|
Name |
Accession |
Description |
Interval |
E-value |
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
256-679 |
9.23e-149 |
|
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: 438.60 E-value: 9.23e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 256 LNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTTKVI 335
Cdd:COG5256 8 LNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 336 TLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVTQLAVAVNKMDQVNWQQERFQE 415
Cdd:COG5256 88 TIIDAPGHRDFVKNMITGASQADAAILVVSAKDG-------VMGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 416 ITGKLGHFLKQAGFKESDVAFIPTSGLSGENLTARSQSsdlTTWYKGMCLLEQIDSFKPPQRSIDKPFRLCVSDVFKDQG 495
Cdd:COG5256 161 VKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDN---MPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQDVYSISG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 496 SGFCVTGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGM---DIIKINVgcifCGPKE-PIK 571
Cdd:COG5256 238 IGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVeknDIKRGDV----AGHPDnPPT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 572 ACTRFRARILVFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLTKGQNALVELQTQRPVALELY 651
Cdd:COG5256 314 VAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEKF 393
|
410 420
....*....|....*....|....*...
gi 110611224 652 KDFKELGRFMLRYGGSTVAAGVVTEIKE 679
Cdd:COG5256 394 KEFPQLGRFAIRDMGQTVAAGVVLDVKP 421
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
253-679 |
7.38e-141 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 418.18 E-value: 7.38e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 253 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTT 332
Cdd:PRK12317 4 KPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 333 KVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEfeaGFEtgGQTREHGLLVRSLGVTQLAVAVNKMDQVNWQQER 412
Cdd:PRK12317 84 YYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAG---GVM--PQTREHVFLARTLGINQLIVAINKMDAVNYDEKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 413 FQEITGKLGHFLKQAGFKESDVAFIPTSGLSGENLTARsqsSDLTTWYKGMCLLEQIDSFKPPQRSIDKPFRLCVSDVFK 492
Cdd:PRK12317 159 YEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKK---SENMPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQDVYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 493 DQGSGFCVTGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGM---DIIKINVgcifCGPKE- 568
Cdd:PRK12317 236 ISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVgkkDIKRGDV----CGHPDn 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 569 PIKACTRFRARILVFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLTKGQNALVELQTQRPVAL 648
Cdd:PRK12317 312 PPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVI 391
|
410 420 430
....*....|....*....|....*....|.
gi 110611224 649 ELYKDFKELGRFMLRYGGSTVAAGVVTEIKE 679
Cdd:PRK12317 392 EKVKEIPQLGRFAIRDMGQTIAAGMVIDVKP 422
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
257-476 |
1.32e-140 |
|
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: 409.57 E-value: 1.32e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTTKVIT 336
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 337 LMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAGFETGGQTREHGLLVRSLGVTQLAVAVNKMDQV--NWQQERFQ 414
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110611224 415 EITGKLGHFLKQAGFKESDVAFIPTSGLSGENLTarsQSSDLTTWYKGMCLLEQIDSFKPPQ 476
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLI---EKSENMPWYKGPTLLEALDSLEPPE 219
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
253-677 |
4.04e-134 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 401.82 E-value: 4.04e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 253 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTT 332
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 333 KVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAGFETGGQTREHGLLVRSLGVTQLAVAVNKMD--QVNWQQ 410
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 411 ERFQEITGKLGHFLKQAGFKESDVAFIPTSGLSGENLTARsqsSDLTTWYKGMCLLEQIDSFKPPQRSIDKPFRLCVSDV 490
Cdd:PTZ00141 165 ERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEK---SDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 491 FKDQGSGFCVTGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINVGCIFCGPK-EP 569
Cdd:PTZ00141 242 YKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKnDP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 570 IKACTRFRARILVFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLTKGQNALVELQTQRPVALE 649
Cdd:PTZ00141 322 AKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVE 401
|
410 420
....*....|....*....|....*...
gi 110611224 650 LYKDFKELGRFMLRYGGSTVAAGVVTEI 677
Cdd:PTZ00141 402 VFNEYPPLGRFAVRDMKQTVAVGVIKSV 429
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
256-679 |
8.11e-98 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 308.17 E-value: 8.11e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 256 LNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTTKVI 335
Cdd:PLN00043 8 INIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 336 TLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAGFETGGQTREHGLLVRSLGVTQLAVAVNKMDQVN--WQQERF 413
Cdd:PLN00043 88 TVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTpkYSKARY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 414 QEITGKLGHFLKQAGFKESDVAFIPTSGLSGENLTARSQSSDlttWYKGMCLLEQIDSFKPPQRSIDKPFRLCVSDVFKD 493
Cdd:PLN00043 168 DEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLD---WYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 494 QGSGFCVTGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINVGCIFCGPK-EPIKA 572
Cdd:PLN00043 245 GGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKdDPAKE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 573 CTRFRARILVFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLTKGQNALVELQTQRPVALELYK 652
Cdd:PLN00043 325 AANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVVETFS 404
|
410 420
....*....|....*....|....*..
