyDQEVFDEIVADYRAF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 160 LTEYGypgdeVPVVAGSALLALQGDeeqekNVLK------------LMEEVDAYIPEPEREtDKPFMMPVEDV------- 220
Cdd:PRK05506 188 AAKLG-----LHDVTFIPISALKGD-----NVVTrsarmpwyegpsLLEHLETVEIASDRN-LKDFRFPVQYVnrpnldf 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 221 --FSitgrGTVATGRVergqiKVGDEVEIVgihEETKKTTVTGVEMFRKMLDYAEAGDNIgallrGITRED---IQRGQV 295
Cdd:PRK05506 257 rgFA----GTVASGVV-----RPGDEVVVL---PSGKTSRVKRIVTPDGDLDEAFAGQAV-----TLTLADeidISRGDM 319
|
....*
gi 1092675938 296 LAAPG 300
Cdd:PRK05506 320 LARAD 324
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
17-312 |
1.99e-26 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 110.39 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 17 TLGHVDHGKTTL-------TAAI-----STVL---AKHGDNKEAAkDYAS-IDNAPEERERGITINTSHIEYETATRHYA 80
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqlASLHndsKRHGTQGEKL-DLALlVDGLQAEREQGITIDVAYRYFSTEKRKFI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 81 HIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVFLNKVDQVD-DPELLELVEMEVRDL 159
Cdd:PRK05124 111 IADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDySEEVFERIREDYLTF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 160 LTEYGYPGD--EVPvvagsaLLALQGD---EEQEK-------NVLKLMEEVDAyipepERETD-KPFMMPVEDV------ 220
Cdd:PRK05124 191 AEQLPGNLDirFVP------LSALEGDnvvSQSESmpwysgpTLLEVLETVDI-----QRVVDaQPFRFPVQYVnrpnld 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 221 ---FSitgrGTVATGRVergqiKVGDEVEIV--GiheetKKTTVTGVEMFRKMLDYAEAGDNIGALLrgiTRE-DIQRGQ 294
Cdd:PRK05124 260 frgYA----GTLASGVV-----KVGDRVKVLpsG-----KESNVARIVTFDGDLEEAFAGEAITLVL---EDEiDISRGD 322
|
330
....*....|....*....
gi 1092675938 295 VLAAPG-TITPHTKFEASV 312
Cdd:PRK05124 323 LLVAADeALQAVQHASADV 341
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-205 |
5.04e-25 |
|
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: 100.75 E-value: 5.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLtaaISTVLAKHGDNKEAAKDYASI-DNAPEERERGITI---NTShIEYETATRHYahIDAPGHAD 89
Cdd:cd01891 4 NIAIIAHVDHGKTTL---VDALLKQSGTFRENEEVGERVmDSNDLERERGITIlakNTA-ITYKDTKINI--IDTPGHAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 90 Y------VKNMItgaaqmDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVfLNKVDQVD-DPellELVEMEVRDLLTE 162
Cdd:cd01891 78 FggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKIDRPDaRP---EEVVDEVFDLFLE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1092675938 163 YGYPGD--EVPVVAGSAL--LALQGDEEQEKNVLKLMEEVDAYIPEP 205
Cdd:cd01891 148 LNATDEqlDFPIVYASAKngWASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-279 |
9.08e-24 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 103.25 E-value: 9.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLtaaISTVLAKHGD-NKEAAKDYASIDNAPEERERGITINTSHIEYETATRHYAHIDAPGHADYVK 92
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGTfDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 93 NMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVfLNKVDQVDDPEllELVEMEVRDLLTEYGYPGDEV-- 170
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARP--DWVVDQVFDLFVNLDATDEQLdf 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 171 PVVAGSALLALQG--DEEQEKNVLKLMEEVDAYIPEPERETDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIV 248
Cdd:PRK10218 161 PIVYASALNGIAGldHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1092675938 249 GIHEETKKTTV----TGVEMFRKMLDYAEAGDNIG 279
Cdd:PRK10218 241 DSEGKTRNAKVgkvlGHLGLERIETDLAEAGDIVA 275
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
18-178 |
5.31e-23 |
|
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: 94.46 E-value: 5.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 18 LGHVDHGKTTLTAAI-STVLAKhgdnKEAakdyasidnapeereRGIT--INTSHIEYETATRHYAHIDAPGHADYvKNM 94
Cdd:cd01887 6 MGHVDHGKTTLLDKIrKTNVAA----GEA---------------GGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 95 ITGAAQM-DGAILVVSAADGPMPQTREHILLAHQVGVPyFVVFLNKVDQVDDPELLelvEMEVRDLLTEYGYPGDE---- 169
Cdd:cd01887 66 RARGASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTEAD---PERVKNELSELGLVGEEwggd 141
|
....*....
