|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-386 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 692.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 1 MSKTAYVRTKPHLNIGTMGHVDHGKTTLTAAITKVLAERGTGTFVPFDRIDRAPEEAARGITINIAHVEYETDTRHYAHV 80
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 81 DMPGHADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKADA-GDEELTDLVELEVRDLLTA 159
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLvDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 160 HGYGGDSVPVVRVSGLKALEGDPRWTASIEALLDAVDTYVPMPERYLDAPFLLSVENVLTITGRGTVVTGAVERGTVRVG 239
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 240 DKVEVLGA--DLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHVVAAPGSVVPSRRFTAQVYVLSAREGGRT 317
Cdd:PRK12736 241 DEVEIVGIkeTQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRH 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 318 TAVSSGYRPQFYIRTADVVGDVDLGE-VAVARPGDTVVMTVELGREMPLEPGLGFAIREGGRTVGAGTVT 386
Cdd:PRK12736 321 TPFFNNYRPQFYFRTTDVTGSIELPEgTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVT 390
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-386 |
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: 684.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 1 MSKTAYVRTKPHLNIGTMGHVDHGKTTLTAAITKVLAERGTGTFVPFDRIDRAPEEAARGITINIAHVEYETDTRHYAHV 80
Cdd:COG0050 1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 81 DMPGHADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKAD-AGDEELTDLVELEVRDLLTA 159
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDmVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 160 HGYGGDSVPVVRVSGLKALEGD--PRWTASIEALLDAVDTYVPMPERYLDAPFLLSVENVLTITGRGTVVTGAVERGTVR 237
Cdd:COG0050 161 YGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 238 VGDKVEVLG--ADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHVVAAPGSVVPSRRFTAQVYVLSAREGG 315
Cdd:COG0050 241 VGDEVEIVGirDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752498825 316 RTTAVSSGYRPQFYIRTADVVGDVDLGE-VAVARPGDTVVMTVELGREMPLEPGLGFAIREGGRTVGAGTVT 386
Cdd:COG0050 321 RHTPFFNGYRPQFYFRTTDVTGVITLPEgVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVT 392
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-386 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 625.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 1 MSKTAYVRTKPHLNIGTMGHVDHGKTTLTAAITKVLAERGTGTFVPFDRIDRAPEEAARGITINIAHVEYETDTRHYAHV 80
Cdd:PRK00049 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 81 DMPGHADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKAD-AGDEELTDLVELEVRDLLTA 159
Cdd:PRK00049 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDmVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 160 HGYGGDSVPVVRVSGLKALEG--DPRWTASIEALLDAVDTYVPMPERYLDAPFLLSVENVLTITGRGTVVTGAVERGTVR 237
Cdd:PRK00049 161 YDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 238 VGDKVEVLG--ADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHVVAAPGSVVPSRRFTAQVYVLSAREGG 315
Cdd:PRK00049 241 VGEEVEIVGirDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752498825 316 RTTAVSSGYRPQFYIRTADVVGDVDLGE-VAVARPGDTVVMTVELGREMPLEPGLGFAIREGGRTVGAGTVT 386
Cdd:PRK00049 321 RHTPFFNGYRPQFYFRTTDVTGVIELPEgVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVT 392
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-386 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 604.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 1 MSKTAYVRTKPHLNIGTMGHVDHGKTTLTAAITKVLAERGTGTFVPFDRIDRAPEEAARGITINIAHVEYETDTRHYAHV 80
Cdd:PRK12735 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 81 DMPGHADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKAD-AGDEELTDLVELEVRDLLTA 159
Cdd:PRK12735 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDmVDDEELLELVEMEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 160 HGYGGDSVPVVRVSGLKALEGD--PRWTASIEALLDAVDTYVPMPERYLDAPFLLSVENVLTITGRGTVVTGAVERGTVR 237
Cdd:PRK12735 161 YDFPGDDTPIIRGSALKALEGDddEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 238 VGDKVEVLG--ADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHVVAAPGSVVPSRRFTAQVYVLSAREGG 315
Cdd:PRK12735 241 VGDEVEIVGikETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752498825 316 RTTAVSSGYRPQFYIRTADVVGDVDLGE-VAVARPGDTVVMTVELGREMPLEPGLGFAIREGGRTVGAGTVT 386
Cdd:PRK12735 321 RHTPFFNGYRPQFYFRTTDVTGTIELPEgVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVA 392
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-386 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 565.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 1 MSKTAYVRTKPHLNIGTMGHVDHGKTTLTAAITKVLAERGTGTFVPFDRIDRAPEEAARGITINIAHVEYETDTRHYAHV 80
Cdd:CHL00071 1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 81 DMPGHADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKAD-AGDEELTDLVELEVRDLLTA 159
Cdd:CHL00071 81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDqVDDEELLELVELEVRELLSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 160 HGYGGDSVPVVRVSGLKALE----------GDPRWTASIEALLDAVDTYVPMPERYLDAPFLLSVENVLTITGRGTVVTG 229
Cdd:CHL00071 161 YDFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 230 AVERGTVRVGDKVEVLGADL--ETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHVVAAPGSVVPSRRFTAQVY 307
Cdd:CHL00071 241 RIERGTVKVGDTVEIVGLREtkTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 308 VLSAREGGRTTAVSSGYRPQFYIRTADVVGDV------DLGEVAVARPGDTVVMTVELGREMPLEPGLGFAIREGGRTVG 381
Cdd:CHL00071 321 ILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIesftadDGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVG 400
|
....*
gi 1752498825 382 AGTVT 386
Cdd:CHL00071 401 AGVVS 405
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-388 |
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: 541.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 1 MSKTAYVRTKPHLNIGTMGHVDHGKTTLTAAITKVLAERGTGTFVPFDRIDRAPEEAARGITINIAHVEYETDTRHYAHV 80
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 81 DMPGHADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKAD-AGDEELTDLVELEVRDLLTA 159
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDmVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 160 HGYGGDSVPVVRVSGLKALEGDPRWTASIEALLDAVDTYVPMPERYLDAPFLLSVENVLTITGRGTVVTGAVERGTVRVG 239
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 240 DKVEVLG--ADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHVVAAPGSVVPSRRFTAQVYVLSAREGGRT 317
Cdd:TIGR00485 241 EEVEIVGlkDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRH 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752498825 318 TAVSSGYRPQFYIRTADVVGDVDLGE-VAVARPGDTVVMTVELGREMPLEPGLGFAIREGGRTVGAGTVTVV 388
Cdd:TIGR00485 321 TPFFSGYRPQFYFRTTDVTGTIELPEgVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKI 392
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
6-388 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 527.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 6 YVRTKPHLNIGTMGHVDHGKTTLTAAITKVLAERGTGTFVPFDRIDRAPEEAARGITINIAHVEYETDTRHYAHVDMPGH 85
Cdd:PLN03127 55 FTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 86 ADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKADA-GDEELTDLVELEVRDLLTAHGYGG 164
Cdd:PLN03127 135 ADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVvDDEELLELVEMELRELLSFYKFPG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 165 DSVPVVRVSGLKALEG--DPRWTASIEALLDAVDTYVPMPERYLDAPFLLSVENVLTITGRGTVVTGAVERGTVRVGDKV 242
Cdd:PLN03127 215 DEIPIIRGSALSALQGtnDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 243 EVLG----ADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHVVAAPGSVVPSRRFTAQVYVLSAREGGRTT 318
Cdd:PLN03127 295 EIVGlrpgGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHT 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752498825 319 AVSSGYRPQFYIRTADVVGDVDLGE-VAVARPGDTVVMTVELGREMPLEPGLGFAIREGGRTVGAGTVTVV 388
Cdd:PLN03127 375 PFFSNYRPQFYLRTADVTGKVELPEgVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKV 445
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
6-388 |
3.40e-166 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 474.10 E-value: 3.40e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 6 YVRTKPHLNIGTMGHVDHGKTTLTAAITKVLAERGTGTFVPFDRIDRAPEEAARGITINIAHVEYETDTRHYAHVDMPGH 85
Cdd:PLN03126 75 FERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 86 ADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKAD-AGDEELTDLVELEVRDLLTAHGYGG 164
Cdd:PLN03126 155 ADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDqVDDEELLELVELEVRELLSSYEFPG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 165 DSVPVVRVSGLKALE----------GDPRWTASIEALLDAVDTYVPMPERYLDAPFLLSVENVLTITGRGTVVTGAVERG 234
Cdd:PLN03126 235 DDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 235 TVRVGDKVEVLG--ADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHVVAAPGSVVPSRRFTAQVYVLSAR 312
Cdd:PLN03126 315 TVKVGETVDIVGlrETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKE 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 313 EGGRTTAVSSGYRPQFYIRTADVVGDV-----DLGEVA-VARPGDTVVMTVELGREMPLEPGLGFAIREGGRTVGAGTVT 386
Cdd:PLN03126 395 EGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESkMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGAGVIQ 474
|
..
