|
Name |
Accession |
Description |
Interval |
E-value |
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
9-438 |
0e+00 |
|
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: 813.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 9 SQDILAYLKQHEQKDLLRFLTCGNVDDGKSTLIGRLLYDSKLIYEDQLQAVTRDSKKVGTtgDAPDLALLVDGLQAEREQ 88
Cdd:COG2895 2 STDIEAYLAQHENKDLLRFITCGSVDDGKSTLIGRLLYDTKSIFEDQLAALERDSKKRGT--QEIDLALLTDGLQAEREQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 89 GITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMD 168
Cdd:COG2895 80 GITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 169 LVEYSPERFTEIQIEYDAFVSQLGDrrpANIQFVPISALNGDNVVNPSAHTPWYKGQTLMSILESVEISRESNKHEFRFP 248
Cdd:COG2895 160 LVDYSEEVFEEIVADYRAFAAKLGL---EDITFIPISALKGDNVVERSENMPWYDGPTLLEHLETVEVAEDRNDAPFRFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 249 VQYVNRPNLDFRGFAGTVALGEINVGDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLNDEIDISRGNVLVRAGE 328
Cdd:COG2895 237 VQYVNRPNLDFRGYAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLEDEIDISRGDVIVAADA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 329 QPLISRSVRASVVWMNEHPLVKGKLYNVKIGTQTVPAKVTNIHYRVNVNTLEHTHVEELELNAIADVVVEFDAPVVFDQY 408
Cdd:COG2895 317 PPEVADQFEATLVWMDEEPLLPGRKYLLKHGTRTVRATVTAIKYRIDVNTLEHEAADSLELNDIGRVTLRLAEPIAFDPY 396
|
410 420 430
....*....|....*....|....*....|
gi 491212272 409 QDSRYTGSFIFIDRLSNVTVGAGMVEAAVE 438
Cdd:COG2895 397 ADNRATGSFILIDRLTNATVGAGMIRGALR 426
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
1-471 |
0e+00 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 797.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 1 MSHQSELISQDILAYLKQHEQKDLLRFLTCGNVDDGKSTLIGRLLYDSKLIYEDQLQAVTRDSKKVGTTGDAPDLALLVD 80
Cdd:PRK05506 1 MSHQSDLIAEDILAYLAQHERKSLLRFITCGSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGTQGDEIDLALLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 81 GLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNI 160
Cdd:PRK05506 81 GLAAEREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 161 VVAINKMDLVEYSPERFTEIQIEYDAFVSQLGdrrPANIQFVPISALNGDNVVNPSAHTPWYKGQTLMSILESVEISRES 240
Cdd:PRK05506 161 VLAVNKMDLVDYDQEVFDEIVADYRAFAAKLG---LHDVTFIPISALKGDNVVTRSARMPWYEGPSLLEHLETVEIASDR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 241 NKHEFRFPVQYVNRPNLDFRGFAGTVALGEINVGDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLNDEIDISRG 320
Cdd:PRK05506 238 NLKDFRFPVQYVNRPNLDFRGFAGTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLADEIDISRG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 321 NVLVRAGEQPLISRSVRASVVWMNEHPLVKGKLYNVKIGTQTVPAKVTNIHYRVNVNTLEHTHVEELELNAIADVVVEFD 400
Cdd:PRK05506 318 DMLARADNRPEVADQFDATVVWMAEEPLLPGRPYLLKHGTRTVPASVAAIKYRVDVNTLERLAAKTLELNEIGRCNLSTD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 401 APVVFDQYQDSRYTGSFIFIDRLSNVTVGAGMVEAA------VEWtaHSNPVTAEDRAARLGQKPAVI---GIS------ 465
Cdd:PRK05506 398 APIAFDPYARNRTTGSFILIDRLTNATVGAGMIDFAlrratnVHW--QASDVSREARAARKGQKPATVwftGLSgsgkst 475
|
....*..
gi 491212272 466 -AQLIEK 471
Cdd:PRK05506 476 iANLVER 482
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
1-438 |
0e+00 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 794.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 1 MSHQSELISQDILAYLKQHEQKDLLRFLTCGNVDDGKSTLIGRLLYDSKLIYEDQLQAVTRDSKKVGTTGDAPDLALLVD 80
Cdd:PRK05124 4 AIAQQIANEGGVEAYLHAQQHKSLLRFLTCGSVDDGKSTLIGRLLHDTKQIYEDQLASLHNDSKRHGTQGEKLDLALLVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 81 GLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNI 160
Cdd:PRK05124 84 GLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 161 VVAINKMDLVEYSPERFTEIQIEYDAFVSQLGDRRpaNIQFVPISALNGDNVVNPSAHTPWYKGQTLMSILESVEISRES 240
Cdd:PRK05124 164 VVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNL--DIRFVPLSALEGDNVVSQSESMPWYSGPTLLEVLETVDIQRVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 241 NKHEFRFPVQYVNRPNLDFRGFAGTVALGEINVGDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLNDEIDISRG 320
Cdd:PRK05124 242 DAQPFRFPVQYVNRPNLDFRGYAGTLASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDEIDISRG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 321 NVLVRAGEQPLISRSVRASVVWMNEHPLVKGKLYNVKIGTQTVPAKVTNIHYRVNVNTLEHTHVEELELNAIADVVVEFD 400
Cdd:PRK05124 322 DLLVAADEALQAVQHASADVVWMAEQPLQPGQSYDIKIAGKKTRARVDAIRYQVDINTLTQREAENLPLNGIGLVELTFD 401
|
410 420 430
....*....|....*....|....*....|....*...
gi 491212272 401 APVVFDQYQDSRYTGSFIFIDRLSNVTVGAGMVEAAVE 438
Cdd:PRK05124 402 EPLVLDPYQQNRVTGGFIFIDRLTNVTVGAGMVREPLA 439
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
25-433 |
0e+00 |
|
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 213679 [Multi-domain] Cd Length: 406 Bit Score: 679.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 25 LRFLTCGNVDDGKSTLIGRLLYDSKLIYEDQLQAVTRDSKKVGTTGDAPDLALLVDGLQAEREQGITIDVAYRYFSTEKR 104
Cdd:TIGR02034 1 LRFLTCGSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTQGGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 105 KFIIADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEYSPERFTEIQIEY 184
Cdd:TIGR02034 81 KFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 185 DAFVSQLGDRrpaNIQFVPISALNGDNVVNPSAHTPWYKGQTLMSILESVEISRESNKHEFRFPVQYVNRPNLDFRGFAG 264
Cdd:TIGR02034 161 LAFAEQLGFR---DVTFIPLSALKGDNVVSRSESMPWYSGPTLLEILETVEVERDAQDLPLRFPVQYVNRPNLDFRGYAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 265 TVALGEINVGDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLNDEIDISRGNVLVRAGEQPLISRSVRASVVWMN 344
Cdd:TIGR02034 238 TIASGSVHVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEIDISRGDLLAAADSAPEVADQFAATLVWMA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 345 EHPLVKGKLYNVKIGTQTVPAKVTNIHYRVNVNTLEHTHVEELELNAIADVVVEFDAPVVFDQYQDSRYTGSFIFIDRLS 424
Cdd:TIGR02034 318 EEPLLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGAAKSLELNEIGRVNLSLDEPIAFDPYAENRTTGAFILIDRLS 397
|
....*....
gi 491212272 425 NVTVGAGMV 433
Cdd:TIGR02034 398 NRTVGAGMI 406
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
26-238 |
4.28e-142 |
|
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: 408.11 E-value: 4.28e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 26 RFLTCGNVDDGKSTLIGRLLYDSKLIYEDQLQAVTRdSKKVGTTGDAPDLALLVDGLQAEREQGITIDVAYRYFSTEKRK 105
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAALER-SKSSGTQGEKLDLALLVDGLQAEREQGITIDVAYRYFSTPKRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 106 FIIADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEYSPERFTEIQIEYD 185
Cdd:cd04166 80 FIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491212272 186 AFVSQLGDRrpaNIQFVPISALNGDNVVNPSAHTPWYKGQTLMSILESVEISR 238
Cdd:cd04166 160 AFAASLGIE---DITFIPISALEGDNVVSRSENMPWYKGPTLLEHLETVEIAS 209
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
31-433 |
1.14e-86 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 274.12 E-value: 1.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 31 GNVDDGKSTLIGRLLYDSKLIYEDQLQAVTRDSKKVGTTGDApdLALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIAD 110
Cdd:COG5256 14 GHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFK--FAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIID 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 111 TPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEYSPERFTEIQIEYDAFVSQ 190
Cdd:COG5256 92 APGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 191 LGdRRPANIQFVPISALNGDNVVNPSAHTPWYKGQTLMSILESVEISRESNKHEFRFPVQYVnrpnLDFRGfAGTVALGE 270
Cdd:COG5256 172 VG-YKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQDV----YSISG-IGTVPVGR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 271 I-----NVGDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLN--DEIDISRGNVLVRAGEQPLISRSVRASVVWM 343
Cdd:COG5256 246 VetgvlKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRgvEKNDIKRGDVAGHPDNPPTVAEEFTAQIVVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 344 NeHPLVKGKLYN--VKIGTQTVPAKVTNIHYRVNVNTleHTHVEE----LELNAIADVVVEFDAPVVFDQYQDSRYTGSF 417
Cdd:COG5256 326 Q-HPSAITVGYTpvFHVHTAQVACTFVELVSKLDPRT--GQVKEEnpqfLKTGDAAIVKIKPTKPLVIEKFKEFPQLGRF 402
|
410
....*....|....*.