gi 1092675938 170 VPVVAGSAL 178
Cdd:cd01887 142 VSIVPISAK 150
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-188 |
3.54e-22 |
|
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: 94.23 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTAAI---STVLAKHG--DNKEAAKDYASIdnapeERERGITINTSHIEYETATRHYAHIDAPGHA 88
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytSGAIRELGsvDKGTTRTDSMEL-----ERQRGITIFSAVASFQWEDTKVNIIDTPGHM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 89 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFvVFLNKVDQ--VDdpelLELVEMEVRDLLTEygyp 166
Cdd:cd04168 76 DFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTI-IFVNKIDRagAD----LEKVYQEIKEKLSP---- 146
|
170 180
....*....|....*....|..
gi 1092675938 167 gDEVPVVAGSALLALQGDEEQE 188
Cdd:cd04168 147 -DIVPMQKVGLYPNICDTNNID 167
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-163 |
1.63e-21 |
|
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: 91.91 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTaaiSTVLAKHGD-NKEAAKDYASIDNAPEERERGITINTSHI----EYETATRHYAH-----ID 83
Cdd:cd01885 2 NICIIAHVDHGKTTLS---DSLLASAGIiSEKLAGKARYLDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinlID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 84 APGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGV-PyfVVFLNKVDQV-----DDPE-----LLELV 152
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVkP--VLVINKIDRLilelkLSPEeayqrLLRIV 156
|
170
....*....|.
gi 1092675938 153 EmEVRDLLTEY 163
Cdd:cd01885 157 E-DVNAIIETY 166
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
4-245 |
1.82e-21 |
|
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: 96.38 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 4 EKYERTKPHVNIgtLGHVDHGKTTLTAAISTVLAKHGdnkEAAkdyasidnapeererGIT--INTSHIEYETAtRHYAH 81
Cdd:TIGR00487 81 DLLVERPPVVTI--MGHVDHGKTSLLDSIRKTKVAQG---EAG---------------GITqhIGAYHVENEDG-KMITF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 82 IDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPyFVVFLNKVDQVD-DPELlelvemeVRDLL 160
Cdd:TIGR00487 140 LDTPGHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEaNPDR-------VKQEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 161 TEYGYP----GDEVPVVAGSALLAlQGDEEQEKNVLkLMEEVDAYIPEPERETDKpfmmPVEDVFSITGRGTVATGRVER 236
Cdd:TIGR00487 212 SEYGLVpedwGGDTIFVPVSALTG-DGIDELLDMIL-LQSEVEELKANPNGQASG----VVIEAQLDKGRGPVATVLVQS 285
|
....*....
gi 1092675938 237 GQIKVGDEV 245
Cdd:TIGR00487 286 GTLRVGDIV 294
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
209-295 |
1.32e-20 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 85.32 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 209 TDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIVGIHeetKKTTVTGVEMFRKMLDYAEAGDNIGALLRGITRE 288
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAG---VTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVK 77
|
....*..
