|
Name |
Accession |
Description |
Interval |
E-value |
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
4-409 |
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: 553.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 4 VLNFVIVGHVDHGKSTLIGRLLYDTDSLQPDRIAEMEKMSKSRGRDENEFAYLLDHLEEERKQGVTIDTTQVFFSTDKRH 83
Cdd:COG2895 17 LLRFITCGSVDDGKSTLIGRLLYDTKSIFEDQLAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPKRK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 84 YVIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQYSEERFKQVQSDVQ 163
Cdd:COG2895 97 FIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 164 EFLASIGASSDITLPIAAAKGDNIAKPSENMPWHKGPTFLDSLDSLKGRIPAEDKSLILPVQDVYK-VDDKRINAGRVEA 242
Cdd:COG2895 177 AFAAKLGLEDITFIPISALKGDNVVERSENMPWYDGPTLLEHLETVEVAEDRNDAPFRFPVQYVNRpNLDFRGYAGTIAS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 243 GCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGESIGITTEDALFLDRGDIVCREGGEPTLADCFRARIFWMSKRPL 322
Cdd:COG2895 257 GTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLEDEIDISRGDVIVAADAPPEVADQFEATLVWMDEEPL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 323 DTSERLFIRCATQQTRCSIDTIEKRIDSSTLKvlEENGTKLENLEVGEVIIKTKKEIAFDDFNSTQEMGRFVLVkDE--- 399
Cdd:COG2895 337 LPGRKYLLKHGTRTVRATVTAIKYRIDVNTLE--HEAADSLELNDIGRVTLRLAEPIAFDPYADNRATGSFILI-DRltn 413
|
410
....*....|
gi 1189696689 400 NIVAGGIITG 409
Cdd:COG2895 414 ATVGAGMIRG 423
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
5-408 |
1.75e-123 |
|
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: 363.87 E-value: 1.75e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 5 LNFVIVGHVDHGKSTLIGRLLYDTDSLQPDRIAEMEKMSKSRGRDENEFAYLLDHLEEERKQGVTIDTTQVFFSTDKRHY 84
Cdd:COG5256 8 LNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 85 VIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQYSEERFKQVQSDVQE 164
Cdd:COG5256 88 TIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 165 FLASIG-ASSDIT-LPIAAAKGDNIAKPSENMPWHKGPTFLDSLDSLKGRIPAEDKSLILPVQDVYKVddKRINA---GR 239
Cdd:COG5256 168 LLKMVGyKVDKIPfIPVSAWKGDNVVKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQDVYSI--SGIGTvpvGR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 240 VEAGCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGESI-----GITTEDalfLDRGDIVCREGGEPTLADCFRARI 314
Cdd:COG5256 246 VETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIgfnvrGVEKND---IKRGDVAGHPDNPPTVAEEFTAQI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 315 FWMSK--------RPLdtserlfIRCATQQTRCSIDTIEKRIDSSTLKVLEENGTKLENLEVGEVIIKTKKEIAFDDFNS 386
Cdd:COG5256 323 VVLQHpsaitvgyTPV-------FHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEKFKE 395
|
410 420
....*....|....*....|..
gi 1189696689 387 TQEMGRFVLVKDENIVAGGIIT 408
Cdd:COG5256 396 FPQLGRFAIRDMGQTVAAGVVL 417
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
5-393 |
7.55e-123 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 362.32 E-value: 7.55e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 5 LNFVIVGHVDHGKSTLIGRLLYDTDSLQPDRIAEMEKMSKSRGRDENEFAYLLDHLEEERKQGVTIDTTQVFFSTDKRHY 84
Cdd:PRK12317 7 LNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 85 VIIDAPGHVEFVKNMITGASQAEAAVLIVDAEE--GVMEQTKRHSYMLNMLGLKQIITVINKMDLVQYSEERFKQVQSDV 162
Cdd:PRK12317 87 TIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 163 QEFLASIG-ASSDIT-LPIAAAKGDNIAKPSENMPWHKGPTFLDSLDSLKGRIPAEDKSLILPVQDVYKVDD-KRINAGR 239
Cdd:PRK12317 167 SKLLKMVGyKPDDIPfIPVSAFEGDNVVKKSENMPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQDVYSISGvGTVPVGR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 240 VEAGCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGESI-----GITTEDalfLDRGDIVCREGGEPTLADCFRARI 314
Cdd:PRK12317 247 VETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIgfnvrGVGKKD---IKRGDVCGHPDNPPTVAEEFTAQI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 315 FWMSK--------RPLdtserlfIRCATQQTRCSIDTIEKRIDSSTLKVLEENGTKLENLEVGEVIIKTKKEIAFDDFNS 386
Cdd:PRK12317 324 VVLQHpsaitvgyTPV-------FHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVIEKVKE 396
|
....*..
gi 1189696689 387 TQEMGRF 393
Cdd:PRK12317 397 IPQLGRF 403
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
5-407 |
3.16e-118 |
|
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: 350.13 E-value: 3.16e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 5 LNFVIVGHVDHGKSTLIGRLLYDTDSLQPDRIAEMEKMSKSRGRDENE--FAYLLDHLEEERKQGVTIDTTQVFFSTDKR 82
Cdd:TIGR02034 1 LRFLTCGSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTQGGEidLALLVDGLQAEREQGITIDVAYRYFSTDKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 83 HYVIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQYSEERFKQVQSDV 162
Cdd:TIGR02034 81 KFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 163 QEFLASIGASSDITLPIAAAKGDNIAKPSENMPWHKGPTFLDSLDSLKGRIPAEDKSLILPVQDVYKVD-DKRINAGRVE 241
Cdd:TIGR02034 161 LAFAEQLGFRDVTFIPLSALKGDNVVSRSESMPWYSGPTLLEILETVEVERDAQDLPLRFPVQYVNRPNlDFRGYAGTIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 242 AGCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGESIGITTEDALFLDRGDIVCREGGEPTLADCFRARIFWMSKRP 321
Cdd:TIGR02034 241 SGSVHVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEIDISRGDLLAAADSAPEVADQFAATLVWMAEEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 322 LDTSERLFIRCATQQTRCSIDTIEKRIDSSTLKVLEENGTKLEnlEVGEVIIKTKKEIAFDDFNSTQEMGRFVLV-KDEN 400
Cdd:TIGR02034 321 LLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGAAKSLELN--EIGRVNLSLDEPIAFDPYAENRTTGAFILIdRLSN 398
|
....*...
gi 1189696689 401 I-VAGGII 407
Cdd:TIGR02034 399 RtVGAGMI 406
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
5-410 |
3.41e-115 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 349.61 E-value: 3.41e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 5 LNFVIVGHVDHGKSTLIGRLLYDTDSLQPDRIAEMEKMSKSRG--RDENEFAYLLDHLEEERKQGVTIDTTQVFFSTDKR 82
Cdd:PRK05506 25 LRFITCGSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQGITIDVAYRYFATPKR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 83 HYVIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQYSEERFKQVQSDV 162
Cdd:PRK05506 105 KFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 163 QEFLASIGASSDITLPIAAAKGDNIAKPSENMPWHKGPTFLDSLDSLKGRIPAEDKSLILPVQDVYKVD-DKRINAGRVE 241
Cdd:PRK05506 185 RAFAAKLGLHDVTFIPISALKGDNVVTRSARMPWYEGPSLLEHLETVEIASDRNLKDFRFPVQYVNRPNlDFRGFAGTVA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 242 AGCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGESIGITTEDALFLDRGDIVCREGGEPTLADCFRARIFWMSKRP 321
Cdd:PRK05506 265 SGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLADEIDISRGDMLARADNRPEVADQFDATVVWMAEEP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 322 LDTSERLFIRCATQQTRCSIDTIEKRIDSSTLKvlEENGTKLENLEVGEVIIKTKKEIAFDDFNSTQEMGRFVLVkDE-- 399
Cdd:PRK05506 345 LLPGRPYLLKHGTRTVPASVAAIKYRVDVNTLE--RLAAKTLELNEIGRCNLSTDAPIAFDPYARNRTTGSFILI-DRlt 421
|
410
....*....|..