gi 491212272 418 IFIDrlSNVTVGAGMV 433
Cdd:COG5256 403 AIRD--MGQTVAAGVV 416
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
31-433 |
1.30e-83 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 266.02 E-value: 1.30e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 31 GNVDDGKSTLIGRLLYDSKLIYEDQLQAVTRDSKKVGTTGDApdLALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIAD 110
Cdd:PRK12317 13 GHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFK--FAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 111 TPGHEQYTRNMATGASTADLAIILIDAR--YGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEYSPERFTEIQIEYDAFV 188
Cdd:PRK12317 91 CPGHRDFVKNMITGASQADAAVLVVAADdaGGVMPQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEVSKLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 189 SQLGdRRPANIQFVPISALNGDNVVNPSAHTPWYKGQTLMSILESVEISRESNKHEFRFPVQYVnrpnLDFRGfAGTVAL 268
Cdd:PRK12317 171 KMVG-YKPDDIPFIPVSAFEGDNVVKKSENMPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQDV----YSISG-VGTVPV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 269 GEI-----NVGDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLN--DEIDISRGNVLVRAGEQPLISRSVRASVV 341
Cdd:PRK12317 245 GRVetgvlKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRgvGKKDIKRGDVCGHPDNPPTVAEEFTAQIV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 342 WMNeHPLVKGKLYN--VKIGTQTVPAKVTNIHYRVNVNTLEhtHVEE----LELNAIADVVVEFDAPVVFDQYQDSRYTG 415
Cdd:PRK12317 325 VLQ-HPSAITVGYTpvFHAHTAQVACTFEELVKKLDPRTGQ--VAEEnpqfIKTGDAAIVKIKPTKPLVIEKVKEIPQLG 401
|
410
....*....|....*...
gi 491212272 416 SFIFIDrlSNVTVGAGMV 433
Cdd:PRK12317 402 RFAIRD--MGQTIAAGMV 417
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
30-236 |
1.79e-69 |
|
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: 222.37 E-value: 1.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 30 CGNVDDGKSTLIGRLLYDSKLIYEDQLQAVTRDSKKVGTTGDApdLALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIA 109
Cdd:cd01883 5 IGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFK--YAWVLDKLKEERERGVTIDVGLAKFETEKYRFTII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 110 DTPGHEQYTRNMATGASTADLAIILIDAR-------YGVQTQTRRHTFIASLLGIKNIVVAINKMDLVE--YSPERFTEI 180
Cdd:cd01883 83 DAPGHRDFVKNMITGASQADVAVLVVSARkgefeagFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTvnWSQERYDEI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491212272 181 QIEYDAFVSQLGdRRPANIQFVPISALNGDNVVNPSAHTPWYKGQTLMSILESVEI 236
Cdd:cd01883 163 KKKVSPFLKKVG-YNPKDVPFIPISGFTGDNLIEKSENMPWYKGPTLLEALDSLEP 217
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
31-347 |
3.81e-63 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 213.07 E-value: 3.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 31 GNVDDGKSTLIGRLLY-----DSKLI--YEDQLQAVTRDSKKvgttgdapdLALLVDGLQAEREQGITIDVAYRYFSTEK 103
Cdd:PTZ00141 14 GHVDSGKSTTTGHLIYkcggiDKRTIekFEKEAAEMGKGSFK---------YAWVLDKLKAERERGITIDIALWKFETPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 104 RKFIIADTPGHEQYTRNMATGASTADLAIILIDARYGV-------QTQTRRHTFIASLLGIKNIVVAINKMDL--VEYSP 174
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEfeagiskDGQTREHALLAFTLGVKQMIVCINKMDDktVNYSQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 175 ERFTEIQIEYDAFVSQLGdRRPANIQFVPISALNGDNVVNPSAHTPWYKGQTLMSILESVEISRESNKHEFRFPVQYVNR 254
Cdd:PTZ00141 165 ERYDEIKKEVSAYLKKVG-YNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQDVYK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 255 -------PnldfrgfAGTVALGEINVGDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTL-NDEI-DISRGNVLVR 325
Cdd:PTZ00141 244 iggigtvP-------VGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVkNVSVkDIKRGYVASD 316
|
330 340
....*....|....*....|...
gi 491212272 326 AGEQPLI-SRSVRASVVWMNeHP 347
Cdd:PTZ00141 317 SKNDPAKeCADFTAQVIVLN-HP 338
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
22-212 |
1.81e-54 |
|
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: 181.95 E-value: 1.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 22 KDLLRFLTCGNVDDGKSTLIGRLLYDSKLIYEDQLqavtrdskkvgttgDAPDLALLVDGLQAEREQGITIDVAYRYFST 101
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGE--------------VKGEGEAGLDNLPEERERGITIKSAAVSFET 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 102 EKRKFIIADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKnIVVAINKMDLVEYspERFTEIQ 181
Cdd:pfam00009 67 KDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDG--AELEEVV 143
|
170 180 190
....*....|....*....|....*....|..
gi 491212272 182 IE-YDAFVSQLGDrRPANIQFVPISALNGDNV 212
Cdd:pfam00009 144 EEvSRELLEKYGE-DGEFVPVVPGSALKGEGV 174
|
|
| CysN_NoDQ_III |
cd04095 |
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of ... |
332-433 |
6.58e-48 |
|
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and is homologous to domain III of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD and CysN. 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: 294010 [Multi-domain] Cd Length: 103 Bit Score: 161.45 E-value: 6.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 332 ISRSVRASVVWMNEHPLVKGKLYNVKIGTQTVPAKVTNIHYRVNVNTLEHTHVEELELNAIADVVVEFDAPVVFDQYQDS 411
Cdd:cd04095 2 VSDQFEATLVWMDEKPLQPGRRYLLKHGTRTVRARVTEIDYRIDVNTLEREPADTLALNDIGRVTLRLAEPLAFDPYAEN 81
|
90 100
....*....|....*....|..
gi 491212272 412 RYTGSFIFIDRLSNVTVGAGMV 433
Cdd:cd04095 82 RATGSFILIDRLTNATVAAGMI 103
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
26-212 |
9.63e-47 |
|
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: 161.31 E-value: 9.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 26 RFLTCGNVDDGKSTLIGRLLYDSKLIYEDQLQAVTrdskkvgttgdapdlalLVDGLQAEREQGITIDVAYRYFSTEKRK 105
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKET-----------------FLDTLKEERERGITIKTGVVEFEWPKRR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 106 FIIADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKnIVVAINKMDLVeySPERFTEIQIEYD 185
Cdd:cd00881 64 INFIDTPGHEDFSKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLP-IIVAVNKIDRV--GEEDFDEVLREIK 140
|
170 180
....*....|....*....|....*....
gi 491212272 186 AFVSQLG--DRRPANIQFVPISALNGDNV 212
Cdd:cd00881 141 ELLKLIGftFLKGKDVPIIPISALTGEGI 169
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
245-325 |
5.40e-44 |
|
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: 150.41 E-value: 5.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 245 FRFPVQYVNRPNLDFRGFAGTVALGEINVGDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLNDEIDISRGNVLV 324
Cdd:cd03695 1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLEDEIDVSRGDLIV 80
|
.
gi 491212272 325 R 325
Cdd:cd03695 81 R 81
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
20-347 |
1.93e-43 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 160.26 E-value: 1.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 20 EQKDLLRFLTCGNVDDGKSTLIGRLLY-----DSKLI--YEDQLQAVTRDSKKvgttgdapdLALLVDGLQAEREQGITI 92
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIYklggiDKRVIerFEKEAAEMNKRSFK---------YAWVLDKLKAERERGITI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 93 DVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTADLAIILIDARYG-------VQTQTRRHTFIASLLGIKNIVVAIN 165
Cdd:PLN00043 74 DIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVKQMICCCN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 166 KMDLV--EYSPERFTEIQIEYDAFVSQLGdRRPANIQFVPISALNGDNVVNPSAHTPWYKGQTLMSILESVEISRESNKH 243
Cdd:PLN00043 154 KMDATtpKYSKARYDEIVKEVSSYLKKVG-YNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 244 EFRFPVQYVNRPnldfrGFAGTVALGEINV-----GDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLNDEI--D 316
Cdd:PLN00043 233 PLRLPLQDVYKI-----GGIGTVPVGRVETgvikpGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAvkD 307
|
330 340 350
....*....|....*....|....*....|.