gi 110611224 653 DFKELGRFMLRYGGSTVAAGVVTEIKE 679
Cdd:PLN00043 405 EYPPLGRFAVRDMRQTVAVGVIKSVEK 431
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
241-676 |
1.71e-94 |
|
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: 298.54 E-value: 1.71e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 241 DVKAELEKRQGgKQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVT 320
Cdd:COG2895 4 DIEAYLAQHEN-KDLLRFITCGSVDDGKSTLIGRLLYDTKSIFEDQLAALERDSKKRGTQEIDLALLTDGLQAEREQGIT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 321 MDVGMTKFETTT-KVItLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVA 399
Cdd:COG2895 83 IDVAYRYFSTPKrKFI-IADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 400 VNKMDQVNWQQERFQEITGKLGHFLKQAGFKesDVAFIPTSGLSGENLTARSQSsdlTTWYKGMCLLEQIDSFKPPQRSI 479
Cdd:COG2895 155 VNKMDLVDYSEEVFEEIVADYRAFAAKLGLE--DITFIPISALKGDNVVERSEN---MPWYDGPTLLEHLETVEVAEDRN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 480 DKPFRLCVSDVFKDQGS--GFCvtGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVgmDIIKI 557
Cdd:COG2895 230 DAPFRFPVQYVNRPNLDfrGYA--GTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLE--DEIDI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 558 NVGCIFCGPKEPIKACTRFRARILVFNiEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEvtkkKPKLLTKGQN-- 635
Cdd:COG2895 306 SRGDVIVAADAPPEVADQFEATLVWMD-EEPLLPGRKYLLKHGTRTVRATVTAIKYRIDVNTLE----HEAADSLELNdi 380
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 110611224 636 ALVELQTQRPVALELYKDFKELGRFML--RYGGSTVAAGVVTE 676
Cdd:COG2895 381 GRVTLRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMIRG 423
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
241-675 |
4.01e-63 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 221.34 E-value: 4.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 241 DVKAELeKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAG--KASFAYAWVLDETGEERERG 318
Cdd:PRK05506 11 DILAYL-AQHERKSLLRFITCGSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 319 VTMDVGMTKFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAV 398
Cdd:PRK05506 90 ITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 399 AVNKMDQVNWQQERFQEITGKLGHFLKQAGFkeSDVAFIPTSGLSGENLTARSQSsdlTTWYKGMCLLEQIDSFKPPQRS 478
Cdd:PRK05506 163 AVNKMDLVDYDQEVFDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSAR---MPWYEGPSLLEHLETVEIASDR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 479 IDKPFRLCVSDVFKDQGS--GFCvtGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVgmDIIK 556
Cdd:PRK05506 238 NLKDFRFPVQYVNRPNLDfrGFA--GTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLA--DEID 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 557 INVGCIFCGPKEPIKACTRFRARILVFNiEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEvtKKKPKLLTKGQNA 636
Cdd:PRK05506 314 ISRGDMLARADNRPEVADQFDATVVWMA-EEPLLPGRPYLLKHGTRTVPASVAAIKYRVDVNTLE--RLAAKTLELNEIG 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 110611224 637 LVELQTQRPVALELYKDFKELGRFML--RYGGSTVAAGVVT 675
Cdd:PRK05506 391 RCNLSTDAPIAFDPYARNRTTGSFILidRLTNATVGAGMID 431
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
256-674 |
1.57e-61 |
|
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 213679 [Multi-domain] Cd Length: 406 Bit Score: 211.08 E-value: 1.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 256 LNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAGK--ASFAYAWVLDETGEERERGVTMDVGMTKFETTTK 333
Cdd:TIGR02034 1 LRFLTCGSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 334 VITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNWQQERF 413
Cdd:TIGR02034 81 KFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 414 QEITGKLGHFLKQAGFkeSDVAFIPTSGLSGENLTARSQSSDlttWYKGMCLLEQIDSFKPPQRSIDKPFRLCVSDVFKD 493
Cdd:TIGR02034 154 ENIKKDYLAFAEQLGF--RDVTFIPLSALKGDNVVSRSESMP---WYSGPTLLEILETVEVERDAQDLPLRFPVQYVNRP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 494 QGS--GFcvTGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLvgMDIIKINVGCIFCGPKEPIK 571
Cdd:TIGR02034 229 NLDfrGY--AGTIASGSVHVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTL--DDEIDISRGDLLAAADSAPE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 572 ACTRFRARiLVFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEvtkkKPKLLTKGQNA--LVELQTQRPVALE 649
Cdd:TIGR02034 305 VADQFAAT-LVWMAEEPLLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLE----KGAAKSLELNEigRVNLSLDEPIAFD 379
|
410 420
....*....|....*....|....*..
gi 110611224 650 LYKDFKELGRFML--RYGGSTVAAGVV 674
Cdd:TIGR02034 380 PYAENRTTGAFILidRLSNRTVGAGMI 406
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
253-475 |
3.07e-60 |
|
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: 200.06 E-value: 3.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 253 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESkkagkasfayawVLDETGEERERGVTMDVGMTKFETTT 332
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 333 KVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVtQLAVAVNKMDQVNwqQER 412
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGV-PIIVFINKMDRVD--GAE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110611224 413 FQEITGKLGH-FLKQAGFKESDVAFIPTSGLSGENLTArsqssdlttwykgmcLLEQIDSFKPP 475
Cdd:pfam00009 139 LEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT---------------LLDALDEYLPS 187
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
257-476 |
4.34e-57 |
|
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: 192.40 E-value: 4.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQeSKKAGKA--SFAYAWVLDETGEERERGVTMDVGMTKFETTTKV 334
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAALER-SKSSGTQgeKLDLALLVDGLQAEREQGITIDVAYRYFSTPKRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 335 ITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNWQQERFQ 414
Cdd:cd04166 80 FIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110611224 415 EITGKLGHFLKQAGFkeSDVAFIPTSGLSGENLTARSQSsdlTTWYKGMCLLEQIDSFKPPQ 476