gi 1189696689 400 -NIVAGGIITGR 410
Cdd:PRK05506 422 nATVGAGMIDFA 433
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
5-410 |
4.68e-108 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 326.49 E-value: 4.68e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 5 LNFVIVGHVDHGKSTLIGRLLYDTDSLQPDRIAEMEKMSKSRGR--DENEFAYLLDHLEEERKQGVTIDTTQVFFSTDKR 82
Cdd:PRK05124 28 LRFLTCGSVDDGKSTLIGRLLHDTKQIYEDQLASLHNDSKRHGTqgEKLDLALLVDGLQAEREQGITIDVAYRYFSTEKR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 83 HYVIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQYSEERFKQVQSDV 162
Cdd:PRK05124 108 KFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 163 QEFLASIGASSDIT-LPIAAAKGDNIAKPSENMPWHKGPTFLDSLDSLKGRIPAEDKSLILPVQDVYKVD-DKRINAGRV 240
Cdd:PRK05124 188 LTFAEQLPGNLDIRfVPLSALEGDNVVSQSESMPWYSGPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPNlDFRGYAGTL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 241 EAGCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGESIGITTEDALFLDRGDIVCREGGEPTLADCFRARIFWMSKR 320
Cdd:PRK05124 268 ASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDEIDISRGDLLVAADEALQAVQHASADVVWMAEQ 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 321 PLDTSERLFIRCATQQTRCSIDTIEKRIDsstLKVLEENGTklENL---EVGEVIIKTKKEIAFDDFNSTQEMGRFVLV- 396
Cdd:PRK05124 348 PLQPGQSYDIKIAGKKTRARVDAIRYQVD---INTLTQREA--ENLplnGIGLVELTFDEPLVLDPYQQNRVTGGFIFId 422
|
410
....*....|....*
gi 1189696689 397 KDENI-VAGGIITGR 410
Cdd:PRK05124 423 RLTNVtVGAGMVREP 437
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
6-210 |
2.18e-103 |
|
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: 304.88 E-value: 2.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 6 NFVIVGHVDHGKSTLIGRLLYDTDSLQPDRIAEMEKMSKSRGRDEN-EFAYLLDHLEEERKQGVTIDTTQVFFSTDKRHY 84
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAALERSKSSGTQGEKlDLALLVDGLQAEREQGITIDVAYRYFSTPKRKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 85 VIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQYSEERFKQVQSDVQE 164
Cdd:cd04166 81 IIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1189696689 165 FLASIGASSDITLPIAAAKGDNIAKPSENMPWHKGPTFLDSLDSLK 210
Cdd:cd04166 161 FAASLGIEDITFIPISALEGDNVVSRSENMPWYKGPTLLEHLETVE 206
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
5-407 |
4.75e-94 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 289.34 E-value: 4.75e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 5 LNFVIVGHVDHGKSTLIGRLLYDTDSLQPDRIAEMEKMSKSRGRDENEFAYLLDHLEEERKQGVTIDTTQVFFSTDKRHY 84
Cdd:PTZ00141 8 INLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 85 VIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVME-------QTKRHSYMLNMLGLKQIITVINKMDL--VQYSEERF 155
Cdd:PTZ00141 88 TIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDktVNYSQERY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 156 KQVQSDVQEFLASIGASSDIT--LPIAAAKGDNIAKPSENMPWHKGPTFLDSLDSLKGRIPAEDKSLILPVQDVYKVDD- 232
Cdd:PTZ00141 168 DEIKKEVSAYLKKVGYNPEKVpfIPISGWQGDNMIEKSDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGi 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 233 KRINAGRVEAGCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGESIG-----ITTEDalfLDRGDIVCREGGEPTL- 306
Cdd:PTZ00141 248 GTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGfnvknVSVKD---IKRGYVASDSKNDPAKe 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 307 ADCFRARIFWMSkRPLDTSERL--FIRCATQQTRCSIDTIEKRIDSSTLKVLEENGTKLENLEVGEVIIKTKKEIAFDDF 384
Cdd:PTZ00141 325 CADFTAQVIVLN-HPGQIKNGYtpVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVF 403
|
410 420
....*....|....*....|....
gi 1189696689 385 NSTQEMGRFVlVKD-ENIVAGGII 407
Cdd:PTZ00141 404 NEYPPLGRFA-VRDmKQTVAVGVI 426
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
6-210 |
4.74e-88 |
|
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: 265.89 E-value: 4.74e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 6 NFVIVGHVDHGKSTLIGRLLYDTDSLQPDRIAEMEKMSKSRGRDENEFAYLLDHLEEERKQGVTIDTTQVFFSTDKRHYV 85
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 86 IIDAPGHVEFVKNMITGASQAEAAVLIVDAEEG-------VMEQTKRHSYMLNMLGLKQIITVINKMDLV--QYSEERFK 156
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1189696689 157 QVQSDVQEFLASIGAS-SDIT-LPIAAAKGDNIAKPSENMPWHKGPTFLDSLDSLK 210
Cdd:cd01883 161 EIKKKVSPFLKKVGYNpKDVPfIPISGFTGDNLIEKSENMPWYKGPTLLEALDSLE 216
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
5-407 |
5.81e-70 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 227.28 E-value: 5.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 5 LNFVIVGHVDHGKSTLIGRLLYDTDSLQPDRIAEMEKMSKSRGRDENEFAYLLDHLEEERKQGVTIDTTQVFFSTDKRHY 84
Cdd:PLN00043 8 INIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 85 VIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVME-------QTKRHSYMLNMLGLKQIITVINKMDLV--QYSEERF 155
Cdd:PLN00043 88 TVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATtpKYSKARY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 156 KQVQSDVQEFLASIGASSDIT--LPIAAAKGDNIAKPSENMPWHKGPTFLDSLDSLKGRIPAEDKSLILPVQDVYKVDD- 232
Cdd:PLN00043 168 DEIVKEVSSYLKKVGYNPDKIpfVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGi 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 233 KRINAGRVEAGCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGESIGITTEDALFLD--RGDIVCREGGEPTL-ADC 309
Cdd:PLN00043 248 GTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDlkRGYVASNSKDDPAKeAAN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 310 FRARIFWMSKR-PLDTSERLFIRCATQQTRCSIDTIEKRIDSSTLKVLEENGTKLENLEVGEVIIKTKKEIAFDDFNSTQ 388
Cdd:PLN00043 328 FTSQVIIMNHPgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVVETFSEYP 407
|
410
....*....|....*....
gi 1189696689 389 EMGRFVLVKDENIVAGGII 407
Cdd:PLN00043 408 PLGRFAVRDMRQTVAVGVI 426
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
2-209 |
7.66e-59 |
|
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: 190.04 E-value: 7.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 2 DNVLNFVIVGHVDHGKSTLIGRLLYDTdslqpdriaemeKMSKSRGRDENEFAYLLDHLEEERKQGVTIDTTQVFFSTDK 81
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYT------------GAISKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 82 RHYVIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKqIITVINKMDLVqySEERFKQVQSD 161
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1189696689 162 VQ-EFLASIGASSDIT--LPIAAAKGDNIakpsenmpwhkgPTFLDSLDSL 209
Cdd:pfam00009 146 VSrELLEKYGEDGEFVpvVPGSALKGEGV------------QTLLDALDEY 184
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
6-187 |
7.01e-48 |
|
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: 7.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 6 NFVIVGHVDHGKSTLIGRLLYDTdslqpdriaemekmsKSRGRDENEFAYLLDHLEEERKQGVTIDTTQVFFSTDKRHYV 85
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQT---------------GAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 86 IIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKqIITVINKMDLVqySEERFKQVQSDVQEF 165
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLP-IIVAVNKIDRV--GEEDFDEVLREIKEL 142
|
170 180
....*....|....*....|....*..
gi 1189696689 166 LASIGASSD-----ITLPIAAAKGDNI 187
Cdd:cd00881 143 LKLIGFTFLkgkdvPIIPISALTGEGI 169
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
5-319 |
1.26e-43 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 157.68 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 5 LNFVIVGHVDHGKSTL---IGRLLYDtdslqpdriaemEKMSKSRGRDEnefaylLDHLEEERKQGVTIDTTQVFFSTDK 81
Cdd:PLN03127 62 VNVGTIGHVDHGKTTLtaaITKVLAE------------EGKAKAVAFDE------IDKAPEEKARGITIATAHVEYETAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 82 RHYVIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQySEERFKQVQSD 161
Cdd:PLN03127 124 RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVD-DEELLELVEME 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 162 VQEFLASIGASSDiTLPI------AAAKG--DNIAKPSenmpwhkgptFLDSLDSLKGRIP----AEDKSLILPVQDVYK 229
Cdd:PLN03127 203 LRELLSFYKFPGD-EIPIirgsalSALQGtnDEIGKNA----------ILKLMDAVDEYIPepvrVLDKPFLMPIEDVFS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 230 VDDK-RINAGRVEAGCIEQGEAVKVI---PSG-QKTKVQSVEKFLEEPERACAGESIG-----ITTEDalfLDRGDIVCR 299
Cdd:PLN03127 272 IQGRgTVATGRVEQGTIKVGEEVEIVglrPGGpLKTTVTGVEMFKKILDQGQAGDNVGlllrgLKRED---VQRGQVICK 348
|
330 340
....*....|....*....|
gi 1189696689 300 EGGEPTlADCFRARIFWMSK 319
Cdd:PLN03127 349 PGSIKT-YKKFEAEIYVLTK 367
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
5-319 |
2.00e-43 |
|
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: 156.09 E-value: 2.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 5 LNFVIVGHVDHGKSTLIGRLlydtdslqpdrIAEMEKMSKSRGRDENEfaylLDHLEEERKQGVTIDTTQVFFSTDKRHY 84
Cdd:TIGR00485 13 VNVGTIGHVDHGKTTLTAAI-----------TTVLAKEGGAAARAYDQ----IDNAPEEKARGITINTAHVEYETETRHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 85 VIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQySEERFKQVQSDVQE 164
Cdd:TIGR00485 78 AHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVD-DEELLELVEMEVRE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 165 FLASIGASSDITlPI------AAAKGDNIakpsenmpWhkGPTFLDSLDSLKGRIP----AEDKSLILPVQDVYKVDDK- 233
Cdd:TIGR00485 157 LLSQYDFPGDDT-PIirgsalKALEGDAE--------W--EAKILELMDAVDEYIPtperEIDKPFLLPIEDVFSITGRg 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 234 RINAGRVEAGCIEQGEAVKV--IPSGQKTKVQSVEKFLEEPERACAGESI-----GITTEDalfLDRGDIVCREGGEPTL 306
Cdd:TIGR00485 226 TVVTGRVERGIIKVGEEVEIvgLKDTRKTTVTGVEMFRKELDEGRAGDNVglllrGIKREE---IERGMVLAKPGSIKPH 302
|
330
....*....|...