gi 1092675938 289 DIQRGQV 295
Cdd:cd03693 78 DIKRGDV 84
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-314 |
1.33e-20 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 93.77 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTaaiSTVLAKHGD-NKEAAKDYASIDNAPEERERGITINTSHI----EYETATRHYAHIDAPGHA 88
Cdd:PRK07560 22 NIGIIAHIDHGKTTLS---DNLLAGAGMiSEELAGEQLALDFDEEEQARGITIKAANVsmvhEYEGKEYLINLIDTPGHV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 89 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGV-PyfVVFLNKVD------QVDDPELLE-LVEM--EVRD 158
Cdd:PRK07560 99 DFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVkP--VLFINKVDrlikelKLTPQEMQQrLLKIikDVNK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 159 LLTEYGYPGDE----VPV----VA-GSAL--LALQGDEEQEKNVlKLMEEVDAY-------------------------I 202
Cdd:PRK07560 177 LIKGMAPEEFKekwkVDVedgtVAfGSALynWAISVPMMQKTGI-KFKDIIDYYekgkqkelaekaplhevvldmvvkhL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 203 PEPeRETDK--------------------------PFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIVGIHEETKK 256
Cdd:PRK07560 256 PNP-IEAQKyripkiwkgdlnsevgkamlncdpngPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNRV 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 257 TTVtGVEM--FRKMLDYAEAGdNIGALLrGItrEDIQRGQVLAAPGTITPhtkFEASVYV 314
Cdd:PRK07560 335 QQV-GIYMgpEREEVEEIPAG-NIAAVT-GL--KDARAGETVVSVEDMTP---FESLKHI 386
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
213-298 |
1.56e-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: 82.19 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 213 FMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIVGIHEETKkttVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQR 292
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR---VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77
|
....*.
gi 1092675938 293 GQVLAA 298
Cdd:cd03696 78 GFVLSE 83
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
227-297 |
2.42e-18 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 78.85 E-value: 2.42e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092675938 227 GTVATGRVERGQIKVGDEVEIVGIHEETKK--TTVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQRGQVLA 297
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKKKivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
4-157 |
5.79e-18 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 85.72 E-value: 5.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 4 EKYERTKphvNIGTLGHVDHGKTTLTaaiSTVLAKHGD-NKEAAKDYASIDNAPEERERGITINTSHI----EYETATRH 78
Cdd:TIGR00490 14 WKPKFIR---NIGIVAHIDHGKTTLS---DNLLAGAGMiSEELAGQQLYLDFDEQEQERGITINAANVsmvhEYEGNEYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 79 YAHIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGV-PyfVVFLNKVDQVDDPELLELVEMEVR 157
Cdd:TIGR00490 88 INLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVkP--VLFINKVDRLINELKLTPQELQER 165
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
4-243 |
9.36e-18 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 85.27 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 4 EKYERTKPHVNIgtLGHVDHGKTTLTAAI-STVLAkhgdNKEAAkdyasidnapeererGITINTS----HIEYETATRH 78
Cdd:CHL00189 238 ENSINRPPIVTI--LGHVDHGKTTLLDKIrKTQIA----QKEAG---------------GITQKIGayevEFEYKDENQK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 79 YAHIDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPyFVVFLNKVDQVDDPelLELVEMEvrd 158
Cdd:CHL00189 297 IVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANAN--TERIKQQ--- 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 159 lLTEYGYP----GDEVPVVAGSALlalqgdeeQEKNVLKLME------EVDAYIPEPERETDKPFMMPVEDVFsitgRGT 228
Cdd:CHL00189 371 -LAKYNLIpekwGGDTPMIPISAS--------QGTNIDKLLEtilllaEIEDLKADPTQLAQGIILEAHLDKT----KGP 437
|
250
....*....|....*
gi 1092675938 229 VATGRVERGQIKVGD 243
Cdd:CHL00189 438 VATILVQNGTLHIGD 452
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
213-297 |
1.56e-17 |
|
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: 76.53 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 213 FMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIVGiheETKKTTVTGVEMFRKMLDYAEAGDNIGALLRGItrEDIQR 292
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP---KGITGRVTSIERFHEEVDEAKAGDIVGIGILGV--KDILT 75
|
....*
gi 1092675938 293 GQVLA 297
Cdd:cd01342 76 GDTLT 80
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-143 |
1.58e-16 |
|
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: 81.25 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 1 MAKEKYERTKphvNIGTLGHVDHGKTTLTAAI---STVLAKHGDNKEAAkdyASIDNAPEERERGITINTS--HIEYETa 75
Cdd:COG0480 1 MAEYPLEKIR---NIGIVAHIDAGKTTLTERIlfyTGAIHRIGEVHDGN---TVMDWMPEEQERGITITSAatTCEWKG- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092675938 76 trhyaH----IDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPyFVVFLNKVDQV 143
Cdd:COG0480 74 -----HkiniIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVP-RIVFVNKMDRE 139
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
18-251 |
3.42e-16 |
|
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: 80.06 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 18 LGHVDHGKTTLTAAI--STVLAKhgdnkEAAkdyasidnapeererGIT--INTSHIEYETatRHYAHIDAPGHADYVKN 93
Cdd:COG0532 10 MGHVDHGKTSLLDAIrkTNVAAG-----EAG---------------GITqhIGAYQVETNG--GKITFLDTPGHEAFTAM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 94 MITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPyFVVFLNKVDQVD-DPELL--ELVEMEVrdLLTEYGypGDeV 170
Cdd:COG0532 68 RARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGaNPDRVkqELAEHGL--VPEEWG--GD-T 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 171 PVVAGSA--------LL---ALQGDeeqeknvlklMEEVDAyipEPER---------ETDKpfmmpvedvfsitGRGTVA 230
Cdd:COG0532 142 IFVPVSAktgegideLLemiLLQAE----------VLELKA---NPDRpargtvieaKLDK-------------GRGPVA 195
|
250 260
....*....|....*....|.
