|
Name |
Accession |
Description |
Interval |
E-value |
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-398 |
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: 829.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 1 MAdKGKFNRTKPHKNIGTIGHVDHGKTTLTSAITKILSLKGFAKALEYGDIDKAPEERARGVTINVHHSEYETDKYHYAH 80
Cdd:COG0050 1 MA-KEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 81 VDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVDDPQLIDLVETEIRELLK 160
Cdd:COG0050 80 VDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 161 KYQFPGDETPIIRGSALKAAEATSlDDEWAKKILELMDAVDNYIPEPVRDTEKPFLMPIEDIFTIEGRGTVVTGRIDRGI 240
Cdd:COG0050 160 KYGFPGDDTPIIRGSALKALEGDP-DPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 241 IKVNEEVEIIGIKPTAKTVVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVIAKPGSVTPHTDFEAEAYILKKEE 320
Cdd:COG0050 239 IKVGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEE 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818807181 321 GGRHNPFFSGYKPQFYIRTTDITGDITLKEGVEMVNPGDTATFTVKLIHPVALEERQRFAFREGGRTIGAGVVTKIVK 398
Cdd:COG0050 319 GGRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-398 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 818.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 1 MAdKGKFNRTKPHKNIGTIGHVDHGKTTLTSAITKILSLKGFAKALEYGDIDKAPEERARGVTINVHHSEYETDKYHYAH 80
Cdd:PRK00049 1 MA-KEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 81 VDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVDDPQLIDLVETEIRELLK 160
Cdd:PRK00049 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 161 KYQFPGDETPIIRGSALKAAEATSlDDEWAKKILELMDAVDNYIPEPVRDTEKPFLMPIEDIFTIEGRGTVVTGRIDRGI 240
Cdd:PRK00049 160 KYDFPGDDTPIIRGSALKALEGDD-DEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 241 IKVNEEVEIIGIKPTAKTVVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVIAKPGSVTPHTDFEAEAYILKKEE 320
Cdd:PRK00049 239 IKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEE 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818807181 321 GGRHNPFFSGYKPQFYIRTTDITGDITLKEGVEMVNPGDTATFTVKLIHPVALEERQRFAFREGGRTIGAGVVTKIVK 398
Cdd:PRK00049 319 GGRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-398 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 793.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 1 MAdKGKFNRTKPHKNIGTIGHVDHGKTTLTSAITKILSLKGFAKALEYGDIDKAPEERARGVTINVHHSEYETDKYHYAH 80
Cdd:PRK12735 1 MA-KEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 81 VDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVDDPQLIDLVETEIRELLK 160
Cdd:PRK12735 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 161 KYQFPGDETPIIRGSALKAAEATSlDDEWAKKILELMDAVDNYIPEPVRDTEKPFLMPIEDIFTIEGRGTVVTGRIDRGI 240
Cdd:PRK12735 160 KYDFPGDDTPIIRGSALKALEGDD-DEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 241 IKVNEEVEIIGIKPTAKTVVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVIAKPGSVTPHTDFEAEAYILKKEE 320
Cdd:PRK12735 239 VKVGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEE 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818807181 321 GGRHNPFFSGYKPQFYIRTTDITGDITLKEGVEMVNPGDTATFTVKLIHPVALEERQRFAFREGGRTIGAGVVTKIVK 398
Cdd:PRK12735 319 GGRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-398 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 762.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 1 MAdKGKFNRTKPHKNIGTIGHVDHGKTTLTSAITKILSLKGFAKALEYGDIDKAPEERARGVTINVHHSEYETDKYHYAH 80
Cdd:PRK12736 1 MA-KEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 81 VDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVDDPQLIDLVETEIRELLK 160
Cdd:PRK12736 80 VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 161 KYQFPGDETPIIRGSALKAAEAtslDDEWAKKILELMDAVDNYIPEPVRDTEKPFLMPIEDIFTIEGRGTVVTGRIDRGI 240
Cdd:PRK12736 160 EYDFPGDDIPVIRGSALKALEG---DPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 241 IKVNEEVEIIGIKPTAKTVVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVIAKPGSVTPHTDFEAEAYILKKEE 320
Cdd:PRK12736 237 VKVGDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEE 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818807181 321 GGRHNPFFSGYKPQFYIRTTDITGDITLKEGVEMVNPGDTATFTVKLIHPVALEERQRFAFREGGRTIGAGVVTKIVK 398
Cdd:PRK12736 317 GGRHTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-398 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 700.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 1 MAdKGKFNRTKPHKNIGTIGHVDHGKTTLTSAITKILSLKGFAKALEYGDIDKAPEERARGVTINVHHSEYETDKYHYAH 80
Cdd:CHL00071 1 MA-REKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 81 VDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVDDPQLIDLVETEIRELLK 160
Cdd:CHL00071 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 161 KYQFPGDETPIIRGSALKAAEATSL-------DDEWAKKILELMDAVDNYIPEPVRDTEKPFLMPIEDIFTIEGRGTVVT 233
Cdd:CHL00071 160 KYDFPGDDIPIVSGSALLALEALTEnpkikrgENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 234 GRIDRGIIKVNEEVEIIGIKPTAKTVVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVIAKPGSVTPHTDFEAEA 313
Cdd:CHL00071 240 GRIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 314 YILKKEEGGRHNPFFSGYKPQFYIRTTDITGDITL-----KEGVEMVNPGDTATFTVKLIHPVALEERQRFAFREGGRTI 388
Cdd:CHL00071 320 YILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTV 399
|
410
....*....|
gi 818807181 389 GAGVVTKIVK 398
Cdd:CHL00071 400 GAGVVSKILK 409
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
4-398 |
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: 688.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 4 KGKFNRTKPHKNIGTIGHVDHGKTTLTSAITKILSLKGFAKALEYGDIDKAPEERARGVTINVHHSEYETDKYHYAHVDC 83
Cdd:TIGR00485 3 KEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 84 PGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVDDPQLIDLVETEIRELLKKYQ 163
Cdd:TIGR00485 83 PGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 164 FPGDETPIIRGSALKAAEAtslDDEWAKKILELMDAVDNYIPEPVRDTEKPFLMPIEDIFTIEGRGTVVTGRIDRGIIKV 243
Cdd:TIGR00485 163 FPGDDTPIIRGSALKALEG---DAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 244 NEEVEIIGIKPTAKTVVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVIAKPGSVTPHTDFEAEAYILKKEEGGR 323
Cdd:TIGR00485 240 GEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818807181 324 HNPFFSGYKPQFYIRTTDITGDITLKEGVEMVNPGDTATFTVKLIHPVALEERQRFAFREGGRTIGAGVVTKIVK 398
Cdd:TIGR00485 320 HTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
5-397 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 687.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 5 GKFNRTKPHKNIGTIGHVDHGKTTLTSAITKILSLKGFAKALEYGDIDKAPEERARGVTINVHHSEYETDKYHYAHVDCP 84
Cdd:PLN03127 53 ATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 85 GHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVDDPQLIDLVETEIRELLKKYQF 164
Cdd:PLN03127 133 GHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKF 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 165 PGDETPIIRGSALKAAEATslDDEWAKK-ILELMDAVDNYIPEPVRDTEKPFLMPIEDIFTIEGRGTVVTGRIDRGIIKV 243
Cdd:PLN03127 213 PGDEIPIIRGSALSALQGT--NDEIGKNaILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 244 NEEVEIIGIKP--TAKTVVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVIAKPGSVTPHTDFEAEAYILKKEEG 321
Cdd:PLN03127 291 GEEVEIVGLRPggPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEG 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818807181 322 GRHNPFFSGYKPQFYIRTTDITGDITLKEGVEMVNPGDTATFTVKLIHPVALEERQRFAFREGGRTIGAGVVTKIV 397
Cdd:PLN03127 371 GRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVL 446
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-398 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 592.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 2 ADKGKFNRTKPHKNIGTIGHVDHGKTTLTSAITKILSLKGFAKALEYGDIDKAPEERARGVTINVHHSEYETDKYHYAHV 81
Cdd:PLN03126 70 AARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 82 DCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVDDPQLIDLVETEIRELLKK 161
Cdd:PLN03126 150 DCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 162 YQFPGDETPIIRGSALKAAEATSL-------DDEWAKKILELMDAVDNYIPEPVRDTEKPFLMPIEDIFTIEGRGTVVTG 234
Cdd:PLN03126 230 YEFPGDDIPIISGSALLALEALMEnpnikrgDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 235 RIDRGIIKVNEEVEIIGIKPTAKTVVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVIAKPGSVTPHTDFEAEAY 314
Cdd:PLN03126 310 RVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVY 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 315 ILKKEEGGRHNPFFSGYKPQFYIRTTDITGDITL-----KEGVEMVNPGDTATFTVKLIHPVALEERQRFAFREGGRTIG 389
Cdd:PLN03126 390 VLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSimndkDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVG 469
|
....*....