gi 1189696689 307 ADcFRARIFWMSK 319
Cdd:TIGR00485 303 TK-FEAEVYVLSK 314
|
|
| tufA |
CHL00071 |
elongation factor Tu |
5-283 |
2.96e-41 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 150.49 E-value: 2.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 5 LNFVIVGHVDHGKSTLIGRLlydtdslqpdrIAEMEKMSKSRGRDENEfaylLDHLEEERKQGVTIDTTQVFFSTDKRHY 84
Cdd:CHL00071 13 VNIGTIGHVDHGKTTLTAAI-----------TMTLAAKGGAKAKKYDE----IDSAPEEKARGITINTAHVEYETENRHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 85 VIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQySEERFKQVQSDVQE 164
Cdd:CHL00071 78 AHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVD-DEELLELVELEVRE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 165 FLASIGASSDIT--------LPIAAAKGDNIAKPSENmPW-HKGPTFLDSLDSLkgrIPAE----DKSLILPVQDVYKVD 231
Cdd:CHL00071 157 LLSKYDFPGDDIpivsgsalLALEALTENPKIKRGEN-KWvDKIYNLMDAVDSY---IPTPerdtDKPFLMAIEDVFSIT 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1189696689 232 DKRINA-GRVEAGCIEQGEAVKVI--PSGQKTKVQSVEKFLEEPERACAGESIGI 283
Cdd:CHL00071 233 GRGTVAtGRIERGTVKVGDTVEIVglRETKTTTVTGLEMFQKTLDEGLAGDNVGI 287
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
5-320 |
4.13e-41 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 149.71 E-value: 4.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 5 LNFVIVGHVDHGKSTL---IGRLLYDTDSLQPDRIAEmekmsksrgrdenefaylLDHLEEERKQGVTIDTTQVFFSTDK 81
Cdd:PRK12736 13 VNIGTIGHVDHGKTTLtaaITKVLAERGLNQAKDYDS------------------IDAAPEEKERGITINTAHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 82 RHYVIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQySEERFKQVQSD 161
Cdd:PRK12736 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVD-DEELLELVEME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 162 VQEFLASIGASSDiTLPI------AAAKGDNiakpsenmPWHKgpTFLDSLDSLKGRIP----AEDKSLILPVQDVYKVD 231
Cdd:PRK12736 154 VRELLSEYDFPGD-DIPVirgsalKALEGDP--------KWED--AIMELMDAVDEYIPtperDTDKPFLMPVEDVFTIT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 232 DK-RINAGRVEAGCIEQGEAVKV--IPSGQKTKVQSVEKFLEEPERACAGESI-----GITTEDalfLDRGDIVCREGGE 303
Cdd:PRK12736 223 GRgTVVTGRVERGTVKVGDEVEIvgIKETQKTVVTGVEMFRKLLDEGQAGDNVgvllrGVDRDE---VERGQVLAKPGSI 299
|
330
....*....|....*..
gi 1189696689 304 PTLADcFRARIFWMSKR 320
Cdd:PRK12736 300 KPHTK-FKAEVYILTKE 315
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
10-283 |
1.06e-39 |
|
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: 146.06 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 10 VGHVDHGKSTL---IGRLLYDtdslqpdriaemEKMSKSRGRDEnefaylLDHLEEERKQGVTIDTTQVFFSTDKRHYVI 86
Cdd:COG0050 18 IGHVDHGKTTLtaaITKVLAK------------KGGAKAKAYDQ------IDKAPEEKERGITINTSHVEYETEKRHYAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 87 IDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQySEERFKQVQSDVQEFL 166
Cdd:COG0050 80 VDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVD-DEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 167 ASIGASSDiTLPI------AAAKGDNIAKPSENMpwhkgptfLDSLDSLKGRIP----AEDKSLILPVQDVYKVDDKRIN 236
Cdd:COG0050 159 SKYGFPGD-DTPIirgsalKALEGDPDPEWEKKI--------LELMDAVDSYIPeperDTDKPFLMPVEDVFSITGRGTV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1189696689 237 A-GRVEAGCIEQGEAVKV--IPSGQKTKVQSVEKFLEEPERACAGESIGI 283
Cdd:COG0050 230 VtGRVERGIIKVGDEVEIvgIRDTQKTVVTGVEMFRKLLDEGEAGDNVGL 279
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
5-283 |
2.12e-39 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 147.07 E-value: 2.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 5 LNFVIVGHVDHGKSTLIGRLLYDTDSLQPdriaemekmSKSRGRDEnefaylLDHLEEERKQGVTIDTTQVFFSTDKRHY 84
Cdd:PLN03126 82 VNIGTIGHVDHGKTTLTAALTMALASMGG---------SAPKKYDE------IDAAPEERARGITINTATVEYETENRHY 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 85 VIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQySEERFKQVQSDVQE 164
Cdd:PLN03126 147 AHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVD-DEELLELVELEVRE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 165 FLASIGASSDITLPIAAAKGDNIAKPSENMPWHKGPT-----FLDSLDSLKGRIPAEDKSLILP----VQDVYKVDDK-R 234
Cdd:PLN03126 226 LLSSYEFPGDDIPIISGSALLALEALMENPNIKRGDNkwvdkIYELMDAVDSYIPIPQRQTDLPfllaVEDVFSITGRgT 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1189696689 235 INAGRVEAGCIEQGEAVKVIPSGQ--KTKVQSVEKFLEEPERACAGESIGI 283
Cdd:PLN03126 306 VATGRVERGTVKVGETVDIVGLREtrSTTVTGVEMFQKILDEALAGDNVGL 356
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
10-301 |
2.27e-39 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 144.95 E-value: 2.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 10 VGHVDHGKSTL---IGRLLYDtdslqpdriaemEKMSKSRGRDEnefaylLDHLEEERKQGVTIDTTQVFFSTDKRHYVI 86
Cdd:PRK00049 18 IGHVDHGKTTLtaaITKVLAK------------KGGAEAKAYDQ------IDKAPEEKARGITINTAHVEYETEKRHYAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 87 IDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQySEERFKQVQSDVQEFL 166
Cdd:PRK00049 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVD-DEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 167 ASIGASSDiTLPI------AAAKGDniakpsENMPWHKgpTFLDSLDSLKGRIP----AEDKSLILPVQDVYKVDDKRIN 236
Cdd:PRK00049 159 SKYDFPGD-DTPIirgsalKALEGD------DDEEWEK--KILELMDAVDSYIPtperAIDKPFLMPIEDVFSISGRGTV 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189696689 237 A-GRVEAGCIEQGEAVKV--IPSGQKTKVQSVEKFLEEPERACAGESI-----GITTEDalfLDRGDIVCREG 301
Cdd:PRK00049 230 VtGRVERGIIKVGEEVEIvgIRDTQKTTVTGVEMFRKLLDEGQAGDNVgallrGIKRED---VERGQVLAKPG 299
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
11-337 |
2.84e-39 |
|
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: 148.52 E-value: 2.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 11 GHVDHGKSTLIGRLlydTdslqpdriaemekmsksrGRDEnefayllDHLEEERKQGVTID-----TTQvffsTDKRHYV 85
Cdd:COG3276 7 GHIDHGKTTLVKAL---T------------------GIDT-------DRLKEEKKRGITIDlgfayLPL----PDGRRLG 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 86 IIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVqySEERFKQVQSDVQEF 165
Cdd:COG3276 55 FVDVPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV--DEEWLELVEEEIREL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 166 LASIG-ASSDItLPIAAAKGDNIAKpsenmpwhkgptFLDSLDSLKGRIPAEDKSLI--LPVQDVYKVDdkriNAGRV-- 240
Cdd:COG3276 133 LAGTFlEDAPI-VPVSAVTGEGIDE------------LRAALDALAAAVPARDADGPfrLPIDRVFSIK----GFGTVvt 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 241 ---EAGCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGESI-----GITTEDalfLDRGDIVCREG-GEPTlaDCFR 311
Cdd:COG3276 196 gtlLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRValnlaGVEKEE---IERGDVLAAPGaLRPT--DRID 270
|
330 340
....*....|....*....|....*...
