|
Name |
Accession |
Description |
Interval |
E-value |
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
242-669 |
7.86e-141 |
|
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: 417.80 E-value: 7.86e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 242 ADQKSHIHMIVIGHVDAGKSTLMGHLLYDTGNVSQRVMHKHEQESKKLGKQSFMYAWVLDETGEERARGITMDVGQSRIE 321
Cdd:COG5256 2 ASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 322 TKTKIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGefesgfeLGGQTREHAILVRSLGVNQLGVVINKLDTVGWS 401
Cdd:COG5256 82 TDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDG-------VMGQTREHAFLARTLGINQLIVAVNKMDAVNYS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 402 QDRFTEIVTKLKSFLKLAGFKDSDVSFTPCSGLTGENLTKKAQEpalTNWYSGRHLLDVIENFKIPERAIDRPLRMSVSD 481
Cdd:COG5256 155 EKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDN---MPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 482 IYKGTGSGFCISGRVETGVLCLNDKVLVGASREQAQVKSLTMNEFPQTCVFAGDQVSVTLPALDINNVTVGCIISDPQTP 561
Cdd:COG5256 232 VYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 562 IPVTTRFQARIIVFNVKVPITMGF-PVLLHHQSliepAVVCKLTASIHK---STGEVVKKKPRCLGNNSCALVELETSRP 637
Cdd:COG5256 312 PTVAEEFTAQIVVLQHPSAITVGYtPVFHVHTA----QVACTFVELVSKldpRTGQVKEENPQFLKTGDAAIVKIKPTKP 387
|
410 420 430
....*....|....*....|....*....|..
gi 45550900 638 ICIERYADFKELGRVMLRVAGVTIAAGMVTKI 669
Cdd:COG5256 388 LVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
242-669 |
1.89e-134 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 401.61 E-value: 1.89e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 242 ADQKSHIHMIVIGHVDAGKSTLMGHLLYDTGNVSQRVMHKHEQESKKLGKQSFMYAWVLDETGEERARGITMDVGQSRIE 321
Cdd:PRK12317 1 AKEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 322 TKTKIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEfesGFElgGQTREHAILVRSLGVNQLGVVINKLDTVGWS 401
Cdd:PRK12317 81 TDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAG---GVM--PQTREHVFLARTLGINQLIVAINKMDAVNYD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 402 QDRFTEIVTKLKSFLKLAGFKDSDVSFTPCSGLTGENLTKKAQEpalTNWYSGRHLLDVIENFKIPERAIDRPLRMSVSD 481
Cdd:PRK12317 156 EKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSEN---MPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 482 IYKGTGSGFCISGRVETGVLCLNDKVLVGASREQAQVKSLTMN--EFPQTcvFAGDQVSVTLPALDINNVTVGCIISDPQ 559
Cdd:PRK12317 233 VYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHheELPQA--EPGDNIGFNVRGVGKKDIKRGDVCGHPD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 560 TPIPVTTRFQARIIVFNVKVPITMGF-PVLLHHQSLIePAVVCKLTASIHKSTGEVVKKKPRCLGNNSCALVELETSRPI 638
Cdd:PRK12317 311 NPPTVAEEFTAQIVVLQHPSAITVGYtPVFHAHTAQV-ACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPL 389
|
410 420 430
....*....|....*....|....*....|.
gi 45550900 639 CIERYADFKELGRVMLRVAGVTIAAGMVTKI 669
Cdd:PRK12317 390 VIEKVKEIPQLGRFAIRDMGQTIAAGMVIDV 420
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
249-468 |
1.56e-128 |
|
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: 378.37 E-value: 1.56e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 249 HMIVIGHVDAGKSTLMGHLLYDTGNVSQRVMHKHEQESKKLGKQSFMYAWVLDETGEERARGITMDVGQSRIETKTKIVT 328
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 329 LLDAPGHKDFIPNMISGATQADVALLVVDATRGEFESGFELGGQTREHAILVRSLGVNQLGVVINKLD--TVGWSQDRFT 406
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDdvTVNWSQERYD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45550900 407 EIVTKLKSFLKLAGFKDSDVSFTPCSGLTGENLTKKaqePALTNWYSGRHLLDVIENFKIPE 468
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEK---SENMPWYKGPTLLEALDSLEPPE 219
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
244-669 |
1.64e-124 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 376.78 E-value: 1.64e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 244 QKSHIHMIVIGHVDAGKSTLMGHLLYDTGNVSQRVMHKHEQESKKLGKQSFMYAWVLDETGEERARGITMDVGQSRIETK 323
Cdd:PTZ00141 4 EKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 324 TKIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFESGFELGGQTREHAILVRSLGVNQLGVVINKLD--TVGWS 401
Cdd:PTZ00141 84 KYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 402 QDRFTEIVTKLKSFLKLAGFKDSDVSFTPCSGLTGENLTKKAQEpalTNWYSGRHLLDVIENFKIPERAIDRPLRMSVSD 481
Cdd:PTZ00141 164 QERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDN---MPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 482 IYKGTGSGFCISGRVETGVLCLNDKVLVGASREQAQVKSLTMNEFPQTCVFAGDQVSVTLPALDINNVTVGCIISDPQT- 560
Cdd:PTZ00141 241 VYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNd 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 561 PIPVTTRFQARIIVFNVKVPITMGF-PVLLHHQSLIepavVCK---LTASIHKSTGEVVKKKPRCLGNNSCALVELETSR 636
Cdd:PTZ00141 321 PAKECADFTAQVIVLNHPGQIKNGYtPVLDCHTAHI----ACKfaeIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTK 396
|
410 420 430
....*....|....*....|....*....|...
gi 45550900 637 PICIERYADFKELGRVMLRVAGVTIAAGMVTKI 669
Cdd:PTZ00141 397 PMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSV 429
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
244-669 |
7.48e-92 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 292.38 E-value: 7.48e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 244 QKSHIHMIVIGHVDAGKSTLMGHLLYDTGNVSQRVMHKHEQESKKLGKQSFMYAWVLDETGEERARGITMDVGQSRIETK 323
Cdd:PLN00043 4 EKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 324 TKIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFESGFELGGQTREHAILVRSLGVNQLGVVINKLD--TVGWS 401
Cdd:PLN00043 84 KYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDatTPKYS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 402 QDRFTEIVTKLKSFLKLAGFKDSDVSFTPCSGLTGENLTKKAQEpalTNWYSGRHLLDVIENFKIPERAIDRPLRMSVSD 481
Cdd:PLN00043 164 KARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTN---LDWYKGPTLLEALDQINEPKRPSDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 482 IYKGTGSGFCISGRVETGVLCLNDKVLVGASREQAQVKSLTMNEFPQTCVFAGDQVSVTLPALDINNVTVGCIISDPQT- 560
Cdd:PLN00043 241 VYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDd 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 561 PIPVTTRFQARIIVFNVKVPITMGF-PVLLHHQSLIEPAVVCKLTaSIHKSTGEVVKKKPRCLGNNSCALVELETSRPIC 639
Cdd:PLN00043 321 PAKEAANFTSQVIIMNHPGQIGNGYaPVLDCHTSHIAVKFAEILT-KIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMV 399
|
410 420 430
....*....|....*....|....*....|
gi 45550900 640 IERYADFKELGRVMLRVAGVTIAAGMVTKI 669
Cdd:PLN00043 400 VETFSEYPPLGRFAVRDMRQTVAVGVIKSV 429
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
242-667 |
1.01e-83 |
|
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: 270.42 E-value: 1.01e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 242 ADQKSHIHM-----IVIGHVDAGKSTLMGHLLYDTGNVSQRVMHKHEQESKKLGKQSFMYAWVLDETGEERARGITMDVG 316
Cdd:COG2895 7 AYLAQHENKdllrfITCGSVDDGKSTLIGRLLYDTKSIFEDQLAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 317 QSRIETKTKIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQLGVVINKLD 396
Cdd:COG2895 87 YRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 397 TVGWSQDRFTEIVTKLKSFLKLAGFKdsDVSFTPCSGLTGENLTKKAQEpalTNWYSGRHLLDVIENFKIPERAIDRPLR 476
Cdd:COG2895 160 LVDYSEEVFEEIVADYRAFAAKLGLE--DITFIPISALKGDNVVERSEN---MPWYDGPTLLEHLETVEVAEDRNDAPFR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 477 MSVSDIYKGTgSGFCI-SGRVETGVLCLNDKVLVGASREQAQVKS-LTMNEfPQTCVFAGDQVSVTL-PALDINNvtvGC 553
Cdd:COG2895 235 FPVQYVNRPN-LDFRGyAGTIASGTVRVGDEVVVLPSGKTSTVKSiVTFDG-DLEEAFAGQSVTLTLeDEIDISR---GD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 554 IISDPQTPIPVTTRFQARIIVFNVKvPITMGFPVLLHHQSLIEPAVVCKLTASIHKSTGEvvKKKPRCLGNNSCALVELE 633
Cdd:COG2895 310 VIVAADAPPEVADQFEATLVWMDEE-PLLPGRKYLLKHGTRTVRATVTAIKYRIDVNTLE--HEAADSLELNDIGRVTLR 386
|
410 420 430
....*....|....*....|....*....|....*.