gi 1092675938 231 TGRVERGQIKVGDEVeIVGIH 251
Cdd:COG0532 196 TVLVQNGTLKVGDIV-VAGTA 215
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-151 |
3.67e-15 |
|
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: 73.84 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTAAIstVLAKH---GDNKEAAKDYASIDNAPEERERGITINTSHIEYETA-TRHYAH----IDAP 85
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDML--IEQTHkrtPSVKLGWKPLRYTDTRKDEQERGISIKSNPISLVLEdSKGKSYliniIDTP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092675938 86 GHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPyFVVFLNKVDQVddpeLLEL 151
Cdd:cd04167 80 GHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLP-MVLVINKIDRL----ILEL 140
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-153 |
4.79e-15 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 76.91 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTAAI---STVLAKHGDNKEAAkdyASIDNAPEERERGITINTSHIEYETATRHYAHIDAPGHADY 90
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIlfyTGKIHKMGEVEDGT---TVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDF 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092675938 91 VKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYfVVFLNKVDQV--DDPELLELVE 153
Cdd:PRK13351 87 TGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPR-LIFINKMDRVgaDLFKVLEDIE 150
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-141 |
7.59e-15 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 76.32 E-value: 7.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 18 LGHVDHGKTTLTAAI---STVLAKHG--DNKEAAKDYAsidnaPEERERGITINTSHIEYETATRHYAHIDAPGHADYVK 92
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfyTGAIHRIGevEDGTTTMDFM-----PEERERGISITSAATTCEWKGHKINLIDTPGHVDFTG 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1092675938 93 NMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPyFVVFLNKVD 141
Cdd:PRK12740 76 EVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVP-RIIFVNKMD 123
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
304-392 |
1.06e-14 |
|
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: 69.34 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 304 PHTKFEASVYVLSKEEggrhtPFFTNYRPQFYFRTTDVTGVVELPEGTEM-----------VMPGDNVEMTVELIHPIAI 372
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekkppdsLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 1092675938 373 EEGT------RFSIREGGRTVGAGTV 392
Cdd:cd01513 77 ERGKefptlgRFALRDGGRTVGAGLI 102
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-141 |
3.19e-14 |
|
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: 72.24 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTAAI---STVLAKHGDNKEaakDYASIDNAPEERERGITINTS--HIEYETaTRHYAhIDAPGHA 88
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALlyaTGAIDRLGRVED---GNTVSDYDPEEKKRKMSIETSvaPLEWNG-HKINL-IDTPGYA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1092675938 89 DYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFvVFLNKVD 141
Cdd:cd04170 76 DFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMD 127
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
14-151 |
7.33e-14 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 73.16 E-value: 7.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTaaiSTVLAKHGDNKE-AAKDYASIDNAPEERERGITINTS----HIEYETATRHYAH------I 82
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLT---DSLVCKAGIISSkNAGDARFTDTRADEQERGITIKSTgislYYEHDLEDGDDKQpflinlI 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092675938 83 DAPGHADYvKNMITGAAQM-DGAILVVSAADGPMPQTrEHIL---LAHQVgVPyfVVFLNKVDQVddpeLLEL 151
Cdd:PTZ00416 98 DSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVLrqaLQERI-RP--VLFINKVDRA----ILEL 161
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
20-155 |
6.87e-13 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 68.39 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 20 HVDHGKTTLT-------AAIS---TVLAKhGDNKEAAKDYASIdnapeERERGITINTSHIEYETATRHYAHIDAPGHAD 89