gi 1189696689 312 ARIFWM--SKRPLDTSERLFIRCATQQT 337
Cdd:COG3276 271 VRLRLLpsAPRPLKHWQRVHLHHGTAEV 298
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
10-283 |
2.25e-37 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 139.59 E-value: 2.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 10 VGHVDHGKSTL---IGRLLYDTDslqpdriaemekMSKSRGRDEnefaylLDHLEEERKQGVTIDTTQVFFSTDKRHYVI 86
Cdd:PRK12735 18 IGHVDHGKTTLtaaITKVLAKKG------------GGEAKAYDQ------IDNAPEEKARGITINTSHVEYETANRHYAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 87 IDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQySEERFKQVQSDVQEFL 166
Cdd:PRK12735 80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVD-DEELLELVEMEVRELL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 167 ASIGASSDITlPI------AAAKGDNiakpsenmPWHKGPTFLDSLDSLKGRIP----AEDKSLILPVQDVYKVDDKRIN 236
Cdd:PRK12735 159 SKYDFPGDDT-PIirgsalKALEGDD--------DEEWEAKILELMDAVDSYIPeperAIDKPFLMPIEDVFSISGRGTV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1189696689 237 A-GRVEAGCIEQGEAVKV--IPSGQKTKVQSVEKFLEEPERACAGESIGI 283
Cdd:PRK12735 230 VtGRVERGIVKVGDEVEIvgIKETQKTTVTGVEMFRKLLDEGQAGDNVGV 279
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
5-288 |
6.59e-37 |
|
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: 141.55 E-value: 6.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 5 LNFVIVGHVDHGKSTLIgRLLYDTDSlqpdriaemekmsksrgrdenefayllDHLEEERKQGVTIDTTQVFFSTDKRHY 84
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLL-KALTGIAA---------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 85 VIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVqySEERFKQVQSDVQE 164
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRV--NEEEIKRTEMFMKQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 165 FLASIGASSDITLPIAAAK-GDNIAKPSENMpwhkgPTFLDSLDSLKgripaEDKSLILPVQDVYKVDDK-RINAGRVEA 242
Cdd:TIGR00475 131 ILNSYIFLKNAKIFKTSAKtGQGIGELKKEL-----KNLLESLDIKR-----IQKPLRMAIDRAFKVKGAgTVVTGTAFS 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1189696689 243 GCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGESIGITTEDA 288
Cdd:TIGR00475 201 GEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDV 246
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
10-179 |
8.26e-37 |
|
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: 132.71 E-value: 8.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 10 VGHVDHGKSTL---IGRLLYDTdslqpdriaemeKMSKSRGRDEnefaylLDHLEEERKQGVTIDTTQVFFSTDKRHYVI 86
Cdd:cd01884 8 IGHVDHGKTTLtaaITKVLAKK------------GGAKAKKYDE------IDKAPEEKARGITINTAHVEYETANRHYAH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 87 IDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVQySEERFKQVQSDVQEFL 166
Cdd:cd01884 70 VDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVD-DEELLELVEMEVRELL 148
|
170
....*....|...
gi 1189696689 167 ASIGASSDITlPI 179
Cdd:cd01884 149 SKYGFDGDDT-PI 160
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
11-188 |
2.26e-35 |
|
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: 128.11 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 11 GHVDHGKSTLIGRLlydtdslqpdriaemekmsksRGRDEnefayllDHLEEERKQGVTIDTTQVFFS-TDKRHYVIIDA 89
Cdd:cd04171 6 GHIDHGKTTLIKAL---------------------TGIET-------DRLPEEKKRGITIDLGFAYLDlPDGKRLGFIDV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 90 PGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVqySEERFKQVQSDVQEFLASI 169
Cdd:cd04171 58 PGHEKFVKNMLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV--DEDRLELVEEEILELLAGT 135
|
170 180
....*....|....*....|
gi 1189696689 170 G-ASSDItLPIAAAKGDNIA 188
Cdd:cd04171 136 FlADAPI-FPVSSVTGEGIE 154
|
|
| CysN_NoDQ_III |
cd04095 |
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of ... |
305-407 |
5.60e-25 |
|
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: 97.89 E-value: 5.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 305 TLADCFRARIFWMSKRPLDTSERLFIRCATQQTRCSIDTIEKRIDSSTLKvlEENGTKLENLEVGEVIIKTKKEIAFDDF 384
Cdd:cd04095 1 EVSDQFEATLVWMDEKPLQPGRRYLLKHGTRTVRARVTEIDYRIDVNTLE--REPADTLALNDIGRVTLRLAEPLAFDPY 78
|
90 100
....*....|....*....|....*.
gi 1189696689 385 NSTQEMGRFVLVkDE---NIVAGGII 407
Cdd:cd04095 79 AENRATGSFILI-DRltnATVAAGMI 103
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
6-187 |
7.39e-24 |
|
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: 97.22 E-value: 7.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 6 NFVIVGHVDHGKSTLIGRLLYDTDSLQPDriaEMEkmsksrgrdenefAYLLDHLEEERKQGVTI--DTTQVFF-STDKR 82
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSER---EMK-------------EQVLDSMDLERERGITIkaQAVRLFYkAKDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 83 HYVI--IDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKqIITVINKMDLVQYSEERFKQVQS 160
Cdd:cd01890 66 EYLLnlIDTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLE-IIPVINKIDLPAADPDRVKQEIE 144
|
170 180
....*....|....*....|....*..
gi 1189696689 161 DVqeflasIGASSDITLPIAAAKGDNI 187
Cdd:cd01890 145 DV------LGLDASEAILVSAKTGLGV 165
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
6-308 |
2.10e-23 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 102.38 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 6 NFVIVGHVDHGKSTLIGRLLydtdsLQPDRIAEMEKMSKsRGRDENEfaylldhLEEERkqGVTI--DTTQVFFSTDKRH 83
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALL-----KQSGTFRANEAVAE-RVMDSND-------LERER--GITIlaKNTAIRYNGTKIN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 84 yvIIDAPGH------VEFVKNMITGasqaeaAVLIVDAEEGVMEQTKrhsYMLNM---LGLKqIITVINKMDlvqYSEER 154
Cdd:TIGR01394 68 --IVDTPGHadfggeVERVLGMVDG------VLLLVDASEGPMPQTR---FVLKKaleLGLK-PIVVINKID---RPSAR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 155 FKQVQSDVQEFLASIGASSD-ITLPIAAAKGDN-IAK-----PSENMpwhkGPTFldslDSLKGRIPAEDKSLILPVQDV 227
Cdd:TIGR01394 133 PDEVVDEVFDLFAELGADDEqLDFPIVYASGRAgWASldlddPSDNM----APLF----DAIVRHVPAPKGDLDEPLQML 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 228 YKVDDK-----RINAGRVEAGCIEQGEAVKVIPSGQKTKVQSVEKFL--EEPERacagesigITTEDAlflDRGDIVCRE 300
Cdd:TIGR01394 205 VTNLDYdeylgRIAIGRVHRGTVKKGQQVALMKRDGTIENGRISKLLgfEGLER--------VEIDEA---GAGDIVAVA 273
|
330
....*....|....
gi 1189696689 301 G------GEpTLAD 308
Cdd:TIGR01394 274 GlediniGE-TIAD 286
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
220-296 |
8.09e-22 |
|
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: 88.78 E-value: 8.09e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189696689 220 LILPVQDVYKVD-DKRINAGRVEAGCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGESIGITTEDALFLDRGDI 296
Cdd:cd03695 1 FRFPVQYVNRPNlDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLEDEIDVSRGDL 78
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
7-188 |
3.02e-21 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 95.89 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 7 FVIVGHVDHGKSTLIgRLLYDTDSlqpdriaemekmsksrgrdenefayllDHLEEERKQGVTIDTTQVFF-STDKRHYV 85
Cdd:PRK10512 3 IATAGHVDHGKTTLL-QAITGVNA---------------------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLG 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 86 IIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIITVINKMDLVqySEERFKQVQSDVQEF 165
Cdd:PRK10512 55 FIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRV--DEARIAEVRRQVKAV 132
|
170 180
....*....|....*....|....
gi 1189696689 166 LASIGAsSDITL-PIAAAKGDNIA 188
Cdd:PRK10512 133 LREYGF-AEAKLfVTAATEGRGID 155
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
6-146 |
4.29e-20 |
|
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: 88.06 E-value: 4.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 6 NFVIVGHVDHGKSTLigrllydTDSLqpdrIAEMEKMS-KSRGRdenefAYLLDHLEEERKQGVTIDTTQV-------FF 77
Cdd:cd01885 2 NICIIAHVDHGKTTL-------SDSL----LASAGIISeKLAGK-----ARYLDTREDEQERGITIKSSAIslyfeyeEE 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189696689 78 STDKRHYVI--IDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTK---RHSYMLNMlglkQIITVINKMD 146
Cdd:cd01885 66 KMDGNDYLInlIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTEtvlRQALEERV----KPVLVINKID 135
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
10-187 |
1.46e-19 |
|
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: 86.17 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 10 VGHVDHGKSTLIGRLlydtDSLQPDRIAEMEKM----------SKSRGRDENEFAYLLDHLEEERKQGvtIDTTQVffst 79
Cdd:cd01888 6 IGHVAHGKTTLVKAL----SGVWTVRHKEELKRnitiklgyanAKIYKCPNCGCPRPYDTPECECPGC--GGETKL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 80 dKRHYVIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVME-QTKRHSYMLNMLGLKQIITVINKMDLVqySEERFKQV 158
Cdd:cd01888 76 -VRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQpQTSEHLAALEIMGLKHIIILQNKIDLV--KEEQALEN 152
|
170 180
....*....|....*....|....*....