gi 491212272 317 ISRGNVLVRAGEQPLISRSVRASVVWMNEHP 347
Cdd:PLN00043 308 LKRGYVASNSKDDPAKEAANFTSQVIIMNHP 338
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
27-370 |
2.85e-35 |
|
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: 139.62 E-value: 2.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 27 FLTCGNVDDGKSTLIGRLlydskliyedqlqavtrdskkvgtTGDApdlallVDGLQAEREQGITIDVAYRYFSTEKRKF 106
Cdd:TIGR00475 3 IATAGHVDHGKTTLLKAL------------------------TGIA------ADRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 107 IIADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEysPERFTEIQIEYDA 186
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVN--EEEIKRTEMFMKQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 187 FVSQLGDRRPANIqfVPISALNGDNVVNPSAHtpwykgqtLMSILESVEISREsnKHEFRFPVQYVnrpnLDFRGFA--- 263
Cdd:TIGR00475 131 ILNSYIFLKNAKI--FKTSAKTGQGIGELKKE--------LKNLLESLDIKRI--QKPLRMAIDRA----FKVKGAGtvv 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 264 -GTVALGEINVGDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLN--DEIDISRGnVLVRAGEQPlisrSVRASV 340
Cdd:TIGR00475 195 tGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMdvEPESLKRG-LLILTPEDP----KLRVVV 269
|
330 340 350
....*....|....*....|....*....|
gi 491212272 341 VWMNEHPLVKGKLYNVKIGTQTVPAKVTNI 370
Cdd:TIGR00475 270 KFIAEVPLLELQPYHIAHGMSVTTGKISLL 299
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
29-367 |
1.54e-33 |
|
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: 134.66 E-value: 1.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 29 TCGNVDDGKSTLIGRLlydskliyedqlqavtrdskkvgtTGDAPDlallvdGLQAEREQGITIDVAYRYFSTEKRKFI- 107
Cdd:COG3276 5 TAGHIDHGKTTLVKAL------------------------TGIDTD------RLKEEKKRGITIDLGFAYLPLPDGRRLg 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 108 IADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEysPERFTEIQIEYDAF 187
Cdd:COG3276 55 FVDVPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVD--EEWLELVEEEIREL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 188 VSQLGdrrPANIQFVPISALNG---DNVVnpsahtpwykgQTLMSILESVEISRESNKheFRFPVQYVnrpnldF--RGF 262
Cdd:COG3276 133 LAGTF---LEDAPIVPVSAVTGegiDELR-----------AALDALAAAVPARDADGP--FRLPIDRV------FsiKGF 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 263 A----GTVALGEINVGDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLN--DEIDISRGNVLVRAGEQPLISR-S 335
Cdd:COG3276 191 GtvvtGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAgvEKEEIERGDVLAAPGALRPTDRiD 270
|
330 340 350
....*....|....*....|....*....|..
gi 491212272 336 VRASVVWMNEHPLVKGKLYNVKIGTQTVPAKV 367
Cdd:COG3276 271 VRLRLLPSAPRPLKHWQRVHLHHGTAEVLARV 302
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
29-327 |
8.07e-27 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 112.35 E-value: 8.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 29 TCGNVDDGKSTLIGrllydskliyedqlqAVTRD-SKKVGTTGDAPDLallVDGLQAEREQGITIDVAYRYFSTEKRKFI 107
Cdd:PRK12736 17 TIGHVDHGKTTLTA---------------AITKVlAERGLNQAKDYDS---IDAAPEEKERGITINTAHVEYETEKRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 108 IADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEySPERFTEIQIEYDAF 187
Cdd:PRK12736 79 HVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVD-DEELLELVEMEVREL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 188 VSQL---GDrrpaNIQFVPIS---ALNGDNvvnpsahtPWYKG-QTLMSILESV--EISRESNKhEFRFPVQYVnrpnLD 258
Cdd:PRK12736 158 LSEYdfpGD----DIPVIRGSalkALEGDP--------KWEDAiMELMDAVDEYipTPERDTDK-PFLMPVEDV----FT 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491212272 259 FRGfAGTVAL-----GEINVGD--EIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLN--DEIDISRGNVLVRAG 327
Cdd:PRK12736 221 ITG-RGTVVTgrverGTVKVGDevEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRgvDRDEVERGQVLAKPG 297
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
29-327 |
3.00e-26 |
|
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: 110.64 E-value: 3.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 29 TCGNVDDGKSTLIGrllydskliyedqlqAVTRD-SKKVGTTGDAPDLallVDGLQAEREQGITIDVAYRYFSTEKRKFI 107
Cdd:TIGR00485 17 TIGHVDHGKTTLTA---------------AITTVlAKEGGAAARAYDQ---IDNAPEEKARGITINTAHVEYETETRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 108 IADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEySPERFTEIQIEYDAF 187
Cdd:TIGR00485 79 HVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVD-DEELLELVEMEVREL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 188 VSQL---GDRRPAnIQFVPISALNGDNVVNPSAHtpwykgqTLMSILESV--EISRESNKhEFRFPVQYVNrpNLDFRG- 261
Cdd:TIGR00485 158 LSQYdfpGDDTPI-IRGSALKALEGDAEWEAKIL-------ELMDAVDEYipTPEREIDK-PFLLPIEDVF--SITGRGt 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491212272 262 -FAGTVALGEINVGDE--IVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLN--DEIDISRGNVLVRAG 327
Cdd:TIGR00485 227 vVTGRVERGIIKVGEEveIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRgiKREEIERGMVLAKPG 297
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
29-438 |
7.16e-26 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 110.86 E-value: 7.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 29 TCGNVDDGKSTLIGrllydskliyedqlqAVTRDSKKVGttGDAPDLALLVDGLQAEREQGITIDVAYRYFSTEKRKFII 108
Cdd:PLN03126 86 TIGHVDHGKTTLTA---------------ALTMALASMG--GSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 109 ADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEySPERFTEIQIEYDAFV 188
Cdd:PLN03126 149 VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVD-DEELLELVELEVRELL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 189 SqlgdrrpaNIQFvpisalNGDNVvnpsahtPWYKGQTLMSI---LESVEISRESNK-----HEFRFPV-QYVNRP---- 255
Cdd:PLN03126 228 S--------SYEF------PGDDI-------PIISGSALLALealMENPNIKRGDNKwvdkiYELMDAVdSYIPIPqrqt 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 256 NLDF------------RGFAGT--VALGEINVGD--EIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLN--DEIDI 317
Cdd:PLN03126 287 DLPFllavedvfsitgRGTVATgrVERGTVKVGEtvDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRgiQKADI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 318 SRGNVLVRAGE-QPLISRSVRASVVWMNE----HPLVKGKLYNVKIGTQTVPAKVTNIhyrvnvntlEHTHVEELELNAI 392
Cdd:PLN03126 367 QRGMVLAKPGSiTPHTKFEAIVYVLKKEEggrhSPFFAGYRPQFYMRTTDVTGKVTSI---------MNDKDEESKMVMP 437
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 491212272 393 AD---VVVEFDAPVVFDQyqdsrytgSFIFIDRLSNVTVGAGMVEAAVE 438
Cdd:PLN03126 438 GDrvkMVVELIVPVACEQ--------GMRFAIREGGKTVGAGVIQSIIE 478
|
|
| tufA |
CHL00071 |
elongation factor Tu |
29-327 |
7.61e-26 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 109.66 E-value: 7.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 29 TCGNVDDGKSTLIGRLLYdskliyedqlqAVTRDSKKVGTTGDAPDLALlvdglqAEREQGITIDVAYRYFSTEKRKFII 108
Cdd:CHL00071 17 TIGHVDHGKTTLTAAITM-----------TLAAKGGAKAKKYDEIDSAP------EEKARGITINTAHVEYETENRHYAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 109 ADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEySPERFTEIQIEYDAFV 188
Cdd:CHL00071 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVD-DEELLELVELEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 189 SQL---GDrrpaNIQFVPISALNGDNVV--NPS---AHTPWY-KGQTLMSILESV--EISRESNKHeFRFPVQYV----N 253
Cdd:CHL00071 159 SKYdfpGD----DIPIVSGSALLALEALteNPKikrGENKWVdKIYNLMDAVDSYipTPERDTDKP-FLMAIEDVfsitG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 254 RpnldfrgfaGTVALGEI-----NVGD--EIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLN--DEIDISRGNVLV 324
Cdd:CHL00071 234 R---------GTVATGRIergtvKVGDtvEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRgiQKEDIERGMVLA 304
|
...
gi 491212272 325 RAG 327
Cdd:CHL00071 305 KPG 307
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
29-212 |
3.36e-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 bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 101.91 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 29 TCGNVDDGKSTLIGRLlydskliyedqlqavtrdskkvgtTGDAPDlallvdGLQAEREQGITIDVAYRYF--STEKRKF 106
Cdd:cd04171 4 TAGHIDHGKTTLIKAL------------------------TGIETD------RLPEEKKRGITIDLGFAYLdlPDGKRLG 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 107 IIaDTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEysPERFTEIQIEYDA 186
Cdd:cd04171 54 FI-DVPGHEKFVKNMLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVD--EDRLELVEEEILE 130
|
170 180
....*....|....*....|....*.
gi 491212272 187 FVSQLGDrrpANIQFVPISALNGDNV 212
Cdd:cd04171 131 LLAGTFL---ADAPIFPVSSVTGEGI 153
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
29-327 |
7.61e-25 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 107.22 E-value: 7.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 29 TCGNVDDGKSTLIgrllydskliyedqlQAVTrdsKKVGTTGDAPDLAL-LVDGLQAEREQGITIDVAYRYFSTEKRKFI 107
Cdd:PLN03127 66 TIGHVDHGKTTLT---------------AAIT---KVLAEEGKAKAVAFdEIDKAPEEKARGITIATAHVEYETAKRHYA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 108 IADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEySPE--RFTEIQI-EY 184
Cdd:PLN03127 128 HVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVD-DEEllELVEMELrEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 185 DAFVSQLGDRRPAnIQFVPISALNGDNvvnpsahtPWYKGQTLMSILESV-----EISRESNKhEFRFPVQYVNrpNLDF 259
Cdd:PLN03127 207 LSFYKFPGDEIPI-IRGSALSALQGTN--------DEIGKNAILKLMDAVdeyipEPVRVLDK-PFLMPIEDVF--SIQG 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491212272 260 RG--FAGTVALGEINVGD--EIVALPSG--KRSTVKEIVTFDGNLEQAVAGQAVTLTLN--DEIDISRGNVLVRAG 327
Cdd:PLN03127 275 RGtvATGRVEQGTIKVGEevEIVGLRPGgpLKTTVTGVEMFKKILDQGQAGDNVGLLLRglKREDVQRGQVICKPG 350
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
29-327 |
9.94e-24 |
|
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: 103.31 E-value: 9.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 29 TCGNVDDGKSTLIGrllydskliyedqlqAVTRD-SKKVGTTGDAPDLallVDGLQAEREQGITIDVAYRYFSTEKRKFI 107
Cdd:COG0050 17 TIGHVDHGKTTLTA---------------AITKVlAKKGGAKAKAYDQ---IDKAPEEKERGITINTSHVEYETEKRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 108 IADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEySPE--RFTEIQI--- 182
Cdd:COG0050 79 HVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVD-DEEllELVEMEVrel 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 183 --EYDaFvsqLGDrrpaNIQFVPIS---ALNGDnvvnpsAHTPWYKG-QTLMSILESV--EISRESNKhEFRFPVQYVnr 254
Cdd:COG0050 158 lsKYG-F---PGD----DTPIIRGSalkALEGD------PDPEWEKKiLELMDAVDSYipEPERDTDK-PFLMPVEDV-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 255 pnldfrgFA----GTVAL-----GEINVGD--EIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLN--DEIDISRGN 321
Cdd:COG0050 221 -------FSitgrGTVVTgrverGIIKVGDevEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRgiKREDVERGQ 293
|
....*.