Cdd:cd04169 10 HPDAGKTTLTeklllfgGAIQeagAVKAR-KSRKHATSDWMEI-----EKQRGISVTSSVMQFEYKGCVINLLDTPGHED 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092675938 90 YVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFvVFLNKVD-QVDDP-ELLELVEME 155
Cdd:cd04169 84 FSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPII-TFINKLDrEGRDPlELLDEIENE 150
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-141 |
1.06e-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: 64.82 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTAAI---STVLAKHGDNKEAAkdyASIDNAPEERERGITINTSHIEYETATRHYAHIDAPGHADY 90
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyyTGRIHKIGEVHGGG---ATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1092675938 91 VKNMITGAAQMDGAILVVSAADGPMPQT----REhillAHQVGVPyFVVFLNKVD 141
Cdd:cd01886 78 TIEVERSLRVLDGAVAVFDAVAGVQPQTetvwRQ----ADRYGVP-RIAFVNKMD 127
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
212-296 |
1.47e-11 |
|
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: 59.81 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 212 PFMMPVEDVFSitGRGTVATGRVERGQIKVGD---------EVEIVGIHEETkkttvtgVEMfrkmlDYAEAGDNIGALL 282
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQklvlmpnktKVEVTGIYIDE-------EEV-----DSAKPGENVKLKL 66
|
90
....*....|....
gi 1092675938 283 RGITREDIQRGQVL 296
Cdd:cd04089 67 KGVEEEDISPGFVL 80
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-205 |
3.92e-11 |
|
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: 61.40 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTAAI--STVLAKHGDNKEAAkdyasIDNAPEERERGITI--NTSHIEY--ETATRHYAH-IDAPG 86
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLleLTGTVSEREMKEQV-----LDSMDLERERGITIkaQAVRLFYkaKDGEEYLLNlIDTPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 87 HADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVfLNKVDQVD-DPellELVEMEVRDLLteyGY 165
Cdd:cd01890 77 HVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPV-INKIDLPAaDP---DRVKQEIEDVL---GL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1092675938 166 PGDEVPVVagSALLALqgdeeqekNVLKLMEEVDAYIPEP 205
Cdd:cd01890 150 DASEAILV--SAKTGL--------GVEDLLEAIVERIPPP 179
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
13-183 |
4.28e-11 |
|
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: 60.85 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 13 VNIGTLGHVDHGKTTLTAAIStvlakhgdnkeaaKDYASIDNAPEERERgiTINTSHIEYETATRHYAHIDAPGHADYVK 92
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLL-------------GNKGSITEYYPGTTR--NYVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 93 ------NMITGAAQM-DGAILVVSAADGPMPQTREhilLAHQV--GVPyFVVFLNKVDQVDDPELlelvEMEVRDLLTEY 163
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKE---IIHHAdsGVP-IILVGNKIDLKDADLK----THVASEFAKLN 138
|
170 180
....*....|....*....|
gi 1092675938 164 GYPGDEVPVVAGSALLALQG 183
Cdd:TIGR00231 139 GEPIIPLSAETGKNIDSAFK 158
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
14-151 |
1.16e-10 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 63.20 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTAaiSTVLAKHGDNKEAAKDYASIDNAPEERERGITINTSHI----EYETAT-RHYAH------- 81
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTD--SLVAAAGIIAQEVAGDVRMTDTRADEAERGITIKSTGIslyyEMTDESlKDFKGerdgney 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092675938 82 ----IDAPGHADYvKNMITGAAQM-DGAILVVSAADGPMPQTrEHIL---LAHQVgVPYFVVflNKVDQVddpeLLEL 151
Cdd:PLN00116 99 linlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVLrqaLGERI-RPVLTV--NKMDRC----FLEL 167
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
212-298 |
1.47e-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: 57.14 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 212 PFMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEIVGIHEetkKTTVTGVEMFRKMLDYAEAGDNIGALLRGITREDIQ 291
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNE---TATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77
|
....*..