gi 818807181 390 AGVVTKIVK 398
Cdd:PLN03126 470 AGVIQSIIE 478
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
12-207 |
3.05e-137 |
|
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: 389.64 E-value: 3.05e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 12 PHKNIGTIGHVDHGKTTLTSAITKILSLKGFAKALEYGDIDKAPEERARGVTINVHHSEYETDKYHYAHVDCPGHADFIK 91
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 92 NMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVDDPQLIDLVETEIRELLKKYQFPGDETPI 171
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 818807181 172 IRGSALKAAEATSlDDEWAKKILELMDAVDNYIPEP 207
Cdd:cd01884 161 VRGSALKALEGDD-PNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
9-398 |
1.77e-92 |
|
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: 284.13 E-value: 1.77e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 9 RTKPHKNIGTIGHVDHGKTTL-------TSAIT--KILSLKGFAKALEYGD------IDKAPEERARGVTINVHHSEYET 73
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLvgrllyeTGAIDehIIEKYEEEAEKKGKESfkfawvMDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 74 DKYHYAHVDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVD-DPQLIDLVE 152
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 153 TEIRELLKKYQFPGDETPIIRGSALKAAEATSLDDE--WAKKiLELMDAVDNyIPEPVRDTEKPFLMPIEDIFTIEGRGT 230
Cdd:COG5256 163 EEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNmpWYNG-PTLLEALDN-LKEPEKPVDKPLRIPIQDVYSISGIGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 231 VVTGRIDRGIIKVNEEVeiIGIKPTAKTVVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVIAKPGSV-TPHTDF 309
Cdd:COG5256 241 VPVGRVETGVLKVGDKV--VFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNPpTVAEEF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 310 EAEAYILkkeeggrHNP--FFSGYKPQFYIRTTDITgdITLKEGVEMVNP---------------GDTATFTVKLIHPVA 372
Cdd:COG5256 319 TAQIVVL-------QHPsaITVGYTPVFHVHTAQVA--CTFVELVSKLDPrtgqvkeenpqflktGDAAIVKIKPTKPLV 389
|
410 420 430
....*....|....*....|....*....|..
gi 818807181 373 LE------ERQRFAFREGGRTIGAGVVTKIVK 398
Cdd:COG5256 390 IEkfkefpQLGRFAIRDMGQTVAAGVVLDVKP 421
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
9-398 |
1.59e-88 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 274.11 E-value: 1.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 9 RTKPHKNIGTIGHVDHGKTTL-------TSAITK--ILSLKGFAKALEYGD------IDKAPEERARGVTINVHHSEYET 73
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLvgrllyeTGAIDEhiIEELREEAKEKGKESfkfawvMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 74 DKYHYAHVDCPGHADFIKNMITGAAQMDGAILVVSAPD--GPMPQTREHILLARQVGVPAMVVFLNKVDMVD-DPQLIDL 150
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 151 VETEIRELLKKYQFPGDETPIIRGSALKAAEATSLDDE--WAKKILeLMDAVDNyIPEPVRDTEKPFLMPIEDIFTIEGR 228
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENmpWYNGPT-LLEALDN-LKPPEKPTDKPLRIPIQDVYSISGV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 229 GTVVTGRIDRGIIKVNEEVEiigIKPTAKT-VVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVIA---KPGSVT 304
Cdd:PRK12317 240 GTVPVGRVETGVLKVGDKVV---FMPAGVVgEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGhpdNPPTVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 305 phTDFEAEAYILkkeeggrHNP--FFSGYKPQFYIRT-------TDITGDITLKEG-VEMVNP-----GDTATFTVKLIH 369
Cdd:PRK12317 317 --EEFTAQIVVL-------QHPsaITVGYTPVFHAHTaqvactfEELVKKLDPRTGqVAEENPqfiktGDAAIVKIKPTK 387
|
410 420 430
....*....|....*....|....*....|....*
gi 818807181 370 PVALEERQ------RFAFREGGRTIGAGVVTKIVK 398
Cdd:PRK12317 388 PLVIEKVKeipqlgRFAIRDMGQTIAAGMVIDVKP 422
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
11-205 |
3.86e-84 |
|
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: 254.37 E-value: 3.86e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 11 KPHKNIGTIGHVDHGKTTLTSAITKILSLKGFAKALEYGD---IDKAPEERARGVTINVHHSEYETDKYHYAHVDCPGHA 87
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 88 DFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPaMVVFLNKVDMVDDPQLIDLVETEIRELLKKYQFPGD 167
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 818807181 168 ETPIIRGSALKaaeatslddewAKKILELMDAVDNYIP 205
Cdd:pfam00009 160 FVPVVPGSALK-----------GEGVQTLLDALDEYLP 186
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
16-393 |
1.43e-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: 243.67 E-value: 1.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 16 IGTIGHVDHGKTTLTSAITKIlslkgfakaleygDIDKAPEERARGVTINVHhseyetdkyhYAH-----------VDCP 84
Cdd:COG3276 3 IGTAGHIDHGKTTLVKALTGI-------------DTDRLKEEKKRGITIDLG----------FAYlplpdgrrlgfVDVP 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 85 GHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVdDPQLIDLVETEIRELLKKYQF 164
Cdd:COG3276 60 GHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGTFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 165 PGdeTPIIRGSA--------LKAAeatslddewakkILELMDAVdnyipePVRDTEKPFLMPIEDIFTIEGRGTVVTGRI 236
Cdd:COG3276 139 ED--APIVPVSAvtgegideLRAA------------LDALAAAV------PARDADGPFRLPIDRVFSIKGFGTVVTGTL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 237 DRGIIKVNEEVEIIgikPTAKTV-VTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVIAKPGSVTPHTDFEAEAYI 315
Cdd:COG3276 199 LSGTVRVGDELELL---PSGKPVrVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 316 LKKEEGgrhnPFFSGYKPQFYIRTTDITGDITLKEGVEmVNPGDTATFTVKLIHPVALEERQRFAFREGG--RTIGAGVV 393
Cdd:COG3276 276 LPSAPR----PLKHWQRVHLHHGTAEVLARVVLLDREE-LAPGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
11-398 |
2.23e-57 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 193.81 E-value: 2.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 11 KPHKNIGTIGHVDHGKTTLTSAItkILSLKGFAK---------ALEYGD--------IDKAPEERARGVTINVHHSEYET 73
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHL--IYKCGGIDKrtiekfekeAAEMGKgsfkyawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 74 DKYHYAHVDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMP-------QTREHILLARQVGVPAMVVFLNKVDM--VDD 144
Cdd:PTZ00141 83 PKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDktVNY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 145 PQ-LIDLVETEIRELLKKYQFPGDETPIIRGSALKAAEATSLDD--EWAKKILeLMDAVDNYIPePVRDTEKPFLMPIED 221
Cdd:PTZ00141 163 SQeRYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDnmPWYKGPT-LLEALDTLEP-PKRPVDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 222 IFTIEGRGTVVTGRIDRGIIKVNeevEIIGIKPTAKTV-VTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVI--A 298
Cdd:PTZ00141 241 VYKIGGIGTVPVGRVETGILKPG---MVVTFAPSGVTTeVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVAsdS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 299 KPGSVTPHTDFEAEAYILkKEEGGRHNpffsGYKPQFYIRTTDI--------------TGDiTLKEGVEMVNPGDTATFT 364
Cdd:PTZ00141 318 KNDPAKECADFTAQVIVL-NHPGQIKN----GYTPVLDCHTAHIackfaeieskidrrSGK-VLEENPKAIKSGDAAIVK 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 818807181 365 VKLIHPVALEERQ------RFAFREGGRTIGAGVVTKIVK 398
Cdd:PTZ00141 392 MVPTKPMCVEVFNeypplgRFAVRDMKQTVAVGVIKSVEK 431
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
15-207 |
1.10e-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: 184.04 E-value: 1.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 15 NIGTIGHVDHGKTTLTSAITKILSLKGFAKALEYGDIDKAPEERARGVTINVHHSEYETDKYHYAHVDCPGHADFIKNMI 94
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 95 TGAAQMDGAILVVSAPDGPMPQTREHILLARQvGVPAMVVFLNKVDMVdDPQLIDLVETEIRELLKKY---QFPGDETPI 171
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIgftFLKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 818807181 172 IRGSALKaaeatslddewAKKILELMDAVDNYIPEP 207
Cdd:cd00881 159 IPISALT-----------GEGIEELLDAIVEHLPPP 183
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
15-351 |
1.52e-55 |
|
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: 192.40 E-value: 1.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 15 NIGTIGHVDHGKTTLTSAITKIlslkgfakaleygDIDKAPEERARGVTINVHHSEYETDKYHYAHVDCPGHADFIKNMI 94
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTGI-------------AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 95 TGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVDDpQLIDLVETEIRELLKKYQFpGDETPIIRG 174
Cdd:TIGR00475 69 AGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNE-EEIKRTEMFMKQILNSYIF-LKNAKIFKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 175 SAlKAAEATSLDDEWAKKILELMDAvdnyipepvRDTEKPFLMPIEDIFTIEGRGTVVTGRIDRGIIKVNEEVEIIGIKP 254
Cdd:TIGR00475 147 SA-KTGQGIGELKKELKNLLESLDI---------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 255 TAKtvVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVIAKPGSVTPHTDFEAEAyilkkeeggrHNPFFSGYKPQ 334
Cdd:TIGR00475 217 EVR--VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDPKLRVVVKFIA----------EVPLLELQPYH 284
|
330
....*....|....*..