Cdd:cd04166 153 EIKADYLAFAASLGI--EDITFIPISALEGDNVVSRSEN---MPWYKGPTLLEHLETVEIAS 209
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
167-679 |
8.75e-56 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 197.53 E-value: 8.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 167 MGFEVPGLTSEENGLSVRAPHKGPPgddvSVASPNIPETGTPKSALPPPSLQTSEELGSTPTPVRKsgklRQQIDVKAEL 246
Cdd:PLN03126 1 MAISASAASSSSSLLLPSSSSSSPS----SSTFSFKSTSGKLKSLTLSSSFLSPFSTTTTSTSQRR----RRSFTVRAAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 247 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMT 326
Cdd:PLN03126 73 GKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 327 KFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 406
Cdd:PLN03126 138 EYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 407 NwQQERFQEITGKLGHFLKQAGFKESDVAFIPTSGLSG-ENLTA-----RSQSSDLTTWYKgmcLLEQIDSFKP-PQRSI 479
Cdd:PLN03126 211 D-DEELLELVELEVRELLSSYEFPGDDIPIISGSALLAlEALMEnpnikRGDNKWVDKIYE---LMDAVDSYIPiPQRQT 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 480 DKPFRLCVSDVFKDQGSGFCVTGKIEAGYIQTGD--RLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKI 557
Cdd:PLN03126 287 DLPFLLAVEDVFSITGRGTVATGRVERGTVKVGEtvDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 558 NVGCIFCGPKEpIKACTRFRARILVFNIE-----VPITKGFPVLLHYQTVSepaVIKRLISVLNKSTGEvtkkkPKLLTK 632
Cdd:PLN03126 367 QRGMVLAKPGS-ITPHTKFEAIVYVLKKEeggrhSPFFAGYRPQFYMRTTD---VTGKVTSIMNDKDEE-----SKMVMP 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 110611224 633 GQNALVELQTQRPVALElykdfkELGRFMLRYGGSTVAAGVVTEIKE 679
Cdd:PLN03126 438 GDRVKMVVELIVPVACE------QGMRFAIREGGKTVGAGVIQSIIE 478
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
247-679 |
1.08e-54 |
|
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: 192.30 E-value: 1.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 247 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMT 326
Cdd:TIGR00485 4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQ---------------IDNAPEEKARGITINTAHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 327 KFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 406
Cdd:TIGR00485 69 EYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 407 NwQQERFQEITGKLGHFLKQAGFKESDVAFIPTSGLSGENLTARSQSSDLTtwykgmcLLEQIDSFKP-PQRSIDKPFRL 485
Cdd:TIGR00485 142 D-DEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEAKILE-------LMDAVDEYIPtPEREIDKPFLL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 486 CVSDVFKDQGSGFCVTGKIEAGYIQTGDR--LLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINVGCIF 563
Cdd:TIGR00485 214 PIEDVFSITGRGTVVTGRVERGIIKVGEEveIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 564 CGPKEpIKACTRFRARILVFNIE-----VPITKGFPVLLHYQTVSEPAVIKRLISVlnkstgevtkkkpKLLTKGQNALV 638
Cdd:TIGR00485 294 AKPGS-IKPHTKFEAEVYVLSKEeggrhTPFFSGYRPQFYFRTTDVTGTIELPEGV-------------EMVMPGDNVKM 359
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 110611224 639 ELQTQRPVALElykdfkELGRFMLRYGGSTVAAGVVTEIKE 679
Cdd:TIGR00485 360 TVELISPIALE------QGMRFAIREGGRTVGAGVVSKILE 394
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
247-679 |
2.98e-54 |
|
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: 190.75 E-value: 2.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 247 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMT 326
Cdd:COG0050 4 EKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQ---------------IDKAPEEKERGITINTSHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 327 KFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 406
Cdd:COG0050 69 EYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 407 NwQQERFQEITGKLGHFLKQAGFKESDVAFIPTSG---LSGENLTArsqssdlttWYKGMC-LLEQIDSFKP-PQRSIDK 481
Cdd:COG0050 142 D-DEELLELVEMEVRELLSKYGFPGDDTPIIRGSAlkaLEGDPDPE---------WEKKILeLMDAVDSYIPePERDTDK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 482 PFRLCVSDVFKDQGSGFCVTGKIEAGYIQTGDR--LLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINV 559
Cdd:COG0050 212 PFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEveIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVER 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 560 GCIFCGPKEpIKACTRFRARILVFNIE-----VPITKGFPVLLHYQTVSEPAVIKrlisvLNKSTGEVtkkkpkllTKGQ 634
Cdd:COG0050 292 GQVLAKPGS-ITPHTKFEAEVYVLSKEeggrhTPFFNGYRPQFYFRTTDVTGVIT-----LPEGVEMV--------MPGD 357
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 110611224 635 NALVELQTQRPVALElykdfKELgRFMLRYGGSTVAAGVVTEIKE 679
Cdd:COG0050 358 NVTMTVELITPIAME-----EGL-RFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
253-679 |
3.07e-54 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 190.93 E-value: 3.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 253 KQLLNLVVIGHVDAGKSTLMGHMLYLLgnvnkrtmhkyeqeSKKAGKASFAYAWVlDETGEERERGVTMDVGMTKFETTT 332
Cdd:PRK12736 10 KPHVNIGTIGHVDHGKTTLTAAITKVL--------------AERGLNQAKDYDSI-DAAPEEKERGITINTAHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 333 KVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNwQQER 412
Cdd:PRK12736 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKVDLVD-DEEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 413 FQEITGKLGHFLKQAGFKESDVAFIPTSGLSGENLTARsqssdlttWYKG-MCLLEQIDSFKP-PQRSIDKPFRLCVSDV 490
Cdd:PRK12736 147 LELVEMEVRELLSEYDFPGDDIPVIRGSALKALEGDPK--------WEDAiMELMDAVDEYIPtPERDTDKPFLMPVEDV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 491 FKDQGSGFCVTGKIEAGYIQTGDR--LLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINVGCIFCGPKE 568
Cdd:PRK12736 219 FTITGRGTVVTGRVERGTVKVGDEveIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 569 pIKACTRFRARILVFNIE-----VPITKGFPVLLHYQTVSEPAVIKrlisvLNKSTGEVtkkkpkllTKGQNALVELQTQ 643
Cdd:PRK12736 299 -IKPHTKFKAEVYILTKEeggrhTPFFNNYRPQFYFRTTDVTGSIE-----LPEGTEMV--------MPGDNVTITVELI 364
|
410 420 430
....*....|....*....|....*....|....*.