gi 1189696689 159 QSDVQEFLASIGASSDITLPIAAAKGDNI 187
Cdd:cd01888 153 YEQIKEFVKGTIAENAPIIPISAQLKYNI 181
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
1-268 |
1.17e-18 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 87.77 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 1 MDNVLNFVIVGHVDHGKSTLIGRLLYDTDSLQpDRiaEMEkmsksrgrdenefAYLLDHLEEERKQGVTIDTTQV---FF 77
Cdd:COG0481 3 QKNIRNFSIIAHIDHGKSTLADRLLELTGTLS-ER--EMK-------------EQVLDSMDLERERGITIKAQAVrlnYK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 78 STDKRHYVI--IDAPGHVEF---VknmitgaSQA----EAAVLIVDAEEGVMEQTKRHSYM-LNMlGLKqIITVINKMDL 147
Cdd:COG0481 67 AKDGETYQLnlIDTPGHVDFsyeV-------SRSlaacEGALLVVDASQGVEAQTLANVYLaLEN-DLE-IIPVINKIDL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 148 VQYSEERFKQVQSDVqeflasIGASSDITLPIAAAKGDNIAkpsenmpwhkgptflDSLDSLKGRIPAEDKSLILPVQ-- 225
Cdd:COG0481 138 PSADPERVKQEIEDI------IGIDASDAILVSAKTGIGIE---------------EILEAIVERIPPPKGDPDAPLQal 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1189696689 226 ------DVYKvddkrinaG-----RVEAGCIEQGEAVKVIPSGQKTKVQSVEKF 268
Cdd:COG0481 197 ifdswyDSYR--------GvvvyvRVFDGTLKKGDKIKMMSTGKEYEVDEVGVF 242
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
3-194 |
1.39e-18 |
|
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: 83.03 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 3 NVLNFVIVGHVDHGKSTLIGRLLydtdslqpdriaemeKMSKSRGRDENEFAYLLDHLEEERKQGVTI--DTTQVFFSTD 80
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALL---------------KQSGTFRENEEVGERVMDSNDLERERGITIlaKNTAITYKDT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 81 KRHyvIIDAPGH------VEFVKNMITGasqaeaAVLIVDAEEGVMEQTKrhsYMLN---MLGLKqIITVINKMDlvqYS 151
Cdd:cd01891 66 KIN--IIDTPGHadfggeVERVLSMVDG------VLLLVDASEGPMPQTR---FVLKkalEAGLK-PIVVINKID---RP 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1189696689 152 EERFKQVQSDVQEFLASIGASSD-ITLPI--AAAK----GDNIAKPSENM 194
Cdd:cd01891 131 DARPEEVVDEVFDLFLELNATDEqLDFPIvyASAKngwaSLNLDDPSEDL 180
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
6-146 |
2.69e-18 |
|
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: 82.70 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 6 NFVIVGHVDHGKSTLIGRLLYDTdslqpdriaemEKMSKSRGRDENEFAYLlDHLEEERKQGVTIDTTQVFF----STDK 81
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQT-----------HKRTPSVKLGWKPLRYT-DTRKDEQERGISIKSNPISLvledSKGK 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189696689 82 RHYV-IIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKR--HSYMLNmlGLKqIITVINKMD 146
Cdd:cd04167 70 SYLInIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERliRHAIQE--GLP-MVLVINKID 134
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
9-159 |
4.80e-18 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 82.67 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 9 IVGHVDHGKSTLIGRLLYDTDSLqpdriaemekmsKSRGRDENEFAYLlDHLEEERKQGVTIDTTQVFFSTDKRHYVIID 88
Cdd:cd04168 4 ILAHVDAGKTTLTESLLYTSGAI------------RELGSVDKGTTRT-DSMELERQRGITIFSAVASFQWEDTKVNIID 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189696689 89 APGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIItVINKMDLVQYSEER-FKQVQ 159
Cdd:cd04168 71 TPGHMDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTII-FVNKIDRAGADLEKvYQEIK 141
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
2-278 |
5.19e-17 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 82.99 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 2 DNVLNFVIVGHVDHGKSTLigrllydTDSLqpdrIAEMEKMSKSRGRDenefAYLLDHLEEERKQGVTIDTTQV--FFST 79
Cdd:PRK07560 18 EQIRNIGIIAHIDHGKTTL-------SDNL----LAGAGMISEELAGE----QLALDFDEEEQARGITIKAANVsmVHEY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 80 DKRHYVI--IDAPGHVEFvKNMITGASQA-EAAVLIVDAEEGVMEQTK---RHSY---------------MLNMLGLK-- 136
Cdd:PRK07560 83 EGKEYLInlIDTPGHVDF-GGDVTRAMRAvDGAIVVVDAVEGVMPQTEtvlRQALrervkpvlfinkvdrLIKELKLTpq 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 137 -------QIITVINKmdLVQ-YSEERFK-QVQSDVQEFLASIGASSD---ITLPIAAAKG------------DNIAKPSE 192
Cdd:PRK07560 162 emqqrllKIIKDVNK--LIKgMAPEEFKeKWKVDVEDGTVAFGSALYnwaISVPMMQKTGikfkdiidyyekGKQKELAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 193 NMPWHKgpTFLD--------SLDSLKGRIPA------------------EDKSLILPVQDVyKVDD--KRINAGRVEAGC 244
Cdd:PRK07560 240 KAPLHE--VVLDmvvkhlpnPIEAQKYRIPKiwkgdlnsevgkamlncdPNGPLVMMVTDI-IVDPhaGEVATGRVFSGT 316
|
330 340 350
....*....|....*....|....*....|....*...