gi 45550900 634 TSRPICIERYADFKELGRVML--RVAGVTIAAGMVT 667
Cdd:COG2895 387 LAEPIAFDPYADNRATGSFILidRLTNATVGAGMIR 422
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
243-667 |
2.07e-56 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 202.47 E-value: 2.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 243 DQKSHIHMIVIGHVDAGKSTLMGHLLYDtgnvSQRVMHKH----EQESKKLGKQS--FMYAWVLDETGEERARGITMDVG 316
Cdd:PRK05506 20 ERKSLLRFITCGSVDDGKSTLIGRLLYD----SKMIFEDQlaalERDSKKVGTQGdeIDLALLVDGLAAEREQGITIDVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 317 QSRIET-KTK-IVTllDAPGHKDFIPNMISGATQADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQLGVVINK 394
Cdd:PRK05506 96 YRYFATpKRKfIVA--DTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 395 LDTVGWSQDRFTEIVTKLKSFLKLAGFkdSDVSFTPCSGLTGENLTKKAqepALTNWYSGRHLLDVIENFKIPERAIDRP 474
Cdd:PRK05506 167 MDLVDYDQEVFDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRS---ARMPWYEGPSLLEHLETVEIASDRNLKD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 475 LRMSVSDIYKGTGS--GFciSGRVETGVLCLNDKVLVGASREQAQVKSLTMNEFPQTCVFAGDQVSVTLpALDInNVTVG 552
Cdd:PRK05506 242 FRFPVQYVNRPNLDfrGF--AGTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTL-ADEI-DISRG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 553 CIISDPQTPIPVTTRFQARIIVFNvKVPITMGFPVLLHHQSLIEPAVVCKLTASIHKSTGEvvKKKPRCLGNNSCALVEL 632
Cdd:PRK05506 318 DMLARADNRPEVADQFDATVVWMA-EEPLLPGRPYLLKHGTRTVPASVAAIKYRVDVNTLE--RLAAKTLELNEIGRCNL 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 45550900 633 ETSRPICIERYADFKELGRVML--RVAGVTIAAGMVT 667
Cdd:PRK05506 395 STDAPIAFDPYARNRTTGSFILidRLTNATVGAGMID 431
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
245-440 |
1.05e-55 |
|
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: 187.73 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 245 KSHIHMIVIGHVDAGKSTLMGHLLYDTGNVSQRVMHKHEQESkklgkqsfmyawVLDETGEERARGITMDVGQSRIETKT 324
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 325 KIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGefesgfeLGGQTREHAILVRSLGVNQLgVVINKLDTVgwSQDR 404
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVPII-VFINKMDRV--DGAE 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 45550900 405 FTEIVTKLKS-FLKLAGFKDSDVSFTPCSGLTGENLT 440
Cdd:pfam00009 139 LEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQ 175
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
561-669 |
9.35e-54 |
|
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: 179.66 E-value: 9.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 561 PIPVTTRFQARIIVFNVKVPITMGFPVLLHHQSLIEPAVVCKLTASIHKSTGEVVKKKPRCLGNNSCALVELETSRPICI 640
Cdd:cd04093 1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80
|
90 100
....*....|....*....|....*....
gi 45550900 641 ERYADFKELGRVMLRVAGVTIAAGMVTKI 669
Cdd:cd04093 81 ETFKDNKELGRFVLRRGGETIAAGIVTEI 109
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
250-467 |
1.22e-53 |
|
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: 183.15 E-value: 1.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 250 MIVIGHVDAGKSTLMGHLLYDTGNVSQRVMHKHEQeSKKLGKQ--SFMYAWVLDETGEERARGITMDVGQSRIETKTKIV 327
Cdd:cd04166 2 FITCGSVDDGKSTLIGRLLYDSKSIFEDQLAALER-SKSSGTQgeKLDLALLVDGLQAEREQGITIDVAYRYFSTPKRKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 328 TLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQLGVVINKLDTVGWSQDRFTE 407
Cdd:cd04166 81 IIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 408 IVTKLKSFLKLAGFkdSDVSFTPCSGLTGENLTKKAQEpalTNWYSGRHLLDVIENFKIP 467
Cdd:cd04166 154 IKADYLAFAASLGI--EDITFIPISALEGDNVVSRSEN---MPWYKGPTLLEHLETVEIA 208
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
244-667 |
1.09e-46 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 172.02 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 244 QKSHIHMIVIGHVDAGKSTLMGHLLYDTGNVSQRVMHKHEQESKKLGKQSFM--YAWVLDETGEERARGITMDVGQSRIE 321
Cdd:PRK05124 24 HKSLLRFLTCGSVDDGKSTLIGRLLHDTKQIYEDQLASLHNDSKRHGTQGEKldLALLVDGLQAEREQGITIDVAYRYFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 322 TKTKIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQLGVVINKLDTVGWS 401
Cdd:PRK05124 104 TEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVDYS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 402 QDRFTEIVTKLKSFLKLAGfKDSDVSFTPCSGLTGENLtkkAQEPALTNWYSGRHLLDVIENFKIPERAIDRPLRMSVSD 481
Cdd:PRK05124 177 EEVFERIREDYLTFAEQLP-GNLDIRFVPLSALEGDNV---VSQSESMPWYSGPTLLEVLETVDIQRVVDAQPFRFPVQY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 482 IYKGTGS--GFCisGRVETGVLCLNDKVLVGASREQAQVKSLTMNEFPQTCVFAGDQVSVTLP-ALDINNvtvGCIISDP 558
Cdd:PRK05124 253 VNRPNLDfrGYA--GTLASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEdEIDISR---GDLLVAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 559 QTPIPVTTRFQARiIVFNVKVPITMGFPVLLHHQSLIEPAVVCKLTASIHKSTGEvvKKKPRCLGNNSCALVELETSRPI 638
Cdd:PRK05124 328 DEALQAVQHASAD-VVWMAEQPLQPGQSYDIKIAGKKTRARVDAIRYQVDINTLT--QREAENLPLNGIGLVELTFDEPL 404
|
410 420 430
....*....|....*....|....*....|.