gi 1752498825 387 VV 388
Cdd:PLN03126 475 SI 476
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
11-202 |
1.22e-126 |
|
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: 362.67 E-value: 1.22e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 11 PHLNIGTMGHVDHGKTTLTAAITKVLAERGTGTFVPFDRIDRAPEEAARGITINIAHVEYETDTRHYAHVDMPGHADYVK 90
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 91 NMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKADA-GDEELTDLVELEVRDLLTAHGYGGDSVPV 169
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMvDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1752498825 170 VRVSGLKALEGD--PRWTASIEALLDAVDTYVPMP 202
Cdd:cd01884 161 VRGSALKALEGDdpNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
8-388 |
3.14e-95 |
|
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: 291.07 E-value: 3.14e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 8 RTKPHLNIGTMGHVDHGKTTL-------TAAIT--------KVLAERGTGTFVPFDRIDRAPEEAARGITINIAHVEYET 72
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLvgrllyeTGAIDehiiekyeEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 73 DTRHYAHVDMPGHADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKADAG--DEELTDLVE 150
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVnySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 151 LEVRDLLTAHGYGGDSVPVVRVSGLKaleGD---------PRWTAsiEALLDAVDTyVPMPERYLDAPFLLSVENVLTIT 221
Cdd:COG5256 163 EEVSKLLKMVGYKVDKIPFIPVSAWK---GDnvvkksdnmPWYNG--PTLLEALDN-LKEPEKPVDKPLRIPIQDVYSIS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 222 GRGTVVTGAVERGTVRVGDKVEVLGADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHV---VAAPGSVVp 298
Cdd:COG5256 237 GIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVaghPDNPPTVA- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 299 sRRFTAQVYVLSareggRTTAVSSGYRPQFYIRTADV-------VGDVD--LGEVAVARP-----GDTVVMTVELGREMP 364
Cdd:COG5256 316 -EEFTAQIVVLQ-----HPSAITVGYTPVFHVHTAQVactfvelVSKLDprTGQVKEENPqflktGDAAIVKIKPTKPLV 389
|
410 420 430
....*....|....*....|....*....|
gi 1752498825 365 LE-----PGLG-FAIREGGRTVGAGTVTVV 388
Cdd:COG5256 390 IEkfkefPQLGrFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-388 |
8.64e-93 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 284.90 E-value: 8.64e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 8 RTKPHLNIGTMGHVDHGKTTL-------TAAI--------TKVLAERGTGTFVPFDRIDRAPEEAARGITINIAHVEYET 72
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLvgrllyeTGAIdehiieelREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 73 DTRHYAHVDMPGHADYVKNMVTGAAQLDGAILVVSALD--GIMPQTAEHVLLARQVGVDHIVVALNKADAG--DEELTDL 148
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVnyDEKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 149 VELEVRDLLTAHGYGGDSVPVVRVSglkALEGD---------PRWTAsiEALLDAVDTyVPMPERYLDAPFLLSVENVLT 219
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFIPVS---AFEGDnvvkksenmPWYNG--PTLLEALDN-LKPPEKPTDKPLRIPIQDVYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 220 ITGRGTVVTGAVERGTVRVGDKVEVLGADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHvVAAPGSVVPS 299
Cdd:PRK12317 236 ISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGD-VCGHPDNPPT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 300 --RRFTAQVYVLSareggRTTAVSSGYRPQFYIRTADV-------VGDVD--LGEVAVARP-----GDTVVMTVELGREM 363
Cdd:PRK12317 315 vaEEFTAQIVVLQ-----HPSAITVGYTPVFHAHTAQVactfeelVKKLDprTGQVAEENPqfiktGDAAIVKIKPTKPL 389
|
410 420 430
....*....|....*....|....*....|.
gi 1752498825 364 PLE-----PGLG-FAIREGGRTVGAGTVTVV 388
Cdd:PRK12317 390 VIEkvkeiPQLGrFAIRDMGQTIAAGMVIDV 420
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-385 |
9.87e-84 |
|
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: 267.55 E-value: 9.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 13 LNIGTMGHVDHGKTTLTAAITkvlaerGTGTfvpfdriDRAPEEAARGITINI--AHVEYEtDTRHYAHVDMPGHADYVK 90
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALT------GIDT-------DRLKEEKKRGITIDLgfAYLPLP-DGRRLGFVDVPGHEKFIK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 91 NMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKADAGDEELTDLVELEVRDLLTAHGYGGdsVPVV 170
Cdd:COG3276 67 NMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVDEEWLELVEEEIRELLAGTFLED--APIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 171 RVSglkALEGdprwtASIEALLDAVDTYV-PMPERYLDAPFLLSVENVLTITGRGTVVTGAVERGTVRVGDKVEVLGADL 249
Cdd:COG3276 145 PVS---AVTG-----EGIDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 250 ETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHVVAAPGSVVPSRRFTAQVYVLSAREggrtTAVSSGYRPQFY 329
Cdd:COG3276 217 PVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPSAP----RPLKHWQRVHLH 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752498825 330 IRTADVVGDVDLGEVAVARPGDTVVMTVELGREMPLEPGLGFAIREGG--RTVGAGTV 385
Cdd:COG3276 293 HGTAEVLARVVLLDREELAPGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-200 |
4.52e-77 |
|
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: 236.27 E-value: 4.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 10 KPHLNIGTMGHVDHGKTTLTAAITKVLAERGTGTFVPFD---RIDRAPEEAARGITINIAHVEYETDTRHYAHVDMPGHA 86
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEgeaGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 87 DYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVdHIVVALNKAD-AGDEELTDLVELEVRDLLTAHGYGGD 165
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGV-PIIVFINKMDrVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1752498825 166 SVPVVRVSGLKALegdprwtaSIEALLDAVDTYVP 200
Cdd:pfam00009 160 FVPVVPGSALKGE--------GVQTLLDALDEYLP 186
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
10-388 |
2.27e-59 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 198.82 E-value: 2.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 10 KPHLNIGTMGHVDHGKTTLTAAIT---------------KVLAERGTGTFVPFDRIDRAPEEAARGITINIAHVEYETDT 74
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 75 RHYAHVDMPGHADYVKNMVTGAAQLDGAILVVSALDGIMP-------QTAEHVLLARQVGVDHIVVALNKADAG----DE 143
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKtvnySQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 144 ELTDLVELEVRDLLTAHGYGGDSVPVVRVSGlkaLEGDPRWTASIE-------ALLDAVDTYVPmPERYLDAPFLLSVEN 216
Cdd:PTZ00141 165 ERYDEIKKEVSAYLKKVGYNPEKVPFIPISG---WQGDNMIEKSDNmpwykgpTLLEALDTLEP-PKRPVDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 217 VLTITGRGTVVTGAVERGTVRVGDKVEVLGADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHvVAAPGSV 296
Cdd:PTZ00141 241 VYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGY-VASDSKN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 297 VPSR---RFTAQVYVLSareggRTTAVSSGYRPQFYIRTADVV--------------GDVDLGEVAVARPGDTVVMTVEL 359
Cdd:PTZ00141 320 DPAKecaDFTAQVIVLN-----HPGQIKNGYTPVLDCHTAHIAckfaeieskidrrsGKVLEENPKAIKSGDAAIVKMVP 394
|
410 420 430
....*....|....*....|....*....|....*
gi 1752498825 360 GREMPLE-----PGLG-FAIREGGRTVGAGTVTVV 388
Cdd:PTZ00141 395 TKPMCVEvfneyPPLGrFAVRDMKQTVAVGVIKSV 429
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
13-293 |
5.52e-56 |
|
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: 193.17 E-value: 5.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 13 LNIGTMGHVDHGKTTLTAAITKVLAergtgtfvpfdriDRAPEEAARGITINIAHVEYETDTRHYAHVDMPGHADYVKNM 92
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 93 VTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKADAGDEELTDLVELEVRDLLTAHGYGGDSvPVVRV 172
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIKRTEMFMKQILNSYIFLKNA-KIFKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 173 SGlKALEGDPRWTASIEALLDAVDTyvpmpeRYLDAPFLLSVENVLTITGRGTVVTGAVERGTVRVGDKVEVLGADLETV 252
Cdd:TIGR00475 147 SA-KTGQGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVR 219
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1752498825 253 VTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHVVAAP 293
Cdd:TIGR00475 220 VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP 260
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
14-202 |
7.16e-51 |
|
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: 168.63 E-value: 7.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLTAAITKVLAERGTGTFVPFDRIDRAPEEAARGITINIAHVEYETDTRHYAHVDMPGHADYVKNMV 93
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 94 TGAAQLDGAILVVSALDGIMPQTAEHVLLARQvGVDHIVVALNKADAGDEELTDLVELEVRDLLTAHGYGGDS---VPVV 170
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRVGEEDFDEVLREIKELLKLIGFTFLKgkdVPII 159
|
170 180 190
....*....|....*....|....*....|..