gi 1189696689 245 IEQGEAVKVIPSGQKTKVQSVEKFL----EEPERACAG 278
Cdd:PRK07560 317 LRKGQEVYLVGAKKKNRVQQVGIYMgperEEVEEIPAG 354
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
10-146 |
1.13e-16 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 82.10 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 10 VGHVDHGKSTLIGRLLYDTDslQPDRIAEMEkmsksrgrdenEFAYLLDHLEEERKQGVTIDTTQVFFSTDKRHYVIIDA 89
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTG--AIHRIGEVE-----------DGTTTMDFMPEERERGISITSAATTCEWKGHKINLIDT 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189696689 90 PGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIItVINKMD 146
Cdd:PRK12740 68 PGHVDFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRII-FVNKMD 123
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
6-187 |
1.22e-16 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 81.05 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 6 NFVIVGHVDHGKSTLIGRLL---YDTDSlqpdriaemekmsksrgrdenefaylldhleEERKQGVTI-----DTT---- 73
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQALTgvwTDRHS-------------------------------EELKRGITIrlgyaDATirkc 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 74 -----QVFFSTDK------------RHYVIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGV-MEQTKRHSYMLNMLGL 135
Cdd:PRK04000 60 pdceePEAYTTEPkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKEHLMALDIIGI 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1189696689 136 KQIITVINKMDLVqySEERFKQVQSDVQEFLASIGASSDITLPIAAAKGDNI 187
Cdd:PRK04000 140 KNIVIVQNKIDLV--SKERALENYEQIKEFVKGTVAENAPIIPVSALHKVNI 189
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
2-146 |
1.46e-16 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 81.63 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 2 DNVLNFVIVGHVDHGKSTLIGRLLYDTDSLqpDRIAEMEkmsksrgrdenEFAYLLDHLEEERKQGVTIDTTQVFFSTDK 81
Cdd:COG0480 7 EKIRNIGIVAHIDAGKTTLTERILFYTGAI--HRIGEVH-----------DGNTVMDWMPEEQERGITITSAATTCEWKG 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189696689 82 RHYVIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIItVINKMD 146
Cdd:COG0480 74 HKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIV-FVNKMD 137
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
1-308 |
1.48e-16 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 81.68 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 1 MDNVLNFVIVGHVDHGKSTLIGRLLYDTDSLqpDRIAEmekmSKSRGRDENEfaylldhLEEERkqGVTIDTTQVFFSTD 80
Cdd:PRK10218 2 IEKLRNIAIIAHVDHGKTTLVDKLLQQSGTF--DSRAE----TQERVMDSND-------LEKER--GITILAKNTAIKWN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 81 KRHYVIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIItVINKMDlvqYSEERFKQVQS 160
Cdd:PRK10218 67 DYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIV-VINKVD---RPGARPDWVVD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 161 DVQEFLASIGASSD-ITLPIAAAKGDN--IAKPSENMPWHKGPTFLDSLDslkgRIPAEDKSLILPVQ-DVYKVDDKR-- 234
Cdd:PRK10218 143 QVFDLFVNLDATDEqLDFPIVYASALNgiAGLDHEDMAEDMTPLYQAIVD----HVPAPDVDLDGPFQmQISQLDYNSyv 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189696689 235 --INAGRVEAGCIEQGEAVKVIPSGQKTKVQSVEKFLEEperacagesIGITTEDALFLDRGDIVCREG-GEPTLAD 308
Cdd:PRK10218 219 gvIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLGH---------LGLERIETDLAEAGDIVAITGlGELNISD 286
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
9-189 |
1.86e-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: 76.36 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 9 IVGHVDHGKSTLIgrllydtDSLQPDRIAEMEKmsksrGrdenefaylldhleeerkqGVT--IDTTQVFFSTDKRHYVI 86
Cdd:cd01887 5 VMGHVDHGKTTLL-------DKIRKTNVAAGEA-----G-------------------GITqhIGAYQVPIDVKIPGITF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 87 IDAPGHVEFvKNMIT-GASQAEAAVLIVDAEEGVMEQTK---RHSYMLNmlglKQIITVINKMDL---VQYSEERFKQVQ 159
Cdd:cd01887 54 IDTPGHEAF-TNMRArGASVTDIAILVVAADDGVMPQTIeaiNHAKAAN----VPIIVAINKIDKpygTEADPERVKNEL 128
|
170 180 190
....*....|....*....|....*....|
gi 1189696689 160 SDVQEFLASIGASSdITLPIAAAKGDNIAK 189
Cdd:cd01887 129 SELGLVGEEWGGDV-SIVPISAKTGEGIDD 157
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
1-284 |
4.67e-16 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 80.06 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 1 MDNVLNFVIVGHVDHGKSTLIGRLLYDTDSL-----QPDRIaeMekmsksrgrDENEfaylldhLEEERkqGVTI--DTT 73
Cdd:COG1217 3 REDIRNIAIIAHVDHGKTTLVDALLKQSGTFrenqeVAERV--M---------DSND-------LERER--GITIlaKNT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 74 QVffstdkrHYV-----IIDAPGH------VEFVKNMITGasqaeaAVLIVDAEEGVMEQTK---RHSymLNmLGLKqII 139
Cdd:COG1217 63 AV-------RYKgvkinIVDTPGHadfggeVERVLSMVDG------VLLLVDAFEGPMPQTRfvlKKA--LE-LGLK-PI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 140 TVINKMDlvqYSEERFKQVQSDVQEFLASIGASSD-ITLPI--AAAK----GDNIAKPSENMpwhkGPTFldslDSLKGR 212
Cdd:COG1217 126 VVINKID---RPDARPDEVVDEVFDLFIELGATDEqLDFPVvyASARngwaSLDLDDPGEDL----TPLF----DTILEH 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 213 IPA----EDKSLILPVQDV-YkvDD--KRINAGRVEAGCIEQGEAVKVIPSG---QKTKVQSVEKFL----EEPERACAG 278
Cdd:COG1217 195 VPApevdPDGPLQMLVTNLdY--SDyvGRIAIGRIFRGTIKKGQQVALIKRDgkvEKGKITKLFGFEglerVEVEEAEAG 272
|
....*.
gi 1189696689 279 ESIGIT 284
Cdd:COG1217 273 DIVAIA 278
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
6-184 |
7.60e-16 |
|
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: 76.86 E-value: 7.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 6 NFVIVGHVDHGKSTLIGRLLYDTDSLqpDRiaemekmsksRGRDENEFAyLLDHLEEERKQGVTIDTTQVFFSTDKRHYV 85
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAI--DR----------LGRVEDGNT-VSDYDPEEKKRKMSIETSVAPLEWNGHKIN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 86 IIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIItVINKMDlvqysEERfkqvqSDVQEF 165
Cdd:cd04170 68 LIDTPGYADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRII-FINKMD-----RAR-----ADFDKT 136
|
170 180
....*....|....*....|....
gi 1189696689 166 LASIGASSD-----ITLPIAAAKG 184
Cdd:cd04170 137 LAALREAFGrpvvpIQLPIGEGDE 160
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
1-158 |
4.54e-15 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 76.91 E-value: 4.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 1 MDNVLNFVIVGHVDHGKSTLIGRLLYDTDSLQpdRIAEMEKmsksrGRDENEFaylldhLEEERKQGVTIDTTQVFFSTD 80
Cdd:PRK13351 5 LMQIRNIGILAHIDAGKTTLTERILFYTGKIH--KMGEVED-----GTTVTDW------MPQEQERGITIESAATSCDWD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 81 KRHYVIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIItVINKMD--------LVQYSE 152
Cdd:PRK13351 72 NHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLI-FINKMDrvgadlfkVLEDIE 150
|
....*.
gi 1189696689 153 ERFKQV 158
Cdd:PRK13351 151 ERFGKR 156
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
6-188 |
4.20e-14 |
|
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: 70.47 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 6 NFVIVGHVDHGKSTLIGRLlydtdslqpdriaeMEKMSKSRgrdenefaylLDHLEEERKQGVTIDTTQVFFSTDKRHYV 85
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKAL--------------SEIASTAA----------FDKNPQSQERGITLDLGFSSFEVDKPKHL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 86 I--------------IDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGlKQIITVINKMDLVQYS 151
Cdd:cd01889 58 EdnenpqienyqitlVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLC-KPLIVVLNKIDLIPEE 136
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189696689 152 E--ERFKQVQSDVQE-FLASIGASSDItLPIAAAKGDNIA 188
Cdd:cd01889 137 ErkRKIEKMKKRLQKtLEKTRLKDSPI-IPVSAKPGEGEA 175
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
8-187 |
2.04e-12 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 65.00 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 8 VIVGHVDHGKSTLIGRLLYDTDSLQpdriaemekmsksrgrdenefAYLLDHleeerkqGVTIDTTQVFFSTDKRHYVII 87
Cdd:COG1100 7 VVVGTGGVGKTSLVNRLVGDIFSLE---------------------KYLSTN-------GVTIDKKELKLDGLDVDLVIW 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 88 DAPGHVEF------VKNMITGASqaeAAVLIVDaeeGVMEQTKRHSYM----LNMLGLK-QIITVINKMDLVqysEERFK 156
Cdd:COG1100 59 DTPGQDEFretrqfYARQLTGAS---LYLFVVD---GTREETLQSLYEllesLRRLGKKsPIILVLNKIDLY---DEEEI 129
|
170 180 190
....*....|....*....|....*....|.
gi 1189696689 157 QVQSDVQEFLASIGASSDItlPIAAAKGDNI 187
Cdd:COG1100 130 EDEERLKEALSEDNIVEVV--ATSAKTGEGV 158
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
81-187 |
4.07e-12 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 67.34 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 81 KRHYVIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVME-QTKRHSYMLNMLGLKQIITVINKMDLVqySEERFKQVQ 159
Cdd:PTZ00327 116 KRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQpQTSEHLAAVEIMKLKHIIILQNKIDLV--KEAQAQDQY 193
|
90 100
....*....|....*....|....*...
gi 1189696689 160 SDVQEFLASIGASSDITLPIAAAKGDNI 187
Cdd:PTZ00327 194 EEIRNFVKGTIADNAPIIPISAQLKYNI 221
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
2-146 |
1.73e-11 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 66.23 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 2 DNVLNFVIVGHVDHGKSTLigrllydTDSL-QPDRIAEMEKMSKSRgrdenefayLLDHLEEERKQGVTIDTTQV--FFS 78
Cdd:PTZ00416 17 DQIRNMSVIAHVDHGKSTL-------TDSLvCKAGIISSKNAGDAR---------FTDTRADEQERGITIKSTGIslYYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 79 TD------KRHYVI--IDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHsymlnmlgLKQIIT-------VIN 143
Cdd:PTZ00416 81 HDledgddKQPFLInlIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETV--------LRQALQerirpvlFIN 152
|
...
gi 1189696689 144 KMD 146
Cdd:PTZ00416 153 KVD 155
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
9-187 |
2.82e-11 |
|
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: 65.17 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 9 IVGHVDHGKSTLIgrllydtDSLQPDRIAEMEkmskSRGRDENEFAYlldHLEEERKQGVTidttqvffstdkrhyvIID 88
Cdd:TIGR00487 92 IMGHVDHGKTSLL-------DSIRKTKVAQGE----AGGITQHIGAY---HVENEDGKMIT----------------FLD 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 89 APGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTK---RHSYMLNMlglkQIITVINKMDLVQYSEERFKQVQSDVQEF 165
Cdd:TIGR00487 142 TPGHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIeaiSHAKAANV----PIIVAINKIDKPEANPDRVKQELSEYGLV 217
|
170 180
....*....|....*....|..