gi 491212272 322 VLVRAG 327
Cdd:COG0050 294 VLAKPG 299
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
29-327 |
2.23e-23 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 102.19 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 29 TCGNVDDGKSTLIGrllydskliyedqlqAVTRD-SKKVGTTGDAPDLallVDGLQAEREQGITIDVAYRYFSTEKRKFI 107
Cdd:PRK00049 17 TIGHVDHGKTTLTA---------------AITKVlAKKGGAEAKAYDQ---IDKAPEEKARGITINTAHVEYETEKRHYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 108 IADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEySPE--RFTEIQI--- 182
Cdd:PRK00049 79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVD-DEEllELVEMEVrel 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 183 --EYDaFvsqLGDrrpaNIQFVPISALNGdnvVNPSAHTPWYKG-QTLMSILESV--EISRESNKhEFRFPVQYVnrpnl 257
Cdd:PRK00049 158 lsKYD-F---PGD----DTPIIRGSALKA---LEGDDDEEWEKKiLELMDAVDSYipTPERAIDK-PFLMPIEDV----- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 258 dfrgFA----GTVALGEI-----NVGD--EIValpsGKRSTVKEIVT----FDGNLEQAVAGQAVTLTLN--DEIDISRG 320
Cdd:PRK00049 221 ----FSisgrGTVVTGRVergiiKVGEevEIV----GIRDTQKTTVTgvemFRKLLDEGQAGDNVGALLRgiKREDVERG 292
|
....*..
gi 491212272 321 NVLVRAG 327
Cdd:PRK00049 293 QVLAKPG 299
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
29-327 |
1.03e-22 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 100.30 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 29 TCGNVDDGKSTLIGrllydskliyedqlqAVTRDSKKVGTtGDAPDLALlVDGLQAEREQGITIDVAYRYFSTEKRKFII 108
Cdd:PRK12735 17 TIGHVDHGKTTLTA---------------AITKVLAKKGG-GEAKAYDQ-IDNAPEEKARGITINTSHVEYETANRHYAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 109 ADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEySPERFTEIQIEYDAFV 188
Cdd:PRK12735 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVD-DEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 189 SQL---GDRRPAnIQFVPISALNGDnvvnpsahTPWYKGQTLMSILESV-----EISRESNKhEFRFPVQYVnrpnldfr 260
Cdd:PRK12735 159 SKYdfpGDDTPI-IRGSALKALEGD--------DDEEWEAKILELMDAVdsyipEPERAIDK-PFLMPIEDV-------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 261 gFA----GTVALGEI-----NVGD--EIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLN--DEIDISRGNVLVRAG 327
Cdd:PRK12735 221 -FSisgrGTVVTGRVergivKVGDevEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRgtKREDVERGQVLAKPG 299
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
29-171 |
8.49e-22 |
|
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: 93.03 E-value: 8.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 29 TCGNVDDGKSTL---IGRLLYDSKLiyedqlqavtRDSKKVGTTGDAPDlallvdglqaEREQGITIDVAYRYFSTEKRK 105
Cdd:cd01884 7 TIGHVDHGKTTLtaaITKVLAKKGG----------AKAKKYDEIDKAPE----------EKARGITINTAHVEYETANRH 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491212272 106 FIIADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVE 171
Cdd:cd01884 67 YAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVD 132
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
27-348 |
7.02e-17 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 83.95 E-value: 7.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 27 FLTCGNVDDGKSTLigrllydskliyedqLQAVTrdskKVGTtgdapdlallvDGLQAEREQGITIDVAYRYFSTEKRK- 105
Cdd:PRK10512 3 IATAGHVDHGKTTL---------------LQAIT----GVNA-----------DRLPEEKKRGMTIDLGYAYWPQPDGRv 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 106 --FIiaDTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVAINKMDLVEysPERFTEIQIE 183
Cdd:PRK10512 53 lgFI--DVPGHEKFLSNMLAGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVD--EARIAEVRRQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 184 YDAfvsQLGDRRPANIQFVPISALNGDNVVNPSAHtpwykgqtlmsiLESVEISRESNKHEFRFPVQyvnrpnldfRGF- 262
Cdd:PRK10512 129 VKA---VLREYGFAEAKLFVTAATEGRGIDALREH------------LLQLPEREHAAQHRFRLAID---------RAFt 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 263 ---AGTV----AL-GEINVGDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLNDEI---DISRGNVLVragEQPL 331
Cdd:PRK10512 185 vkgAGLVvtgtALsGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAGDAekeQINRGDWLL---ADAP 261
|
330
....*....|....*..
gi 491212272 332 ISRSVRASVVWMNEHPL 348
Cdd:PRK10512 262 PEPFTRVIVELQTHTPL 278
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
106-212 |
9.16e-16 |
|
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: 75.20 E-value: 9.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 106 FIiaDTPGHEQYTrNM-ATGASTADLAIILIDARYGVQTQTrrhtfIASLLGIKN----IVVAINKMDL---VEYSPERF 177
Cdd:cd01887 53 FI--DTPGHEAFT-NMrARGASVTDIAILVVAADDGVMPQT-----IEAINHAKAanvpIIVAINKIDKpygTEADPERV 124
|
90 100 110
....*....|....*....|....*....|....*
gi 491212272 178 TEIQIEYDAFVSQLGdrrpANIQFVPISALNGDNV 212
Cdd:cd01887 125 KNELSELGLVGEEWG----GDVSIVPISAKTGEGI 155
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
85-369 |
2.37e-14 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 74.89 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 85 EREQGITIDVAY--------------RYFSTEK------------RKFIIADTPGHEQYTRNMATGASTADLAIILIDAR 138
Cdd:PRK04000 40 ELKRGITIRLGYadatirkcpdceepEAYTTEPkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAAN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 139 YGV-QTQTRRHTFIASLLGIKNIVVAINKMDLV--EYSPERFTEIQieydAFVSqlgDRRPANIQFVPISALNGDNVvnp 215
Cdd:PRK04000 120 EPCpQPQTKEHLMALDIIGIKNIVIVQNKIDLVskERALENYEQIK----EFVK---GTVAENAPIIPVSALHKVNI--- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 216 sahtpwykgQTLMSILESvEI---SRESNKHefrfPVQY------VNRPNL---DFRG--FAGTVALGEINVGDEIVALP 281
Cdd:PRK04000 190 ---------DALIEAIEE-EIptpERDLDKP----PRMYvarsfdVNKPGTppeKLKGgvIGGSLIQGVLKVGDEIEIRP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 282 ------SGK------RSTVKEIVTFDGNLEQAVAGQAV--------TLTLNDEIdisRGNVLVRAGEQPLISRSVRA--- 338
Cdd:PRK04000 256 gikveeGGKtkwepiTTKIVSLRAGGEKVEEARPGGLVgvgtkldpSLTKADAL---AGSVAGKPGTLPPVWESLTIevh 332
|
330 340 350
....*....|....*....|....*....|....*...