gi 1752498825 171 RVSGLKALegdprwtaSIEALLDAVDTYVPMP 202
Cdd:cd00881 160 PISALTGE--------GIEELLDAIVEHLPPP 183
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
15-287 |
6.74e-47 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 169.08 E-value: 6.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 15 IGTMGHVDHGKTTLTAAITKVLAergtgtfvpfdriDRAPEEAARGITINIAHVEY-ETDTRHYAHVDMPGHADYVKNMV 93
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 94 TGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKADAGDEELTDLVELEVRDLLTAHGYGGDSVPVVrvs 173
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRRQVKAVLREYGFAEAKLFVT--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 174 glKALEGdprwtASIEALLDAVDTyVPMPERYLDAPFLLSVENVLTITGRGTVVTGAVERGTVRVGDKVEVLGADLETVV 253
Cdd:PRK10512 147 --AATEG-----RGIDALREHLLQ-LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRV 218
|
250 260 270
....*....|....*....|....*....|....*
gi 1752498825 254 TGLETFGRPMEEAQAGDNVALLLRG-VPRDAVRRG 287
Cdd:PRK10512 219 RGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-306 |
2.94e-43 |
|
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: 155.63 E-value: 2.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 1 MSKTAYVRTKPH-----LNIGTMGHVDHGKTTLT---------------AAITKVLAERGTgtfvpfDRIDRAP------ 54
Cdd:COG2895 1 MSTDIEAYLAQHenkdlLRFITCGSVDDGKSTLIgrllydtksifedqlAALERDSKKRGT------QEIDLALltdglq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 55 EEAARGITINIAHVEYETDTRHYAHVDMPGHADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVA 134
Cdd:COG2895 75 AEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 135 LNKADAGD--EELTDLVELEVRDLLTAHGYggDSVPVVRVSglkALEGDPRWTASI-------EALLDAVDTyVPMPERY 205
Cdd:COG2895 155 VNKMDLVDysEEVFEEIVADYRAFAAKLGL--EDITFIPIS---ALKGDNVVERSEnmpwydgPTLLEHLET-VEVAEDR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 206 LDAPFLLSVENVL--TITGRGtvVTGAVERGTVRVGDKVEVLGADLETVVTGLETFGRPMEEAQAGDNVALLLrgvpRDA 283
Cdd:COG2895 229 NDAPFRFPVQYVNrpNLDFRG--YAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTL----EDE 302
|
330 340
....*....|....*....|....*.
gi 1752498825 284 --VRRGHVVAAPGSV-VPSRRFTAQV 306
Cdd:COG2895 303 idISRGDVIVAADAPpEVADQFEATL 328
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
14-176 |
3.62e-43 |
|
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: 149.56 E-value: 3.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLT---------------AAITKVLAERGTGTF----VpfdrIDRAPEEAARGITINIAHVEYETDT 74
Cdd:cd01883 1 NLVVIGHVDAGKSTLTghllyklggvdkrtiEKYEKEAKEMGKESFkyawV----LDKLKEERERGVTIDVGLAKFETEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 75 RHYAHVDMPGHADYVKNMVTGAAQLDGAILVVSALDG-------IMPQTAEHVLLARQVGVDHIVVALNKADAG----DE 143
Cdd:cd01883 77 YRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVtvnwSQ 156
|
170 180 190
....*....|....*....|....*....|...
gi 1752498825 144 ELTDLVELEVRDLLTAHGYGGDSVPVVRVSGLK 176
Cdd:cd01883 157 ERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFT 189
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
15-196 |
8.23e-42 |
|
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: 144.67 E-value: 8.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 15 IGTMGHVDHGKTTLTAAITkvlaerGTGTfvpfdriDRAPEEAARGITINI--AHVEYETDTRhYAHVDMPGHADYVKNM 92
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALT------GIET-------DRLPEEKKRGITIDLgfAYLDLPDGKR-LGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 93 VTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKADAGDEELTDLVELEVRDLLTahGYGGDSVPVVRV 172
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDEDRLELVEEEILELLA--GTFLADAPIFPV 145
|
170 180
....*....|....*....|....
gi 1752498825 173 SglkALEGDprwtaSIEALLDAVD 196
Cdd:cd04171 146 S---SVTGE-----GIEELKNYLD 161
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
8-388 |
1.85e-41 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 151.40 E-value: 1.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 8 RTKPHLNIGTMGHVDHGKTTLTA-------AITKVLAERGTGTFVPFDR--------IDRAPEEAARGITINIAHVEYET 72
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGhliyklgGIDKRVIERFEKEAAEMNKrsfkyawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 73 DTRHYAHVDMPGHADYVKNMVTGAAQLDGAILVVSALDGIMP-------QTAEHVLLARQVGVDHIVVALNKADAGDEEL 145
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTPKY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 146 T----DLVELEVRDLLTAHGYGGDSVPVVRVSGlkaLEGDPRWTASIE-------ALLDAVDTyVPMPERYLDAPFLLSV 214
Cdd:PLN00043 163 SkaryDEIVKEVSSYLKKVGYNPDKIPFVPISG---FEGDNMIERSTNldwykgpTLLEALDQ-INEPKRPSDKPLRLPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 215 ENVLTITGRGTVVTGAVERGTVRVGDKVEVLGADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHvVAAPG 294
Cdd:PLN00043 239 QDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGY-VASNS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 295 SVVPSR---RFTAQVYVLSareggRTTAVSSGYRP-------QFYIRTADVVGDVDL---------------GEVAVARP 349
Cdd:PLN00043 318 KDDPAKeaaNFTSQVIIMN-----HPGQIGNGYAPvldchtsHIAVKFAEILTKIDRrsgkelekepkflknGDAGFVKM 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 1752498825 350 GDTVVMTVELGREMPlePGLGFAIREGGRTVGAGTVTVV 388
Cdd:PLN00043 393 IPTKPMVVETFSEYP--PLGRFAVRDMRQTVAVGVIKSV 429
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
11-300 |
7.15e-40 |
|
translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Pssm-ID: 274720 [Multi-domain] Cd Length: 406 Bit Score: 146.35 E-value: 7.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 11 PHLNIGTMGHVDHGKTTLTAAITKVLaergtgtfvpfdrIDRAPEEAARGITINIAHV-----------EYETDT----- 74
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELKRGISIRLGYAdaeiykcpecdGPECYTtepvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 75 ----------RHYAHVDMPGHADYVKNMVTGAAQLDGAILVVSALDGI-MPQTAEHVLLARQVGVDHIVVALNKADAGDE 143
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPCpQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 144 ELTDLVELEVRDLLtaHGYGGDSVPVVRVSGLKalegdprwTASIEALLDAVDTYVPMPERYLDAPFLLSVENVLTITGR 223
Cdd:TIGR03680 150 EKALENYEEIKEFV--KGTVAENAPIIPVSALH--------NANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNKP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 224 GT--------VVTGAVERGTVRVGDKVEVLGA------------DLETVVTGLETFGRPMEEAQAGDNVAL-------LL 276
Cdd:TIGR03680 220 GTppeklkggVIGGSLIQGKLKVGDEIEIRPGikvekggktkwePIYTEITSLRAGGYKVEEARPGGLVGVgtkldpaLT 299
|
330 340
....*....|....*....|....
gi 1752498825 277 RGvprDAVrRGHVVAAPGSVVPSR 300
Cdd:TIGR03680 300 KA---DAL-AGQVVGKPGTLPPVW 319
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
298-385 |
1.04e-38 |
|
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.