gi 110611224 644 RPVALElykdfkELGRFMLRYGGSTVAAGVVTEIKE 679
Cdd:PRK12736 365 HPIAME------QGLKFAIREGGRTVGAGTVTEILD 394
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
238-676 |
1.22e-52 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 188.58 E-value: 1.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 238 QQIDVKAELEKRQGgKQLLNLVVIGHVDAGKSTLMGHMLYllgnvnkRTMHKYE-------QESKKAGKASFA--YAWVL 308
Cdd:PRK05124 11 NEGGVEAYLHAQQH-KSLLRFLTCGSVDDGKSTLIGRLLH-------DTKQIYEdqlaslhNDSKRHGTQGEKldLALLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 309 DETGEERERGVTMDVGMTKFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLV 388
Cdd:PRK05124 83 DGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 389 RSLGVTQLAVAVNKMDQVNWQQERFQEITGKLGHFLKQAGfKESDVAFIPTSGLSGENLTARSQSsdlTTWYKGMCLLEQ 468
Cdd:PRK05124 156 TLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLP-GNLDIRFVPLSALEGDNVVSQSES---MPWYSGPTLLEV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 469 IDSFKPPQRSIDKPFRLCVSDV------FKdqgsGFCvtGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAG 542
Cdd:PRK05124 232 LETVDIQRVVDAQPFRFPVQYVnrpnldFR----GYA--GTLASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 543 DHVNLTLvgMDIIKINVGCIFCGPKEPIKACTRFRARIlVFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEv 622
Cdd:PRK05124 306 EAITLVL--EDEIDISRGDLLVAADEALQAVQHASADV-VWMAEQPLQPGQSYDIKIAGKKTRARVDAIRYQVDINTLT- 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 110611224 623 tkkKPKLLTKGQNA--LVELQTQRPVALELYKDFKELGRFML--RYGGSTVAAGVVTE 676
Cdd:PRK05124 382 ---QREAENLPLNGigLVELTFDEPLVLDPYQQNRVTGGFIFidRLTNVTVGAGMVRE 436
|
|
| tufA |
CHL00071 |
elongation factor Tu |
247-677 |
1.32e-50 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 181.31 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 247 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMT 326
Cdd:CHL00071 4 EKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDE---------------IDSAPEEKARGITINTAHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 327 KFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 406
Cdd:CHL00071 69 EYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 407 NwQQERFQEITGKLGHFLKQAGFKESDVAFIPTSGLsgENLTARSQSSDLT----TWY-KGMCLLEQIDSFKP-PQRSID 480
Cdd:CHL00071 142 D-DEELLELVELEVRELLSKYDFPGDDIPIVSGSAL--LALEALTENPKIKrgenKWVdKIYNLMDAVDSYIPtPERDTD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 481 KPFRLCVSDVFKDQGSGFCVTGKIEAGYIQTGD--RLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKIN 558
Cdd:CHL00071 219 KPFLMAIEDVFSITGRGTVATGRIERGTVKVGDtvEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 559 VGCIFCGPKEpIKACTRFRARILVFNIE-----VPITKGFpvllhyqtvsEPAVIKRLISVlnksTGEVTKKKPKLLTKG 633
Cdd:CHL00071 299 RGMVLAKPGT-ITPHTKFEAQVYILTKEeggrhTPFFPGY----------RPQFYVRTTDV----TGKIESFTADDGSKT 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 110611224 634 QNAL--------VELQTqrPVALElykdfKELgRFMLRYGGSTVAAGVVTEI 677
Cdd:CHL00071 364 EMVMpgdrikmtVELIY--PIAIE-----KGM-RFAIREGGRTVGAGVVSKI 407
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
569-677 |
2.02e-50 |
|
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: 170.80 E-value: 2.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 569 PIKACTRFRARILVFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLTKGQNALVELQTQRPVAL 648
Cdd:cd04093 1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80
|
90 100
....*....|....*....|....*....
gi 110611224 649 ELYKDFKELGRFMLRYGGSTVAAGVVTEI 677
Cdd:cd04093 81 ETFKDNKELGRFVLRRGGETIAAGIVTEI 109
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
247-679 |
2.46e-50 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 180.03 E-value: 2.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 247 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMT 326
Cdd:PRK12735 4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQ---------------IDNAPEEKARGITINTSHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 327 KFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 406
Cdd:PRK12735 69 EYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 407 NwQQERFQEITGKLGHFLKQAGFKESDVAFIPTSGLSGENLTARSQSSDlttwyKGMCLLEQIDSFKP-PQRSIDKPFRL 485
Cdd:PRK12735 142 D-DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGDDDEEWEA-----KILELMDAVDSYIPePERAIDKPFLM 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 486 CVSDVFKDQGSGFCVTGKIEAGYIQTGD--RLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINVGCIF 563
Cdd:PRK12735 216 PIEDVFSISGRGTVVTGRVERGIVKVGDevEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 564 CGPKEpIKACTRFRARILVFNIE-----VPITKGFPVLLHYQTVSEPAVIKrlisvLNKSTGEVtkkkpkllTKGQNALV 638
Cdd:PRK12735 296 AKPGS-IKPHTKFEAEVYVLSKEeggrhTPFFNGYRPQFYFRTTDVTGTIE-----LPEGVEMV--------MPGDNVKM 361
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 110611224 639 ELQTQRPVALElykdfKELgRFMLRYGGSTVAAGVVTEIKE 679
Cdd:PRK12735 362 TVELIAPIAME-----EGL-RFAIREGGRTVGAGVVAKIIE 396
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
253-677 |
2.84e-49 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 178.87 E-value: 2.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 253 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMTKFETTT 332
Cdd:PLN03127 59 KPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDE---------------IDKAPEEKARGITIATAHVEYETAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 333 KVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNwQQER 412
Cdd:PLN03127 124 RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVD-DEEL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 413 FQEITGKLGHFLKQAGFKESDVAFIPTSGLSgenltARSQSSDLTTWYKGMCLLEQIDSFKP-PQRSIDKPFRLCVSDVF 491
Cdd:PLN03127 196 LELVEMELRELLSFYKFPGDEIPIIRGSALS-----ALQGTNDEIGKNAILKLMDAVDEYIPePVRVLDKPFLMPIEDVF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 492 KDQGSGFCVTGKIEAGYIQTGDRL----LAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINVGCIFCGPK 567
Cdd:PLN03127 271 SIQGRGTVATGRVEQGTIKVGEEVeivgLRPGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 568 EpIKACTRFRARILVFNIEVPiTKGFPVLLHYQtvsePAVIKRLISVlnksTGEVTKKKPKLLTK-GQNALVELQTQRPV 646
Cdd:PLN03127 351 S-IKTYKKFEAEIYVLTKDEG-GRHTPFFSNYR----PQFYLRTADV----TGKVELPEGVKMVMpGDNVTAVFELISPV 420
|
410 420 430
....*....|....*....|....*....|.