gi 491212272 339 ---SVVWMNEH----PLVKGKLYNVKIGTQTVPAKVTN 369
Cdd:PRK04000 333 lleRVVGTKEElkvePIKTGEPLMLNVGTATTVGVVTS 370
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
33-183 |
1.11e-13 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 69.48 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 33 VDDGKSTLIGRLLYDSKLIYEDQLQAVTRDSkkvgttgdapdlallvdgLQAEREQGITID---VAYRYFSTEKRKFII- 108
Cdd:cd01890 9 IDHGKSTLADRLLELTGTVSEREMKEQVLDS------------------MDLERERGITIKaqaVRLFYKAKDGEEYLLn 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491212272 109 -ADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKnIVVAINKMDLVEYSPERfTEIQIE 183
Cdd:cd01890 71 lIDTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLE-IIPVINKIDLPAADPDR-VKQEIE 144
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
80-209 |
1.72e-13 |
|
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: 68.93 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 80 DGLQAEREQGITIDVAYRYFSTEKRK--------------FIIADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQT 145
Cdd:cd01889 30 DKNPQSQERGITLDLGFSSFEVDKPKhlednenpqienyqITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQT 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491212272 146 RRHTFIASLLGIKnIVVAINKMDLVEYSpERFTEIQIEYDAFVSQLGDRRPANIQFVPISALNG 209
Cdd:cd01889 110 AECLVIGELLCKP-LIVVLNKIDLIPEE-ERKRKIEKMKKRLQKTLEKTRLKDSPIIPVSAKPG 171
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
89-212 |
3.13e-13 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 72.56 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 89 GIT-----IDVAYRYFStEKRKFIIADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTrrhtfIASLLGIKN---- 159
Cdd:CHL00189 276 GITqkigaYEVEFEYKD-ENQKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQT-----IEAINYIQAanvp 349
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 491212272 160 IVVAINKMDLVEYSPERFTEIQIEYDAFVSQLGdrrpANIQFVPISALNGDNV 212
Cdd:CHL00189 350 IIVAINKIDKANANTERIKQQLAKYNLIPEKWG----GDTPMIPISASQGTNI 398
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
89-212 |
1.01e-12 |
|
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: 70.57 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 89 GITIDVAYRYFSTEKRKFII-ADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKnIVVAINKM 167
Cdd:TIGR00487 119 GITQHIGAYHVENEDGKMITfLDTPGHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKI 197
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 491212272 168 DLVEYSPERFTEIQIEYDAFVSQLGdrrpANIQFVPISALNGDNV 212
Cdd:TIGR00487 198 DKPEANPDRVKQELSEYGLVPEDWG----GDTIFVPVSALTGDGI 238
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
245-324 |
3.32e-12 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 62.28 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 245 FRFPVQYVNRPNLDFRGFAGTVALGEINVGDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLNDEIDISRGNVLV 324
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGVKDILTGDTLT 80
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
104-212 |
4.32e-12 |
|
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: 64.98 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 104 RKFIIADTPGHEQYTRNMATGASTADLAIILIDARYGV-QTQTRRHTFIASLLGIKNIVVAINKMDLVeySPERFTEIQI 182
Cdd:cd01888 77 RHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCpQPQTSEHLAALEIMGLKHIIILQNKIDLV--KEEQALENYE 154
|
90 100 110
....*....|....*....|....*....|.
gi 491212272 183 EYDAFV-SQLGDRRPaniqFVPISALNGDNV 212
Cdd:cd01888 155 QIKEFVkGTIAENAP----IIPISAQLKYNI 181
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
332-433 |
5.86e-12 |
|
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: 62.03 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 332 ISRSVRASVVWMN-EHPLVKGKLYNVKIGTQTVPAKVTNIHYRVNVNTLEHTHVEELELNAIADVVVEFDAPVVFDQYQD 410
Cdd:cd01513 2 AVWKFDAKVIVLEhPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEKKPPDSLQPGENGTVEVELQKPVVLERGKE 81
|
90 100
....*....|....*....|...
gi 491212272 411 SRYTGSFIFIDRlsNVTVGAGMV 433
Cdd:cd01513 82 FPTLGRFALRDG--GRTVGAGLI 102
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
33-181 |
2.45e-11 |
|
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: 63.79 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 33 VDDGKSTLIGRLLYDSKLIyeDQLQAVTRdskkvGTTgdapdlalLVDGLQAEREQGITIDVAYRYFSTEKRKFIIADTP 112
Cdd:cd04168 8 VDAGKTTLTESLLYTSGAI--RELGSVDK-----GTT--------RTDSMELERQRGITIFSAVASFQWEDTKVNIIDTP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491212272 113 GHEQYTRNMATGASTADLAIILIDARYGVQTQTRrhtFIASLLGIKNI--VVAINKMDLVEYSPER-FTEIQ 181
Cdd:cd04168 73 GHMDFIAEVERSLSVLDGAILVISAVEGVQAQTR---ILFRLLRKLNIptIIFVNKIDRAGADLEKvYQEIK 141
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
89-212 |
1.55e-10 |
|
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: 63.49 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 89 GIT--IDvAYRyFSTEKRK--FIiaDTPGHEQYTrNM-ATGASTADLAIILIDARYGVQTQTR---RHtfiASLLGIKnI 160
Cdd:COG0532 36 GITqhIG-AYQ-VETNGGKitFL--DTPGHEAFT-AMrARGAQVTDIVILVVAADDGVMPQTIeaiNH---AKAAGVP-I 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 491212272 161 VVAINKMDLVEYSPERFTEIQIEYDAFVSQLGdrrpANIQFVPISALNGDNV 212
Cdd:COG0532 107 IVAINKIDKPGANPDRVKQELAEHGLVPEEWG----GDTIFVPVSAKTGEGI 154
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
30-212 |
1.78e-10 |
|
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: 59.78 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 30 CGNVDDGKSTLIGRLLYDSkliyedqlqaVTRDSKKVGTTgdapdlallvdglqaereqgITIDVAYRYFSTEKRKFIIA 109
Cdd:cd00882 3 VGRGGVGKSSLLNALLGGE----------VGEVSDVPGTT--------------------RDPDVYVKELDKGKVKLVLV 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 110 DTPGHEQYTRNMATG-----ASTADLAIILIDARYGVQTQTRRHTFIASLLGI-KNIVVAINKMDLVEYSPERFTEIQIE 183
Cdd:cd00882 53 DTPGLDEFGGLGREElarllLRGADLILLVVDSTDRESEEDAKLLILRRLRKEgIPIILVGNKIDLLEEREVEELLRLEE 132
|
170 180
....*....|....*....|....*....
gi 491212272 184 ydafvsqlgDRRPANIQFVPISALNGDNV 212
Cdd:cd00882 133 ---------LAKILGVPVFEVSAKTGEGV 152
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
101-370 |
1.93e-10 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 63.10 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 101 TEKRKFIIADTPGHEQYTRNMATGASTADLAIILIDARYGV-QTQTRRHTFIASLLGIKNIVVAINKMDLV--EYSPERF 177
Cdd:PTZ00327 114 TLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCpQPQTSEHLAAVEIMKLKHIIILQNKIDLVkeAQAQDQY 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 178 TEIQieydAFVS-QLGDRRPaniqFVPISALNGDNVvnpsahtpwykGQTLMSILESVEISRESNKHEFRFPVQY---VN 253
Cdd:PTZ00327 194 EEIR----NFVKgTIADNAP----IIPISAQLKYNI-----------DVVLEYICTQIPIPKRDLTSPPRMIVIRsfdVN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 254 RPNLD---FRG--FAGTVALGEINVGDEIVALP-------SGK------RSTVKEIVTFDGNLEQAVAGQAV-------- 307
Cdd:PTZ00327 255 KPGEDienLKGgvAGGSILQGVLKVGDEIEIRPgiiskdsGGEftcrpiRTRIVSLFAENNELQYAVPGGLIgvgttidp 334
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491212272 308 TLTLNDEIdisRGNVLVRAGEQPLISRSVRASVVWMNE---------------HPLVKGKLYNVKIGTQTVPAKVTNI 370
Cdd:PTZ00327 335 TLTRADRL---VGQVLGYPGKLPEVYAEIEIQYYLLRRllgvksqdgkkatkvAKLKKGESLMINIGSTTTGGRVVGI 409
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
32-212 |
2.92e-10 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 59.37 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 32 NVddGKSTLIGRLLYDSKLIYEDQlqavtrdskkVGTTGDApdlallvdglqaereqgitIDVAYRYfstEKRKFIIADT 111
Cdd:cd01895 12 NV--GKSSLLNALLGEERVIVSDI----------AGTTRDS-------------------IDVPFEY---DGQKYTLIDT 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 112 PG----------HEQYTRNMATGA-STADLAIILIDARYGVQTQTRRhtfIASLL---GiKNIVVAINKMDLVEYSPERF 177
Cdd:cd01895 58 AGirkkgkvtegIEKYSVLRTLKAiERADVVLLVLDASEGITEQDLR---IAGLIleeG-KALIIVVNKWDLVEKDEKTM 133
|
170 180 190
....*....|....*....|....*....|....*
gi 491212272 178 TEIQIEYDAFVSQLGDrrpanIQFVPISALNGDNV 212
Cdd:cd01895 134 KEFEKELRRKLPFLDY-----APIVFISALTGQGV 163
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
34-168 |
3.06e-10 |
|
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: 61.07 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 34 DDGKSTLIGRLLYDSKLIYEDQlqAVT-RDSKKVGTTgdapdlallvDGLQAEREQGITIDVAYRYFSTEKRKFIIADTP 112
Cdd:cd04169 12 DAGKTTLTEKLLLFGGAIQEAG--AVKaRKSRKHATS----------DWMEIEKQRGISVTSSVMQFEYKGCVINLLDTP 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 491212272 113 GHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKnIVVAINKMD 168
Cdd:cd04169 80 GHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLD 134
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
33-168 |
3.30e-10 |
|
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: 59.53 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 33 VDDGKSTLIGRLLYDSKLIYEDQLQAVtrdskkvgttgdapdlaLLVDGLQAEREQGITI---DVAYRYFSTekrKFIIA 109
Cdd:cd01891 11 VDHGKTTLVDALLKQSGTFRENEEVGE-----------------RVMDSNDLERERGITIlakNTAITYKDT---KINII 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491212272 110 DTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRrhtFI---ASLLGIKNIVVaINKMD 168
Cdd:cd01891 71 DTPGHADFGGEVERVLSMVDGVLLLVDASEGPMPQTR---FVlkkALEAGLKPIVV-INKID 128
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
31-239 |
5.40e-10 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 61.89 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 31 GNVDDGKSTLIGRLLYDSKliyedqlqavtrdskKVGTTGDAPDLALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIAD 110
Cdd:PRK13351 15 AHIDAGKTTLTERILFYTG---------------KIHKMGEVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 111 TPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKnIVVAINKMDLVEysperfteiqIEYDAFVSQ 190
Cdd:PRK13351 80 TPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIP-RLIFINKMDRVG----------ADLFKVLED 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491212272 191 LGDR---RPANIQfVPISALNG-----DNVVNPSAH-------TPWYKGQTLMSILESVEISRE 239
Cdd:PRK13351 149 IEERfgkRPLPLQ-LPIGSEDGfegvvDLITEPELHfsegdggSTVEEGPIPEELLEEVEEARE 211
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
264-323 |
8.06e-10 |
|
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: 55.23 E-value: 8.06e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491212272 264 GTVALGEINVGDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQ--AVTLTLNDEIDISRGNVL 323
Cdd:cd03696 20 GTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDrvALNLTGVDAKELERGFVL 81
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
32-212 |
1.03e-09 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 57.47 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 32 NVddGKSTLIGRLLyDSKLiyedqlqAVTrdSKKVGTTGDapdlallvdglqaeREQGItidvayryFSTEKRKFIIADT 111
Cdd:cd04163 13 NV--GKSTLLNALV-GQKI-------SIV--SPKPQTTRN--------------RIRGI--------YTDDDAQIIFVDT 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 112 PG-HEQYTR------NMATGAST-ADLAIILIDARYGVqtqTRRHTFIASLLG--IKNIVVAINKMDLVEYSPERFTEIQ 181
Cdd:cd04163 59 PGiHKPKKKlgermvKAAWSALKdVDLVLFVVDASEWI---GEGDEFILELLKksKTPVILVLNKIDLVKDKEDLLPLLE 135
|
170 180 190
....*....|....*....|....*....|.