Pssm-ID: 294006 [Multi-domain] Cd Length: 90 Bit Score: 133.79 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 298 PSRRFTAQVYVLSAREGGRTTAVSSGYRPQFYIRTADVVGDVDLGE-VAVARPGDTVVMTVELGREMPLEPGLGFAIREG 376
Cdd:cd03707 2 PHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEgVEMVMPGDNVKMTVELIHPIALEEGLRFAIREG 81
|
....*....
gi 1752498825 377 GRTVGAGTV 385
Cdd:cd03707 82 GRTVGAGVV 90
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
11-355 |
2.87e-38 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 141.91 E-value: 2.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 11 PHLNIGTMGHVDHGKTTLTAAITkvlaerGTGTfvpfdriDRAPEEAARGITINIAHVE--------------YETDT-- 74
Cdd:PRK04000 8 PEVNIGMVGHVDHGKTTLVQALT------GVWT-------DRHSEELKRGITIRLGYADatirkcpdceepeaYTTEPkc 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 75 ----------RHYAHVDMPGHADYVKNMVTGAAQLDGAILVVSALDGI-MPQTAEHVLLARQVGVDHIVVALNKADAGDE 143
Cdd:PRK04000 75 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 144 EltDLVE--LEVRDLLTahGYGGDSVPVVRVSGLKAlegdprwtASIEALLDAVDTYVPMPERYLDAPFLLSVENVLTIT 221
Cdd:PRK04000 155 E--RALEnyEQIKEFVK--GTVAENAPIIPVSALHK--------VNIDALIEAIEEEIPTPERDLDKPPRMYVARSFDVN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 222 GRGT--------VVTGAVERGTVRVGDKVEVL-GADLE-----------TVVTGLETFGRPMEEAQAGDNVAL------- 274
Cdd:PRK04000 223 KPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKVEeggktkwepitTKIVSLRAGGEKVEEARPGGLVGVgtkldps 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 275 LLRGvprDAVrRGHVVAAPGSVVPSR-RFTAQVYVLS----AREGGRTTAVSSGYRPQFYIRTADVVGDV-----DLGEV 344
Cdd:PRK04000 303 LTKA---DAL-AGSVAGKPGTLPPVWeSLTIEVHLLErvvgTKEELKVEPIKTGEPLMLNVGTATTVGVVtsarkDEAEV 378
|
410
....*....|....*.
gi 1752498825 345 AVARP-----GDTVVM 355
Cdd:PRK04000 379 KLKRPvcaeeGDRVAI 394
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-386 |
8.66e-37 |
|
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: 138.05 E-value: 8.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 8 RTKPHLNIGTMGHVDHGKTTLTAAITkvlaerGTGTfvpfdriDRAPEEAARGITINIAHVE--------------YETD 73
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALT------GVWT-------DRHSEELKRGITIRLGYADatfykcpnceppeaYTTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 74 T------------RHYAHVDMPGHADYVKNMVTGAAQLDGAILVVSALDGI-MPQTAEHVLLARQVGVDHIVVALNKADA 140
Cdd:COG5257 68 PkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 141 GD--------EELTDLVElevrdlltahGYGGDSVPVVRVSGLKAlegdprwtASIEALLDAVDTYVPMPERYLDAPFLL 212
Cdd:COG5257 148 VSkeralenyEQIKEFVK----------GTVAENAPIIPVSAQHK--------VNIDALIEAIEEEIPTPERDLSKPPRM 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 213 SVENVLTITGRGT--------VVTGAVERGTVRVGDKVEVL-GADLE-----------TVVTGLETFGRPMEEAQAGDNV 272
Cdd:COG5257 210 LVARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEkggktkyepitTTVVSLRAGGEEVEEAKPGGLV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 273 AL-------LLRGvprDAVrRGHVVAAPGSVVPSR-RFTAQVY----VLSAREGGRTTAVSSGYRPQFYIRTADVVGDvd 340
Cdd:COG5257 290 AVgtkldpsLTKS---DSL-VGSVAGKPGTLPPVLdSLTMEVHllerVVGTKEEVKVEPIKTGEPLMLNVGTATTVGV-- 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1752498825 341 lgeVAVARPGdtvVMTVELGREMPLEPGLGFAI--REGG--RTVGAGTVT 386
Cdd:COG5257 364 ---VTSARKD---EIEVKLKRPVCAEKGSRVAIsrRIGGrwRLIGWGIIK 407
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
12-386 |
2.26e-35 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 136.22 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 12 HLNIGTMGHVDHGKTTLTAAITKVLAERGTGTFVPFdrIDRAPEEAARGITINIAHVEY--------------------- 70
Cdd:COG5258 122 HIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLSADLSYAVYgfdddgpvrmknplrktdrar 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 71 --ETDTRHYAHVDMPGHADYVKNMVTG--AAQLDGAILVVSALDGIMPQTAEH--VLLARQVGVdhiVVALNKADAGDEE 144
Cdd:COG5258 200 vvEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLAMDLPV---IVAITKIDKVDDE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 145 LTDLVELEVRDLL-----------TAHG-------YGGDSVPVVRVSGLkALEGdprwtasiealLDAVDTYVPM-PERY 205
Cdd:COG5258 277 RVEEVEREIENLLrivgrtpleveSRHDvdaaieeINGRVVPILKTSAV-TGEG-----------LDLLDELFERlPKRA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 206 LDA--PFLLSVENVLTITGRGTVVTGAVERGTVRVGDKVEV----LGADLETVVTGLETFGRPMEEAQAGDNVALLLRGV 279
Cdd:COG5258 345 TDEdePFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIgptkDGSFREVEVKSIEMHYHRVDKAEAGRIVGIALKGV 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 280 PRDAVRRGHVVAAPGS-VVPSRRFTAQVYVLSareggRTTAVSSGYRPQFY---IRTADVVGDVDLGEVavaRPGDTVVM 355
Cdd:COG5258 425 EEEELERGMVLLPRDAdPKAVREFEAEVMVLN-----HPTTIKEGYEPVVHletISEAVRFEPIDKGYL---LPGDSGRV 496
|
410 420 430
....*....|....*....|....*....|..
gi 1752498825 356 TVE-LGREMPLEPGLGFAIREgGRTVGAGTVT 386
Cdd:COG5258 497 RLRfKYRPYYVEEGQRFVFRE-GRSKGVGTVT 527
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
210-294 |
2.20e-33 |
|
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: 119.55 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 210 FLLSVENVLTITGRGTVVTGAVERGTVRVGDKVEVLG--ADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRG 287
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGfkETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 1752498825 288 HVVAAPG 294
Cdd:cd03697 81 MVLAKPG 87
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
295-388 |
3.63e-32 |
|
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: 116.98 E-value: 3.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 295 SVVPSRRFTAQVYVLSAREGGRTTAVSSGYRPQFYIRTADVVGDV-------DLGEVA----VARPGDTVVMTVELGREM 363
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFvellhklDPGGVSenpeFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 1752498825 364 PLEPGLGFAIREGGRTVGAGTVTVV 388
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
14-274 |
4.01e-28 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 115.86 E-value: 4.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLtaaITKVLaeRGTGTF----VPFDRI-DRAPEEAARGITI---NIAhVEYEtDTRhYAHVDMPGH 85
Cdd:TIGR01394 3 NIAIIAHVDHGKTTL---VDALL--KQSGTFraneAVAERVmDSNDLERERGITIlakNTA-IRYN-GTK-INIVDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 86 ADY------VKNMVtgaaqlDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVaLNKADAGDEELTDLVElEVRDLLTA 159
Cdd:TIGR01394 75 ADFggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPSARPDEVVD-EVFDLFAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 160 HGYGGDSV--PVVRVSGLK---ALEGDPRwTASIEALLDAVDTYVPMPERYLDAPFLLSVENVLTITGRGTVVTGAVERG 234
Cdd:TIGR01394 147 LGADDEQLdfPIVYASGRAgwaSLDLDDP-SDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRG 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1752498825 235 TVRVGDKVEVLGADlETVVTG-----LETFG---RPMEEAQAGDNVAL 274
Cdd:TIGR01394 226 TVKKGQQVALMKRD-GTIENGrisklLGFEGlerVEIDEAGAGDIVAV 272
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
13-204 |
2.56e-27 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 106.97 E-value: 2.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 13 LNIGTMGHVDHGKTTLTAAITKVLAergtgtfvpfdriDRAPEEAARGITINI-------------------AHVEYETD 73
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWT-------------VRHKEELKRNITIKLgyanakiykcpncgcprpyDTPECECP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 74 T--------RHYAHVDMPGHADYVKNMVTGAAQLDGAILVVSALDGI-MPQTAEHVLLARQVGVDHIVVALNKADAGDEE 144
Cdd:cd01888 68 GcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCpQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 145 LTDLVELEVRDLLtaHGYGGDSVPVVRVSglkALEGdprwtASIEALLDAVDTYVPMPER 204
Cdd:cd01888 148 QALENYEQIKEFV--KGTIAENAPIIPIS---AQLK-----YNIDVLCEYIVKKIPTPPR 197
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-181 |
6.82e-27 |
|
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: 106.11 E-value: 6.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 17 TMGHVDHGKTTLTAAI---TKVLAE-----------RGTGtfvpFDRIDRA------PEEAARGITINIAHVEYETDTRH 76
Cdd:cd04166 4 TCGSVDDGKSTLIGRLlydSKSIFEdqlaalersksSGTQ----GEKLDLAllvdglQAEREQGITIDVAYRYFSTPKRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 77 YAHVDMPGHADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKADAGD--EELTDLVELEVR 154
Cdd:cd04166 80 FIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDydEEVFEEIKADYL 159
|
170 180
....*....|....*....|....*..