gi 45550900 639 CIERYADFKELGRVML--RVAGVTIAAGMVT 667
Cdd:PRK05124 405 VLDPYQQNRVTGGFIFidRLTNVTVGAGMVR 435
|
|
| tufA |
CHL00071 |
elongation factor Tu |
233-669 |
3.96e-43 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 160.51 E-value: 3.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 233 ARQLYEKeradQKSHIHMIVIGHVDAGKSTLmghllydTGNVSQRVmhkheqeSKKLGKQSFMYAWVlDETGEERARGIT 312
Cdd:CHL00071 2 AREKFER----KKPHVNIGTIGHVDHGKTTL-------TAAITMTL-------AAKGGAKAKKYDEI-DSAPEEKARGIT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 313 MDVGQSRIETKTKIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQLGVVI 392
Cdd:CHL00071 63 INTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 393 NKLDTVgwSQDRFTEIVTK-LKSFLKLAGFKDSDVSFTPCSGL------TGENLTKKAQEPALTNWYSgrhLLDVIENF- 464
Cdd:CHL00071 136 NKEDQV--DDEELLELVELeVRELLSKYDFPGDDIPIVSGSALlalealTENPKIKRGENKWVDKIYN---LMDAVDSYi 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 465 KIPERAIDRPLRMSVSDIYKGTGSGFCISGRVETGVLCLNDKV-LVG-ASREQAQVKSLTMneFPQTC--VFAGDQVSVT 540
Cdd:CHL00071 211 PTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVeIVGlRETKTTTVTGLEM--FQKTLdeGLAGDNVGIL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 541 LPALDINNVTVGCIISDPQTPIPvTTRFQARIIVFNV-----KVPITMGF-PvllhhQSLIEPAVVCKLTASIHKSTGEv 614
Cdd:CHL00071 289 LRGIQKEDIERGMVLAKPGTITP-HTKFEAQVYILTKeeggrHTPFFPGYrP-----QFYVRTTDVTGKIESFTADDGS- 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 45550900 615 vKKKPRCLGNNSCALVELETsrPICIEryadfKELgRVMLRVAGVTIAAGMVTKI 669
Cdd:CHL00071 362 -KTEMVMPGDRIKMTVELIY--PIAIE-----KGM-RFAIREGGRTVGAGVVSKI 407
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
252-468 |
8.38e-42 |
|
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: 149.75 E-value: 8.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLYDTGNVSQRVMHKheqeskklgkqsfmyAWVLDETGEERARGITMDVGQSRIETKTKIVTLLD 331
Cdd:cd00881 4 VIGHVDHGKTTLTGSLLYQTGAIDRRGTRK---------------ETFLDTLKEERERGITIKTGVVEFEWPKRRINFID 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 332 APGHKDFIPNMISGATQADVALLVVDATRGEfesgfelGGQTREHaILVRSLGVNQLGVVINKLDTVGwsQDRFTEIVTK 411
Cdd:cd00881 69 TPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREH-LNIALAGGLPIIVAVNKIDRVG--EEDFDEVLRE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 412 LKSFLKLAGF---KDSDVSFTPCSGLTGEnltkkaqepaltnwySGRHLLDVIENFKIPE 468
Cdd:cd00881 139 IKELLKLIGFtflKGKDVPIIPISALTGE---------------GIEELLDAIVEHLPPP 183
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
156-669 |
3.38e-40 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 154.00 E-value: 3.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 156 APAAPVLPKTVSKTVPTPPPKiSLKEPRRGFEIPSPKVPSSPVVSGRNTPVDisagddiSRSSATVFKVSKEQAVRNARQ 235
Cdd:PLN03126 2 AISASAASSSSSLLLPSSSSS-SPSSSTFSFKSTSGKLKSLTLSSSFLSPFS-------TTTTSTSQRRRRSFTVRAARG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 236 LYEKeradQKSHIHMIVIGHVDAGKSTLMGHLLYDTGNVSQRVMHKHEQeskklgkqsfmyawvLDETGEERARGITMDV 315
Cdd:PLN03126 74 KFER----KKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 316 GQSRIETKTKIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQLGVVINKL 395
Cdd:PLN03126 135 ATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 396 DTVgwSQDRFTEIVT-KLKSFLKLAGFKDSDVSFTPCSGLTG-ENLTKKAQEPALTNWYSGR--HLLDVIENF-KIPERA 470
Cdd:PLN03126 208 DQV--DDEELLELVElEVRELLSSYEFPGDDIPIISGSALLAlEALMENPNIKRGDNKWVDKiyELMDAVDSYiPIPQRQ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 471 IDRPLRMSVSDIYKGTGSGFCISGRVETGVLCLNDKVLVGASREQAQVKSLTMNEFPQTC--VFAGDQVSVTLPALDINN 548
Cdd:PLN03126 286 TDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILdeALAGDNVGLLLRGIQKAD 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 549 VTVGCIISDPQTPIPvTTRFQARIIVFNVK-----VPITMGFpvllHHQSLIEPAVVCKLTASIHKSTGEvvKKKPRCLG 623
Cdd:PLN03126 366 IQRGMVLAKPGSITP-HTKFEAIVYVLKKEeggrhSPFFAGY----RPQFYMRTTDVTGKVTSIMNDKDE--ESKMVMPG 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 45550900 624 NNSCALVELETsrPICIERYAdfkelgRVMLRVAGVTIAAGMVTKI 669
Cdd:PLN03126 439 DRVKMVVELIV--PVACEQGM------RFAIREGGKTVGAGVIQSI 476
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
245-669 |
4.21e-38 |
|
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: 146.08 E-value: 4.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 245 KSHIHMIVIGHVDAGKSTLMGHLlydtgnvsQRVMHKHeqeskklGKQSFMYAWVLDETGEERARGITMDVGQSRIETKT 324
Cdd:TIGR00485 10 KPHVNVGTIGHVDHGKTTLTAAI--------TTVLAKE-------GGAAARAYDQIDNAPEEKARGITINTAHVEYETET 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 325 KIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQLGVVINKLDTVgwSQDR 404
Cdd:TIGR00485 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV--DDEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 405 FTEIVT-KLKSFLKLAGFKDSDVSFTPCSGLTGENLTKKAQEPALtnwysgrHLLD-VIENFKIPERAIDRPLRMSVSDI 482
Cdd:TIGR00485 146 LLELVEmEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEAKIL-------ELMDaVDEYIPTPEREIDKPFLLPIEDV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 483 YKGTGSGFCISGRVETGVLCLNDKVLVGASRE--QAQVKSLTMNEFPQTCVFAGDQVSVTLPALDINNVTVGCIISDPQT 560
Cdd:TIGR00485 219 FSITGRGTVVTGRVERGIIKVGEEVEIVGLKDtrKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 561 PIPvTTRFQARIIVFNVK-----VPITMGFPVLLHHQSliepavvCKLTASIHKSTG-EVVKKkprclGNNSCALVELET 634
Cdd:TIGR00485 299 IKP-HTKFEAEVYVLSKEeggrhTPFFSGYRPQFYFRT-------TDVTGTIELPEGvEMVMP-----GDNVKMTVELIS 365
|
410 420 430
....*....|....*....|....*....|....*
gi 45550900 635 srPICIERYADFKelgrvmLRVAGVTIAAGMVTKI 669
Cdd:TIGR00485 366 --PIALEQGMRFA------IREGGRTVGAGVVSKI 392
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
238-574 |
4.71e-38 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 145.86 E-value: 4.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 238 EKERADQ-KSHIHMIVIGHVDAGKSTLmghllydTGNVSqRVMhkheqeSKKLGKQSFMYAWVlDETGEERARGITMDVG 316
Cdd:PRK12736 2 AKEKFDRsKPHVNIGTIGHVDHGKTTL-------TAAIT-KVL------AERGLNQAKDYDSI-DAAPEEKERGITINTA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 317 QSRIETKTKIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQLGVVINKLD 396
Cdd:PRK12736 67 HVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKVD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 397 TVGwsQDRFTEIV-TKLKSFLKLAGFKDSDVSFTPCSGLTGENlTKKAQEPALtnwysgRHLLDVIENF-KIPERAIDRP 474
Cdd:PRK12736 140 LVD--DEELLELVeMEVRELLSEYDFPGDDIPVIRGSALKALE-GDPKWEDAI------MELMDAVDEYiPTPERDTDKP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 475 LRMSVSDIYKGTGSGFCISGRVETGVLCLNDKV-LVGASREQ-AQVKSLTMNEFPQTCVFAGDQVSVTLPALDINNVTVG 552
Cdd:PRK12736 211 FLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVeIVGIKETQkTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERG 290
|
330 340
....*....|....*....|..
gi 45550900 553 CIISDPQTPIPvTTRFQARIIV 574
Cdd:PRK12736 291 QVLAKPGSIKP-HTKFKAEVYI 311
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
474-557 |
3.56e-36 |
|
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: 130.33 E-value: 3.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 474 PLRMSVSDIYKGTGSGFCISGRVETGVLCLNDKVLVGASREQAQVKSLTMNEFPQTCVFAGDQVSVTLPALDINNVTVGC 553
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
....
gi 45550900 554 IISD 557
Cdd:cd16267 81 ILCD 84
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
245-574 |
3.51e-35 |
|
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: 137.59 E-value: 3.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 245 KSHIHMIVIGHVDAGKSTLmghllydTGNVSqRVMHKHeqeskklGKQSFMYAWVLDETGEERARGITMDVGQSRIETKT 324
Cdd:COG0050 10 KPHVNIGTIGHVDHGKTTL-------TAAIT-KVLAKK-------GGAKAKAYDQIDKAPEEKERGITINTSHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 325 KIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQLGVVINKLDTVgwSQDR 404
Cdd:COG0050 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV--DDEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 405 FTEIV-TKLKSFLKLAGFKDSDVSFTPCSGLtgenltkKAQE-PALTNWYSG-RHLLDVI-ENFKIPERAIDRPLRMSVS 480
Cdd:COG0050 146 LLELVeMEVRELLSKYGFPGDDTPIIRGSAL-------KALEgDPDPEWEKKiLELMDAVdSYIPEPERDTDKPFLMPVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 481 DIYKGTGSGFCISGRVETGVLCLNDKV-LVGASREQAQV--------KSLTMNEfpqtcvfAGDQVSVTLPALDINNVTV 551
Cdd:COG0050 219 DVFSITGRGTVVTGRVERGIIKVGDEVeIVGIRDTQKTVvtgvemfrKLLDEGE-------AGDNVGLLLRGIKREDVER 291
|
330 340
....*....|....*....|...