gi 1092675938 292 RGQVLAA 298
Cdd:cd16267 78 VGSILCD 84
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
213-298 |
2.29e-10 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 56.84 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 213 FMMPVEDVFSITGRGTVATGRVERGQIKVGDEVEI----VGiheETKKTTVTGVEMFRKMLDYAEAGDNIGALLRGITRE 288
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLgpdaDG---KFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRE 77
|
90
....*....|
gi 1092675938 289 DIQRGQVLAA 298
Cdd:cd03694 78 SLRKGMVLVS 87
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
20-285 |
4.82e-10 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 61.19 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 20 HVDHGKTTL-------TAAIST------VLakhgdnkeaakdyasiDNAPEERERGITINtSHieyeTATRHYAH----- 81
Cdd:COG0481 14 HIDHGKSTLadrllelTGTLSEremkeqVL----------------DSMDLERERGITIK-AQ----AVRLNYKAkdget 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 82 -----IDAPGHADY---VKNMItgAAqMDGAILVVSAADGPMPQTREHILLA----HQVgVPyfVvfLNKVD-QVDDPel 148
Cdd:COG0481 73 yqlnlIDTPGHVDFsyeVSRSL--AA-CEGALLVVDASQGVEAQTLANVYLAlendLEI-IP--V--INKIDlPSADP-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 149 lELVEMEVRDLLteyGYPGDEVPVVagSAllalqgdeeqeK---NVLKLMEEVDAYIPEPERETDKPFMMPVEDVFSITG 225
Cdd:COG0481 143 -ERVKQEIEDII---GIDASDAILV--SA-----------KtgiGIEEILEAIVERIPPPKGDPDAPLQALIFDSWYDSY 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092675938 226 RGTVATGRVERGQIKVGDEVEIVGiheeTKKT-TVTGVEMF---RKMLDYAEAGDnIGALLRGI 285
Cdd:COG0481 206 RGVVVYVRVFDGTLKKGDKIKMMS----TGKEyEVDEVGVFtpkMTPVDELSAGE-VGYIIAGI 264
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
217-297 |
1.84e-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: 51.14 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 217 VEDVFSITGRgTVATGRVERGQIKVGDEVEIVGIHeetkkTTVTGVEMFRKMLDYAEAGDNIGALLRGITRedIQRGQVL 296
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKVKGDKGV-----ALIRAIEREHRKVDFAVAGDEVALILEGKIK--VKEGDVL 76
|
.
gi 1092675938 297 A 297
Cdd:cd16265 77 E 77
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
212-297 |
6.58e-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: 49.81 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 212 PFMMPVEDVFSiTGRGTVATGRVERGQIKVGDEVEIVGIHE--ETKKTTVTGVEMfrkmLDYAEAGDNIGALLRGITRED 289
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQdaEVKNIIRNSDEE----TDWAIAGDTVTLRLRGIEVED 75
|
....*...
gi 1092675938 290 IQRGQVLA 297
Cdd:cd03698 76 IQPGDILS 83
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
18-155 |
1.03e-07 |
|
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: 54.05 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 18 LGHVDHGKTTLTAAI--STVLAKH--GDNKEAAKDYASIDNApeERERGITINTSHIEYETATRHYahIDAPGHADYVKN 93
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIrgTAVVKKEagGITQHIGASEVPTDVI--EKICGDLLKSFKIKLKIPGLLF--IDTPGHEAFTNL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092675938 94 MITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPyFVVFLNKVDQV------DDPELLELVEME 155
Cdd:TIGR00491 86 RKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKIDRIpgwkshEGYPFLESINKQ 152
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
18-143 |
2.68e-07 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 52.49 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 18 LGHVDHGKTTLTAAI--STVLAKhgdnkEAAkdyasidnapeererGIT--INTSHIEYETATRhYAH------------ 81
Cdd:PRK04004 12 LGHVDHGKTTLLDKIrgTAVAAK-----EAG---------------GITqhIGATEVPIDVIEK-IAGplkkplpiklki 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092675938 82 -----IDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPyFVVFLNKVDQV 143
Cdd:PRK04004 71 pgllfIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTP-FVVAANKIDRI 136
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
227-304 |
3.30e-07 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 47.95 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 227 GTVATGRVERGQIKVGDEVEIVGIHEETKKTTVTGVEMFRKM----LDYAEAGDNIGalLRGItrEDIQRGQVLAAPGTI 302
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLerveVEEAEAGDIVA--IAGL--EDITIGDTICDPEVP 90
|
..