gi 1752498825 155 DLLTAHGyggdsVPVVRVSGLKALEGD 181
Cdd:cd04166 160 AFAASLG-----IEDITFIPISALEGD 181
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
10-306 |
1.23e-25 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 108.86 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 10 KPHLNIGTMGHVDHGKTTLT---------------AAITKVLAERGTGTfvpfDRIDRA------PEEAARGITINIAHV 68
Cdd:PRK05506 22 KSLLRFITCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVGTQG----DEIDLAllvdglAAEREQGITIDVAYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 69 EYETDTRHYAHVDMPGHADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVALNKAD--AGDEELT 146
Cdd:PRK05506 98 YFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDlvDYDQEVF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 147 DLVELEVRDLltAHGYGGDSVPVVRVSglkALEGDPRWTASIE-------ALLDAVDTyVPMPERYLDAPFLLSVENVL- 218
Cdd:PRK05506 178 DEIVADYRAF--AAKLGLHDVTFIPIS---ALKGDNVVTRSARmpwyegpSLLEHLET-VEIASDRNLKDFRFPVQYVNr 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 219 -TITGRGtvVTGAVERGTVRVGDKVEVLGADLETVVTGLETFGRPMEEAQAGDNVALLLrgvpRDA--VRRGHVVAAPGS 295
Cdd:PRK05506 252 pNLDFRG--FAGTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTL----ADEidISRGDMLARADN 325
|
330
....*....|..
gi 1752498825 296 VVP-SRRFTAQV 306
Cdd:PRK05506 326 RPEvADQFDATV 337
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-173 |
1.38e-25 |
|
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: 102.06 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLTAAITKVLAergTGTFvpfdriDRAPEEAARGITINIAHVEYETDTRHYAH-------------- 79
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIAS---TAAF------DKNPQSQERGITLDLGFSSFEVDKPKHLEdnenpqienyqitl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 80 VDMPGHADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDhIVVALNKADAGDEELTDLVELEVRDLL-- 157
Cdd:cd01889 73 VDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKP-LIVVLNKIDLIPEEERKRKIEKMKKRLqk 151
|
170
....*....|....*.
gi 1752498825 158 TAHGYGGDSVPVVRVS 173
Cdd:cd01889 152 TLEKTRLKDSPIIPVS 167
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
14-274 |
6.82e-25 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 106.26 E-value: 6.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLTAAITKvlaerGTGTF----VPFDRI-DRAPEEAARGITI---NIAhVEYEtDTRhyahVDMPGH 85
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLK-----QSGTFrenqEVAERVmDSNDLERERGITIlakNTA-VRYK-GVKin-iVDTPGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 86 ADY------VKNMVtgaaqlDGAILVVSALDGIMPQTaEHVL---LARqvGVDHIVVaLNKADAGDEELTDLVElEVRDL 156
Cdd:COG1217 80 ADFggeverVLSMV------DGVLLLVDAFEGPMPQT-RFVLkkaLEL--GLKPIVV-INKIDRPDARPDEVVD-EVFDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 157 ---LTAHgyggDS---VPVVRVSGL-----KALEGDprwTASIEALLDAVDTYVPMPERYLDAPFLLSVENV-----Lti 220
Cdd:COG1217 149 fieLGAT----DEqldFPVVYASARngwasLDLDDP---GEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLdysdyV-- 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752498825 221 tgrGTVVTGAVERGTVRVGDKVEVLGADLETV---VTGLETF---GR-PMEEAQAGDNVAL 274
Cdd:COG1217 220 ---GRIAIGRIFRGTIKKGQQVALIKRDGKVEkgkITKLFGFeglERvEVEEAEAGDIVAI 277
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
18-280 |
1.02e-24 |
|
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: 106.01 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 18 MGHVDHGKTTLTAAITKvlaergtgtfvpfdrIDRAPEEAArGITINIA--HVEYEtDTRHYAHVDMPGHADYVKNMVTG 95
Cdd:TIGR00487 93 MGHVDHGKTSLLDSIRK---------------TKVAQGEAG-GITQHIGayHVENE-DGKMITFLDTPGHEAFTSMRARG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 96 AAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDhIVVALNKADAGDEELtDLVELEVRDL-LTAHGYGGDSVpVVRVSg 174
Cdd:TIGR00487 156 AKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEANP-DRVKQELSEYgLVPEDWGGDTI-FVPVS- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 175 lkALEGDprwtaSIEALLDA------VDTYVPMPERYLDApfllSVENVLTITGRGTVVTGAVERGTVRVGDKVeVLGAD 248
Cdd:TIGR00487 232 --ALTGD-----GIDELLDMillqseVEELKANPNGQASG----VVIEAQLDKGRGPVATVLVQSGTLRVGDIV-VVGAA 299
|
250 260 270
....*....|....*....|....*....|...
gi 1752498825 249 LETVVTGLETFGRPMEEAQAGDNVALL-LRGVP 280
Cdd:TIGR00487 300 YGRVRAMIDENGKSVKEAGPSKPVEILgLSDVP 332
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
56-306 |
5.58e-24 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 103.07 E-value: 5.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 56 EAARGITINIAHVEYETDTRHYAHVDMPGHADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVAL 135
Cdd:PRK05124 88 EREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 136 NKAD--AGDEELTDLVELEVRDLltAHGYGGDsvPVVRVSGLKALEGDPRWTASI-------EALLDAVDTyVPMPERYL 206
Cdd:PRK05124 168 NKMDlvDYSEEVFERIREDYLTF--AEQLPGN--LDIRFVPLSALEGDNVVSQSEsmpwysgPTLLEVLET-VDIQRVVD 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 207 DAPFLLSVENVL--TITGRGtvVTGAVERGTVRVGDKVEVLGADLETVVTGLETFGRPMEEAQAGDNVALLLrgvpRDAV 284
Cdd:PRK05124 243 AQPFRFPVQYVNrpNLDFRG--YAGTLASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVL----EDEI 316
|
250 260
....*....|....*....|....*
gi 1752498825 285 --RRGHVVAAPGSVVP-SRRFTAQV 306
Cdd:PRK05124 317 diSRGDLLVAADEALQaVQHASADV 341
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-244 |
7.52e-24 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 102.39 E-value: 7.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 13 LNIGTMGHVDHGKTTLTAAITKVLAERgtgtfvpFDRidrapeEAARGITINIAHV---------------------EYE 71
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVVKALSGVKTVR-------FKR------EKVRNITIKLGYAnakiykcpkcprptcyqsygsSKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 72 TDT------------RHYAHVDMPGHADYVKNMVTGAAQLDGAILVVSALDGI-MPQTAEHVLLARQVGVDHIVVALNKA 138
Cdd:PTZ00327 102 DNPpcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCpQPQTSEHLAAVEIMKLKHIIILQNKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 139 DAGDEELTDLVELEVRDLLTahGYGGDSVPVVRVSG-LKalegdprwtASIEALLDAVDTYVPMPERYLDAPFLLSV--- 214
Cdd:PTZ00327 182 DLVKEAQAQDQYEEIRNFVK--GTIADNAPIIPISAqLK---------YNIDVVLEYICTQIPIPKRDLTSPPRMIVirs 250
|
250 260 270
....*....|....*....|....*....|....*..
gi 1752498825 215 -------ENVLTItgRGTVVTGAVERGTVRVGDKVEV 244
Cdd:PTZ00327 251 fdvnkpgEDIENL--KGGVAGGSILQGVLKVGDEIEI 285
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
18-176 |
1.69e-21 |
|
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: 90.22 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 18 MGHVDHGKTTLTAAItkvlaeRGTgtfvpfdriDRAPEEAaRGITINIA--HVEYETDTRHYAHVDMPGHADYvKNMVTG 95
Cdd:cd01887 6 MGHVDHGKTTLLDKI------RKT---------NVAAGEA-GGITQHIGayQVPIDVKIPGITFIDTPGHEAF-TNMRAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 96 AAQL-DGAILVVSALDGIMPQTAEHVLLARQVGVDhIVVALNKAD--AGDEELTDlvelEVRDLLTAHG-----YGGDsV 167
Cdd:cd01887 69 GASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDkpYGTEADPE----RVKNELSELGlvgeeWGGD-V 142
|
....*....