gi 110611224 647 ALELYKdfkelgRFMLRYGGSTVAAGVVTEI 677
Cdd:PLN03127 421 PLEPGQ------RFALREGGRTVGAGVVSKV 445
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
247-679 |
1.16e-48 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 175.76 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 247 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLgnvnkrtmhkyeqeSKKAGKASFAYAWVlDETGEERERGVTMDVGMT 326
Cdd:PRK00049 4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITKVL--------------AKKGGAEAKAYDQI-DKAPEEKARGITINTAHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 327 KFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 406
Cdd:PRK00049 69 EYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 407 NwQQERFQEITGKLGHFLKQAGFKESDVAFIPTSGLSgenltARSQSSDlTTWYKG-MCLLEQIDSFKP-PQRSIDKPFR 484
Cdd:PRK00049 142 D-DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALK-----ALEGDDD-EEWEKKiLELMDAVDSYIPtPERAIDKPFL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 485 LCVSDVFKDQGSGFCVTGKIEAGYIQTGD--RLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINVGCI 562
Cdd:PRK00049 215 MPIEDVFSISGRGTVVTGRVERGIIKVGEevEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 563 FCGPKEpIKACTRFRARILVFNIE-----VPITKGFPVLLHYQTVSEPAVIKrlisvLNKSTGEVtkkkpkllTKGQNAL 637
Cdd:PRK00049 295 LAKPGS-ITPHTKFEAEVYVLSKEeggrhTPFFNGYRPQFYFRTTDVTGVIE-----LPEGVEMV--------MPGDNVE 360
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 110611224 638 VELQTQRPVALElykdfKELgRFMLRYGGSTVAAGVVTEIKE 679
Cdd:PRK00049 361 MTVELIAPIAME-----EGL-RFAIREGGRTVGAGVVTKIIE 396
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
482-564 |
9.80e-47 |
|
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: 159.60 E-value: 9.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 482 PFRLCVSDVFKDQGSGFCVTGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINVGC 561
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
...
gi 110611224 562 IFC 564
Cdd:cd16267 81 ILC 83
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
262-677 |
2.71e-43 |
|
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: 165.47 E-value: 2.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 262 GHVDAGKSTLMghmlyllgnvnkrtmhkyeqeskKA--GKASfayawvlDETGEERERGVTMDVGMTKFETTT-KVITLM 338
Cdd:COG3276 7 GHIDHGKTTLV-----------------------KAltGIDT-------DRLKEEKKRGITIDLGFAYLPLPDgRRLGFV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 339 DAPGHKDFIPNMITGAAQADVAVLVVDASrgefeagfEtgG---QTREHGLLVRSLGVTQLAVAVNKMDQVN--WQQERF 413
Cdd:COG3276 57 DVPGHEKFIKNMLAGAGGIDLVLLVVAAD--------E--GvmpQTREHLAILDLLGIKRGIVVLTKADLVDeeWLELVE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 414 QEITGKL-GHFLKQAgfkesdvAFIPTSGLSGENLTArsqssdlttwykgmcLLEQIDSF--KPPQRSIDKPFRLCVSDV 490
Cdd:COG3276 127 EEIRELLaGTFLEDA-------PIVPVSAVTGEGIDE---------------LRAALDALaaAVPARDADGPFRLPIDRV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 491 FKDQGSGFCVTGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINVGCIFCGPkEPI 570
Cdd:COG3276 185 FSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAP-GAL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 571 KACTRFRARI-LVFNIEVPITKGFPVLLHYQTvSEpaVIKRlISVLNKSTgevtkkkpklLTKGQNALVELQTQRPVALe 649
Cdd:COG3276 264 RPTDRIDVRLrLLPSAPRPLKHWQRVHLHHGT-AE--VLAR-VVLLDREE----------LAPGEEALAQLRLEEPLVA- 328
|
410 420 430
....*....|....*....|....*....|
gi 110611224 650 LYKDfkelgRFMLRYGGS--TVAAGVVTEI 677
Cdd:COG3276 329 ARGD-----RFILRDYSPrrTIGGGRVLDP 353
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
257-475 |
3.44e-41 |
|
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: 148.21 E-value: 3.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYeqeskkagkasfayaWVLDETGEERERGVTMDVGMTKFETTTKVIT 336
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 337 LMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEfeagfetGGQTREHgLLVRSLGVTQLAVAVNKMDQVNwqQERFQEI 416
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREH-LNIALAGGLPIIVAVNKIDRVG--EEDFDEV 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110611224 417 TGKLGHFLKQAGF---KESDVAFIPTSGLSGEnltarsqssdlttwyKGMCLLEQIDSFKPP 475
Cdd:cd00881 136 LREIKELLKLIGFtflKGKDVPIIPISALTGE---------------GIEELLDAIVEHLPP 182
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
256-622 |
2.83e-39 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 153.11 E-value: 2.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 256 LNLVVIGHVDAGKSTLmghmLYLLGNVNKrtmhkyeqeskkagkasfayawvlDETGEERERGVTMDVGMTKFETTTKVI 335
Cdd:TIGR00475 1 MIIATAGHVDHGKTTL----LKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 336 TLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVTQLAVAVNKMDQVNwqQERFQE 415
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEG-------VMTQTGEHLAVLDLLGIPHTIVVITKADRVN--EEEIKR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 416 ITGKLGHFLKQAGFKESDVAFIpTSGLSGENLtarsqsSDLTTWYKGmcLLEQIDSfkppqRSIDKPFRLCVSDVFKDQG 495
Cdd:TIGR00475 124 TEMFMKQILNSYIFLKNAKIFK-TSAKTGQGI------GELKKELKN--LLESLDI-----KRIQKPLRMAIDRAFKVKG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 496 SGFCVTGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINVGCIFCGPKEPikactr 575
Cdd:TIGR00475 190 AGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDP------ 263
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 110611224 576 FRARILVFNIEVPITKGFPVLLHYQTvsepAVIKRLISVLNKSTGEV 622
Cdd:TIGR00475 264 KLRVVVKFIAEVPLLELQPYHIAHGM----SVTTGKISLLDKGIALL 306
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
256-475 |
2.25e-31 |
|
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: 121.15 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 256 LNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQEskkagkasfayawvlDETGEERERGVTMDVGMTKFETTTKVI 335
Cdd:cd01884 3 VNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEI---------------DKAPEEKARGITINTAHVEYETANRHY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 336 TLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNwQQERFQE 415
Cdd:cd01884 68 AHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD-DEELLEL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110611224 416 ITGKLGHFLKQAGFKESDVAFIPTSGLSG-ENLtarsqssDLTTWYKG-MCLLEQIDSFKPP 475
Cdd:cd01884 140 VEMEVRELLSKYGFDGDDTPIVRGSALKAlEGD-------DPNKWVDKiLELLDALDSYIPT 194
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
262-599 |
2.99e-26 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 113.99 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 262 GHVDAGKSTLmghmLYLLGNVNKrtmhkyeqeskkagkasfayawvlDETGEERERGVTMDVGMTKF-ETTTKVITLMDA 340
Cdd:PRK10512 7 GHVDHGKTTL----LQAITGVNA------------------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 341 PGHKDFIPNMITGAAQADVAVLVVDASRGEFeagfetgGQTREHGLLVRSLGVTQLAVAVNKMDQVNwqQERFQEITGKL 420
Cdd:PRK10512 59 PGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHLAILQLTGNPMLTVALTKADRVD--EARIAEVRRQV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 421 GHFLKQAGFkeSDVAFIPTSGLSGENLTArsqssdlttwykgmcLLEQIDSFKPPQRSIDKPFRLCVSDVFKDQGSGFCV 500
Cdd:PRK10512 130 KAVLREYGF--AEAKLFVTAATEGRGIDA---------------LREHLLQLPEREHAAQHRFRLAIDRAFTVKGAGLVV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 501 TGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGmDIIK--INVG--CIFCGPKEPIKactrf 576
Cdd:PRK10512 193 TGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAG-DAEKeqINRGdwLLADAPPEPFT----- 266
|
330 340
....*....|....*....|....