gi 491212272 182 IEYDAFVsqlgdrrPANIqfVPISALNGDNV 212
Cdd:cd04163 136 KLKELHP-------FAEI--FPISALKGENV 157
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
32-212 |
1.49e-09 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 59.29 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 32 NVddGKSTLIGRLLyDSKLiyedqlqAVTrdSKKVGTTGDapdlallvdglqaeREQGItidvayryFSTEKRKFIIADT 111
Cdd:PRK00089 15 NV--GKSTLLNALV-GQKI-------SIV--SPKPQTTRH--------------RIRGI--------VTEDDAQIIFVDT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 112 PG-HEQYTR------NMATGA-STADLAIILIDARYGVQTQTRrhtFIASLL--GIKNIVVAINKMDLVEYSPERFTEIQ 181
Cdd:PRK00089 61 PGiHKPKRAlnramnKAAWSSlKDVDLVLFVVDADEKIGPGDE---FILEKLkkVKTPVILVLNKIDLVKDKEELLPLLE 137
|
170 180 190
....*....|....*....|....*....|.
gi 491212272 182 ieydaFVSQLGDrrPANIqfVPISALNGDNV 212
Cdd:PRK00089 138 -----ELSELMD--FAEI--VPISALKGDNV 159
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
31-212 |
9.52e-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: 54.69 E-value: 9.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 31 GNVDDGKSTLIGRLLYDSKLIYEDQLQaVTRDskkvgttgdapdlallvDGLQAEREQGITIdvayryfstekrKFIIAD 110
Cdd:TIGR00231 8 GHPNVGKSTLLNSLLGNKGSITEYYPG-TTRN-----------------YVTTVIEEDGKTY------------KFNLLD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 111 TPGHE-------QYTRNMATGASTADLAIILIDARYGVQTQTRrhTFIASLLGIKNIVVAINKMDLVeysperfteiQIE 183
Cdd:TIGR00231 58 TAGQEdydairrLYYPQVERSLRVFDIVILVLDVEEILEKQTK--EIIHHADSGVPIILVGNKIDLK----------DAD 125
|
170 180
....*....|....*....|....*....
gi 491212272 184 YDAFVSQLGDRRPANIqFVPISALNGDNV 212
Cdd:TIGR00231 126 LKTHVASEFAKLNGEP-IIPLSAETGKNI 153
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
31-318 |
1.15e-08 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 57.80 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 31 GNVDDGKSTLIGRLLYdskliyedqlQAVTRDSKkvgttgdAPDLALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIAD 110
Cdd:PRK10218 12 AHVDHGKTTLVDKLLQ----------QSGTFDSR-------AETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 111 TPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVaINKMDLVEYSPERFTEiQIeYDAFVSQ 190
Cdd:PRK10218 75 TPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVD-QV-FDLFVNL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 191 LGDRRPANIQFVPISALNG----DNVVNPSAHTPWYkgQTLMSILESVEISRESnkhefrfPVQyVNRPNLDFRGFAGTV 266
Cdd:PRK10218 152 DATDEQLDFPIVYASALNGiaglDHEDMAEDMTPLY--QAIVDHVPAPDVDLDG-------PFQ-MQISQLDYNSYVGVI 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491212272 267 ALGEINVG-----DEIVALPSGKRS---TVKEIVTFDG----NLEQAVAGQAVTLTLNDEIDIS 318
Cdd:PRK10218 222 GIGRIKRGkvkpnQQVTIIDSEGKTrnaKVGKVLGHLGleriETDLAEAGDIVAITGLGELNIS 285
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
32-212 |
1.71e-08 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 56.96 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 32 NVddGKSTLIGRLLYDSKLIYEDQlqAvtrdskkvGTTGDApdlallvdglqaereqgitIDVAYRYfstEKRKFIIADT 111
Cdd:COG1160 185 NV--GKSSLINALLGEERVIVSDI--A--------GTTRDS-------------------IDTPFER---DGKKYTLIDT 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 112 PG----------HEQYTRNMATGA-STADLAIILIDARYGVQTQTRRhtfIASLLgIKN---IVVAINKMDLVEysperf 177
Cdd:COG1160 231 AGirrkgkvdegIEKYSVLRTLRAiERADVVLLVIDATEGITEQDLK---IAGLA-LEAgkaLVIVVNKWDLVE------ 300
|
170 180 190
....*....|....*....|....*....|....*...
gi 491212272 178 tEIQIEYDAFVSQLgDRRPANIQFVP---ISALNGDNV 212
Cdd:COG1160 301 -KDRKTREELEKEI-RRRLPFLDYAPivfISALTGQGV 336
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
33-234 |
2.30e-08 |
|
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: 54.54 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 33 VDDGKSTLIGRLLYDSKLIyedqlqavtrdSKKVGTTgdapdlALLVDGLQAEREQGITIDVA-------YRYFSTEKRK 105
Cdd:cd01885 9 VDHGKTTLSDSLLASAGII-----------SEKLAGK------ARYLDTREDEQERGITIKSSaislyfeYEEEKMDGND 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 106 FII--ADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTR---RHTFIAsllGIKNIVVaINKMDLV----EYSPE- 175
Cdd:cd01885 72 YLInlIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTEtvlRQALEE---RVKPVLV-INKIDRLilelKLSPEe 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491212272 176 ---RFTEIQIEYDAFVSQL--GDRRPANIQFVPIsalNGdNVVNPSAHTPW----YKGQTLMSILESV 234
Cdd:cd01885 148 ayqRLLRIVEDVNAIIETYapEEFKQEKWKFSPQ---KG-NVAFGSALDGWgftiIKFADIYAVLEMV 211
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
31-214 |
2.43e-08 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 53.40 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 31 GNVddGKSTLIGRLLydskliyedqlqavtrdSKKVGTTGDAPdlallvdglqaereqGITID-VAYRYFSTEKRKFIIA 109
Cdd:cd00880 6 PNV--GKSSLLNALL-----------------GQNVGIVSPIP---------------GTTRDpVRKEWELLPLGPVVLI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 110 DTPG-----HEQYTRNMAT--GASTADLAIILIDARygvQTQTRRHTFIASLLGIKN-IVVAINKMDLVEYSPERFTEIQ 181
Cdd:cd00880 52 DTPGldeegGLGRERVEEArqVADRADLVLLVVDSD---LTPVEEEAKLGLLRERGKpVLLVLNKIDLVPESEEEELLRE 128
|
170 180 190
....*....|....*....|....*....|...
gi 491212272 182 IEYDAFvsqlgdrrpANIQFVPISALNGDNVVN 214
Cdd:cd00880 129 RKLELL---------PDLPVIAVSALPGEGIDE 152
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
31-168 |
2.74e-08 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 56.67 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 31 GNVDDGKSTLIGRLLYDSKLIyeDQLQAVTRDSkkvgTTGDAPDLallvdglqaEREQGITIDVAYRYFSTEKRKFIIAD 110
Cdd:PRK12740 2 GHSGAGKTTLTEAILFYTGAI--HRIGEVEDGT----TTMDFMPE---------ERERGISITSAATTCEWKGHKINLID 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 491212272 111 TPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVaINKMD 168
Cdd:PRK12740 67 TPGHVDFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIF-VNKMD 123
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
245-323 |
2.87e-08 |
|
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: 50.97 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 245 FRFPVQYVNRPNLDfrGF--AGTVALGEINVGDEIVALPSGKRSTVKEIVTFDGNLEQAVAGQAVTLTLN--DEIDISRG 320
Cdd:cd16267 2 FRLSVSDVFKGQGS--GFtvSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTgiDPNHLRVG 79
|
...