gi 1752498825 168 PVVRVSGLK 176
Cdd:cd01887 143 SIVPISAKT 151
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
298-386 |
2.84e-20 |
|
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: 84.59 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 298 PSRRFTAQVYVLSAREGGRTTAVSSGYRPQFYIRTADVVGDVDL-GEVAVARPGDTVVMTVELGREMPLEPGLGFAIREG 376
Cdd:cd03706 2 MHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLpEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLREG 81
|
90
....*....|
gi 1752498825 377 GRTVGAGTVT 386
Cdd:cd03706 82 GRTIGTGVVT 91
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
210-292 |
3.94e-19 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 81.03 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 210 FLLSVENVLTITGRGTVVTGAVERGTVRVGDKVEVLGADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHV 289
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
...
gi 1752498825 290 VAA 292
Cdd:cd03696 81 LSE 83
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
18-261 |
9.58e-19 |
|
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: 87.76 E-value: 9.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 18 MGHVDHGKTTLTAAI--TKVLA-ERGtgtfvpfdridrapeeaarGITINIA--HVeyETDTRHYAHVDMPGHADYVKNM 92
Cdd:COG0532 10 MGHVDHGKTSLLDAIrkTNVAAgEAG-------------------GITQHIGayQV--ETNGGKITFLDTPGHEAFTAMR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 93 VTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVdHIVVALNKAD--AGDEELtdlveleVRDLLTAHG-----YGGD 165
Cdd:COG0532 69 ARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGV-PIIVAINKIDkpGANPDR-------VKQELAEHGlvpeeWGGD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 166 sVPVVRVSGLKAlEGdprwtasIEALLDAVdtyvpmperyldapfLLSVEnVLTIT------------------GRGTVV 227
Cdd:COG0532 141 -TIFVPVSAKTG-EG-------IDELLEMI---------------LLQAE-VLELKanpdrpargtvieakldkGRGPVA 195
|
250 260 270
....*....|....*....|....*....|....
gi 1752498825 228 TGAVERGTVRVGDkvevlgadleTVVTGlETFGR 261
Cdd:COG0532 196 TVLVQNGTLKVGD----------IVVAG-TAYGR 218
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
1-125 |
1.91e-18 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 87.23 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 1 MSKTAYVRtkphlNIGTMGHVDHGKTTLT-----AA--ITKVLAerGTGTFVPFDridraPEEAARGITINIAHV----E 69
Cdd:PRK07560 14 MKNPEQIR-----NIGIIAHIDHGKTTLSdnllaGAgmISEELA--GEQLALDFD-----EEEQARGITIKAANVsmvhE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1752498825 70 YETDTRHYAHVDMPGHADYvKNMVTGAAQ-LDGAILVVSALDGIMPQTaEHVLlaRQ 125
Cdd:PRK07560 82 YEGKEYLINLIDTPGHVDF-GGDVTRAMRaVDGAIVVVDAVEGVMPQT-ETVL--RQ 134
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
6-240 |
3.63e-18 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 86.42 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 6 YVRTKPHLNIgtMGHVDHGKTTLTAAItkvlaeRGTGTfvpfdridrAPEEAArGITINIA----HVEYETDTRHYAHVD 81
Cdd:CHL00189 240 SINRPPIVTI--LGHVDHGKTTLLDKI------RKTQI---------AQKEAG-GITQKIGayevEFEYKDENQKIVFLD 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 82 MPGHADYvKNMVTGAAQL-DGAILVVSALDGIMPQTAEHVLLARQVGVDhIVVALNKADAGDEEL----TDLVELEvrdl 156
Cdd:CHL00189 302 TPGHEAF-SSMRSRGANVtDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANANTerikQQLAKYN---- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 157 LTAHGYGGDsVPVVRVSGLKAlegdprwtASIEALLDAVDTYVPMPERYLDAPFLLS---VENVLTITgRGTVVTGAVER 233
Cdd:CHL00189 376 LIPEKWGGD-TPMIPISASQG--------TNIDKLLETILLLAEIEDLKADPTQLAQgiiLEAHLDKT-KGPVATILVQN 445
|
....*..
gi 1752498825 234 GTVRVGD 240
Cdd:CHL00189 446 GTLHIGD 452
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
1-145 |
3.84e-18 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 86.49 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 1 MSKTAYVRtkphlNIGTMGHVDHGKTTLT-------AAITKVLAerGTGTFVPFDRidrapEEAARGITINIAHV----E 69
Cdd:TIGR00490 13 MWKPKFIR-----NIGIVAHIDHGKTTLSdnllagaGMISEELA--GQQLYLDFDE-----QEQERGITINAANVsmvhE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752498825 70 YETDTRHYAHVDMPGHADYVKNMVTGAAQLDGAILVVSALDGIMPQTaEHVLlaRQVGVDHI--VVALNKADAGDEEL 145
Cdd:TIGR00490 81 YEGNEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVL--RQALKENVkpVLFINKVDRLINEL 155
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
14-202 |
1.26e-17 |
|
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: 80.33 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLTAAITKvlaerGTGTF----VPFDRI-DRAPEEAARGITI---NIAhVEYEtDTRhYAHVDMPGH 85
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLK-----QSGTFreneEVGERVmDSNDLERERGITIlakNTA-ITYK-DTK-INIIDTPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 86 ADY------VKNMVtgaaqlDGAILVVSALDGIMPQTaEHVLL-ARQVGVDHIVVaLNKADAGDEELTDLVElEVRDLLT 158
Cdd:cd01891 76 ADFggeverVLSMV------DGVLLLVDASEGPMPQT-RFVLKkALEAGLKPIVV-INKIDRPDARPEEVVD-EVFDLFL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1752498825 159 AHGYGGD--SVPVVRVSGLK--ALEGDPRWTASIEALLDAVDTYVPMP 202
Cdd:cd01891 147 ELNATDEqlDFPIVYASAKNgwASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
14-160 |
2.20e-17 |
|
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: 80.74 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLTAAI---TKVLAERGT---GTfvpfDRIDRAPEEAARGITINIAHVEYETDTRHYAHVDMPGHAD 87
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytSGAIRELGSvdkGT----TRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMD 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752498825 88 YVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVaLNKADAGDEELTDLVElEVRDLLTAH 160
Cdd:cd04168 77 FIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIF-VNKIDRAGADLEKVYQ-EIKEKLSPD 147
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
14-274 |
8.90e-17 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 82.06 E-value: 8.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLtaaITKVLAERGTgtfvpFDR--------IDRAPEEAARGITINIAHVEYETDTRHYAHVDMPGH 85
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGT-----FDSraetqervMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 86 ADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVaLNKADAGDEElTDLVELEVRDLLTAHGYGGD 165
Cdd:PRK10218 79 ADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGAR-PDWVVDQVFDLFVNLDATDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 166 SV--PVVRVSGLKALEG--DPRWTASIEALLDAVDTYVPMPERYLDAPFLLSVENVLTITGRGTVVTGAVERGTVRVGDK 241
Cdd:PRK10218 157 QLdfPIVYASALNGIAGldHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1752498825 242 VEVLGADLET-------VVT--GLETFGRPMeeAQAGDNVAL 274
Cdd:PRK10218 237 VTIIDSEGKTrnakvgkVLGhlGLERIETDL--AEAGDIVAI 276
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
14-139 |
1.08e-16 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 78.04 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLT---AAITKVLAERGTGTfvpfDRI-DRAPEEAARGITI---NIA-HVEYETDTRHYAH-----V 80
Cdd:cd01885 2 NICIIAHVDHGKTTLSdslLASAGIISEKLAGK----ARYlDTREDEQERGITIkssAISlYFEYEEEKMDGNDylinlI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752498825 81 DMPGHADYVKNmVTGAAQL-DGAILVVSALDGIMPQTaEHVLlaRQVGVDHI--VVALNKAD 139
Cdd:cd01885 78 DSPGHVDFSSE-VTAALRLtDGALVVVDAVEGVCVQT-ETVL--RQALEERVkpVLVINKID 135
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
14-139 |
7.67e-15 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 76.24 E-value: 7.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLTAAI---TKVLAERGT---GTFVpfdrIDRAPEEAARGITIN--IAHVEYEtDTRHYAhVDMPGH 85
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERIlfyTGAIHRIGEvhdGNTV----MDWMPEEQERGITITsaATTCEWK-GHKINI-IDTPGH 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1752498825 86 ADYVKNMVTGAAQLDGAILVVSALDGIMPQTaEHVL-LARQVGVDHIVVaLNKAD 139
Cdd:COG0480 85 VDFTGEVERSLRVLDGAVVVFDAVAGVEPQT-ETVWrQADKYGVPRIVF-VNKMD 137
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
207-289 |
2.29e-14 |
|
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: 67.98 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 207 DAPFLLSVENVLTITGRGTVVTGAVERGTVRVGDKVEVLGADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRR 286
Cdd:cd03693 2 DKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIKR 81
|
...