gi 110611224 577 raRILV-FNIEVPITKGFPVLLHY 599
Cdd:PRK10512 267 --RVIVeLQTHTPLTQWQPLHIHH 288
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
569-677 |
2.60e-24 |
|
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: 97.72 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 569 PIKACTRFRARILVFNIEV-----PITKGFPVLLHYQTVSEPAVIKRLISVLNksTGEVTKKKPKLLTkGQNALVELQTQ 643
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEggrhtPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSENPEFVMP-GDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|....
gi 110611224 644 RPVALELYKdfkelgRFMLRYGGSTVAAGVVTEI 677
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
262-447 |
5.70e-23 |
|
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: 96.14 E-value: 5.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 262 GHVDAGKSTLMghmlyllgnvnkrtmhkyeqeskKA--GKASfayawvlDETGEERERGVTMDVGMTKFE-TTTKVITLM 338
Cdd:cd04171 6 GHIDHGKTTLI-----------------------KAltGIET-------DRLPEEKKRGITIDLGFAYLDlPDGKRLGFI 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 339 DAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNwqQERFQEITG 418
Cdd:cd04171 56 DVPGHEKFVKNMLAGAGGIDAVLLVVAADEGIMP-------QTREHLEILELLGIKKGLVVLTKADLVD--EDRLELVEE 126
|
170 180
....*....|....*....|....*....
gi 110611224 419 KLGHFLKQAGFKESDVafIPTSGLSGENL 447
Cdd:cd04171 127 EILELLAGTFLADAPI--FPVSSVTGEGI 153
|
|
| HBS1_N |
pfam08938 |
HBS1 N-terminus; This domain is found at the N-terminus of HBS1 proteins. It interacts with ... |
45-123 |
3.02e-22 |
|
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: 90.72 E-value: 3.02e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110611224 45 RDNPEEEYGYEDLRESsnsllNHQLSEIDQARLYSCLDHMREVLGDAVPDDILTEAILKHKFDVQKALSVVLEQDGVQP 123
Cdd:pfam08938 1 DDYDDEEEEEEEEEEA-----DDELSDEDQELLNSCLPQVREVLGDSITDKQIKEALWHYYFDVEKAVDYLLNKFKKKK 74
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
571-677 |
4.34e-22 |
|
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: 91.46 E-value: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 571 KACTRFRARILVfnIEVP---ITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLTKGQNALVELQTQRPVA 647
Cdd:cd03704 1 PVVTEFEAQIVI--LDLLksiITAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPIC 78
|
90 100 110
....*....|....*....|....*....|
gi 110611224 648 LELYKDFKELGRFMLRYGGSTVAAGVVTEI 677
Cdd:cd03704 79 LETFKDFPQLGRFTLRDEGKTIAIGKVLKL 108
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
571-674 |
6.03e-20 |
|
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: 85.14 E-value: 6.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 571 KACTRFRARILVFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLtkGQNALVELQTQRPVALEL 650
Cdd:cd01513 1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEKKPPDSLQP--GENGTVEVELQKPVVLER 78
|
90 100
....*....|....*....|....
gi 110611224 651 YKDFKELGRFMLRYGGSTVAAGVV 674
Cdd:cd01513 79 GKEFPTLGRFALRDGGRTVGAGLI 102
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
257-445 |
1.87e-17 |
|
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: 80.87 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMghmlyllgnvnkrtmhkyEQESKKAGKASFayawvlDETGEERERGVTMDVGMTKFETTTKV-- 334
Cdd:cd01889 2 NVGLLGHVDSGKTSLA------------------KALSEIASTAAF------DKNPQSQERGITLDLGFSSFEVDKPKhl 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 335 ------------ITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRgefeaGFETggQTREHgLLVRSLGVTQLAVAVNK 402
Cdd:cd01889 58 ednenpqienyqITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKK-----GIQT--QTAEC-LVIGELLCKPLIVVLNK 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110611224 403 MD--QVNWQQERFQEITGKLGHFLKQAGFKesDVAFIPTSGLSGE 445
Cdd:cd01889 130 IDliPEEERKRKIEKMKKRLQKTLEKTRLK--DSPIIPVSAKPGE 172
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
482-564 |
2.38e-15 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 71.36 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 482 PFRLCVSDVFKDQGSgfCVTGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINVGC 561
Cdd:cd04089 1 PLRMPILDKYKDMGT--VVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78
|
...