gi 1189696689 166 LASIGASSdITLPIAAAKGDNI 187
Cdd:TIGR00487 218 PEDWGGDT-IFVPVSALTGDGI 238
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
220-298 |
3.04e-11 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 59.20 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 220 LILPVQDVYKVDDK-RINAGRVEAGCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGESIGITTEDALFLDRGDIVC 298
Cdd:cd01342 1 LVMQVFKVFYIPGRgRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGVKDILTGDTLT 80
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
6-146 |
9.88e-11 |
|
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: 61.84 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 6 NFVIVGHVDHGKSTLIGRLLYdtdslqpdrIAEMEKMSKS-RGRDENEFAyLLDHLEEERKQGVTIDTTQVFFSTDKRHY 84
Cdd:cd04169 4 TFAIISHPDAGKTTLTEKLLL---------FGGAIQEAGAvKARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVI 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189696689 85 VIIDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKqIITVINKMD 146
Cdd:cd04169 74 NLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLD 134
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-156 |
1.26e-10 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 63.20 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 1 MD---NVLNFVIVGHVDHGKSTLigrllydTDSLqpdrIAEMEKMSKSRGRDenefAYLLDHLEEERKQGVTIDTTQV-- 75
Cdd:PLN00116 13 MDkkhNIRNMSVIAHVDHGKSTL-------TDSL----VAAAGIIAQEVAGD----VRMTDTRADEAERGITIKSTGIsl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 76 FF------------STDKRHYVI--IDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKrhSYMLNMLG--LKQII 139
Cdd:PLN00116 78 YYemtdeslkdfkgERDGNEYLInlIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTE--TVLRQALGerIRPVL 155
|
170 180
....*....|....*....|..
gi 1189696689 140 TViNKMD-----LVQYSEERFK 156
Cdd:PLN00116 156 TV-NKMDrcfleLQVDGEEAYQ 176
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
3-169 |
3.21e-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: 58.60 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 3 NVLNFVIVGHVDHGKSTLIGRLLydtdslqpdriaemekmsksrgrdenefaylldhlEEER-----KQGVTIDTTQVFF 77
Cdd:cd01895 1 DPIKIAIIGRPNVGKSSLLNALL-----------------------------------GEERvivsdIAGTTRDSIDVPF 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 78 STDKRHYVIIDAPG---------HVEF--VKNMITGASQAEAAVLIVDAEEGVMEQTKRhsymlnMLGL-----KQIITV 141
Cdd:cd01895 46 EYDGQKYTLIDTAGirkkgkvteGIEKysVLRTLKAIERADVVLLVLDASEGITEQDLR------IAGLileegKALIIV 119
|
170 180
....*....|....*....|....*...
gi 1189696689 142 INKMDLVQYSEERFKQVQSDVQEFLASI 169
Cdd:cd01895 120 VNKWDLVEKDEKTMKEFEKELRRKLPFL 147
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
217-304 |
1.75e-09 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 54.50 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 217 DKSLILPVQDVYKV-DDKRINAGRVEAGCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGESIG-----ITTEDalf 290
Cdd:cd03693 2 DKPLRLPIQDVYKIgGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGfnvkgVSVKD--- 78
|
90
....*....|....
gi 1189696689 291 LDRGDiVCREGGEP 304
Cdd:cd03693 79 IKRGD-VAGDSKND 91
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
9-194 |
2.28e-08 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 55.99 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 9 IVGHVDHGKSTLIgrllydtDSLQPDRIAEMEK--MSKSRGRDENEFAYlldhleeerkqgvtidttqvffSTDKRHYVI 86
Cdd:CHL00189 249 ILGHVDHGKTTLL-------DKIRKTQIAQKEAggITQKIGAYEVEFEY----------------------KDENQKIVF 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 87 IDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRhsyMLNMLGLKQ--IITVINKMDLVQYSEERFKQVQSDVQE 164
Cdd:CHL00189 300 LDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIE---AINYIQAANvpIIVAINKIDKANANTERIKQQLAKYNL 376
|
170 180 190
....*....|....*....|....*....|
gi 1189696689 165 FLASIGASSDItLPIAAAKGDNIAKPSENM 194
Cdd:CHL00189 377 IPEKWGGDTPM-IPISASQGTNIDKLLETI 405
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
6-146 |
3.21e-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: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 6 NFVIVGHVDHGKSTLIGRLLYDTDslqpdRIAemeKMSKSRGRDEnefayLLDHLEEERKQGVTIDTTQVFFSTDKRHYV 85
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTG-----RIH---KIGEVHGGGA-----TMDWMEQERERGITIQSAATTCFWKDHRIN 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 86 IIDAPGHVEFVknmitgasqAE---------AAVLIVDAEEGVMEQTKRHSYMLNMLGLKQIItVINKMD 146
Cdd:cd01886 68 IIDTPGHVDFT---------IEverslrvldGAVAVFDAVAGVQPQTETVWRQADRYGVPRIA-FVNKMD 127
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
8-187 |
8.30e-08 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 51.30 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 8 VIVGHVDHGKSTLIGRLLYDtdslqpdriaemekmsksrgrdenefayllDHLEEERKQGVTIDTTQVFFSTD--KRHYV 85
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGG------------------------------EVGEVSDVPGTTRDPDVYVKELDkgKVKLV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 86 IIDAPGHVEFVKNMITG-----ASQAEAAVLIVDAEEGVMEQTKRHSYMLNMLGLKQ-IITVINKMDLVQYSEERfkqvQ 159
Cdd:cd00882 51 LVDTPGLDEFGGLGREElarllLRGADLILLVVDSTDRESEEDAKLLILRRLRKEGIpIILVGNKIDLLEEREVE----E 126
|
170 180
....*....|....*....|....*...
gi 1189696689 160 SDVQEFLASIGASSdiTLPIAAAKGDNI 187
Cdd:cd00882 127 LLRLEELAKILGVP--VFEVSAKTGEGV 152
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
6-187 |
8.71e-08 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 51.60 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 6 NFVIVGHVDHGKSTLIGRLLYDTDSlqpdriaemekmsksrgrdenefaylldhlEEERKQGVTIDTTQVFFSTDKRHYV 85
Cdd:TIGR00231 3 KIVIVGHPNVGKSTLLNSLLGNKGS------------------------------ITEYYPGTTRNYVTTVIEEDGKTYK 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 86 --IIDAPGHVEFVKNMITGASQAEA-------AVLIVDAEEGVMEQTK--RHSYMLNmlglKQIITVINKMDLvqyseeR 154
Cdd:TIGR00231 53 fnLLDTAGQEDYDAIRRLYYPQVERslrvfdiVILVLDVEEILEKQTKeiIHHADSG----VPIILVGNKIDL------K 122
|
170 180 190
....*....|....*....|....*....|...
gi 1189696689 155 FKQVQSDVQEFLASIGASSDItlPIAAAKGDNI 187
Cdd:TIGR00231 123 DADLKTHVASEFAKLNGEPII--PLSAETGKNI 153
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
307-407 |
1.78e-07 |
|
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: 48.93 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 307 ADCFRARIFWMSK-RPLDTSERLFIRCATQQTRCSIDTIEKRIDSSTLKvlEENGTKLENLEVGEVIIKTKKEIAFDDFN 385
Cdd:cd01513 3 VWKFDAKVIVLEHpKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE--KKPPDSLQPGENGTVEVELQKPVVLERGK 80
|
90 100
....*....|....*....|..
gi 1189696689 386 STQEMGRFVLVKDENIVAGGII 407
Cdd:cd01513 81 EFPTLGRFALRDGGRTVGAGLI 102
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
8-144 |
5.71e-07 |
|
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: 48.00 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 8 VIVGHVDHGKSTLIGRLLydtdslqpDRIAEMEKMSksrgrdenefaylldhleeerkqGVTIDTTQVFFSTDKRHYVII 87
Cdd:pfam01926 3 ALVGRPNVGKSTLINALT--------GAKAIVSDYP-----------------------GTTRDPNEGRLELKGKQIILV 51
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189696689 88 DAPGHVE--FVKNMITGA----SQAEAAVLIVDAEEGVMEQTKRhsyMLNMLG--LKQIITVINK 144
Cdd:pfam01926 52 DTPGLIEgaSEGEGLGRAflaiIEADLILFVVDSEEGITPLDEE---LLELLRenKKPIILVLNK 113
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
222-298 |
7.16e-07 |
|
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: 46.74 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 222 LPVQDVYKVDDKRIN-AGRVEAGCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGE--SIGITTEDALFLDRGDIVC 298
Cdd:cd16267 4 LSVSDVFKGQGSGFTvSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDnvTLTLTGIDPNHLRVGSILC 83
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
2-167 |
8.42e-07 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 50.82 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 2 DNVLNFVIVGHVDHGKSTLIGRLLydtdslqpdriaemekmsksrGrdenefaylldhleEER-----KQGVTIDTTQVF 76
Cdd:PRK00093 171 DEPIKIAIIGRPNVGKSSLINALL---------------------G--------------EERvivsdIAGTTRDSIDTP 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 77 FSTDKRHYVIIDAPG---------HVEFVKNMITGAS--QAEAAVLIVDAEEGVMEQTKRhsymlnMLGL-----KQIIT 140
Cdd:PRK00093 216 FERDGQKYTLIDTAGirrkgkvteGVEKYSVIRTLKAieRADVVLLVIDATEGITEQDLR------IAGLaleagRALVI 289
|
170 180
....*....|....*....|....*..