gi 818807181 335 FYIRTTDITGDITLKEG 351
Cdd:TIGR00475 285 IAHGMSVTTGKISLLDK 301
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
304-393 |
9.78e-55 |
|
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: 175.39 E-value: 9.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 304 TPHTDFEAEAYILKKEEGGRHNPFFSGYKPQFYIRTTDITGDITLKEGVEMVNPGDTATFTVKLIHPVALEERQRFAFRE 383
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
|
90
....*....|
gi 818807181 384 GGRTIGAGVV 393
Cdd:cd03707 81 GGRTVGAGVV 90
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
215-301 |
5.39e-50 |
|
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: 163.07 E-value: 5.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 215 FLMPIEDIFTIEGRGTVVTGRIDRGIIKVNEEVEIIGIKPTAKTVVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKG 294
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 818807181 295 QVIAKPG 301
Cdd:cd03697 81 MVLAKPG 87
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
12-393 |
5.89e-49 |
|
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: 170.62 E-value: 5.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 12 PHKNIGTIGHVDHGKTTLTSAITKILSlkgfakaleygdiDKAPEERARGVTINVHHSE---------YETDKY------ 76
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVWT-------------DTHSEELKRGISIRLGYADaeiykcpecDGPECYttepvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 77 -----------HYAHVDCPGHADFIKNMITGAAQMDGAILVVSAPDG-PMPQTREHILLARQVGVPAMVVFLNKVDMVDD 144
Cdd:TIGR03680 70 pncgsetellrRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 145 PQLIDLVEtEIRELLKKYQfpGDETPIIRGSALKAAeatslddewakKILELMDAVDNYIPEPVRDTEKPFLMPIEDIFT 224
Cdd:TIGR03680 150 EKALENYE-EIKEFVKGTV--AENAPIIPVSALHNA-----------NIDALLEAIEKFIPTPERDLDKPPLMYVARSFD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 225 IEGRGT--------VVTGRIDRGIIKVNEEVEII-GIKPTAK---------TVVTGIEMFNKSLDQGQAGDNAGIllrGT 286
Cdd:TIGR03680 216 VNKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKGgktkwepiyTEITSLRAGGYKVEEARPGGLVGV---GT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 287 K------KEDVQKGQVIAKPGSVTP-HTDFEAEAYILKK----EEGGRHNPFFSGYKPQFYIRTTDITGDITlkegvemv 355
Cdd:TIGR03680 293 KldpaltKADALAGQVVGKPGTLPPvWESLELEVHLLERvvgtEEELKVEPIKTGEVLMLNVGTATTVGVVT-------- 364
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 818807181 356 NPGDTATfTVKLIHPVALEERQRFAF--REGGR--TIGAGVV 393
Cdd:TIGR03680 365 SARKDEI-EVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 405
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
12-393 |
2.23e-47 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 166.57 E-value: 2.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 12 PHKNIGTIGHVDHGKTTLTSAITKILSlkgfakaleygdiDKAPEERARGVTI-------------NVHHSEYETDKYHY 78
Cdd:PRK04000 8 PEVNIGMVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIrlgyadatirkcpDCEEPEAYTTEPKC 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 79 AH-------------VDCPGHADFIKNMITGAAQMDGAILVVSAPDG-PMPQTREHILLARQVGVPAMVVFLNKVDMVDD 144
Cdd:PRK04000 75 PNcgsetellrrvsfVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 145 PQLIDLVEtEIRELLKKYQFpgDETPIIRGSALKAAeatslddewakKILELMDAVDNYIPEPVRDTEKPFLM------- 217
Cdd:PRK04000 155 ERALENYE-QIKEFVKGTVA--ENAPIIPVSALHKV-----------NIDALIEAIEEEIPTPERDLDKPPRMyvarsfd 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 218 ------PIEDIftiegRGTVVTGRIDRGIIKVNEEVEII-GIKPTAK---------TVVTGIEMFNKSLDQGQAGDNAGI 281
Cdd:PRK04000 221 vnkpgtPPEKL-----KGGVIGGSLIQGVLKVGDEIEIRpGIKVEEGgktkwepitTKIVSLRAGGEKVEEARPGGLVGV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 282 llrGTK------KEDVQKGQVIAKPGSVTP-HTDFEAEAYILKK----EEGGRHNPFFSGYKPQFYIRTTDITGDITLKE 350
Cdd:PRK04000 296 ---GTKldpsltKADALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLNVGTATTVGVVTSAR 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 818807181 351 GVEMvnpgdtatfTVKLIHPVALEERQRFAF--REGGR--TIGAGVV 393
Cdd:PRK04000 373 KDEA---------EVKLKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 410
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
9-398 |
1.73e-45 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 162.57 E-value: 1.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 9 RTKPHKNIGTIGHVDHGKTTLTSAItkILSLKGFAK----------------ALEYG-DIDKAPEERARGVTINVHHSEY 71
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHL--IYKLGGIDKrvierfekeaaemnkrSFKYAwVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 72 ETDKYHYAHVDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMP-------QTREHILLARQVGVPAMVVFLNKVDMVD- 143
Cdd:PLN00043 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 144 --DPQLIDLVETEIRELLKKYQFPGDETPIIRGSALKAAEAT--SLDDEWAKKIlELMDAVDNyIPEPVRDTEKPFLMPI 219
Cdd:PLN00043 161 kySKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIerSTNLDWYKGP-TLLEALDQ-INEPKRPSDKPLRLPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 220 EDIFTIEGRGTVVTGRIDRGIIKVNeevEIIGIKPTAKTV-VTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVI- 297
Cdd:PLN00043 239 QDVYKIGGIGTVPVGRVETGVIKPG---MVVTFGPTGLTTeVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAs 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 298 -AKPGSVTPHTDFEAEAYILKK--EEGGRHNPFFSGYKPQFYIRTTDITGDITLKEGVEM------VNPGDTATFTVKLI 368
Cdd:PLN00043 316 nSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDAGFVKMIPT 395
|
410 420 430
....*....|....*....|....*....|....*.
gi 818807181 369 HPVALEERQ------RFAFREGGRTIGAGVVTKIVK 398
Cdd:PLN00043 396 KPMVVETFSeypplgRFAVRDMRQTVAVGVIKSVEK 431
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
9-394 |
6.64e-45 |
|
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: 160.00 E-value: 6.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 9 RTKPHKNIGTIGHVDHGKTTLTSAITKILSlkgfakaleygdiDKAPEERARGVTINVHHSE--------------YETD 74
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYADatfykcpnceppeaYTTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 75 KYHYAH------------VDCPGHADFIKNMITGAAQMDGAILVVSAPDG-PMPQTREHILLARQVGVPAMVVFLNKVDM 141
Cdd:COG5257 68 PKCPNCgsetellrrvsfVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 142 VDDPQLIDLVEtEIRELLKKYQFpgDETPIIRGSALKAAeatslddewakKILELMDAVDNYIPEPVRDTEKPFLMPIED 221
Cdd:COG5257 148 VSKERALENYE-QIKEFVKGTVA--ENAPIIPVSAQHKV-----------NIDALIEAIEEEIPTPERDLSKPPRMLVAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 222 IFTIEGRGT--------VVTGRIDRGIIKVNEEVEII-GIKPTAK---------TVVTGIEMFNKSLDQGQAGdnaGILL 283
Cdd:COG5257 214 SFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKGgktkyepitTTVVSLRAGGEEVEEAKPG---GLVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 284 RGTK------KEDVQKGQVIAKPGSVTP-HTDFEAEAYILKKEEGGRHNpffsgykpqfyirtTDItGDITLKEGVeMVN 356
Cdd:COG5257 291 VGTKldpsltKSDSLVGSVAGKPGTLPPvLDSLTMEVHLLERVVGTKEE--------------VKV-EPIKTGEPL-MLN 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 818807181 357 PGdTAT------------FTVKLIHPVALEERQRFAF--REGG--RTIGAGVVT 394
Cdd:COG5257 355 VG-TATtvgvvtsarkdeIEVKLKRPVCAEKGSRVAIsrRIGGrwRLIGWGIIK 407
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
15-178 |
2.29e-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: 2.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 15 NIGTIGHVDHGKTTLTSaitKILSLKGF----------AKALEYGD--------IDKAPEERARGVTINVHHSEYETDKY 76
Cdd:cd01883 1 NLVVIGHVDAGKSTLTG---HLLYKLGGvdkrtiekyeKEAKEMGKesfkyawvLDKLKEERERGVTIDVGLAKFETEKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 77 HYAHVDCPGHADFIKNMITGAAQMDGAILVVSAPDG-------PMPQTREHILLARQVGVPAMVVFLNKVDMVDDP---Q 146
Cdd:cd01883 78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNwsqE 157
|
170 180 190
....*....|....*....|....*....|..