gi 1092675938 303 TP 304
Cdd:cd03691 91 EP 92
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
213-298 |
5.78e-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: 46.79 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 213 FMMPVEDV--FSITGRGTVatGRVERGQIKVGDEVEIVgihEETKKTTVTGVEMFRKMLDYAEAGDNIGALLrgiTRE-D 289
Cdd:cd03695 1 FRFPVQYVnrPNLDFRGYA--GTIASGSIRVGDEVTVL---PSGKTSRVKSIVTFDGELDSAGAGEAVTLTL---EDEiD 72
|
....*....
gi 1092675938 290 IQRGQVLAA 298
Cdd:cd03695 73 VSRGDLIVR 81
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
18-178 |
1.19e-06 |
|
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: 48.22 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 18 LGHVDHGKTTLTAAIStvlakhgdnkeaakdYASIDNAPEERERGITINTSHIEYETATRHYAHIDAPGHADYVKNMITG 97
Cdd:cd00882 3 VGRGGVGKSSLLNALL---------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 98 AAQM-----DGAILVVSAADGPMPQTREHILLAHQV--GVPyFVVFLNKVDQVDDPELLELVEMEVRDLLTeygypgdEV 170
Cdd:cd00882 68 LARLllrgaDLILLVVDSTDRESEEDAKLLILRRLRkeGIP-IILVGNKIDLLEEREVEELLRLEELAKIL-------GV 139
|
....*...
gi 1092675938 171 PVVAGSAL 178
Cdd:cd00882 140 PVFEVSAK 147
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
308-395 |
1.29e-05 |
|
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in the cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 294007 [Multi-domain] Cd Length: 87 Bit Score: 43.28 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 308 FEASVYVLSkeeggrH-TPFFTNYRPQFYFRTTDVTGVVELPEGtEMVMPGDNVEMTVELI-HPIAIEEGTRFSIREgGR 385
Cdd:cd03708 6 FEAEVLVLH------HpTTISPGYQPVVHCGTIRQTARIISIDK-EVLRTGDRALVRFRFLyRPEYLREGQRLIFRE-GR 77
|
90
....*....|
gi 1092675938 386 TVGAGTVTSI 395
Cdd:cd03708 78 TKGIGTVTKV 87
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
14-157 |
1.86e-05 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 45.36 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 14 NIGTLGHVDHGKTTLTAAIS------------TVLAKHG------------------DNKEAAKDYAsiDNAPEERERGI 63
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTqgeldngrgkarLNLFRHKhevesgrtssvsndilgfDSDGEVVNYP--DNHLGELDVEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 64 TINTSHIEYetatrhyaHIDAPGHADYVKNMITG--AAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVfLNKVD 141
Cdd:cd04165 79 CEKSSKVVT--------FIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVV-VTKID 149
|
170
....*....|....*.