gi 1189696689 141 VINKMDLVqySEERFKQVQSDVQEFLA 167
Cdd:PRK00093 290 VVNKWDLV--DEKTMEEFKKELRRRLP 314
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
2-167 |
2.46e-06 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 49.25 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 2 DNVLNFVIVGHVDHGKSTLIGRLLydtdslqpdriaemekmsksrgrdenefaylldhlEEER-----KQGVTIDTTQVF 76
Cdd:COG1160 173 DDPIKIAIVGRPNVGKSSLINALL-----------------------------------GEERvivsdIAGTTRDSIDTP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 77 FSTDKRHYVIIDAPG---------HVEFVKNMITGAS--QAEAAVLIVDAEEGVMEQTKRhsymlnMLGL-----KQIIT 140
Cdd:COG1160 218 FERDGKKYTLIDTAGirrkgkvdeGIEKYSVLRTLRAieRADVVLLVIDATEGITEQDLK------IAGLaleagKALVI 291
|
170 180
....*....|....*....|....*..
gi 1189696689 141 VINKMDLVQYSEERFKQVQSDVQEFLA 167
Cdd:COG1160 292 VVNKWDLVEKDRKTREELEKEIRRRLP 318
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
9-157 |
1.06e-05 |
|
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: 47.32 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 9 IVGHVDHGKSTLIgrllydtDSLQPDRIAEMEKmsksrGrdenefaylldhleeerkqGVT--IDTTQVffSTDKRHYVI 86
Cdd:COG0532 9 VMGHVDHGKTSLL-------DAIRKTNVAAGEA-----G-------------------GITqhIGAYQV--ETNGGKITF 55
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189696689 87 IDAPGHVEFVKNMITGASQAEAAVLIVDAEEGVMEQTK---RHSymlnmlglKQ----IITVINKMDLVQYSEERFKQ 157
Cdd:COG0532 56 LDTPGHEAFTAMRARGAQVTDIVILVVAADDGVMPQTIeaiNHA--------KAagvpIIVAINKIDKPGANPDRVKQ 125
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
8-187 |
1.56e-05 |
|
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: 44.93 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 8 VIVGHVDHGKSTLIGRLLYDTdslqpdrIAEMEKMSksrgrdenefaylldhleeerkqGVTIDTTQVFFSTD-KRHYVI 86
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLGQN-------VGIVSPIP-----------------------GTTRDPVRKEWELLpLGPVVL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 87 IDAPG-------HVEFVKNMITGASQAEAAVLIVDAEEGVMEQTKRHsYMLNMLGLKQIItVINKMDLVQYSEERFKQVQ 159
Cdd:cd00880 51 IDTPGldeegglGRERVEEARQVADRADLVLLVVDSDLTPVEEEAKL-GLLRERGKPVLL-VLNKIDLVPESEEEELLRE 128
|
170 180
....*....|....*....|....*...
gi 1189696689 160 SDVQEFLAsigasSDItLPIAAAKGDNI 187
Cdd:cd00880 129 RKLELLPD-----LPV-IAVSALPGEGI 150
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
6-146 |
1.24e-04 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 43.97 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 6 NFVIVGHVDHGKSTLIGRLLYDTDSLQpdrIAEMEKmsksrGRDENEFAyLLDHLEEERKQGVTIDTTQVFFstDKRHYV 85
Cdd:PRK00741 12 TFAIISHPDAGKTTLTEKLLLFGGAIQ---EAGTVK-----GRKSGRHA-TSDWMEMEKQRGISVTSSVMQF--PYRDCL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189696689 86 I--IDAPGHVEFvknmitgaSQ--------AEAAVLIVDAEEGVMEQTKRhsyMLNMLGLKQ--IITVINKMD 146
Cdd:PRK00741 81 InlLDTPGHEDF--------SEdtyrtltaVDSALMVIDAAKGVEPQTRK---LMEVCRLRDtpIFTFINKLD 142
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
220-298 |
2.95e-04 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 39.41 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 220 LILPVQDVYKVDDKRINAGRVEAGCIEQGEAVKVIPSGQKTKVQSV-EKFLEEPERACAGESI-----GITTEDalfLDR 293
Cdd:cd03698 2 FRLSIDDKYKSPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIiRNSDEETDWAIAGDTVtlrlrGIEVED---IQP 78
|
....*
gi 1189696689 294 GDIVC 298
Cdd:cd03698 79 GDILS 83
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
68-187 |
3.40e-04 |
|
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: 40.91 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 68 VTIDTTQVffstdkrhyVIIDAPGHVE--------FVKNMITGASQAEAAVLIVDAEEGVmeqTKRHSYMLNML-GLKQ- 137
Cdd:cd04163 46 YTDDDAQI---------IFVDTPGIHKpkkklgerMVKAAWSALKDVDLVLFVVDASEWI---GEGDEFILELLkKSKTp 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1189696689 138 IITVINKMDLVQYSEERFKQVqsdvqEFLASIGASSDItLPIAAAKGDNI 187
Cdd:cd04163 114 VILVLNKIDLVKDKEDLLPLL-----EKLKELHPFAEI-FPISALKGENV 157
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
220-299 |
4.67e-04 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 38.62 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 220 LILPVQDVYKvdDKRINA-GRVEAGCIEQGEAVKVIPSGQKTKVQSVEKFLEEPERACAGESI-----GITTEDalfLDR 293
Cdd:cd04089 2 LRMPILDKYK--DMGTVVmGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVklklkGVEEED---ISP 76
|
....*.
gi 1189696689 294 GDIVCR 299
Cdd:cd04089 77 GFVLCS 82
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
328-407 |
7.29e-04 |
|
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to ribosomes. EF-1 is composed of four subunits: the alpha chain, which binds GTP and aminoacyl-tRNAs; the gamma chain that probably plays a role in anchoring the complex to other cellular components; and the beta and delta (or beta') chains. This model represents the alpha subunit, which is the counterpart of bacterial EF-Tu for archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha).
Pssm-ID: 294004 [Multi-domain] Cd Length: 104 Bit Score: 38.71 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 328 LFIRCAtqQTRCSIDTIEKRIDSSTLKVLEENGTKLENLEVGEVIIKTKKEIAFDDFNSTQEMGRFvLVKDEN-IVAGGI 406
Cdd:cd03705 27 LDCHTA--HVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVETFSEYPPLGRF-AVRDMRqTVAVGV 103
|
.
gi 1189696689 407 I 407
Cdd:cd03705 104 I 104
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
68-187 |
1.20e-03 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 40.42 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 68 VTIDTTQVffstdkrhyVIIDAPG-HV------EF-VKNMITGASQAEAAVLIVDAEEGVMEQTKrhsYMLNMLGLKQI- 138
Cdd:PRK00089 48 VTEDDAQI---------IFVDTPGiHKpkralnRAmNKAAWSSLKDVDLVLFVVDADEKIGPGDE---FILEKLKKVKTp 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1189696689 139 -ITVINKMDLVQYSEERFKQVQsdvqeFLASIGASSDItLPIAAAKGDNI 187
Cdd:PRK00089 116 vILVLNKIDLVKDKEELLPLLE-----ELSELMDFAEI-VPISALKGDNV 159
|
|
| PRK04213 |
PRK04213 |
GTP-binding protein EngB; |
64-185 |
6.57e-03 |
|
GTP-binding protein EngB;
Pssm-ID: 179790 [Multi-domain] Cd Length: 201 Bit Score: 37.59 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189696689 64 RKQGVTIDTTQVffstDKRHYVIIDAPG----------HVEFVKNMI-----TGASQAEAAVLIVDAeEGVMEQTKRHS- 127
Cdd:PRK04213 38 KRPGVTRKPNHY----DWGDFILTDLPGfgfmsgvpkeVQEKIKDEIvryieDNADRILAAVLVVDG-KSFIEIIERWEg 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189696689 128 -----------YMLNMLGLKQIItVINKMDLVQYSEERFKQVqSDVQEFLASIGASSDITLPIAAAKGD 185
Cdd:PRK04213 113 rgeipidvemfDFLRELGIPPIV-AVNKMDKIKNRDEVLDEI-AERLGLYPPWRQWQDIIAPISAKKGG 179
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
371-408 |
8.62e-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: 35.98 E-value: 8.62e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1189696689 371 VIIKTKKEIAFDDFNSTQEMGRFVLVKDENIVAGGIIT 408
Cdd:cd04093 70 VEIELERPIPLETFKDNKELGRFVLRRGGETIAAGIVT 107
|
|
| |