gi 491212272 321 NVL 323
Cdd:cd16267 80 SIL 82
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
30-168 |
3.50e-08 |
|
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: 56.21 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 30 CGNVDDGKSTLIGRLLYDSKLIYedqlqavtrdskKVG------TTGDAPDLallvdglqaEREQGITIDVAYRYFSTEK 103
Cdd:COG0480 15 VAHIDAGKTTLTERILFYTGAIH------------RIGevhdgnTVMDWMPE---------EQERGITITSAATTCEWKG 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491212272 104 RKFIIADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVaINKMD 168
Cdd:COG0480 74 HKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVF-VNKMD 137
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
33-318 |
4.07e-08 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 55.80 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 33 VDDGKSTLIGRLLYDSKLIYEDQlQAVTR--DSKkvgttgdapDLallvdglqaEREQGITI---DVAYRYFSTekrKFI 107
Cdd:COG1217 15 VDHGKTTLVDALLKQSGTFRENQ-EVAERvmDSN---------DL---------ERERGITIlakNTAVRYKGV---KIN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 108 IADTPGH-------EqytRNMatgaSTADLAIILIDARYGVQTQTRrhtFI---ASLLGIKNIVVaINKMDlveySPE-R 176
Cdd:COG1217 73 IVDTPGHadfggevE---RVL----SMVDGVLLLVDAFEGPMPQTR---FVlkkALELGLKPIVV-INKID----RPDaR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 177 FTEIQIE-YDAFVSqLGdrrpAN---IQFvPI---SALNGDNVVNPSAhtpwyKGQTLMSILESVeisresnkhefrfpV 249
Cdd:COG1217 138 PDEVVDEvFDLFIE-LG----ATdeqLDF-PVvyaSARNGWASLDLDD-----PGEDLTPLFDTI--------------L 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 250 QYVNRP-------------NLDFRGFAGTVAL-----GEINVGDEIVAL-PSGKRSTVK--EIVTFDG----NLEQAVAG 304
Cdd:COG1217 193 EHVPAPevdpdgplqmlvtNLDYSDYVGRIAIgrifrGTIKKGQQVALIkRDGKVEKGKitKLFGFEGlervEVEEAEAG 272
|
330
....*....|....
gi 491212272 305 QAVTLTLNDEIDIS 318
Cdd:COG1217 273 DIVAIAGIEDINIG 286
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
33-206 |
4.55e-08 |
|
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: 54.42 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 33 VDDGKSTLIGRLLYDSKLIyedqlqavtrdsKKVGTT--GDApdlalLVDGLQAEREQGITIDVAYRYFSTEKRKFIIAD 110
Cdd:cd01886 8 IDAGKTTTTERILYYTGRI------------HKIGEVhgGGA-----TMDWMEQERERGITIQSAATTCFWKDHRINIID 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 111 TPGHEQYT----RNMAtgasTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVaINKMDLVEYSPERFTEiQIEyda 186
Cdd:cd01886 71 TPGHVDFTieveRSLR----VLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAF-VNKMDRTGADFYRVVE-QIR--- 141
|
170 180
....*....|....*....|
gi 491212272 187 fvSQLGdRRPANIQfVPISA 206
Cdd:cd01886 142 --EKLG-ANPVPLQ-LPIGA 157
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
32-212 |
5.91e-08 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 54.22 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 32 NVddGKSTLIGRLLyDSKLiyedqlqAVTrdSKKVGTTGDapdlallvdglqaeREQGItidvayryFSTEKRKFIIADT 111
Cdd:COG1159 13 NV--GKSTLLNALV-GQKV-------SIV--SPKPQTTRH--------------RIRGI--------VTREDAQIVFVDT 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 112 PG-HEQYTR------NMATGA-STADLAIILIDARYGVqtqTRRHTFIASLL---GIKnIVVAINKMDLVeySPERFTEI 180
Cdd:COG1159 59 PGiHKPKRKlgrrmnKAAWSAlEDVDVILFVVDATEKI---GEGDEFILELLkklKTP-VILVINKIDLV--KKEELLPL 132
|
170 180 190
....*....|....*....|....*....|..
gi 491212272 181 QIEYdafvSQLGDrrPANIqfVPISALNGDNV 212
Cdd:COG1159 133 LAEY----SELLD--FAEI--VPISALKGDNV 156
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
36-168 |
8.35e-08 |
|
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: 53.75 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 36 GKSTLIGRLLYDSKLIYedqlqavTRDSKKVGTTgdapdlalLVDGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHE 115
Cdd:cd04170 11 GKTTLAEALLYATGAID-------RLGRVEDGNT--------VSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 491212272 116 QYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKNIVVaINKMD 168
Cdd:cd04170 76 DFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIF-INKMD 127
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
31-212 |
9.54e-08 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 51.91 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 31 GNVDDGKSTLIGRLLYDskliyedqlqavTRDSKKVGTTgdapdlallvdglqaereQGITIDVAYRYFSTEKRKFIIAD 110
Cdd:COG1100 10 GTGGVGKTSLVNRLVGD------------IFSLEKYLST------------------NGVTIDKKELKLDGLDVDLVIWD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 111 TPG-------HEQYTRNMatgaSTADLAIILIDARYGVQTQTRR--HTFIASLLGIKNIVVAINKMDLveYSPERFTEIQ 181
Cdd:COG1100 60 TPGqdefretRQFYARQL----TGASLYLFVVDGTREETLQSLYelLESLRRLGKKSPIILVLNKIDL--YDEEEIEDEE 133
|
170 180 190
....*....|....*....|....*....|.
gi 491212272 182 IEYDAFVSQLGDRrpaniqFVPISALNGDNV 212
Cdd:COG1100 134 RLKEALSEDNIVE------VVATSAKTGEGV 158
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
33-183 |
1.22e-07 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 54.25 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 33 VDDGKSTLIGRLLYDSKLIYEDQLQAVTRDSKkvgttgdapDLallvdglqaEREQGITID---VAYRYFSTEKRKFII- 108
Cdd:COG0481 15 IDHGKSTLADRLLELTGTLSEREMKEQVLDSM---------DL---------ERERGITIKaqaVRLNYKAKDGETYQLn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 109 -ADTPGHEQYT----RNMAT--GastadlAIILIDARYGVQTQTrrhtfIASL-LGIKN---IVVAINKMDLVEYSPERF 177
Cdd:COG0481 77 lIDTPGHVDFSyevsRSLAAceG------ALLVVDASQGVEAQT-----LANVyLALENdleIIPVINKIDLPSADPERV 145
|
....*.
gi 491212272 178 TEiQIE 183
Cdd:COG0481 146 KQ-EIE 150
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
30-168 |
3.07e-07 |
|
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: 51.11 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 30 CGNVDDGKSTLIGRLLYDskliyedqlqavTRDSKKVGTTGDAPDLALlvDGLQAEREQGITIDVAYRYFSTEKRK---- 105
Cdd:cd04167 6 AGHLHHGKTSLLDMLIEQ------------THKRTPSVKLGWKPLRYT--DTRKDEQERGISIKSNPISLVLEDSKgksy 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491212272 106 -FIIADTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKnIVVAINKMD 168
Cdd:cd04167 72 lINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLP-MVLVINKID 134
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
32-212 |
1.91e-06 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 50.43 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 32 NVddGKSTLIGRLLYDSKLIYEDQlqAvtrdskkvGTTGDApdlallvdglqaereqgitIDVAYRYfstEKRKFIIADT 111
Cdd:PRK00093 183 NV--GKSSLINALLGEERVIVSDI--A--------GTTRDS-------------------IDTPFER---DGQKYTLIDT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 112 PG----------HEQYTRNMATGAST-ADLAIILIDARYGVQTQTRRhtfIASLLgIKN---IVVAINKMDLVEysperf 177
Cdd:PRK00093 229 AGirrkgkvtegVEKYSVIRTLKAIErADVVLLVIDATEGITEQDLR---IAGLA-LEAgraLVIVVNKWDLVD------ 298
|
170 180 190
....*....|....*....|....*....|....*...
gi 491212272 178 teiQIEYDAFVSQLgDRRPANIQFVP---ISALNGDNV 212
Cdd:PRK00093 299 ---EKTMEEFKKEL-RRRLPFLDYAPivfISALTGQGV 332
|
|
| prfC |
TIGR00503 |
peptide chain release factor 3; This translation releasing factor, RF-3 (prfC) was originally ... |
34-183 |
2.41e-06 |
|
peptide chain release factor 3; This translation releasing factor, RF-3 (prfC) was originally described as stop codon-independent, in contrast to peptide chain release factor 1 (RF-1, prfA) and RF-2 (prfB). RF-1 and RF-2 are closely related to each other, while RF-3 is similar to elongation factors EF-Tu and EF-G; RF-1 is active at UAA and UAG and RF-2 is active at UAA and UGA. More recently, RF-3 was shown to be active primarily at UGA stop codons in E. coli. All bacteria and organelles have RF-1. The Mycoplasmas and organelles, which translate UGA as Trp rather than as a stop codon, lack RF-2. RF-3, in contrast, seems to be rare among bacteria and is found so far only in Escherichia coli and some other gamma subdivision Proteobacteria, in Synechocystis PCC6803, and in Staphylococcus aureus. [Protein synthesis, Translation factors]
Pssm-ID: 129594 [Multi-domain] Cd Length: 527 Bit Score: 50.29 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 34 DDGKSTLIGRLLydsklIYEDQLQAV----TRDSKKVGTTgdapdlallvDGLQAEREQGITIDVAYRYFSTEKRKFIIA 109
Cdd:TIGR00503 21 DAGKTTITEKVL-----LYGGAIQTAgavkGRGSQRHAKS----------DWMEMEKQRGISITTSVMQFPYRDCLVNLL 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491212272 110 DTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKnIVVAINKMDLVEYSP-ERFTEIQIE 183
Cdd:TIGR00503 86 DTPGHEDFSEDTYRTLTAVDNCLMVIDAAKGVETRTRKLMEVTRLRDTP-IFTFMNKLDRDIRDPlELLDEVENE 159
|
|
| FeoB |
cd01879 |
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
89-212 |
1.16e-05 |
|
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.