gi 818807181 147 LIDLVETEIRELLKKYQFPGDETPIIRGSALK 178
Cdd:cd01883 158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGFT 189
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
13-397 |
4.32e-44 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 160.48 E-value: 4.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 13 HKNIGTIGHVDHGKTTLTSA-ITKIL-----SLKGFakaleygdIDKAPEERARGVTINVHHSEY--------------- 71
Cdd:COG5258 122 HIVVGVAGHVDHGKSTLVGTlVTGKLddgngGTRSF--------LDVQPHEVERGLSADLSYAVYgfdddgpvrmknplr 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 72 ---------ETDKYHYaHVDCPGHADFIKNMITG--AAQMDGAILVVSAPDGPMPQTREH--ILLArqVGVPAMVVfLNK 138
Cdd:COG5258 194 ktdrarvveESDKLVS-FVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLA--MDLPVIVA-ITK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 139 VDMVDDPQlIDLVETEIRELLKKYqfpgDETPII---RGSALKAAE-------------ATSLDDewakkiLELMDAVDN 202
Cdd:COG5258 270 IDKVDDER-VEEVEREIENLLRIV----GRTPLEvesRHDVDAAIEeingrvvpilktsAVTGEG------LDLLDELFE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 203 YIPEPVRDTEKPFLMPIEDIFTIEGRGTVVTGRIDRGIIKVNEEVeIIGikPTA-----KTVVTGIEMFNKSLDQGQAGD 277
Cdd:COG5258 339 RLPKRATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDEL-LIG--PTKdgsfrEVEVKSIEMHYHRVDKAEAGR 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 278 NAGILLRGTKKEDVQKGQVIAKPGS-VTPHTDFEAEAYILkkeeggrHNP--FFSGYKPQFYIRTTDITGDITlKEGVEM 354
Cdd:COG5258 416 IVGIALKGVEEEELERGMVLLPRDAdPKAVREFEAEVMVL-------NHPttIKEGYEPVVHLETISEAVRFE-PIDKGY 487
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 818807181 355 VNPGDTATFTVK-LIHPVALEERQRFAFREgGRTIGAGVVTKIV 397
Cdd:COG5258 488 LLPGDSGRVRLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVTDIL 530
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
302-396 |
1.37e-41 |
|
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: 142.02 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 302 SVTPHTDFEAEAYILKKEEGGRHNPFFSGYKPQFYIRTTDITGDIT----------LKEGVEMVNPGDTATFTVKLIHPV 371
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhkldpggVSENPEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 818807181 372 ALEERQRFAFREGGRTIGAGVVTKI 396
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
16-294 |
9.33e-41 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 152.51 E-value: 9.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 16 IGTIGHVDHGKTTLTSAITKIlslkgfakaleygDIDKAPEERARGVTINVHHSEY-ETDKYHYAHVDCPGHADFIKNMI 94
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGV-------------NADRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 95 TGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVDDPQlIDLVETEIRELLKKYQFPgdETPIIRG 174
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEAR-IAEVRRQVKAVLREYGFA--EAKLFVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 175 SalkAAEATSLdDEWAKKILELmdavdnyiPEPVRDTEKPFLMPIEDIFTIEGRGTVVTGRIDRGIIKVNEEVEIIGI-K 253
Cdd:PRK10512 147 A---ATEGRGI-DALREHLLQL--------PEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVnK 214
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 818807181 254 PTAktvVTGIEMFNKSLDQGQAGDNAGILLRG-TKKEDVQKG 294
Cdd:PRK10512 215 PMR---VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
16-177 |
1.97e-40 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 141.20 E-value: 1.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 16 IGTIGHVDHGKTTLTSAITkilslkGFakaleygDIDKAPEERARGVTINVHHS--EYETDKyHYAHVDCPGHADFIKNM 93
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALT------GI-------ETDRLPEEKKRGITIDLGFAylDLPDGK-RLGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 94 ITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVDDPQLiDLVETEIRELLKKYQFPGdeTPIIR 173
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDEDRL-ELVEEEILELLAGTFLAD--APIFP 144
|
....
gi 818807181 174 GSAL 177
Cdd:cd04171 145 VSSV 148
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
18-311 |
1.06e-36 |
|
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: 138.30 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 18 TIGHVDHGKTTL-------TSAIT--KILSLKGFAKALEYGDIDKAP------EERARGVTINVHHSEYETDKYHYAHVD 82
Cdd:COG2895 22 TCGSVDDGKSTLigrllydTKSIFedQLAALERDSKKRGTQEIDLALltdglqAEREQGITIDVAYRYFSTPKRKFIIAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 83 CPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVD-DPQLIDLVETEIRELLKK 161
Cdd:COG2895 102 TPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDySEEVFEEIVADYRAFAAK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 162 YQFPgDET--PIirgSALK------AAEATSlddeWAK--KILELMDAVDNyipePVRDTEKPFLMPIEDI--FTIEGRG 229
Cdd:COG2895 182 LGLE-DITfiPI---SALKgdnvveRSENMP----WYDgpTLLEHLETVEV----AEDRNDAPFRFPVQYVnrPNLDFRG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 230 tvVTGRIDRGIIKVNEEVEIIgikPTAKT-VVTGIEMFNKSLDQGQAGDNAGILLrgtKKE-DVQKGQVIAKPGSV-TPH 306
Cdd:COG2895 250 --YAGTIASGTVRVGDEVVVL---PSGKTsTVKSIVTFDGDLEEAFAGQSVTLTL---EDEiDISRGDVIVAADAPpEVA 321
|
....*
gi 818807181 307 TDFEA 311
Cdd:COG2895 322 DQFEA 326
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
304-396 |
2.98e-31 |
|
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: 114.25 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 304 TPHTDFEAEAYILKKEEGGRHNPFFSGYKPQFYIRTTDITGDITLKEGVEMVNPGDTATFTVKLIHPVALEERQRFAFRE 383
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
|
90
....*....|...
gi 818807181 384 GGRTIGAGVVTKI 396
Cdd:cd03706 81 GGRTIGTGVVTKL 93
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-305 |
1.74e-30 |
|
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: 122.80 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 14 KNIGTIGHVDHGKTTLtsaITKILSLKGFAKALEYGD---IDKAPEERARGVTINVHHSEYETDKYHYAHVDCPGHADF- 89
Cdd:TIGR01394 2 RNIAIIAHVDHGKTTL---VDALLKQSGTFRANEAVAervMDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 90 -----IKNMItgaaqmDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVfLNKVDMVDdpQLIDLVETEIRELLkkYQF 164
Cdd:TIGR01394 79 geverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPS--ARPDEVVDEVFDLF--AEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 165 PGDET----PIIRGSALKAAEATSLDDEwAKKILELMDAVDNYIPEPVRDTEKPFLMPIEDIFTIEGRGTVVTGRIDRGI 240
Cdd:TIGR01394 148 GADDEqldfPIVYASGRAGWASLDLDDP-SDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGT 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818807181 241 IKVNEEVEII---GIKPTAK-TVVTGIEMFNKS-LDQGQAGD---NAGIllrgtkkEDVQKGQVIAKPGSVTP 305
Cdd:TIGR01394 227 VKKGQQVALMkrdGTIENGRiSKLLGFEGLERVeIDEAGAGDivaVAGL-------EDINIGETIADPEVPEA 292
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-197 |
2.21e-30 |
|
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: 115.16 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 15 NIGTIGHVDHGKTTLTSAITKILSLKGFakaleygdiDKAPEERARGVTINVHHSEYETDKYHYAH-------------- 80
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIASTAAF---------DKNPQSQERGITLDLGFSSFEVDKPKHLEdnenpqienyqitl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 81 VDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPaMVVFLNKVDMVDDPQ---LIDLVETEIRE 157
Cdd:cd01889 73 VDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKP-LIVVLNKIDLIPEEErkrKIEKMKKRLQK 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 818807181 158 LLKKYQFPgdETPIIRGSALKAAEATSLDDEWAKKILELM 197
Cdd:cd01889 152 TLEKTRLK--DSPIIPVSAKPGEGEAELGGELKNLIVLPL 189
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
18-201 |
6.30e-29 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 111.89 E-value: 6.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 18 TIGHVDHGKTTL-------TSAIT-----KILSLKGFAKALEYGD----IDKAPEERARGVTINVHHSEYETDKYHYAHV 81
Cdd:cd04166 4 TCGSVDDGKSTLigrllydSKSIFedqlaALERSKSSGTQGEKLDlallVDGLQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 82 DCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVD-DPQLIDLVETEIRELLK 160
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDyDEEVFEEIKADYLAFAA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 818807181 161 KYQFPgDETPI-IrgSALKAAEATSLDDE--W--AKKILELMDAVD 201
Cdd:cd04166 164 SLGIE-DITFIpI--SALEGDNVVSRSENmpWykGPTLLEHLETVE 206
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
15-305 |
9.66e-29 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 117.81 E-value: 9.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 15 NIGTIGHVDHGKTTLTSAItkilsLK--G-FAK-------ALEYGDIdkapeERARGVTI---N--VHHSEYetdkyhya 79
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDAL-----LKqsGtFREnqevaerVMDSNDL-----ERERGITIlakNtaVRYKGV-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 80 H---VDCPGHADF------IKNMItgaaqmDGAILVVSAPDGPMPQTRehILL--ARQVGVPAMVVfLNKVDMVD-DPQ- 146
Cdd:COG1217 70 KiniVDTPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLkkALELGLKPIVV-INKIDRPDaRPDe 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 147 --------LIDLVETEirELLkkyqfpgdETPIIRGSALKAAEATSLDDEwAKKILELMDAVDNYIPEPVRDTEKPFLMp 218
Cdd:COG1217 141 vvdevfdlFIELGATD--EQL--------DFPVVYASARNGWASLDLDDP-GEDLTPLFDTILEHVPAPEVDPDGPLQM- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 219 ieDIFTIE-----GRgtVVTGRIDRGIIKVNEEVEIIGIKPTAKTV-VTGIEMFN----KSLDQGQAGD---NAGIllrg 285
Cdd:COG1217 209 --LVTNLDysdyvGR--IAIGRIFRGTIKKGQQVALIKRDGKVEKGkITKLFGFEglerVEVEEAEAGDivaIAGI---- 280
|
330 340
....*....|....*....|
gi 818807181 286 tkkEDVQKGQVIAKPGSVTP 305
Cdd:COG1217 281 ---EDINIGDTICDPENPEA 297
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
15-250 |
8.79e-28 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 113.95 E-value: 8.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 15 NIGTIGHVDHGKTTLTSAITKILSLK-------------GFAKALEYgDIDKAPEERArgvtINVHHSEYETD------- 74
Cdd:PTZ00327 36 NIGTIGHVAHGKSTVVKALSGVKTVRfkrekvrnitiklGYANAKIY-KCPKCPRPTC----YQSYGSSKPDNppcpgcg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 75 -----KYHYAHVDCPGHADFIKNMITGAAQMDGAILVVSAPDG-PMPQTREHILLARQVGVPAMVVFLNKVDMVDDPQLI 148
Cdd:PTZ00327 111 hkmtlKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 149 DLVEtEIRELLKKYQfpGDETPIIRGSA-LKaaeatslddewaKKILELMDAVDNYIPEPVRDTEKPFLM---------- 217
Cdd:PTZ00327 191 DQYE-EIRNFVKGTI--ADNAPIIPISAqLK------------YNIDVVLEYICTQIPIPKRDLTSPPRMivirsfdvnk 255
|
250 260 270
....*....|....*....|....*....|...