gi 1752498825 287 GHV 289
Cdd:cd03693 82 GDV 84
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
18-140 |
2.48e-14 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 74.39 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 18 MGHVDHGKTTLTAAI---TKVLAERGT---GTFVpfdrIDRAPEEAARGITIN--IAHVEYEtDTRHYAhVDMPGHADYV 89
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfyTGAIHRIGEvedGTTT----MDFMPEERERGISITsaATTCEWK-GHKINL-IDTPGHVDFT 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1752498825 90 KNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVaLNKADA 140
Cdd:PRK12740 75 GEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIF-VNKMDR 124
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
14-202 |
3.93e-14 |
|
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: 69.87 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLTAAI---TKVLAERG-TGTFVpfDRIDRapeEAARGITI--NIAHVEYETDTRH---YAHVDMPG 84
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSEREmKEQVL--DSMDL---ERERGITIkaQAVRLFYKAKDGEeylLNLIDTPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 85 HADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVdHIVVALNKAD--AGDeelTDLVELEVRDLLtahgy 162
Cdd:cd01890 77 HVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNL-EIIPVINKIDlpAAD---PDRVKQEIEDVL----- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1752498825 163 GGDSVPVVRVSGlKALEGdprwtasIEALLDAVDTYVPMP 202
Cdd:cd01890 148 GLDASEAILVSA-KTGLG-------VEDLLEAIVERIPPP 179
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
14-150 |
5.95e-14 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 71.47 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLTAAI---TKVLAERGT---GTFVpfdrIDRAPEEAARGITIN--IAHVEYEtDTRHYAhVDMPGH 85
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALlyaTGAIDRLGRvedGNTV----SDYDPEEKKRKMSIEtsVAPLEWN-GHKINL-IDTPGY 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752498825 86 ADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVaLNKADAGDEELTDLVE 150
Cdd:cd04170 75 ADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIF-INKMDRARADFDKTLA 138
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
14-150 |
6.63e-14 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 73.06 E-value: 6.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLTAAI---TKVLAERGT---GTFVpfdrIDRAPEEAARGITINIAHVEYETDTRHYAHVDMPGHAD 87
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIlfyTGKIHKMGEvedGTTV----TDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHID 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752498825 88 YvKNMVTGA-AQLDGAILVVSALDGIMPQTAEHVLLARQVGVDHIVVaLNKADAGDEELTDLVE 150
Cdd:PRK13351 86 F-TGEVERSlRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIF-INKMDRVGADLFKVLE 147
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
224-291 |
3.16e-13 |
|
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: 64.21 E-value: 3.16e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752498825 224 GTVVTGAVERGTVRVGDKVEVLGAD-----LETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHVVA 291
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGtgkkkIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
210-291 |
1.08e-11 |
|
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: 60.36 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 210 FLLSVENVLTITGRGTVVTGAVERGTVRVGDKVEVLGADLETVVTGLETFGRPMEEAQAGDNVALLLRGVprDAVRRGHV 289
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGV--KDILTGDT 78
|
..
gi 1752498825 290 VA 291
Cdd:cd01342 79 LT 80
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-150 |
1.37e-11 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 66.23 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 1 MSKTAYVRtkphlNIGTMGHVDHGKTTLT-AAITK--VLAERGTGTfvpfDRI-DRAPEEAARGITINIA----HVEYET 72
Cdd:PTZ00416 13 MDNPDQIR-----NMSVIAHVDHGKSTLTdSLVCKagIISSKNAGD----ARFtDTRADEQERGITIKSTgislYYEHDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 73 DTRHYAH------VDMPGHADYvKNMVTGAAQL-DGAILVVSALDGIMPQTaEHVLlaRQVGVDHI--VVALNKADAGDE 143
Cdd:PTZ00416 84 EDGDDKQpflinlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVDRAIL 159
|
....*..
gi 1752498825 144 ELTDLVE 150
Cdd:PTZ00416 160 ELQLDPE 166
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-139 |
1.35e-10 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 63.20 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 1 MSKTAYVRtkphlNIGTMGHVDHGKTTLT---AAITKVLAERGTGTFvpfdRI-DRAPEEAARGITI------------- 63
Cdd:PLN00116 13 MDKKHNIR-----NMSVIAHVDHGKSTLTdslVAAAGIIAQEVAGDV----RMtDTRADEAERGITIkstgislyyemtd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 64 -NIAHVEYETDTRHYA--HVDMPGHADYvKNMVTGAAQL-DGAILVVSALDGIMPQTaEHVLlaRQVGVDHI--VVALNK 137
Cdd:PLN00116 84 eSLKDFKGERDGNEYLinLIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQALGERIrpVLTVNK 159
|
..
gi 1752498825 138 AD 139
Cdd:PLN00116 160 MD 161
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
223-289 |
3.04e-10 |
|
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: 55.95 E-value: 3.04e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752498825 223 RGTVVTGAVERGTVRVGDKVEVLGADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGHV 289
Cdd:cd04089 13 MGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGFV 79
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
214-291 |
3.42e-10 |
|
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: 56.15 E-value: 3.42e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752498825 214 VENVLTITGRgTVVTGAVERGTVRVGDKVEvlGADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRdaVRRGHVVA 291
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKVK--GDKGVALIRAIEREHRKVDFAVAGDEVALILEGKIK--VKEGDVLE 77
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
14-116 |
4.62e-10 |
|
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: 59.81 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLTAAI------TKVLAERGTGTFVpfdrIDRAPEEAARGITINIAHVEYETDTRHYAHVDMPGHAD 87
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyytgrIHKIGEVHGGGAT----MDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVD 76
|
90 100
....*....|....*....|....*....
gi 1752498825 88 YVKNMVTGAAQLDGAILVVSALDGIMPQT 116
Cdd:cd01886 77 FTIEVERSLRVLDGAVAVFDAVAGVQPQT 105
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
14-139 |
7.07e-10 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 58.43 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLT---AAITKVLAERGTGTFVPFDRIDRAPEEAARGITINIAHV-EYETDTRHYAHV----DMPGH 85
Cdd:cd04167 2 NVCIAGHLHHGKTSLLdmlIEQTHKRTPSVKLGWKPLRYTDTRKDEQERGISIKSNPIsLVLEDSKGKSYLiniiDTPGH 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1752498825 86 ADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEhvlLARQVGVD--HIVVALNKAD 139
Cdd:cd04167 82 VNFMDEVAAALRLCDGVVLVVDVVEGLTSVTER---LIRHAIQEglPMVLVINKID 134
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
209-292 |
1.41e-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: 54.44 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 209 PFLLSVENVLTITGRGTVVTGAVERGTVRVGDKVEVLGADLETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAVRRGH 288
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
....
gi 1752498825 289 VVAA 292
Cdd:cd16267 81 ILCD 84
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
210-292 |
1.81e-09 |
|
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: 54.15 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 210 FLLSVENVLTITGRGTVVTGAVERGTVRVGDKVeVLGAD-----LETVVTGLETFGRPMEEAQAGDNVALLLRGVPRDAV 284
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLGPDadgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79
|
....*...