gi 45550900 552 GCIISDPQTPIPvTTRFQARIIV 574
Cdd:COG0050 292 GQVLAKPGSITP-HTKFEAEVYV 313
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
245-510 |
4.62e-34 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 134.16 E-value: 4.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 245 KSHIHMIVIGHVDAGKSTLmghllydTGNVSqRVMhkheqeSKKLGKQSFMYAWVlDETGEERARGITMDVGQSRIETKT 324
Cdd:PRK00049 10 KPHVNVGTIGHVDHGKTTL-------TAAIT-KVL------AKKGGAEAKAYDQI-DKAPEEKARGITINTAHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 325 KIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQLGVVINKLDTVgwSQDR 404
Cdd:PRK00049 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV--DDEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 405 FTEIV-TKLKSFLKLAGFKDSDVSFTPCSGLtgenltkKAQEPALTN-WYSG-RHLLDVIENF-KIPERAIDRPLRMSVS 480
Cdd:PRK00049 146 LLELVeMEVRELLSKYDFPGDDTPIIRGSAL-------KALEGDDDEeWEKKiLELMDAVDSYiPTPERAIDKPFLMPIE 218
|
250 260 270
....*....|....*....|....*....|.
gi 45550900 481 DIYKGTGSGFCISGRVETGVLCLNDKV-LVG 510
Cdd:PRK00049 219 DVFSISGRGTVVTGRVERGIIKVGEEVeIVG 249
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
245-669 |
5.42e-34 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 135.34 E-value: 5.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 245 KSHIHMIVIGHVDAGKSTLmghllydTGNVSQRVMHKheqeskklGKQSFMYAWVLDETGEERARGITMDVGQSRIETKT 324
Cdd:PLN03127 59 KPHVNVGTIGHVDHGKTTL-------TAAITKVLAEE--------GKAKAVAFDEIDKAPEEKARGITIATAHVEYETAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 325 KIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQLGVVINKLDTVgwSQDR 404
Cdd:PLN03127 124 RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVV--DDEE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 405 FTEIVT----KLKSFLKLAGFKDSDVSFTPCSGLTGEN--LTKKAQepaltnwysgRHLLDVIENF-KIPERAIDRPLRM 477
Cdd:PLN03127 195 LLELVEmelrELLSFYKFPGDEIPIIRGSALSALQGTNdeIGKNAI----------LKLMDAVDEYiPEPVRVLDKPFLM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 478 SVSDIYKGTGSGFCISGRVETGVLCLNDKV-LVGASREQAQVKSLTMNE-FPQTCVF--AGDQVSVTLPALDINNVTVGC 553
Cdd:PLN03127 265 PIEDVFSIQGRGTVATGRVEQGTIKVGEEVeIVGLRPGGPLKTTVTGVEmFKKILDQgqAGDNVGLLLRGLKREDVQRGQ 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 554 IISDPQTpIPVTTRFQARIIVFNVK-----VPITMGFpvllhhqsliEPAVVCKlTASIhksTGEVVKKKPRCL---GNN 625
Cdd:PLN03127 345 VICKPGS-IKTYKKFEAEIYVLTKDeggrhTPFFSNY----------RPQFYLR-TADV---TGKVELPEGVKMvmpGDN 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 45550900 626 SCALVELETSRPIcieryadfkELG-RVMLRVAGVTIAAGMVTKI 669
Cdd:PLN03127 410 VTAVFELISPVPL---------EPGqRFALREGGRTVGAGVVSKV 445
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
250-666 |
2.32e-33 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 135.81 E-value: 2.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 250 MIV--IGHVDAGKSTLMGHLlydTGnvsqrvmhkheQESkklgkqsfmyawvlDETGEERARGITMDVGQSRIETKT-KI 326
Cdd:COG3276 1 MIIgtAGHIDHGKTTLVKAL---TG-----------IDT--------------DRLKEEKKRGITIDLGFAYLPLPDgRR 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 327 VTLLDAPGHKDFIPNMISGATQADVALLVVDATrgEfesgfelgG---QTREH-AILvRSLGVNQLGVVINKLDTVgwSQ 402
Cdd:COG3276 53 LGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAAD--E--------GvmpQTREHlAIL-DLLGIKRGIVVLTKADLV--DE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 403 DRFTEIVTKLKSFLKLAGFKDSDVSftPCSGLTGENLtkkaqePALTNwysgrHLLDVIEnfKIPERAIDRPLRMSVsD- 481
Cdd:COG3276 120 EWLELVEEEIRELLAGTFLEDAPIV--PVSAVTGEGI------DELRA-----ALDALAA--AVPARDADGPFRLPI-Dr 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 482 ---IyKGTG---SGFCISGRVETGvlclnDKVLVGASREQAQVKSLTMNEFPQTCVFAGDQVSVTLPALDINNVTVGCII 555
Cdd:COG3276 184 vfsI-KGFGtvvTGTLLSGTVRVG-----DELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 556 SDPQTPIPvTTRFQARI-IVFNVKVPITMGFPVLLHHqsliepavvckLTASIhksTGEVVKKKPRCLGNNSCALVELET 634
Cdd:COG3276 258 AAPGALRP-TDRIDVRLrLLPSAPRPLKHWQRVHLHH-----------GTAEV---LARVVLLDREELAPGEEALAQLRL 322
|
410 420 430
....*....|....*....|....*....|....
gi 45550900 635 SRPICIeRYADfkelgRVMLRVAG--VTIAAGMV 666
Cdd:COG3276 323 EEPLVA-ARGD-----RFILRDYSprRTIGGGRV 350
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
245-574 |
1.64e-32 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 129.96 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 245 KSHIHMIVIGHVDAGKSTLmghllydTGNVSqRVMhkheqeSKKLGKQSFMYAWVlDETGEERARGITMDVGQSRIETKT 324
Cdd:PRK12735 10 KPHVNVGTIGHVDHGKTTL-------TAAIT-KVL------AKKGGGEAKAYDQI-DNAPEEKARGITINTSHVEYETAN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 325 KIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQLGVVINKLDTVgwSQDR 404
Cdd:PRK12735 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV--DDEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 405 FTEIV-TKLKSFLKLAGFKDSDVSFTPCSGLTG-ENLTKKAQEPALtnwysgRHLLDVIENF-KIPERAIDRPLRMSVSD 481
Cdd:PRK12735 146 LLELVeMEVRELLSKYDFPGDDTPIIRGSALKAlEGDDDEEWEAKI------LELMDAVDSYiPEPERAIDKPFLMPIED 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 482 IYKGTGSGFCISGRVETGVLCLNDKV-LVGASREQAQV--------KSLTMNEfpqtcvfAGDQVSVTLPALDINNVTVG 552
Cdd:PRK12735 220 VFSISGRGTVVTGRVERGIVKVGDEVeIVGIKETQKTTvtgvemfrKLLDEGQ-------AGDNVGVLLRGTKREDVERG 292
|
330 340
....*....|....*....|..
gi 45550900 553 CIISDPQTPIPvTTRFQARIIV 574
Cdd:PRK12735 293 QVLAKPGSIKP-HTKFEAEVYV 313
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
563-669 |
1.55e-25 |
|
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions: N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 294003 [Multi-domain] Cd Length: 108 Bit Score: 101.48 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 563 PVTTRFQARI-IVFNVKVPITMGFPVLLHHQSLIEPAVVCKLTASIHKSTGEVVKKKPRCLGNNSCALVELETSRPICIE 641
Cdd:cd03704 1 PVVTEFEAQIvILDLLKSIITAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLE 80
|
90 100
....*....|....*....|....*...
gi 45550900 642 RYADFKELGRVMLRVAGVTIAAGMVTKI 669
Cdd:cd03704 81 TFKDFPQLGRFTLRDEGKTIAIGKVLKL 108
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
247-398 |
4.89e-25 |
|
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: 103.05 E-value: 4.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 247 HIHMIVIGHVDAGKSTLmghllydTGNVSqRVMhkheqeSKKLGKQSFMYAWVlDETGEERARGITMDVGQSRIETKTKI 326
Cdd:cd01884 2 HVNVGTIGHVDHGKTTL-------TAAIT-KVL------AKKGGAKAKKYDEI-DKAPEEKARGITINTAHVEYETANRH 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45550900 327 VTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQLGVVINKLDTV 398
Cdd:cd01884 67 YAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMV 131
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
254-439 |
2.31e-24 |
|
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: 99.99 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 254 GHVDAGKSTLMGHLlydTGnvsqrvmhkheQESkklgkqsfmyawvlDETGEERARGITMDVGQSRIETKT-KIVTLLDA 332
Cdd:cd04171 6 GHIDHGKTTLIKAL---TG-----------IET--------------DRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 333 PGHKDFIPNMISGATQADVALLVVDATRGefesgfeLGGQTREHAILVRSLGVNQLGVVINKLDTVgwSQDRFTEIVTKL 412
Cdd:cd04171 58 PGHEKFVKNMLAGAGGIDAVLLVVAADEG-------IMPQTREHLEILELLGIKKGLVVLTKADLV--DEDRLELVEEEI 128
|
170 180
....*....|....*....|....*..