gi 818807181 218 PIEDIFTIegRGTVVTGRIDRGIIKVNEEVEII 250
Cdd:PTZ00327 256 PGEDIENL--KGGVAGGSILQGVLKVGDEIEIR 286
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
15-209 |
9.05e-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: 108.51 E-value: 9.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 15 NIGTIGHVDHGKTTLTSAITKILSLK-------------GFAKAleygDIDKAPEERARGVTINVH-----HSEYETDKY 76
Cdd:cd01888 2 NIGTIGHVAHGKTTLVKALSGVWTVRhkeelkrnitiklGYANA----KIYKCPNCGCPRPYDTPEcecpgCGGETKLVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 77 HYAHVDCPGHADFIKNMITGAAQMDGAILVVSAPDG-PMPQTREHILLARQVGVPAMVVFLNKVDMVDDPQLIDLVEtEI 155
Cdd:cd01888 78 HVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQALENYE-QI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 818807181 156 RELLKKYQfpGDETPIIRGSALKAAeatslddewakKILELMDAVDNYIPEPVR 209
Cdd:cd01888 157 KEFVKGTI--AENAPIIPISAQLKY-----------NIDVLCEYIVKKIPTPPR 197
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-207 |
2.81e-23 |
|
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: 96.12 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 14 KNIGTIGHVDHGKTTLTSAITKilSLKGFAKALEYGD--IDKAPEERARGVTINVHHSEYETDKYHYAHVDCPGHADF-- 89
Cdd:cd01891 3 RNIAIIAHVDHGKTTLVDALLK--QSGTFRENEEVGErvMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFgg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 90 ----IKNMItgaaqmDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVfLNKVDMVDdpQLIDLVETEIRELLKKYQFP 165
Cdd:cd01891 81 everVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKIDRPD--ARPEEVVDEVFDLFLELNAT 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 818807181 166 GD--ETPIIRGSALKAAEATSLDDEwAKKILELMDAVDNYIPEP 207
Cdd:cd01891 152 DEqlDFPIVYASAKNGWASLNLDDP-SEDLDPLFETIIEHVPAP 194
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
18-311 |
3.30e-23 |
|
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: 100.14 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 18 TIGHVDHGKTTLTSAI---TKILSLKGFA--------KALEYGDIDKA------PEERARGVTINVHHSEYETDKYHYAH 80
Cdd:TIGR02034 5 TCGSVDDGKSTLIGRLlhdTKQIYEDQLAalerdskkHGTQGGEIDLAllvdglQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 81 VDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVD-DPQLIDLVETEIRELL 159
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDyDEEVFENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 160 KKYQFpgDETPIIRGSALK----AAEATSLDDEWAKKILELMDAVDnyIPEPVRDTekPFLMPIEDIF--TIEGRGtvVT 233
Cdd:TIGR02034 165 EQLGF--RDVTFIPLSALKgdnvVSRSESMPWYSGPTLLEILETVE--VERDAQDL--PLRFPVQYVNrpNLDFRG--YA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 234 GRIDRGIIKVNEEVEIIgikPTAKTV-VTGIEMFNKSLDQGQAGDnaGILLRGTKKEDVQKGQVIAKPGSVTPHTD-FEA 311
Cdd:TIGR02034 237 GTIASGSVHVGDEVVVL---PSGRSSrVARIVTFDGDLEQARAGQ--AVTLTLDDEIDISRGDLLAAADSAPEVADqFAA 311
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-277 |
3.34e-23 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 101.71 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 14 KNIGTIGHVDHGKTTLtsaITKILSLKG-FAKALEYGD--IDKAPEERARGVTINVHHSEYETDKYHYAHVDCPGHADFI 90
Cdd:PRK10218 6 RNIAIIAHVDHGKTTL---VDKLLQQSGtFDSRAETQErvMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 91 KNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVfLNKVDMVDDPQliDLVETEIRELLKKYQFPGDET- 169
Cdd:PRK10218 83 GEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARP--DWVVDQVFDLFVNLDATDEQLd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 170 -PIIRGSALKAAEATSLDDeWAKKILELMDAVDNYIPEPVRDTEKPFLMPIEDIFTIEGRGTVVTGRIDRGIIKVNEEVE 248
Cdd:PRK10218 160 fPIVYASALNGIAGLDHED-MAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVT 238
|
250 260 270
....*....|....*....|....*....|....