gi 110611224 562 IFC 564
Cdd:cd04089 79 VLC 81
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
257-420 |
5.33e-15 |
|
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: 74.97 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMGHMLYLLGNVNKRTmhkyeqeSKKAGKASfayawvLDETGEERERGVTMDVGMTKFETTTKVIT 336
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELG-------SVDKGTTR------TDSMELERQRGITIFSAVASFQWEDTKVN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 337 LMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVTQLaVAVNKMDQVNWQQER-FQE 415
Cdd:cd04168 68 IIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTRILFRLLRKLNIPTI-IFVNKIDRAGADLEKvYQE 139
|
....*
gi 110611224 416 ITGKL 420
Cdd:cd04168 140 IKEKL 144
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
260-447 |
4.67e-14 |
|
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: 70.58 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 260 VIGHVDAGKSTLMGHMlyllgnvnkrtmhkyeQESKKAGKasfayawvldETGeererGVTMDVGMTKFETTTKV--ITL 337
Cdd:cd01887 5 VMGHVDHGKTTLLDKI----------------RKTNVAAG----------EAG-----GITQHIGAYQVPIDVKIpgITF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 338 MDAPGHKDFIpNMIT-GAAQADVAVLVVDASRGeFEAgfetggQTREHGLLVRSLGVtQLAVAVNKMDQVNWQQ---ERF 413
Cdd:cd01887 54 IDTPGHEAFT-NMRArGASVTDIAILVVAADDG-VMP------QTIEAINHAKAANV-PIIVAINKIDKPYGTEadpERV 124
|
170 180 190
....*....|....*....|....*....|....
gi 110611224 414 QEITGKLGHFLKQAGfkeSDVAFIPTSGLSGENL 447
Cdd:cd01887 125 KNELSELGLVGEEWG---GDVSIVPISAKTGEGI 155
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
482-564 |
5.88e-14 |
|
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: 67.53 E-value: 5.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 482 PFRLCVSDVFKDQgSGFCVTGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEP-VDWAAAGDHVNLTLVGMDIIKINVG 560
Cdd:cd03698 1 PFRLSIDDKYKSP-RGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEeTDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....
gi 110611224 561 CIFC 564
Cdd:cd03698 80 DILS 83
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
257-416 |
1.28e-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: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMGHMLYLLGNVNKRtmhkyeqESKKAGKAsfayawVLDETGEERERGVTMDVGMTKFETTTKVIT 336
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRL-------GRVEDGNT------VSDYDPEEKKRKMSIETSVAPLEWNGHKIN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 337 LMDAPGHKDFIPNMITGAAQADVAVLVVDAsrgefEAGFEtgGQTREHGLLVRSLGVTQLaVAVNKMDQVNwqqERFQEI 416
Cdd:cd04170 68 LIDTPGYADFVGETLSALRAVDAALIVVEA-----QSGVE--VGTEKVWEFLDDAKLPRI-IFINKMDRAR---ADFDKT 136
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
257-487 |
1.58e-13 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 72.96 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLmghmlyllgnVNKRTmhkyeqeskkaGKasfayaWVlDETGEERERGVTMDVGMTKFE------- 329
Cdd:PRK04000 11 NIGMVGHVDHGKTTL----------VQALT-----------GV------WT-DRHSEELKRGITIRLGYADATirkcpdc 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 330 ------TTTKV-------------ITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAgfetggQTREHGLLVRS 390
Cdd:PRK04000 63 eepeayTTEPKcpncgsetellrrVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEHLMALDI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 391 LGVTQLAVAVNKMDQVNWQQ--ERFQEITGklghFLKqaGFKESDVAFIPTSGLSGENLTArsqssdlttwykgmcLLEQ 468
Cdd:PRK04000 137 IGIKNIVIVQNKIDLVSKERalENYEQIKE----FVK--GTVAENAPIIPVSALHKVNIDA---------------LIEA 195
|
250 260
....*....|....*....|
gi 110611224 469 IDSF-KPPQRSIDKPFRLCV 487
Cdd:PRK04000 196 IEEEiPTPERDLDKPPRMYV 215
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
257-407 |
1.05e-12 |
|
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: 71.23 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMGHMLYLLGNVNKrtMHKYEqeskkAGKAsfayawVLDETGEERERGVTMDVGMTKFETTTKVIT 336
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHR--IGEVH-----DGNT------VMDWMPEEQERGITITSAATTCEWKGHKIN 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110611224 337 LMDAPGHKDFIPNMITGAAQADVAVLVVDASRGeFEAGFET-GGQTREHGLLVrslgvtqlAVAVNKMDQVN 407
Cdd:COG0480 78 IIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG-VEPQTETvWRQADKYGVPR--------IVFVNKMDREG 140
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
253-567 |
1.07e-12 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 71.28 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 253 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTmhkyEQESKkagkasfayawVLDETGEERERGVTMDVGMTKFETTT 332
Cdd:PRK10218 3 EKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRA----ETQER-----------VMDSNDLEKERGITILAKNTAIKWND 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 333 KVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAGFETGGQTREHGLlvrslgvtQLAVAVNKMD----QVNW 408
Cdd:PRK10218 68 YRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGL--------KPIVVINKVDrpgaRPDW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 409 QQERFQEITGKLghflkQAGFKESDVAFIPTSGLSG-ENLTARSQSSDLTTWYKGMclleqIDSFKPPQRSIDKPFRLCV 487
Cdd:PRK10218 140 VVDQVFDLFVNL-----DATDEQLDFPIVYASALNGiAGLDHEDMAEDMTPLYQAI-----VDHVPAPDVDLDGPFQMQI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 488 SDVFKDQGSGFCVTGKIEAGYIQTGDRLLAMpPNETCTAKG--------ITLHDEPVDWAAAGDHVNLTLVGmdiiKINV 559
Cdd:PRK10218 210 SQLDYNSYVGVIGIGRIKRGKVKPNQQVTII-DSEGKTRNAkvgkvlghLGLERIETDLAEAGDIVAITGLG----ELNI 284
|
....*...