gi 45550900 413 KSFLKLAGFKDSDVsfTPCSGLTGENL 439
Cdd:cd04171 129 LELLAGTFLADAPI--FPVSSVTGEGI 153
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
252-412 |
5.81e-19 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 86.52 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLYDTGNVSQ--RVMHKHEQeskklgkqsfmyawvLDETGEERARGITMDVGQSRIETKTKIVTL 329
Cdd:cd04168 4 ILAHVDAGKTTLTESLLYTSGAIRElgSVDKGTTR---------------TDSMELERQRGITIFSAVASFQWEDTKVNI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 330 LDAPGHKDFIPNMISGATQADVALLVVDATRGefesgfeLGGQTRehaILVRSLgvNQLGV----VINKLDTVGWSQDR- 404
Cdd:cd04168 69 IDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTR---ILFRLL--RKLNIptiiFVNKIDRAGADLEKv 136
|
....*...
gi 45550900 405 FTEIVTKL 412
Cdd:cd04168 137 YQEIKEKL 144
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
250-597 |
2.73e-16 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 82.41 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 250 MIVI--GHVDAGKSTLMGHLlydTGNVSQRVmhkheqeskklgkqsfmyawvldetGEERARGITMDVGQSRI-ETKTKI 326
Cdd:PRK10512 1 MIIAtaGHVDHGKTTLLQAI---TGVNADRL-------------------------PEEKKRGMTIDLGYAYWpQPDGRV 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 327 VTLLDAPGHKDFIPNMISGATQADVALLVVDATRGefesgfeLGGQTREHAILVRSLGVNQLGVVINKLDTVgwSQDRFT 406
Cdd:PRK10512 53 LGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDG-------VMAQTREHLAILQLTGNPMLTVALTKADRV--DEARIA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 407 EIVTKLKSFLKLAGFkdSDVSFTPCSGLTGENLtkkaqePALTnwysgRHLLDVIENfkipERAIDRPLRMSVSDIYKGT 486
Cdd:PRK10512 124 EVRRQVKAVLREYGF--AEAKLFVTAATEGRGI------DALR-----EHLLQLPER----EHAAQHRFRLAIDRAFTVK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 487 GSGFCISGRVETGVLCLNDKV-LVGASReQAQVKSLTMNEFPQTCVFAGDQVSVTLpALDINNVTVG---CIISDPqTPI 562
Cdd:PRK10512 187 GAGLVVTGTALSGEVKVGDTLwLTGVNK-PMRVRGLHAQNQPTEQAQAGQRIALNI-AGDAEKEQINrgdWLLADA-PPE 263
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 45550900 563 PVTtrfqaRIIV-FNVKVPITMGFPVLLHHQ--------SLIEP 597
Cdd:PRK10512 264 PFT-----RVIVeLQTHTPLTQWQPLHIHHAashvtgrvSLLED 302
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
252-420 |
2.26e-15 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 75.79 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLY---DTGNVSQRVM---HKHEQESkklGKQSFMYAWVL--DETGE--ERARGITMDVGQSRIE 321
Cdd:cd04165 4 VVGNVDAGKSTLLGVLTQgelDNGRGKARLNlfrHKHEVES---GRTSSVSNDILgfDSDGEvvNYPDNHLGELDVEICE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 322 TKTKIVTLLDAPGHKDFIPNMISGAT--QADVALLVVDATRGefesgfeLGGQTREHAILVRSLGVnQLGVVINKLDTVg 399
Cdd:cd04165 81 KSSKVVTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGANAG-------IIGMTKEHLGLALALKV-PVFVVVTKIDMT- 151
|
170 180
....*....|....*....|.
gi 45550900 400 wSQDRFTEIVTKLKSFLKLAG 420
Cdd:cd04165 152 -PANVLQETLKDLKRLLKSPG 171
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
248-437 |
2.36e-15 |
|
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: 74.71 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 248 IHMIVIGHVDAGKSTLMGHLlydTGNVSQRVMHKHEQESKklgkqsfmyawvldetgeeraRGITMDVGQSRIETKTKI- 326
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKAL---SEIASTAAFDKNPQSQE---------------------RGITLDLGFSSFEVDKPKh 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 327 -------------VTLLDAPGHKDFIPNMISGATQADVALLVVDATRGefesgfeLGGQTREHaILVRSLGVNQLGVVIN 393
Cdd:cd01889 57 lednenpqienyqITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQTAEC-LVIGELLCKPLIVVLN 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45550900 394 KLDTVGWSQDRFTEivTKLKSFLK--LAGFKDSDVSFTPCSGLTGE 437
Cdd:cd01889 129 KIDLIPEEERKRKI--EKMKKRLQktLEKTRLKDSPIIPVSAKPGE 172
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
252-439 |
2.94e-15 |
|
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: 74.05 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLlydtgnvsqrvmhkheQESKklgkqsfmyawvldeTGEERARGITMDVGQSRIETKTKI--VTL 329
Cdd:cd01887 5 VMGHVDHGKTTLLDKI----------------RKTN---------------VAAGEAGGITQHIGAYQVPIDVKIpgITF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 330 LDAPGHKDFIpNMIS-GATQADVALLVVDATRGefesgfeLGGQTREhAI-LVRSLGVnQLGVVINKLDTVGwSQDRFTE 407
Cdd:cd01887 54 IDTPGHEAFT-NMRArGASVTDIAILVVAADDG-------VMPQTIE-AInHAKAANV-PIIVAINKIDKPY-GTEADPE 122
|
170 180 190
....*....|....*....|....*....|...
gi 45550900 408 IVTKLKSFLKLAGFKDS-DVSFTPCSGLTGENL 439
Cdd:cd01887 123 RVKNELSELGLVGEEWGgDVSIVPISAKTGEGI 155
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
563-666 |
3.88e-15 |
|
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: 71.66 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 563 PVTTRFQARIIVFNVKVPITMGFPVLLHHQSLIEPAVVCKLTASIHKSTGEvvKKKPRCLGNNSCALVELETSRPICIER 642
Cdd:cd01513 1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE--KKPPDSLQPGENGTVEVELQKPVVLER 78
|
90 100
....*....|....*....|....
gi 45550900 643 YADFKELGRVMLRVAGVTIAAGMV 666
Cdd:cd01513 79 GKEFPTLGRFALRDGGRTVGAGLI 102
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
568-666 |
8.60e-15 |
|
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: 70.68 E-value: 8.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 568 FQARIIVFNVKVPITMGF-PVLLHHQSLIEpavvCK---LTASIHKSTGEVVKKKPRCLGNNSCALVELETSRPICIERY 643
Cdd:cd03705 6 FTAQVIILNHPGQIKAGYtPVLDCHTAHVA----CKfaeLKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVETF 81
|
90 100
....*....|....*....|...
gi 45550900 644 ADFKELGRVMLRVAGVTIAAGMV 666
Cdd:cd03705 82 SEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
471-561 |
1.02e-14 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 69.91 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 471 IDRPLRMSVSDIYKGTGSGFCISGRVETGVLCLNDKVLVGASREQAQVKSLTMNEFPQTCVFAGDQVSVTLPALDINNVT 550
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
90
....*....|.
gi 45550900 551 VGCIISDPQTP 561
Cdd:cd03693 81 RGDVAGDSKND 91
|
|
| HBS1_N |
pfam08938 |
HBS1 N-terminus; This domain is found at the N-terminus of HBS1 proteins. It interacts with ... |
83-148 |
2.58e-14 |
|
HBS1 N-terminus; This domain is found at the N-terminus of HBS1 proteins. It interacts with the ribosomal protein rpS3 at the mRNA entry site.
Pssm-ID: 462642 Cd Length: 76 Bit Score: 68.38 E-value: 2.58e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45550900 83 DSESFQMPQLDEIEQAKLSSCVDEVRSVVGDAVSERRIVETSMKFDYDMQKILDEILNEETNKSAK 148
Cdd:pfam08938 11 EEEEEADDELSDEDQELLNSCLPQVREVLGDSITDKQIKEALWHYYFDVEKAVDYLLNKFKKKKPK 76
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
252-414 |
1.23e-13 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 71.47 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLYDTGNVSQRvmhkheqESKKLGKQsfmyawVLDETGEERARGITMDVGQSRIETKTKIVTLLD 331
Cdd:cd04170 4 LVGHSGSGKTTLAEALLYATGAIDRL-------GRVEDGNT------VSDYDPEEKKRKMSIETSVAPLEWNGHKINLID 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 332 APGHKDFIPNMISGATQADVALLVVDATrgefeSGFELGgqTREHAILVRSLGVNQLgVVINKLDTVGwsqDRFTEIVTK 411
Cdd:cd04170 71 TPGYADFVGETLSALRAVDAALIVVEAQ-----SGVEVG--TEKVWEFLDDAKLPRI-IFINKMDRAR---ADFDKTLAA 139
|
...