gi 818807181 249 IIGIKPTAKT-----VVTGIEMFNKSLDQGQAGD 277
Cdd:PRK10218 239 IIDSEGKTRNakvgkVLGHLGLERIETDLAEAGD 272
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
14-315 |
5.08e-20 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 92.23 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 14 KNIGTIGHVDHGKTTLTS---AITKILS--LKGFAKALEYGDidkapEERARGVTIN------VHhsEYETDKYHYAHVD 82
Cdd:PRK07560 21 RNIGIIAHIDHGKTTLSDnllAGAGMISeeLAGEQLALDFDE-----EEQARGITIKaanvsmVH--EYEGKEYLINLID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 83 CPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTrEHILlaRQV---GV-PamVVFLNKVD-----MVDDPQ-----LI 148
Cdd:PRK07560 94 TPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQAlreRVkP--VLFINKVDrlikeLKLTPQemqqrLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 149 DLVeTEIRELLKKYqfpgDETPIIRGSALKAAEAT----SLDDEWA-------------KKILE---------------- 195
Cdd:PRK07560 169 KII-KDVNKLIKGM----APEEFKEKWKVDVEDGTvafgSALYNWAisvpmmqktgikfKDIIDyyekgkqkelaekapl 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 196 ---LMDAVDNYIPEPVR-------------------------DTEKPFLMPIEDIFTIEGRGTVVTGRIDRGIIKVNEEV 247
Cdd:PRK07560 244 hevVLDMVVKHLPNPIEaqkyripkiwkgdlnsevgkamlncDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEV 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 248 EIIGIKPTAKTVVTGIEM--FNKSLDQGQAGDNAGILlrGTKkeDVQKGQVIAKPGSVTPhtdFEAEAYI 315
Cdd:PRK07560 324 YLVGAKKKNRVQQVGIYMgpEREEVEEIPAGNIAAVT--GLK--DARAGETVVSVEDMTP---FESLKHI 386
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
15-200 |
1.36e-19 |
|
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: 86.91 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 15 NIGTIGHVDHGKTTLTS-------AITKILSLKGFAKALEYGDIdkapeERARGVTINVHHSEYETDKYHYAHVDCPGHA 87
Cdd:cd04168 1 NIGILAHVDAGKTTLTEsllytsgAIRELGSVDKGTTRTDSMEL-----ERQRGITIFSAVASFQWEDTKVNIIDTPGHM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 88 DFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAmVVFLNKVDM--VDDPQLIDlvetEIRELLKKYQFP 165
Cdd:cd04168 76 DFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPT-IIFVNKIDRagADLEKVYQ----EIKEKLSPDIVP 150
|
170 180 190
....*....|....*....|....*....|....*
gi 818807181 166 GDEtpiiRGSALKAAEATSLDDEWAKKILELMDAV 200
Cdd:cd04168 151 MQK----VGLYPNICDTNNIDDEQIETVAEGNDEL 181
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-207 |
2.68e-19 |
|
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: 85.75 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 14 KNIGTIGHVDHGKTTLTS---AITKILSLK--GFAKALeygdiDKAPEERARGVTI---NVH-HSEYETDKYHYAH---- 80
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDsllASAGIISEKlaGKARYL-----DTREDEQERGITIkssAISlYFEYEEEKMDGNDylin 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 81 -VDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTR---EHILLARqvgvPAMVVFLNKVDMV-----DDP------ 145
Cdd:cd01885 76 lIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTEtvlRQALEER----VKPVLVINKIDRLilelkLSPeeayqr 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818807181 146 --QLIDLVETEIREL------LKKYQFPGDETPIIRGSALkaaeatsldDEWA------KKILELMDAVDNYIPEP 207
Cdd:cd01885 152 llRIVEDVNAIIETYapeefkQEKWKFSPQKGNVAFGSAL---------DGWGftiikfADIYAVLEMVVKHLPSP 218
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
18-311 |
3.87e-19 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 89.22 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 18 TIGHVDHGKTTLtsaITKIL--SLKGFAKALE------------YGDIDKA------PEERARGVTINVHHSEYETDKYH 77
Cdd:PRK05506 29 TCGSVDDGKSTL---IGRLLydSKMIFEDQLAalerdskkvgtqGDEIDLAllvdglAAEREQGITIDVAYRYFATPKRK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 78 YAHVDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVD-DPQLIDLVETEIR 156
Cdd:PRK05506 106 FIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDyDQEVFDEIVADYR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 157 ELLKKYQFPgDETPI-IrgSALKAAEATSLDDE--WAK--KILELMDAVdnYIPEPVRDteKPFLMPIEDI------Fti 225
Cdd:PRK05506 186 AFAAKLGLH-DVTFIpI--SALKGDNVVTRSARmpWYEgpSLLEHLETV--EIASDRNL--KDFRFPVQYVnrpnldF-- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 226 egRGtvVTGRIDRGIIKVNEEVEIIgikPTAKTV-VTGIEMFNKSLDQGQAGDnaGILLRGTKKEDVQKGQVIAKPGSVT 304
Cdd:PRK05506 257 --RG--FAGTVASGVVRPGDEVVVL---PSGKTSrVKRIVTPDGDLDEAFAGQ--AVTLTLADEIDISRGDMLARADNRP 327
|
....*...
gi 818807181 305 PHTD-FEA 311
Cdd:PRK05506 328 EVADqFDA 335
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
18-315 |
1.00e-18 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 87.66 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 18 TIGHVDHGKTTLtsaITKIL------------SL----KGFAKALEYGD----IDKAPEERARGVTINVHHSEYETDKYH 77
Cdd:PRK05124 32 TCGSVDDGKSTL---IGRLLhdtkqiyedqlaSLhndsKRHGTQGEKLDlallVDGLQAEREQGITIDVAYRYFSTEKRK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 78 YAHVDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVFLNKVDMVD-DPQLIDLVETEIR 156
Cdd:PRK05124 109 FIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDySEEVFERIREDYL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 157 ELLKkyQFPGD-ETPIIRGSALK----AAEATSLDdeWAK--KILELMDAVDNyipepVRDTE-KPFLMPI-------ED 221
Cdd:PRK05124 189 TFAE--QLPGNlDIRFVPLSALEgdnvVSQSESMP--WYSgpTLLEVLETVDI-----QRVVDaQPFRFPVqyvnrpnLD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 222 IftiegRGtvVTGRIDRGIIKVNEEVEII--GIKPTAKTVVTgiemFNKSLDQGQAGDNAGILLrgtKKE-DVQKGQVIA 298
Cdd:PRK05124 260 F-----RG--YAGTLASGVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGEAITLVL---EDEiDISRGDLLV 325
|
330
....*....|....*..
gi 818807181 299 KPGSvTPHTDFEAEAYI 315
Cdd:PRK05124 326 AADE-ALQAVQHASADV 341
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
211-297 |
1.80e-18 |
|
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: 79.54 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 211 TEKPFLMPIEDIFTIEGRGTVVTGRIDRGIIKVNEEVEiigIKPTAKTV-VTGIEMFNKSLDQGQAGDNAGILLRGTKKE 289
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVT---FAPAGVTGeVKSVEMHHEPLEEAIPGDNVGFNVKGVSVK 77
|
....*...
gi 818807181 290 DVQKGQVI 297
Cdd:cd03693 78 DIKRGDVA 85
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
20-178 |
3.00e-18 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 81.36 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 20 GHVDHGKTTLTSAITKIlslkgfakaleygdidKAPEERARGVT--INVHHSEYETDKYHYAHVDCPGHADFiKNMITGA 97
Cdd:cd01887 7 GHVDHGKTTLLDKIRKT----------------NVAAGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 98 AQM-DGAILVVSAPDGPMPQTREHILLARQVGVPaMVVFLNKVDMVDDPQ-LIDLVETEIRELLKKYQFPGDETPIIRGS 175
Cdd:cd01887 70 ASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTEaDPERVKNELSELGLVGEEWGGDVSIVPIS 148
|
...
gi 818807181 176 ALK 178
Cdd:cd01887 149 AKT 151
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
18-247 |
4.08e-18 |
|
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: 85.98 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 18 TI-GHVDHGKTTLTSAITKIlslkgfakaleygdidKAPEERARGVT--INVHHSEYEtDKYHYAHVDCPGHADFIKNMI 94
Cdd:TIGR00487 91 TImGHVDHGKTSLLDSIRKT----------------KVAQGEAGGITqhIGAYHVENE-DGKMITFLDTPGHEAFTSMRA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 95 TGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPaMVVFLNKVDMVD-DPqliDLVETEIRELLKKYQFPGDETPIIR 173
Cdd:TIGR00487 154 RGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEaNP---DRVKQELSEYGLVPEDWGGDTIFVP 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818807181 174 GSALKAAEAtsldDEWAKKILeLMDAVDNYIPEPVRDTEKPFLmpieDIFTIEGRGTVVTGRIDRGIIKVNEEV 247
Cdd:TIGR00487 230 VSALTGDGI----DELLDMIL-LQSEVEELKANPNGQASGVVI----EAQLDKGRGPVATVLVQSGTLRVGDIV 294
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
215-299 |
4.11e-18 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 78.34 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 215 FLMPIEDIFTIEGRGTVVTGRIDRGIIKVNEEVEIIGIKPTAKtvVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKG 294
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR--VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
gi 818807181 295 QVIAK 299
Cdd:cd03696 79 FVLSE 83
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-265 |
1.74e-17 |
|
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: 84.56 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 1 MADKGKFNRTKPH--KNIGTIGHVDHGKTTLTSaitKILSLKGFAKALEYGD---IDKAPEERARGVTIN------VHhs 69
Cdd:TIGR00490 5 MIDKIKELMWKPKfiRNIGIVAHIDHGKTTLSD---NLLAGAGMISEELAGQqlyLDFDEQEQERGITINaanvsmVH-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 70 EYETDKYHYAHVDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAmVVFLNKVDMVD-----D 144
Cdd:TIGR00490 80 EYEGNEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKP-VLFINKVDRLInelklT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 145 PQ-----LIDLVeTEIRELLK---------KYQFPGDETPIIRGSALK--AAEATSLD------------------DEWA 190
Cdd:TIGR00490 159 PQelqerFIKII-TEVNKLIKamapeefrdKWKVRVEDGSVAFGSAYYnwAISVPSMKktgigfkdiykyckedkqKELA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 191 KKI---LELMDAVDNYIPEPVR-------------------------DTEKPFLMPIEDIFTIEGRGTVVTGRIDRGIIK 242
Cdd:TIGR00490 238 KKSplhQVVLDMVIRHLPSPIEaqkyripviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIR 317
|
330 340
....*....|....*....|...