gi 1092675938 142 QVDDPELLELVEMEVR 157
Cdd:cd04165 150 MTPANVLQETLKDLKR 165
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
20-153 |
2.16e-05 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 46.28 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 20 HVDHGKTTLT-------AAIS---TVLAKhGDNKEAAKDYASIdnapeERERGITINTSHIEYEtatrhYAHI-----DA 84
Cdd:PRK00741 18 HPDAGKTTLTeklllfgGAIQeagTVKGR-KSGRHATSDWMEM-----EKQRGISVTSSVMQFP-----YRDClinllDT 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092675938 85 PGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFvVFLNKVD-QVDDP-ELLELVE 153
Cdd:PRK00741 87 PGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTPIF-TFINKLDrDGREPlELLDEIE 156
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
102-215 |
5.97e-05 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 44.59 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 102 DGAILVVSAADGPMPQTREHILLAHQVGVPYFVVfLNKVDQVDDPELLELVEmEVRDLlteygYPGDE-VPVvagSALla 180
Cdd:COG1159 84 DVILFVVDATEKIGEGDEFILELLKKLKTPVILV-INKIDLVKKEELLPLLA-EYSEL-----LDFAEiVPI---SAL-- 151
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1092675938 181 lqgdeeQEKNVLKLMEEVDAYIPE-----PERE-TDKP--FMM 215
Cdd:COG1159 152 ------KGDNVDELLDEIAKLLPEgppyyPEDQiTDRPerFLA 188
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
91-215 |
6.91e-05 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 44.27 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 91 VKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPYFVVfLNKVDQVDDPELLELVEMEVRDLlteygYPGDE- 169
Cdd:PRK00089 75 NKAAWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILV-LNKIDLVKDKEELLPLLEELSEL-----MDFAEi 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1092675938 170 VPVvagSALlalqgdeeQEKNVLKLMEEVDAYIPE-----PERE-TDKP--FMM 215
Cdd:PRK00089 149 VPI---SAL--------KGDNVDELLDVIAKYLPEgppyyPEDQiTDRPerFLA 191
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
98-178 |
2.07e-04 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 41.46 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 98 AAQMDGAILVVSAADGPMPQTREHILLaHQVGVPYFVVFlNKVDQVDDPELLELVEMEVRDLLteygypgDEVPVVAGSA 177
Cdd:cd00880 74 ADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVL-NKIDLVPESEEEELLRERKLELL-------PDLPVIAVSA 144
|
.
gi 1092675938 178 L 178
Cdd:cd00880 145 L 145
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
82-143 |
3.82e-04 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 42.56 E-value: 3.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092675938 82 IDAPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAHQVGVPyFVVFLNKVDQV 143
Cdd:PRK14845 531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTP-FVVAANKIDLI 591
|
|
| eIF2_gamma_II |
cd03688 |
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily ... |
210-300 |
9.69e-04 |
|
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily represents domain II of the gamma subunit of eukaryotic translation initiation factor 2 (eIF2-gamma) found in eukaryota and archaea. eIF2 is a G protein that delivers the methionyl initiator tRNA to the small ribosomal subunit and releases it upon GTP hydrolysis after the recognition of the initiation codon. eIF2 is composed of three subunits, alpha, beta and gamma. Subunit gamma shows strongest conservation, and it confers both tRNA binding and GTP/GDP binding.
Pssm-ID: 293889 [Multi-domain] Cd Length: 113 Bit Score: 38.70 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 210 DKPFMMPVEDVFSITGRGT--------VATGRVERGQIKVGDEVEIV-GI-HEETKK-------TTVTGVEMFRKMLDYA 272
Cdd:cd03688 3 DKPPRMIVIRSFDVNKPGTevddlkggVIGGSLIQGVLKVGDEIEIRpGIvVKKGGKttcrpifTKIVSLFAEGNDLEEA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1092675938 273 EAGDNIG---ALLRGITREDIQRGQVLAAPG 300
Cdd:cd03688 83 VPGGLIGvgtKLDPTLTKADRLVGQVVGEPG 113
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
364-395 |
1.29e-03 |
|
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.
Pssm-ID: 294008 [Multi-domain] Cd Length: 109 Bit Score: 38.29 E-value: 1.29e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1092675938 364 VELIHPIAIEEGT------RFSIREGGRTVGAGTVTSI 395
Cdd:cd04093 72 IELERPIPLETFKdnkelgRFVLRRGGETIAAGIVTEI 109
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
102-201 |
7.52e-03 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 37.06 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092675938 102 DGAILVVSAADGPMPQTREHILLAHQVGVPYFVVfLNKVDQVDDPELLELVEMEVRDLlteygYPGDEV-PVvagSALla 180
Cdd:cd04163 84 DLVLFVVDASEWIGEGDEFILELLKKSKTPVILV-LNKIDLVKDKEDLLPLLEKLKEL-----HPFAEIfPI---SAL-- 152
|
90 100
....*....|....*....|.
gi 1092675938 181 lqgdeeQEKNVLKLMEEVDAY 201
Cdd:cd04163 153 ------KGENVDELLEYIVEY 167
|
|
| |