gi 45550900 412 LKS 414
Cdd:cd04170 140 LRE 142
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
251-507 |
6.53e-13 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 71.04 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 251 IVIGHVDAGKSTLMGHLlydTGnvsqrvmhkheqeskklgkqsfmyAWVlDETGEERARGITMDVGQSRIE--------- 321
Cdd:PRK04000 13 GMVGHVDHGKTTLVQAL---TG------------------------VWT-DRHSEELKRGITIRLGYADATirkcpdcee 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 322 --------------TKTKI---VTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFESgfelggQTREHAILVRSLG 384
Cdd:PRK04000 65 peayttepkcpncgSETELlrrVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEHLMALDIIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 385 VNQLGVVINKLDTVgwSQDRFTEIVTKLKSFLKlaGFKDSDVSFTPCSGLTGENLTKkaqepaltnwysgrhLLDVIENF 464
Cdd:PRK04000 139 IKNIVIVQNKIDLV--SKERALENYEQIKEFVK--GTVAENAPIIPVSALHKVNIDA---------------LIEAIEEE 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 45550900 465 -KIPERAIDRPLRMSVS---DIYK-GTG----SGFCISGRVETGVLCLNDKV 507
Cdd:PRK04000 200 iPTPERDLDKPPRMYVArsfDVNKpGTPpeklKGGVIGGSLIQGVLKVGDEI 251
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
249-559 |
7.48e-13 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 71.66 E-value: 7.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 249 HMIVIGHVDAGKSTLMGHLLYDTGNVSQRVmhkHEQESkklgkqsfmyawVLDETGEERARGITMDVGQSRIETKTKIVT 328
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA---ETQER------------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 329 LLDAPGHKDFIPNMISGATQADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQLgVVINKLDTVGWSQDRFTEI 408
Cdd:PRK10218 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPI-VVINKVDRPGARPDWVVDQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 409 VTKLksFLKLAGfKDSDVSF-----TPCSGLTGENLTKKAQEpaLTNWYSGrhlldVIENFKIPERAIDRPLRMSVSDIY 483
Cdd:PRK10218 144 VFDL--FVNLDA-TDEQLDFpivyaSALNGIAGLDHEDMAED--MTPLYQA-----IVDHVPAPDVDLDGPFQMQISQLD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 484 KGTGSGFCISGRVETGVLCLNDKVLV----GASREQAQVKSLT---MNEFPQTCVFAGDQVSVT-LPALDINNVtvgciI 555
Cdd:PRK10218 214 YNSYVGVIGIGRIKRGKVKPNQQVTIidseGKTRNAKVGKVLGhlgLERIETDLAEAGDIVAITgLGELNISDT-----V 288
|
....
gi 45550900 556 SDPQ 559
Cdd:PRK10218 289 CDTQ 292
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
561-669 |
9.88e-13 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 64.59 E-value: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 561 PIPVTTRFQARIIVFN-----VKVPITMGFPVLLHHQSLIEPAVVCKLtasIHKSTGEVVKKKPRCLGNNSCALVELETS 635
Cdd:pfam03143 1 PIKPHTKFEAQVYILNkeeggRHTPFFNGYRPQFYFRTADVTGKFVEL---LHKLDPGGVSENPEFVMPGDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|....
gi 45550900 636 RPICIERYADFkelgrvMLRVAGVTIAAGMVTKI 669
Cdd:pfam03143 78 KPIALEKGQRF------AIREGGRTVAAGVVTEI 105
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
252-396 |
5.79e-12 |
|
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: 64.92 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLYDTG------NVSQRVMHKHEQEskklgkqsfmyawvldetgeeRARGITMDVGQSRIETKTK 325
Cdd:cd01891 7 IIAHVDHGKTTLVDALLKQSGtfreneEVGERVMDSNDLE---------------------RERGITILAKNTAITYKDT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 326 IVTLLDAPGHKDF------IPNMISGatqadvALLVVDATRGEFEsgfelggQTRehAILVRSLgvnQLG----VVINKL 395
Cdd:cd01891 66 KINIIDTPGHADFggeverVLSMVDG------VLLLVDASEGPMP-------QTR--FVLKKAL---EAGlkpiVVINKI 127
|
.
gi 45550900 396 D 396
Cdd:cd01891 128 D 128
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
252-361 |
7.82e-12 |
|
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: 64.48 E-value: 7.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLYDTGNVSQRVMhkHEQeskklgkqsfmyawVLDETGEERARGITMDVGQSRIETKTK-----I 326
Cdd:cd01890 5 IIAHIDHGKSTLADRLLELTGTVSEREM--KEQ--------------VLDSMDLERERGITIKAQAVRLFYKAKdgeeyL 68
|
90 100 110
....*....|....*....|....*....|....*.
gi 45550900 327 VTLLDAPGHKDFiPNMISGATQA-DVALLVVDATRG 361
Cdd:cd01890 69 LNLIDTPGHVDF-SYEVSRSLAAcEGALLVVDATQG 103
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
253-417 |
1.49e-11 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 67.46 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 253 IGHVDAGKSTLMGHLLYDTGNVSQrvMHK-HEQESkklgkqsfmyawVLDETGEERARGITMDVGQSRIETKTKIVTLLD 331
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHR--IGEvEDGTT------------TMDFMPEERERGISITSAATTCEWKGHKINLID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 332 APGHKDFIPNMISGATQADVALLVVDATrgefeSGFELGGQT--REhailVRSLGVNQLgVVINKLDTVGwsqDRFTEIV 409
Cdd:PRK12740 67 TPGHVDFTGEVERALRVLDGAVVVVCAV-----GGVEPQTETvwRQ----AEKYGVPRI-IFVNKMDRAG---ADFFRVL 133
|
....*...
gi 45550900 410 TKLKSFLK 417
Cdd:PRK12740 134 AQLQEKLG 141
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
252-563 |
1.93e-11 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 66.97 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLYDTG------NVSQRVMHKHEQEskklgkqsfmyawvldetgeeRARGITmdvgqsrIETK-- 323
Cdd:COG1217 11 IIAHVDHGKTTLVDALLKQSGtfrenqEVAERVMDSNDLE---------------------RERGIT-------ILAKnt 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 324 ------TKIvTLLDAPGHKDF------IPNMisgatqADVALLVVDAtrgeFEsgfelgG---QTR---EHAIlvrslgv 385
Cdd:COG1217 63 avrykgVKI-NIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlKKAL------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 386 nQLG----VVINKLD----TVGWSQDRfteiVTKLksFLKLaGFKDSDVSFtP---CSGLTG-ENLTKKAQEPALTnwys 453
Cdd:COG1217 119 -ELGlkpiVVINKIDrpdaRPDEVVDE----VFDL--FIEL-GATDEQLDF-PvvyASARNGwASLDLDDPGEDLT---- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 454 grHLLDVI-ENFKIPERAIDRPLRMSVSDI----YKGTgsgfcIS-GRVETGVLCLNDKVLV---GASREQAQVKSLTMN 524
Cdd:COG1217 186 --PLFDTIlEHVPAPEVDPDGPLQMLVTNLdysdYVGR-----IAiGRIFRGTIKKGQQVALikrDGKVEKGKITKLFGF 258
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 45550900 525 E----FPQTCVFAGDQVSVTlpalDINNVTVGCIISDPQTPIP 563
Cdd:COG1217 259 EglerVEVEEAEAGDIVAIA----GIEDINIGDTICDPENPEA 297
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
252-436 |
2.47e-11 |
|
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: 63.79 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLYDTGNVSQrvmhkheqesKKLGKQSFMyawvlDETGEERARGITMD---------VGQSRIET 322
Cdd:cd01885 5 IIAHVDHGKTTLSDSLLASAGIISE----------KLAGKARYL-----DTREDEQERGITIKssaislyfeYEEEKMDG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 323 KTKIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGefesgfeLGGQTreHAILVRSLGVN-QLGVVINKLD----- 396
Cdd:cd01885 70 NDYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDAVEG-------VCVQT--ETVLRQALEERvKPVLVINKIDrlile 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45550900 397 ---TVGWSQDRFTEI---VTKLKSFLKLAGFKDSDVSFTP-------CSGLTG 436
Cdd:cd01885 141 lklSPEEAYQRLLRIvedVNAIIETYAPEEFKQEKWKFSPqkgnvafGSALDG 193
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
252-396 |
4.53e-11 |
|
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: 63.06 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLYDTgnvsqrvmHKHEQESKKLGKQsFMYawvLDETGEERARGITMD------VGQSRiETKTK 325
Cdd:cd04167 5 IAGHLHHGKTSLLDMLIEQT--------HKRTPSVKLGWKP-LRY---TDTRKDEQERGISIKsnpislVLEDS-KGKSY 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45550900 326 IVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGefesgfeLGGQTREhaiLVRSLGVNQLGV--VINKLD 396
Cdd:cd04167 72 LINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEG-------LTSVTER---LIRHAIQEGLPMvlVINKID 134
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
253-417 |
2.91e-10 |
|
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: 60.36 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 253 IGHVDAGKSTLmghllydTGNVS--QRVMHKHEQESK---KLGkqsfmYA----WVLDETGEERArGITMDVGQSRIETK 323
Cdd:cd01888 6 IGHVAHGKTTL-------VKALSgvWTVRHKEELKRNitiKLG-----YAnakiYKCPNCGCPRP-YDTPECECPGCGGE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 324 TKI---VTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFESgfelggQTREHAILVRSLGVNQLGVVINKLDTVgw 400
Cdd:cd01888 73 TKLvrhVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQP------QTSEHLAALEIMGLKHIIILQNKIDLV-- 144
|
170
....*....|....*..