gi 818807181 243 VNEEVEIIGIKPTAKTVVTGIEM 265
Cdd:TIGR00490 318 PGMEVYIVDRKAKARIQQVGVYM 340
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
15-140 |
2.72e-17 |
|
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: 81.10 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 15 NIGTIGHVDHGKTTLTSAI---TKILSLKGfakALEYGD--IDKAPEERARGVTIN--VHHSEYETDKYHYahVDCPGHA 87
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALlyaTGAIDRLG---RVEDGNtvSDYDPEEKKRKMSIEtsVAPLEWNGHKINL--IDTPGYA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 818807181 88 DFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMvVFLNKVD 140
Cdd:cd04170 76 DFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMD 127
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
229-298 |
1.38e-16 |
|
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: 73.84 E-value: 1.38e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818807181 229 GTVVTGRIDRGIIKVNEEVEIIG---IKPTAKTVVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQKGQVIA 298
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPngtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
14-140 |
1.47e-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: 81.63 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 14 KNIGTIGHVDHGKTTLTSAItkilslkgfakaLEY-GDIDKA-------------PEERARGVTIN--VHHSEYETDKYH 77
Cdd:COG0480 10 RNIGIVAHIDAGKTTLTERI------------LFYtGAIHRIgevhdgntvmdwmPEEQERGITITsaATTCEWKGHKIN 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818807181 78 YahVDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMvVFLNKVD 140
Cdd:COG0480 78 I--IDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRI-VFVNKMD 137
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
15-161 |
1.49e-16 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 81.54 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 15 NIGTIGHVDHGKTTLTSAitkILSLKGfaKALEYGDIDKA-------PEERARGVTI--NVHHSEYetDKYHYAHVDCPG 85
Cdd:PRK13351 10 NIGILAHIDAGKTTLTER---ILFYTG--KIHKMGEVEDGttvtdwmPQEQERGITIesAATSCDW--DNHRINLIDTPG 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818807181 86 HADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMvVFLNKVDMVDDpQLIDLVEtEIRELLKK 161
Cdd:PRK13351 83 HIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRL-IFINKMDRVGA-DLFKVLE-DIEERFGK 155
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
19-140 |
3.50e-16 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 80.17 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 19 IGHVDHGKTTLTSAI---TKILSLKGfakALEYGD--IDKAPEERARGVTINVHHSEYETDKYHYAHVDCPGHADFIKNM 93
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfyTGAIHRIG---EVEDGTttMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 818807181 94 ITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMvVFLNKVD 140
Cdd:PRK12740 78 ERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNKMD 123
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
305-393 |
7.50e-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: 67.03 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 305 PHTDFEAEAYILKKEEggrhnPFFSGYKPQFYIRTTDITGDITL-----------KEGVEMVNPGDTATFTVKLIHPVAL 373
Cdd:cd01513 2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKllskedgktkeKKPPDSLQPGENGTVEVELQKPVVL 76
|
90 100
....*....|....*....|....*.
gi 818807181 374 EE------RQRFAFREGGRTIGAGVV 393
Cdd:cd01513 77 ERgkefptLGRFALRDGGRTVGAGLI 102
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-207 |
2.99e-13 |
|
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: 67.56 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 14 KNIGTIGHVDHGKTTLTSAI---TKILSLKGFAKALeygdIDKAPEERARGVTINVH-----HSEYETDKYHYAHVDCPG 85
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLlelTGTVSEREMKEQV----LDSMDLERERGITIKAQavrlfYKAKDGEEYLLNLIDTPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 86 HADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVpAMVVFLNKVDMVD-DPqliDLVETEIRELLkkyqf 164
Cdd:cd01890 77 HVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNL-EIIPVINKIDLPAaDP---DRVKQEIEDVL----- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 818807181 165 pG-DETPIIRGSAlKAAEAtslddewakkILELMDAVDNYIPEP 207
Cdd:cd01890 148 -GlDASEAILVSA-KTGLG----------VEDLLEAIVERIPPP 179
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
11-140 |
6.01e-13 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 70.46 E-value: 6.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 11 KPH--KNIGTIGHVDHGKTTLTSAitkILSLKGFAKALEYGD---IDKAPEERARGVTIN-------VHHSEYETDKYH- 77
Cdd:PTZ00416 15 NPDqiRNMSVIAHVDHGKSTLTDS---LVCKAGIISSKNAGDarfTDTRADEQERGITIKstgislyYEHDLEDGDDKQp 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818807181 78 --YAHVDCPGHADFiKNMITGAAQM-DGAILVVSAPDGPMPQTrEHILlaRQvgvpAM------VVFLNKVD 140
Cdd:PTZ00416 92 flINLIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQ----ALqerirpVLFINKVD 155
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-140 |
6.67e-13 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 67.29 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 14 KNIGTIGHVDHGKTTLTS-----AITKILSLKGFAKALEYgdIDKAPEERARGVTINVHH-SEYETDKYHYAHV----DC 83
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDmlieqTHKRTPSVKLGWKPLRY--TDTRKDEQERGISIKSNPiSLVLEDSKGKSYLiniiDT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 818807181 84 PGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPaMVVFLNKVD 140
Cdd:cd04167 79 PGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLP-MVLVINKID 134
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
215-298 |
1.03e-12 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 63.05 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 215 FLMPIEDIFTIEGRGTVVTGRIDRGIIKVNEEVEIIGIkpTAKTVVTGIEMFNKSLDQGQAGDNAGILLRGtkKEDVQKG 294
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPK--GITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTG 76
|
....
gi 818807181 295 QVIA 298
Cdd:cd01342 77 DTLT 80
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
19-178 |
1.29e-12 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 69.48 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 19 IGHVDHGKTTLTSAITKilslkgfakaleygdiDKAPEERARGVTINVHHSE----YETDKYHYAHVDCPGHADFIKNMI 94
Cdd:CHL00189 250 LGHVDHGKTTLLDKIRK----------------TQIAQKEAGGITQKIGAYEvefeYKDENQKIVFLDTPGHEAFSSMRS 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 95 TGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPaMVVFLNKVDMVDDPqlIDLVETEirelLKKYQFP----GDETP 170
Cdd:CHL00189 314 RGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANAN--TERIKQQ----LAKYNLIpekwGGDTP 386
|
....*...
gi 818807181 171 IIRGSALK 178
Cdd:CHL00189 387 MIPISASQ 394
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
18-140 |
2.51e-12 |
|
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: 68.12 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 18 TI-GHVDHGKTTLTSAI--TKIlslkgfakaleygdidkAPEErARGVT--INVHHSEYETDKYhyAHVDCPGHADFIKN 92
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNV-----------------AAGE-AGGITqhIGAYQVETNGGKI--TFLDTPGHEAFTAM 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 818807181 93 MITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPaMVVFLNKVD 140
Cdd:COG0532 68 RARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKID 114
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
15-140 |
2.79e-12 |
|
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: 66.36 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 15 NIGTIGHVDHGKTTLTSaitKILSLKGFAKALeyGDIDKA-------PEERARGVTINVHHSEYETDKYHYAHVDCPGHA 87
Cdd:cd01886 1 NIGIIAHIDAGKTTTTE---RILYYTGRIHKI--GEVHGGgatmdwmEQERERGITIQSAATTCFWKDHRINIIDTPGHV 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 818807181 88 DFIKNMITGAAQMDGAILVVSAPDGPMPQT----REhillARQVGVPaMVVFLNKVD 140
Cdd:cd01886 76 DFTIEVERSLRVLDGAVAVFDAVAGVQPQTetvwRQ----ADRYGVP-RIAFVNKMD 127
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
215-298 |
3.38e-11 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 59.16 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 215 FLMPIEDIFTIEGRGTVVTGRIDRGIIKVNEEVeIIGikPTA-----KTVVTGIEMFNKSLDQGQAGDNAGILLRGTKKE 289
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLG--PDAdgkfrPVTVKSIHRNRQPVDRARAGQSASFALKKIKRE 77
|
....*....
gi 818807181 290 DVQKGQVIA 298
Cdd:cd03694 78 SLRKGMVLV 86
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
14-185 |
1.65e-10 |
|
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: 59.31 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 14 KNIGTIGHVDHGKTTLTSAITKilslkgfakaleygdIDKAPEERARGVT--INVHHSEYETDKYHYAHVDCPGHADFIK 91
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLG---------------NKGSITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 92 ------NMITGAAQM-DGAILVVSAPDGPMPQTREHILLARQvGVPaMVVFLNKVDMVDDPqlidlVETEIRELLKKYQF 164
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHHADS-GVP-IILVGNKIDLKDAD-----LKTHVASEFAKLNG 139
|
170 180
....*....|....*....|.
gi 818807181 165 PgdetPIIRGSALKAAEATSL 185
Cdd:TIGR00231 140 E----PIIPLSAETGKNIDSA 156
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
214-297 |
9.67e-09 |
|
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.