Pssm-ID: 206667 [Multi-domain] Cd Length: 159 Bit Score: 45.52 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 89 GITIDVAYRYFSTEKRKFIIADTPG---------HEQYTRNMATGAStADLAIILIDArygvqTQTRRHTFIASLL---G 156
Cdd:cd01879 29 GVTVEKKEGEFKLGGKEIEIVDLPGtysltpyseDEKVARDFLLGEE-PDLIVNVVDA-----TNLERNLYLTLQLlelG 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 491212272 157 IkNIVVAINKMDLVEyspERftEIQIEYDAFVSQLGdrrpanIQFVPISALNGDNV 212
Cdd:cd01879 103 L-PVVVALNMIDEAE---KR--GIKIDLDKLSELLG------VPVVPTSARKGEGI 146
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
8-145 |
1.69e-05 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 47.55 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 8 ISQDILAYLKQHEQkdlLR-FLTCGNVDDGKSTLIGRLLYDSKLIYEDqlqavtrdskkvgTTGDApdLALlvDGLQAER 86
Cdd:PRK07560 6 MVEKILELMKNPEQ---IRnIGIIAHIDHGKTTLSDNLLAGAGMISEE-------------LAGEQ--LAL--DFDEEEQ 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491212272 87 EQGITIDVA--YRYFSTEKRKFII--ADTPGHEQY----TRNMatgaSTADLAIILIDARYGVQTQT 145
Cdd:PRK07560 66 ARGITIKAAnvSMVHEYEGKEYLInlIDTPGHVDFggdvTRAM----RAVDGAIVVVDAVEGVMPQT 128
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
110-170 |
2.51e-05 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 47.19 E-value: 2.51e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491212272 110 DTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIasLLGIKN-IVVAINKMDLV 170
Cdd:PRK14845 532 DTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINI--LRQYKTpFVVAANKIDLI 591
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
32-166 |
2.81e-05 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 43.38 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 32 NVddGKSTLIGRLLydskliyedqlqavtrdsKKVGTTGDAPdlallvdglqaereqGITIDVAYRYFSTEKRKFIIADT 111
Cdd:pfam01926 9 NV--GKSTLINALT------------------GAKAIVSDYP---------------GTTRDPNEGRLELKGKQIILVDT 53
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491212272 112 PGH-EQYTRNMATGAS-----TADLAIILIDARYGVQTQTRRhtfIASLLG--IKNIVVAINK 166
Cdd:pfam01926 54 PGLiEGASEGEGLGRAflaiiEADLILFVVDSEEGITPLDEE---LLELLRenKKPIILVLNK 113
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
106-170 |
5.06e-05 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 45.94 E-value: 5.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491212272 106 FIiaDTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTrrhtfIASLLGIKN----IVVAINKMDLV 170
Cdd:PRK04004 75 FI--DTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQT-----IEAINILKRrktpFVVAANKIDRI 136
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
110-170 |
1.36e-04 |
|
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: 44.81 E-value: 1.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491212272 110 DTPGHEQYTRNMATGASTADLAIILIDARYGVQTQTRRHTFIASLLGIKnIVVAINKMDLV 170
Cdd:TIGR00491 75 DTPGHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKIDRI 134
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
108-206 |
1.38e-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: 42.92 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 108 IADTPG-------HEQYTRNMAtgaSTADLAIILIDARYgVQTQTRRHtFIASLL--GIKNIVVAINKMDLVEYSPERFt 178
Cdd:cd09912 50 LVDTPGlnstiehHTEITESFL---PRADAVIFVLSADQ-PLTESERE-FLKEILkwSGKKIFFVLNKIDLLSEEELEE- 123
|
90 100
....*....|....*....|....*...
gi 491212272 179 eiQIEYDAFVSQLGDRRPANIQFVPISA 206
Cdd:cd09912 124 --VLEYSREELGVLELGGGEPRIFPVSA 149
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
32-212 |
1.93e-04 |
|
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206681 [Multi-domain] Cd Length: 157 Bit Score: 42.04 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 32 NVddGKSTLIGRLLYDSKLIYEDQlQAVTRDSKkvgttgdapdlallvdglqaereqgitidvaYRYFSTEKRKFIIADT 111
Cdd:cd01894 7 NV--GKSTLFNRLTGRRDAIVSDT-PGVTRDRK-------------------------------YGEAEWGGREFILIDT 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 112 PG--------HEQYTRNMATGASTADLAIILIDARYGVQTQTRrhtFIASLL--GIKNIVVAINKMDlveySPERFTEIq 181
Cdd:cd01894 53 GGiepddegiSKEIREQAEIAIEEADVILFVVDGREGLTPADE---EIAKYLrkSKKPVILVVNKID----NIKEEEEA- 124
|
170 180 190
....*....|....*....|....*....|.
gi 491212272 182 ieYDAFvsQLGDRRPaniqfVPISALNGDNV 212
Cdd:cd01894 125 --AEFY--SLGFGEP-----IPISAEHGRGI 146
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
32-212 |
3.67e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 43.11 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 32 NVddGKSTLIGRLLYDSKLIYEDQlQAVTRDSKkvgttgdapdlallvdglqaereqgitidvaYRYFSTEKRKFIIADT 111
Cdd:PRK00093 11 NV--GKSTLFNRLTGKRDAIVADT-PGVTRDRI-------------------------------YGEAEWLGREFILIDT 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 112 PG----HEQYTRNMA----TGASTADLAIILIDARYGVQTQTRrhtFIASLL---GiKNIVVAINKMDlveySPERFTEI 180
Cdd:PRK00093 57 GGiepdDDGFEKQIReqaeLAIEEADVILFVVDGRAGLTPADE---EIAKILrksN-KPVILVVNKVD----GPDEEADA 128
|
170 180 190
....*....|....*....|....*....|..
gi 491212272 181 qieYDAFvsQLGDRRPaniqfVPISALNGDNV 212
Cdd:PRK00093 129 ---YEFY--SLGLGEP-----YPISAEHGRGI 150
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
264-324 |
5.73e-04 |
|
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: 38.40 E-value: 5.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491212272 264 GTVAL-----GEINVGDEIVALPSGK-----RSTVKEIVTFDGNLEQAVAGQAVTLTLN--DEIDISRGNVLV 324
Cdd:pfam03144 1 GTVATgrvesGTLKKGDKVRILPNGTgkkkiVTRVTSLLMFHAPLREAVAGDNAGLILAgvGLEDIRVGDTLT 73
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
32-212 |
2.97e-03 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 40.01 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 32 NVddGKSTLIGRLlydskliyedqlqAVTRDSkkvgttgdapdlalLVDglqaeREQGITIDVAYRYFSTEKRKFIIADT 111
Cdd:COG1160 12 NV--GKSTLFNRL-------------TGRRDA--------------IVD-----DTPGVTRDRIYGEAEWGGREFTLIDT 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 112 PG-----HEQYTRNMATGA----STADLAIILIDARYGVqTQTRRHtfIASLL---GiKNIVVAINKMDlveySPERFTE 179
Cdd:COG1160 58 GGiepddDDGLEAEIREQAelaiEEADVILFVVDGRAGL-TPLDEE--IAKLLrrsG-KPVILVVNKVD----GPKREAD 129
|
170 180 190
....*....|....*....|....*....|...
gi 491212272 180 IqieYDAFvsQLGDRRPaniqfVPISALNGDNV 212
Cdd:COG1160 130 A---AEFY--SLGLGEP-----IPISAEHGRGV 152
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
332-434 |
6.85e-03 |
|
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.
Pssm-ID: 294008 [Multi-domain] Cd Length: 109 Bit Score: 36.37 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 332 ISRSVRASVVWMNEH-PLVKGKLYNVKIGTQTVPAKVTNIHYRVNVNTLEHT--HVEELELNAIADVVVEFDAPVVFDQY 408
Cdd:cd04093 4 TTSKFEARIVTFDLQvPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIkkKPRCLGKNQSAVVEIELERPIPLETF 83
|
90 100
....*....|....*....|....*.
gi 491212272 409 QDSRYTGSFIFidRLSNVTVGAGMVE 434
Cdd:cd04093 84 KDNKELGRFVL--RRGGETIAAGIVT 107
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
158-212 |
8.97e-03 |
|
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.
Pssm-ID: 206685 [Multi-domain] Cd Length: 170 Bit Score: 37.40 E-value: 8.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 491212272 158 KNIVVAINKMDLVEySPERFTEIQIEYDAFVsqlgdrrpaNIQFVPISALNGDNV 212
Cdd:cd01898 115 KPRIVVLNKIDLLD-AEERFEKLKELLKELK---------GKKVFPISALTGEGL 159
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
125-212 |
9.15e-03 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 37.09 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491212272 125 ASTADLAIILIDARYGVQTQTRRhtfIASLLGIKNIVVAINKMDLVEYSPERFTEiqieydafvsqlgdrrpANIQFVPI 204
Cdd:cd04164 80 IEEADLVLLVVDASEGLDEEDLE---ILELPAKKPVIVVLNKSDLLSDAEGISEL-----------------NGKPIIAI 139
|
....*...
gi 491212272 205 SALNGDNV 212
Cdd:cd04164 140 SAKTGEGI 147
|
|
| |