gi 45550900 401 SQDRFTEIVTKLKSFLK 417
Cdd:cd01888 145 KEEQALENYEQIKEFVK 161
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
252-399 |
3.08e-10 |
|
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: 63.53 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLYDTGnvsqrVMHK----HEQESkklgkqsfmyawVLDETGEERARGITMDVGQSRIETKTKIV 327
Cdd:COG0480 14 IVAHIDAGKTTLTERILFYTG-----AIHRigevHDGNT------------VMDWMPEEQERGITITSAATTCEWKGHKI 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45550900 328 TLLDAPGHKDFIPNMISGATQADVALLVVDATrgefeSGFELGGQT--REhailvrslgVNQLGV----VINKLDTVG 399
Cdd:COG0480 77 NIIDTPGHVDFTGEVERSLRVLDGAVVVFDAV-----AGVEPQTETvwRQ---------ADKYGVprivFVNKMDREG 140
|
|
| CysN_NoDQ_III |
cd04095 |
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of ... |
564-666 |
1.63e-08 |
|
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: 52.44 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 564 VTTRFQARIIVFNVKvPITMGFPVLLHHQSLIEPAVVCKLTASIHKSTGEVVKKKPrcLGNNSCALVELETSRPICIERY 643
Cdd:cd04095 2 VSDQFEATLVWMDEK-PLQPGRRYLLKHGTRTVRARVTEIDYRIDVNTLEREPADT--LALNDIGRVTLRLAEPLAFDPY 78
|
90 100
....*....|....*....|....*
gi 45550900 644 ADFKELGRVML--RVAGVTIAAGMV 666
Cdd:cd04095 79 AENRATGSFILidRLTNATVAAGMI 103
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
252-413 |
2.34e-08 |
|
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: 55.68 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLY------DTGNVSQRvmhkheqESKKLGKQSFMyawvldetGEERARGI--TMDVGQsrIETK 323
Cdd:cd04169 7 IISHPDAGKTTLTEKLLLfggaiqEAGAVKAR-------KSRKHATSDWM--------EIEKQRGIsvTSSVMQ--FEYK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 324 TKIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRGefesgfeLGGQTREHAILVRSLGVNQLgVVINKLDTVGwsQD 403
Cdd:cd04169 70 GCVINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG-------VEPQTRKLFEVCRLRGIPII-TFINKLDREG--RD 139
|
170
....*....|...
gi 45550900 404 RFT---EIVTKLK 413
Cdd:cd04169 140 PLElldEIENELG 152
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
250-361 |
2.66e-08 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 57.37 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 250 MIVIGHVDAGKSTLMGHLLYDTGNVSqrvmhkheqeSKKLGKQSFMyawvlDETGEERARGITM-DVGQS------RIET 322
Cdd:PTZ00416 22 MSVIAHVDHGKSTLTDSLVCKAGIIS----------SKNAGDARFT-----DTRADEQERGITIkSTGISlyyehdLEDG 86
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 45550900 323 KTK---IVTLLDAPGHKDFIPNMISGATQADVALLVVDATRG 361
Cdd:PTZ00416 87 DDKqpfLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEG 128
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
252-439 |
4.09e-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: 53.23 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLYDTgnvsqrvmhkheqeskklgkqsfmyawvLDETGEERARGITMDVGQSRIETKTKIVTLLD 331
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGE----------------------------VGEVSDVPGTTRDPDVYVKELDKGKVKLVLVD 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 332 APGHKDFIPNMISGAT-----QADVALLVVDATRGEFEsgfelggQTREHAILVRSLGVNQ-LGVVINKLDTVGwsqdrf 405
Cdd:cd00882 54 TPGLDEFGGLGREELArlllrGADLILLVVDSTDRESE-------EDAKLLILRRLRKEGIpIILVGNKIDLLE------ 120
|
170 180 190
....*....|....*....|....*....|....
gi 45550900 406 TEIVTKLKSFLKLAGFKdsDVSFTPCSGLTGENL 439
Cdd:cd00882 121 EREVEELLRLEELAKIL--GVPVFEVSAKTGEGV 152
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
489-556 |
8.00e-08 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 49.57 E-value: 8.00e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45550900 489 GFCISGRVETGVLCLNDKVLV-----GASREQAQVKSLTMNEFPQTCVFAGDQVSVTLPALDINNVTVGCIIS 556
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRIlpngtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
474-557 |
9.04e-08 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 49.81 E-value: 9.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 474 PLRMSVSDIYKGTgSGFCISGRVETGVLCLNDKVLVGASREQAQVKSLTMNEFPQT-CVFAGDQVSVTLPALDINNVTVG 552
Cdd:cd03698 1 PFRLSIDDKYKSP-RGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEETdWAIAGDTVTLRLRGIEVEDIQPG 79
|
....*
gi 45550900 553 CIISD 557
Cdd:cd03698 80 DILSS 84
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
252-417 |
1.81e-07 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 54.57 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLYDTGNVSQR-VMHKHEQESkklgkqsfmyawvlDETGEERARGITMDVGQSRIETKTKIVTLL 330
Cdd:PRK13351 13 ILAHIDAGKTTLTERILFYTGKIHKMgEVEDGTTVT--------------DWMPQEQERGITIESAATSCDWDNHRINLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 331 DAPGHKDFIPNMISGATQADVALLVVDATRG---EFESGFElggQTREHailvrslGVNQLgVVINKLDTVGwsqDRFTE 407
Cdd:PRK13351 79 DTPGHIDFTGEVERSLRVLDGAVVVFDAVTGvqpQTETVWR---QADRY-------GIPRL-IFINKMDRVG---ADLFK 144
|
170
....*....|
gi 45550900 408 IVTKLKSFLK 417
Cdd:PRK13351 145 VLEDIEERFG 154
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
477-557 |
3.00e-07 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 48.37 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 477 MSVSDIYKGTGSGFCISGRVETGVLCLNDKVLVG----ASREQAQVKSLTMNEFPQTCVFAGDQVSVTLPALDINNVTVG 552
Cdd:cd03694 3 FQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGpdadGKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKG 82
|
....*
gi 45550900 553 CIISD 557
Cdd:cd03694 83 MVLVS 87
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
239-361 |
6.86e-07 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 52.56 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 239 KERADQKSHIHMI-VIGHVDAGKSTLMGHLLYDTGNVSQRVMhkheqeskklGKQSFMyawvlDETGEERARGITMDVGQ 317
Cdd:PRK07560 11 LELMKNPEQIRNIgIIAHIDHGKTTLSDNLLAGAGMISEELA----------GEQLAL-----DFDEEEQARGITIKAAN 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 45550900 318 ----SRIETKTKIVTLLDAPGHKDFipnmiSG-ATQA----DVALLVVDATRG 361
Cdd:PRK07560 76 vsmvHEYEGKEYLINLIDTPGHVDF-----GGdVTRAmravDGAIVVVDAVEG 123
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
243-361 |
2.00e-06 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 51.26 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 243 DQKSHI-HMIVIGHVDAGKSTLMGHLLYDTGNVSQRVMhkheqeskklGKQSFMyawvlDETGEERARGIT--------- 312
Cdd:PLN00116 14 DKKHNIrNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVA----------GDVRMT-----DTRADEAERGITikstgisly 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 45550900 313 -------MDVGQSRIETKTKIVTLLDAPGHKDFIPNMISGATQADVALLVVDATRG 361
Cdd:PLN00116 79 yemtdesLKDFKGERDGNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEG 134
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
252-441 |
1.25e-05 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 48.68 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLlydtgnvsqrvmHKHEQESKKLGkqsfmyawvldetgeerarGITMDVGQSRIETK----TKIV 327
Cdd:CHL00189 249 ILGHVDHGKTTLLDKI------------RKTQIAQKEAG-------------------GITQKIGAYEVEFEykdeNQKI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 328 TLLDAPGHKDFiPNMIS-GATQADVALLVVDATRGefesgfeLGGQTREhAILVRSLGVNQLGVVINKLDTVGWSQDRFT 406
Cdd:CHL00189 298 VFLDTPGHEAF-SSMRSrGANVTDIAILIIAADDG-------VKPQTIE-AINYIQAANVPIIVAINKIDKANANTERIK 368
|
170 180 190
....*....|....*....|....*....|....*.