Pssm-ID: 293912 [Multi-domain] Cd Length: 84 Bit Score: 52.13 E-value: 9.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 214 PFLMPIEDIFTIEGRGTVVTGRIDRGIIKVNEEVEIIGIKPTAktVVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQK 293
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETA--TVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78
|
....
gi 818807181 294 GQVI 297
Cdd:cd16267 79 GSIL 82
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
214-298 |
1.13e-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: 51.73 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 214 PFLMPIEDIFTiEGRGTVVTGRIDRGIIKVNEEVEIIGIKPTAktVVTGIEM-FNKSLDQGQAGDNAGILLRGTKKEDVQ 292
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDA--EVKNIIRnSDEETDWAIAGDTVTLRLRGIEVEDIQ 77
|
....*.
gi 818807181 293 KGQVIA 298
Cdd:cd03698 78 PGDILS 83
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
11-140 |
2.47e-08 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 55.89 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 11 KPH--KNIGTIGHVDHGKTTLTS---AITKILSLKgfakalEYGDI---DKAPEERARGVTI----------------NV 66
Cdd:PLN00116 15 KKHniRNMSVIAHVDHGKSTLTDslvAAAGIIAQE------VAGDVrmtDTRADEAERGITIkstgislyyemtdeslKD 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818807181 67 HHSEYETDKYHYAHVDCPGHADFiKNMITGAAQM-DGAILVVSAPDGPMPQTrEHIL---LARQVgVPAMVVflNKVD 140
Cdd:PLN00116 89 FKGERDGNEYLINLIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVLrqaLGERI-RPVLTV--NKMD 161
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
19-178 |
3.54e-08 |
|
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: 52.46 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 19 IGHVDHGKTTLTSAITkilslkgfakaleYGDIDKAPEERARGVTINVHHSEYETDKYHYAHVDCPGHADFIKNMITGAA 98
Cdd:cd00882 3 VGRGGVGKSSLLNALL-------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 99 QM-----DGAILVVSAPDGPMP--QTREHILLARQVGVPaMVVFLNKVDMVDDPQLIDLVETEIRELLKKyqfpgdeTPI 171
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEedAKLLILRRLRKEGIP-IILVGNKIDLLEEREVEELLRLEELAKILG-------VPV 141
|
....*..
gi 818807181 172 IRGSALK 178
Cdd:cd00882 142 FEVSAKT 148
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
214-297 |
1.58e-07 |
|
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: 48.64 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 214 PFLMPIEDIFtiEGRGTVVTGRIDRGIIKVNEEVEIIGIKPTAKtvVTGIEMFNKSLDQGQAGDNAGILLRGTKKEDVQK 293
Cdd:cd04089 1 PLRMPILDKY--KDMGTVVMGKVESGTIRKGQKLVLMPNKTKVE--VTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISP 76
|
....
gi 818807181 294 GQVI 297
Cdd:cd04089 77 GFVL 80
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
19-155 |
1.73e-07 |
|
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: 52.21 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 19 IGHVDHGKTTLTSAI---TKILSLKGFAKALEYG--------DIdkapeERARGVTINVHHSEYETDKYHYAHVDCPGHA 87
Cdd:cd04169 8 ISHPDAGKTTLTEKLllfGGAIQEAGAVKARKSRkhatsdwmEI-----EKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 88 DFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPaMVVFLNKVDM-VDDP-QLIDLVETEI 155
Cdd:cd04169 83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDReGRDPlELLDEIENEL 151
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
219-298 |
3.43e-07 |
|
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: 47.67 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 219 IEDIFTIeGRGTVVTGRIDRGIIKVNEEVeiigIKPTAKTVVTGIEMFNKSLDQGQAGDNAGILLRGtkKEDVQKGQVIA 298
Cdd:cd16265 5 VEKVFKI-LGRQVLTGEVESGVIYVGYKV----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVLE 77
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
15-161 |
2.61e-06 |
|
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: 48.06 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 15 NIGTIGHVDHGKTTLTSAITKiLSL---KGFAKAleygDIDKAPEERARGVTINV------HHSEYETDKYHYAH----- 80
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQ-GELdngRGKARL----NLFRHKHEVESGRTSSVsndilgFDSDGEVVNYPDNHlgeld 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 81 -------------VDCPGHADFIKNMITG--AAQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVfLNKVDMVDDP 145
Cdd:cd04165 76 veiceksskvvtfIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVV-VTKIDMTPAN 154
|
170
....*....|....*.
gi 818807181 146 QLIDLVeTEIRELLKK 161
Cdd:cd04165 155 VLQETL-KDLKRLLKS 169
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
19-142 |
3.06e-06 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 49.04 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 19 IGHVDHGKTTLTSAITKilslkgfakaleygdiDKAPEERARGVTINVHHSEYETD----------KYHYAHV------- 81
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIRG----------------TAVVKKEAGGITQHIGASEVPTDviekicgdllKSFKIKLkipgllf 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818807181 82 -DCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPaMVVFLNKVDMV 142
Cdd:TIGR00491 74 iDTPGHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKIDRI 134
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
309-396 |
8.55e-06 |
|
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: 43.66 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 309 FEAEAYILkkeeggRHNPFFS-GYKPQFYIRTTDITGDITLKEGvEMVNPGDTATFTVKLI-HPVALEERQRFAFREgGR 386
Cdd:cd03708 6 FEAEVLVL------HHPTTISpGYQPVVHCGTIRQTARIISIDK-EVLRTGDRALVRFRFLyRPEYLREGQRLIFRE-GR 77
|
90
....*....|
gi 818807181 387 TIGAGVVTKI 396
Cdd:cd03708 78 TKGIGTVTKV 87
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
343-396 |
6.71e-05 |
|
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: 41.76 E-value: 6.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 343 TGDITlKEGVEMVNPGDTATFTVKLIHPVALEERQ------RFAFREGGRTIGAGVVTKI 396
Cdd:cd04093 51 TGEVI-KKKPRCLGKNQSAVVEIELERPIPLETFKdnkelgRFVLRRGGETIAAGIVTEI 109
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
20-140 |
1.57e-04 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 43.63 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 20 GHVDHGKTTL------TS-------AITK--------ILSLKGFAKALeygdIDKAPEErargVTINvhhseyetdkyHY 78
Cdd:PRK04004 13 GHVDHGKTTLldkirgTAvaakeagGITQhigatevpIDVIEKIAGPL----KKPLPIK----LKIP-----------GL 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818807181 79 AHVDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPaMVVFLNKVD 140
Cdd:PRK04004 74 LFIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTP-FVVAANKID 134
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
81-162 |
8.58e-04 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 41.79 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 81 VDCPGHADFIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVGVPaMVVFLNKVDMV-------DDPQLIDL--- 150
Cdd:PRK14845 531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTP-FVVAANKIDLIpgwniseDEPFLLNFneq 609
|
90
....*....|....*....
gi 818807181 151 -------VETEIRELLKKY 162
Cdd:PRK14845 610 dqhalteLEIKLYELIGKL 628
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
15-138 |
9.37e-04 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 38.75 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 15 NIGTIGHVDHGKTTLTSAITKILSLKGfakaleygdiDKApeerarGVTINVHHSEYETDKYHYAHVDCPG--HADFIKN 92
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVS----------DYP------GTTRDPNEGRLELKGKQIILVDTPGliEGASEGE 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 818807181 93 MITGA----AQMDGAILVVSAPDGPMPQTREHILLARQVGVPAMVVfLNK 138
Cdd:pfam01926 65 GLGRAflaiIEADLILFVVDSEEGITPLDEELLELLRENKKPIILV-LNK 113
|
|
| CobW-like |
cd03112 |
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ... |
101-158 |
2.00e-03 |
|
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.
Pssm-ID: 349766 Cd Length: 198 Bit Score: 39.04 E-value: 2.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 101 DGAILVVSAPDGP--MPQTREHILLARQVGVpAMVVFLNKVDMVDDPQLiDLVETEIREL 158
Cdd:cd03112 118 DGVVTVVDAKNFLkqLDEEDVSDLAVDQIAF-ADVIVLNKTDLVDEEEL-EALRARIRAL 175
|
|
| selB_III |
cd15491 |
Domain III of selenocysteine-specific translation elongation factor; This family represents ... |
335-393 |
4.62e-03 |
|
Domain III of selenocysteine-specific translation elongation factor; This family represents domain III of bacterial selenocysteine (Sec)-specific elongation factor (EFSec), homologous to domain III of EF-Tu. SelB is a specialized translation elongation factor responsible for the co-translational incorporation of selenocysteine into proteins by recoding of a UGA stop codon in the presence of a downstream mRNA hairpin loop, called Sec insertion sequence (SECIS) element.
Pssm-ID: 294012 [Multi-domain] Cd Length: 87 Bit Score: 35.88 E-value: 4.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818807181 335 FYIRTTDITGDITLKEGvEMVNPGDTATFTVKLIHPVALEERQRFAFREGG--RTIGAGVV 393
Cdd:cd15491 28 LHLGTSEVLGRVVLLDR-DELAPGEEALAQLRLEEPVVAKRGDRFILRSYSpmRTIGGGRV 87
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
215-299 |
7.03e-03 |
|
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: 35.23 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818807181 215 FLMPIEDI--FTIEGRGtvVTGRIDRGIIKVNEEVEIIgikPTAKTV-VTGIEMFNKSLDQGQAGDNAGILLrgTKKEDV 291
Cdd:cd03695 1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTVL---PSGKTSrVKSIVTFDGELDSAGAGEAVTLTL--EDEIDV 73
|
....*...
gi 818807181 292 QKGQVIAK 299
Cdd:cd03695 74 SRGDLIVR 81
|
|
| |