gi 1752498825 285 RRGHVVAA 292
Cdd:cd03694 80 RKGMVLVS 87
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
18-265 |
1.87e-09 |
|
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: 59.44 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 18 MGHVDHGKTTLTAAI--TKVLAERGTG-------TFVPFDRIDRAPEEAARGITIniahveyETDTRHYAHVDMPGHADY 88
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIrgTAVVKKEAGGitqhigaSEVPTDVIEKICGDLLKSFKI-------KLKIPGLLFIDTPGHEAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 89 VKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDhIVVALNKAD-----------------------AGDEEL 145
Cdd:TIGR00491 83 TNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKIDripgwkshegypflesinkqeqrVRQNLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 146 TDLVELEVRdlLTAHGYGGD----------SVPVVRVSGLKAlEGDPRWTASIEALldavdtyvpmPERYLDAPFLLSVE 215
Cdd:TIGR00491 162 KQVYNLVIQ--LAEQGFNAErfdrirdftkTVAIIPVSAKTG-EGIPELLAILAGL----------AQNYLENKLKLAIE 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 216 N--------VLTITGRGTVVTGAVERGTVRVGDKVEVLGADlETVVTGLETF--GRPMEE 265
Cdd:TIGR00491 229 GpakgtileVKEEQGLGYTIDAVIYDGILRKGDIIVLAGID-DVIVTRVRAIlkPRPLQE 287
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
14-145 |
3.35e-09 |
|
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: 55.46 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 14 NIGTMGHVDHGKTTLTAAITKVlaergtgtfvpfdriDRAPEEAARGITINIA--HVEYETDTRHYAHVDMPGHADYVK- 90
Cdd:TIGR00231 3 KIVIVGHPNVGKSTLLNSLLGN---------------KGSITEYYPGTTRNYVttVIEEDGKTYKFNLLDTAGQEDYDAi 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752498825 91 -----NMVTGAAQ-LDGAILVVSALDGIMPQTAEHVLLARQvGVDhIVVALNKADAGDEEL 145
Cdd:TIGR00231 68 rrlyyPQVERSLRvFDIVILVLDVEEILEKQTKEIIHHADS-GVP-IILVGNKIDLKDADL 126
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
18-139 |
9.62e-09 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 57.11 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 18 MGHVDHGKTTLTAAI--TKVlAERGTG--------TFVPFDRIDRAPEEAARGITINIahveyetDTRHYAHVDMPGHAD 87
Cdd:PRK04004 12 LGHVDHGKTTLLDKIrgTAV-AAKEAGgitqhigaTEVPIDVIEKIAGPLKKPLPIKL-------KIPGLLFIDTPGHEA 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1752498825 88 YVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDhIVVALNKAD 139
Cdd:PRK04004 84 FTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTP-FVVAANKID 134
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
297-385 |
5.85e-08 |
|
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: 50.47 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 297 VPSRRFTAQVYVLsAREGGrttaVSSGYRPQFYIRTADV------------VGDVDLGEVAVARPGDTVVMTVELGREMP 364
Cdd:cd01513 1 QAVWKFDAKVIVL-EHPKP----IRPGYKPVMDVGTAHVpgriakllskedGKTKEKKPPDSLQPGENGTVEVELQKPVV 75
|
90 100
....*....|....*....|....*..
gi 1752498825 365 LE-----PGLG-FAIREGGRTVGAGTV 385
Cdd:cd01513 76 LErgkefPTLGrFALRDGGRTVGAGLI 102
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
18-173 |
9.73e-06 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 45.53 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 18 MGHVDHGKTTLTAAITK---VLAERGTGTFVPFDRIDRAPEEAARGITIniahveyetdtrhyahVDMPGHADYVKNMVT 94
Cdd:cd00882 3 VGRGGVGKSSLLNALLGgevGEVSDVPGTTRDPDVYVKELDKGKVKLVL----------------VDTPGLDEFGGLGRE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 95 GAA-----QLDGAILVVSALDGIMPQTAEHVLLARQVGVD-HIVVALNKADAGDEELTDLVELEVRDLLTAHgyggdsVP 168
Cdd:cd00882 67 ELArlllrGADLILLVVDSTDRESEEDAKLLILRRLRKEGiPIILVGNKIDLLEEREVEELLRLEELAKILG------VP 140
|
....*
gi 1752498825 169 VVRVS 173
Cdd:cd00882 141 VFEVS 145
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
229-276 |
1.55e-05 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 42.94 E-value: 1.55e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1752498825 229 GAVERGTVRVGDKVEVLGADLETVVTGLETFGRPMEEAQAGDNVALLL 276
Cdd:cd03695 20 GTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTL 67
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
209-291 |
1.31e-04 |
|
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: 40.18 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 209 PFLLSVENVLTiTGRGTVVTGAVERGTVRVGDKVEVLGADLETVVTGLETFGRP-MEEAQAGDNVALLLRGVPRDAVRRG 287
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEeTDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....
gi 1752498825 288 HVVA 291
Cdd:cd03698 80 DILS 83
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
224-274 |
2.25e-04 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 39.86 E-value: 2.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752498825 224 GTVVTGAVERGTVRVGDKVEVLGADLETV---VTGLETF---GR-PMEEAQAGDNVAL 274
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEkgrVTKLFGFeglERvEVEEAEAGDIVAI 72
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
296-386 |
2.40e-04 |
|
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.
Pssm-ID: 294008 [Multi-domain] Cd Length: 109 Bit Score: 40.22 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 296 VVPSRRFTAQVYVLSAreggrTTAVSSGYRPQFYIRTADVVG---------DVDLGEVAVARP-----GDTVVMTVELGR 361
Cdd:cd04093 2 VATTSKFEARIVTFDL-----QVPILKGTPVVLHRHSLSEPAtisklvstlDKSTGEVIKKKPrclgkNQSAVVEIELER 76
|
90 100 110
....*....|....*....|....*....|.
gi 1752498825 362 EMPLEP-----GLG-FAIREGGRTVGAGTVT 386
Cdd:cd04093 77 PIPLETfkdnkELGrFVLRRGGETIAAGIVT 107
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
13-180 |
4.48e-04 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 40.61 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 13 LNIGTMGHVDHGKTTLTAAI--TKVLAERGTGTfvpfdridrapeeaargiTINIAHVEYETDtRHYAHVDMPG------ 84
Cdd:cd09912 1 FLLAVVGEFSAGKSTLLNALlgEEVLPTGVTPT------------------TAVITVLRYGLL-KGVVLVDTPGlnstie 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 85 -HADYVKNMVtgaAQLDGAILVVSAlDGIMPQTAEHVL-LARQVGVDHIVVALNKADAGDEELTDLVELEVRDLLTAHGY 162
Cdd:cd09912 62 hHTEITESFL---PRADAVIFVLSA-DQPLTESEREFLkEILKWSGKKIFFVLNKIDLLSEEELEEVLEYSREELGVLEL 137
|
170
....*....|....*...
gi 1752498825 163 GGDSVPVVRVSGLKALEG 180
Cdd:cd09912 138 GGGEPRIFPVSAKEALEA 155
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
302-385 |
2.10e-03 |
|
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to ribosomes. EF-1 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 model represents the alpha subunit, which is the counterpart of bacterial EF-Tu for archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha).
Pssm-ID: 294004 [Multi-domain] Cd Length: 104 Bit Score: 37.17 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 302 FTAQVYVLSareggRTTAVSSGYRPQFYIRTADV-------VGDVD--LGEVAVARP-----GDTVVMTVELGREMPLE- 366
Cdd:cd03705 6 FTAQVIILN-----HPGQIKAGYTPVLDCHTAHVackfaelKEKIDrrTGKKLEENPkflksGDAAIVKMVPTKPLCVEt 80
|
90 100
....*....|....*....|....
gi 1752498825 367 ----PGLG-FAIREGGRTVGAGTV 385
Cdd:cd03705 81 fseyPPLGrFAVRDMRQTVAVGVI 104
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
80-139 |
3.30e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 39.87 E-value: 3.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 80 VDMPGHADYVKNMVTGAAQLDGAILVVSALDGIMPQTAEHVLLARQVGVDhIVVALNKAD 139
Cdd:PRK14845 531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTP-FVVAANKID 589
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
20-116 |
3.41e-03 |
|
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: 38.73 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 20 HVDHGKTTLTAAI---TKVLAE------RGTGTFVPFDRIDRapeEAARGITINIAHVEYETDTRHYAHVDMPGHADYVK 90
Cdd:cd04169 10 HPDAGKTTLTEKLllfGGAIQEagavkaRKSRKHATSDWMEI---EKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSE 86
|
90 100
....*....|....*....|....*...
gi 1752498825 91 NM--VTGAAqlDGAILVVSALDGIMPQT 116
Cdd:cd04169 87 DTyrTLTAV--DSAVMVIDAAKGVEPQT 112
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
297-386 |
4.91e-03 |
|
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: 35.96 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 297 VPSRRFTAQVYVLSareggRTTAVSSGYRPQFY---IRTADVVGDVDlgeVAVARPGDTVVMTVE-LGREMPLEPGLGFA 372
Cdd:cd03708 1 RACWEFEAEVLVLH-----HPTTISPGYQPVVHcgtIRQTARIISID---KEVLRTGDRALVRFRfLYRPEYLREGQRLI 72
|
90
....*....|....
gi 1752498825 373 IREgGRTVGAGTVT 386
Cdd:cd03708 73 FRE-GRTKGIGTVT 85
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
299-386 |
7.32e-03 |
|
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. 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: 294003 [Multi-domain] Cd Length: 108 Bit Score: 35.99 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498825 299 SRRFTAQVYVLsarEGGRTTaVSSGYRPQFYIRTA--DVV------------GDVDLGEVAVARPGDTVVMTVELGREMP 364
Cdd:cd03704 3 VTEFEAQIVIL---DLLKSI-ITAGYSAVLHIHTAveEVTitkllatidkktGKKKKKKPKFVKSGQVVIARLETARPIC 78
|
90 100
....*....|....*....|....*...
gi 1752498825 365 LE-----PGLG-FAIREGGRTVGAGTVT 386
Cdd:cd03704 79 LEtfkdfPQLGrFTLRDEGKTIAIGKVL 106
|
|
| |