gi 45550900 407 EIVTKLKSF-LKLAGfkdsDVSFTPCSGLTGENLTK 441
Cdd:CHL00189 369 QQLAKYNLIpEKWGG----DTPMIPISASQGTNIDK 400
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
252-441 |
9.53e-05 |
|
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: 43.13 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLYDTGnvsqrvmhkheqeskklgkqsfmyawVLDETGEerarGITMDV--GQSRIETKTKIVTL 329
Cdd:TIGR00231 6 IVGHPNVGKSTLLNSLLGNKG--------------------------SITEYYP----GTTRNYvtTVIEEDGKTYKFNL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 330 LDAPGHKDFIPNMISGATQADVALLVVDAT--RGEFESGfeLGGQTREhAILVRSLGVNQLgVVINKLDTVGWSQDrfte 407
Cdd:TIGR00231 56 LDTAGQEDYDAIRRLYYPQVERSLRVFDIVilVLDVEEI--LEKQTKE-IIHHADSGVPII-LVGNKIDLKDADLK---- 127
|
170 180 190
....*....|....*....|....*....|....
gi 45550900 408 ivTKLKSFLKLAGFKDsdvsFTPCSGLTGENLTK 441
Cdd:TIGR00231 128 --THVASEFAKLNGEP----IIPLSAETGKNIDS 155
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
475-557 |
4.07e-04 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 39.43 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 475 LRMSVSDIYKGTGSGFCISGRVETGVLCLNDKVLVGASREQAQVKSLTMNEFPQTCVFAGDQVSVTLPALDINNVTVGCI 554
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
...
gi 45550900 555 ISD 557
Cdd:cd03696 81 LSE 83
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
248-441 |
6.13e-04 |
|
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: 41.26 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 248 IHMIVIGHVDAGKSTLMGHLLydtgnvsqrvmhkheqeskklgkqsfmyawvldetGEERA-----RGITMDVGQSRIET 322
Cdd:cd01895 3 IKIAIIGRPNVGKSSLLNALL-----------------------------------GEERVivsdiAGTTRDSIDVPFEY 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 323 KTKIVTLLDAPG-----HKDFIPNMISGA------TQADVALLVVDATRGEFESGFELGGQTREH--AILvrslgvnqlg 389
Cdd:cd01895 48 DGQKYTLIDTAGirkkgKVTEGIEKYSVLrtlkaiERADVVLLVLDASEGITEQDLRIAGLILEEgkALI---------- 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45550900 390 VVINKLDTVGWSQDRFTEIVTKLKSflKLAGFKDSDVSFTpcSGLTGENLTK 441
Cdd:cd01895 118 IVVNKWDLVEKDEKTMKEFEKELRR--KLPFLDYAPIVFI--SALTGQGVDK 165
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
475-556 |
7.62e-04 |
|
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: 38.78 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 475 LRMSVSDIYKGTGSGFCISGRVETGVLCLNDKVLVGASREQAQVKSLTMNEFPQTCVFAGDQvsVTLPALDINNVTVGCI 554
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDI--VGIGILGVKDILTGDT 78
|
..
gi 45550900 555 IS 556
Cdd:cd01342 79 LT 80
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
252-439 |
7.68e-04 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 40.69 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLydtgnvsqrvmhkheqeskklGKQSFmyawvldETGEerARGITMDVGQSRIETKTKI-VTLL 330
Cdd:cd00880 2 IFGRPNVGKSSLLNALL---------------------GQNVG-------IVSP--IPGTTRDPVRKEWELLPLGpVVLI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 331 DAPG-------HKDFIPNMISGATQADVALLVVDATRGEFESGFELGgqtREHAILVRSLgvnqlgVVINKLDTVGWSQD 403
Cdd:cd00880 52 DTPGldeegglGRERVEEARQVADRADLVLLVVDSDLTPVEEEAKLG---LLRERGKPVL------LVLNKIDLVPESEE 122
|
170 180 190
....*....|....*....|....*....|....*.
gi 45550900 404 RfteivtKLKSFLKLAGFKDSDVsfTPCSGLTGENL 439
Cdd:cd00880 123 E------ELLRERKLELLPDLPV--IAVSALPGEGI 150
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
475-548 |
9.12e-04 |
|
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: 38.32 E-value: 9.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45550900 475 LRMSVSDIYKGTGS--GFCisGRVETGVLCLNDKVLVGASREQAQVKSLTMNEFPQTCVFAGDQVSVTL-PALDINN 548
Cdd:cd03695 1 FRFPVQYVNRPNLDfrGYA--GTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLeDEIDVSR 75
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
252-396 |
1.09e-03 |
|
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: 41.92 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLmghllydtgnvsqrvmhkheqeskklgkqsfmyawvLD---ET----GEerARGITMDVGQSRIETKT 324
Cdd:COG0532 9 VMGHVDHGKTSL------------------------------------LDairKTnvaaGE--AGGITQHIGAYQVETNG 50
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45550900 325 KIVTLLDAPGHKDFIpNMIS-GATQADVALLVVDATRGefesgfeLGGQTRE---HAilvRSLGVnQLGVVINKLD 396
Cdd:COG0532 51 GKITFLDTPGHEAFT-AMRArGAQVTDIVILVVAADDG-------VMPQTIEainHA---KAAGV-PIIVAINKID 114
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
258-482 |
1.77e-03 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 40.80 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 258 AGKSTLMGHLLydtGN----VSQRVmhkheqeskklgkqsfmyawvldETGEERARGI-TMDVGQsrietktkIVtLLDA 332
Cdd:PRK00089 16 VGKSTLLNALV---GQkisiVSPKP-----------------------QTTRHRIRGIvTEDDAQ--------II-FVDT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 333 PG-HKdfiPN------M----ISGATQADVALLVVDATRGefesgfeLGGQTREHAILVRSLGVNQLgVVINKLDTVgws 401
Cdd:PRK00089 61 PGiHK---PKralnraMnkaaWSSLKDVDLVLFVVDADEK-------IGPGDEFILEKLKKVKTPVI-LVLNKIDLV--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 402 QDRfTEIVTKLKSFLKLAGFKDsdvsFTPCSGLTGENLtkkaqepaltnwysgRHLLDVI-----ENFKI-PERAI-DRP 474
Cdd:PRK00089 127 KDK-EELLPLLEELSELMDFAE----IVPISALKGDNV---------------DELLDVIakylpEGPPYyPEDQItDRP 186
|
....*...
gi 45550900 475 LRMSVSDI 482
Cdd:PRK00089 187 ERFLAAEI 194
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
252-361 |
2.36e-03 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 40.89 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLYDTGNVsqrvmhkHEQESKKlGKQSFMYA---WVldetgE-ERARGI--TMDVGQsrIETKTK 325
Cdd:PRK00741 15 IISHPDAGKTTLTEKLLLFGGAI-------QEAGTVK-GRKSGRHAtsdWM-----EmEKQRGIsvTSSVMQ--FPYRDC 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 45550900 326 IVTLLDAPGHKDFIPNMISGATQADVALLVVDATRG 361
Cdd:PRK00741 80 LINLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKG 115
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
252-338 |
2.38e-03 |
|
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: 40.17 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 252 VIGHVDAGKSTLMGHLLYDTGnVSQRVMHKHEQESkklgkqsfmyawVLDETGEERARGITMdvgQSRIET---KTKIVT 328
Cdd:cd01886 4 IIAHIDAGKTTTTERILYYTG-RIHKIGEVHGGGA------------TMDWMEQERERGITI---QSAATTcfwKDHRIN 67
|
90
....*....|
gi 45550900 329 LLDAPGHKDF 338
Cdd:cd01886 68 IIDTPGHVDF 77
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
327-507 |
4.02e-03 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 39.99 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 327 VTLLDAPGHKDFIPNMISGATQADVALLVVDATRGEFESgfelggQTREHAILVRSLGVNQLGVVINKLDTVGWS--QDR 404
Cdd:PTZ00327 119 VSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQP------QTSEHLAAVEIMKLKHIIILQNKIDLVKEAqaQDQ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550900 405 FTEIvtklKSFLKlaGFKDSDVSFTPCSGLTGENLTkkaqepaltnwysgrHLLDVIEN-FKIPERAIDRPLRMSVS--- 480
Cdd:PTZ00327 193 YEEI----RNFVK--GTIADNAPIIPISAQLKYNID---------------VVLEYICTqIPIPKRDLTSPPRMIVIrsf 251
|
170 180 190
....*....|....*....|....*....|..
gi 45550900 481 DIYK-GTG----SGFCISGRVETGVLCLNDKV 507
Cdd:PTZ00327 252 DVNKpGEDienlKGGVAGGSILQGVLKVGDEI 283
|
|
| |