gi 110611224 560 GCIFCGPK 567
Cdd:PRK10218 285 SDTVCDTQ 292
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
257-475 |
1.10e-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: 66.79 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHkyEQeskkagkasfayawVLDETGEERERGVTMD---VGM--TKFETT 331
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSEREMK--EQ--------------VLDSMDLERERGITIKaqaVRLfyKAKDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 332 TKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGeFEAgfetggQTREHGLLVRSLGVTQLAVaVNKMDQVNWQQE 411
Cdd:cd01890 66 EYLLNLIDTPGHVDFSYEVSRSLAACEGALLVVDATQG-VEA------QTLANFYLALENNLEIIPV-INKIDLPAADPD 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110611224 412 RF-QEITGKLghflkqaGFKESDVafIPTSGLSGENLTArsqssdlttwykgmcLLEQI-DSFKPP 475
Cdd:cd01890 138 RVkQEIEDVL-------GLDASEA--ILVSAKTGLGVED---------------LLEAIvERIPPP 179
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
261-407 |
4.81e-11 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 65.92 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 261 IGHVDAGKSTLMGHMLYLLGNVNKrtMHKYEqeskkaGKASfayawVLDETGEERERGVTMDVGMTKFETTTKVITLMDA 340
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHR--IGEVE------DGTT-----TMDFMPEERERGISITSAATTCEWKGHKINLIDT 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110611224 341 PGHKDFIPNMITGAAQADVAVLVVDASRGEfEAGFETG-GQTREHGLLVrslgvtqlAVAVNKMDQVN 407
Cdd:PRK12740 68 PGHVDFTGEVERALRVLDGAVVVVCAVGGV-EPQTETVwRQAEKYGVPR--------IIFVNKMDRAG 126
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
257-569 |
5.30e-11 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 65.81 E-value: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMGHMLYLLG------NVNKRTMHKYEQEskkagkasfayawvldetgeeRERGVTM-------DV 323
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQSGtfrenqEVAERVMDSNDLE---------------------RERGITIlakntavRY 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 324 GMTKfetttkvITLMDAPGHKDF------IPNMitgaaqADVAVLVVDAsrgeFEagfetgG---QTR-------EHGLL 387
Cdd:COG1217 67 KGVK-------INIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlkkalELGLK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 388 VrslgvtqlAVAVNKMDQ--------VNWQQERFQEitgkLGHFLKQAgfkesDVAFIPTSGLSG---ENLTArsQSSDL 456
Cdd:COG1217 124 P--------IVVINKIDRpdarpdevVDEVFDLFIE----LGATDEQL-----DFPVVYASARNGwasLDLDD--PGEDL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 457 TtwykgmCLLEQI-DSFKPPQRSIDKPFRLCVSDVFKDQGSGFCVTGKIEAGYIQTGDRLLAMPPNETcTAKG-IT---- 530
Cdd:COG1217 185 T------PLFDTIlEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALIKRDGK-VEKGkITklfg 257
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 110611224 531 ---LHDEPVDWAAAGDHVnlTLVGMDiiKINVGCIFCGPKEP 569
Cdd:COG1217 258 fegLERVEVEEAEAGDIV--AIAGIE--DINIGDTICDPENP 295
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
479-569 |
4.18e-10 |
|
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: 56.81 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 479 IDKPFRLCVSDVFKDQGSGFCVTGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKIN 558
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
90
....*....|.
gi 110611224 559 VGCIFCGPKEP 569
Cdd:cd03693 81 RGDVAGDSKND 91
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
571-674 |
5.14e-10 |
|
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: 56.82 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 571 KACTRFRARILVFNIEVPITKGF-PVLlHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLTKGQNALVELQTQRPVALE 649
Cdd:cd03705 1 KEAKSFTAQVIILNHPGQIKAGYtPVL-DCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVE 79
|
90 100
....*....|....*....|....*
gi 110611224 650 LYKDFKELGRFMLRYGGSTVAAGVV 674
Cdd:cd03705 80 TFSEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
257-369 |
7.41e-10 |
|
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: 59.55 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMGHMLYLLGNVNkrtmhkyeqeSKKAGKASFayawvLDETGEERERGVTMD---VGMtKFETTTK 333
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGIIS----------EKLAGKARY-----LDTREDEQERGITIKssaISL-YFEYEEE 65
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 110611224 334 -------VITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRG 369
Cdd:cd01885 66 kmdgndyLINLIDSPGHVDFSSEVTAALRLTDGALVVVDAVEG 108
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
257-369 |
7.68e-10 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 58.76 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMGHMLYLLG------NVNKRTMHKYEQeskkagkasfayawvldetgeERERGVTMDVGMTKFET 330
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGtfreneEVGERVMDSNDL---------------------ERERGITILAKNTAITY 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 110611224 331 TTKVITLMDAPGHKDF------IPNMitgaaqADVAVLVVDASRG 369
Cdd:cd01891 63 KDTKINIIDTPGHADFggeverVLSM------VDGVLLLVDASEG 101
|
|
| CysN_NoDQ_III |
cd04095 |
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of ... |
575-674 |
1.11e-09 |
|
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: 55.90 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 575 RFRARILVFNiEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEvtkkKPKLLTKGQN--ALVELQTQRPVALELYK 652
Cdd:cd04095 5 QFEATLVWMD-EKPLQPGRRYLLKHGTRTVRARVTEIDYRIDVNTLE----REPADTLALNdiGRVTLRLAEPLAFDPYA 79
|
90 100
....*....|....*....|....
gi 110611224 653 DFKELGRFML--RYGGSTVAAGVV 674
Cdd:cd04095 80 ENRATGSFILidRLTNATVAAGMI 103
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
256-449 |
1.24e-09 |
|
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: 58.43 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 256 LNLVVIGHVDAGKSTLmghmLYLLGNVnkRTM-HKYEQESKKAGKASFAYAWV-----------LDETGEERERGVtmdv 323
Cdd:cd01888 1 INIGTIGHVAHGKTTL----VKALSGV--WTVrHKEELKRNITIKLGYANAKIykcpncgcprpYDTPECECPGCG---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 324 GMTKFEtttKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASrgefeagfET--GGQTREHGLLVRSLGVTQLAVAVN 401
Cdd:cd01888 71 GETKLV---RHVSFVDCPGHEILMATMLSGAAVMDGALLLIAAN--------EPcpQPQTSEHLAALEIMGLKHIIILQN 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 110611224 402 KMDQVnwQQERFQEitgklgHFLKQAGFKESDVA----FIPTSGLSGENLTA 449
Cdd:cd01888 140 KIDLV--KEEQALE------NYEQIKEFVKGTIAenapIIPISAQLKYNIDV 183
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
257-452 |
2.06e-09 |
|
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: 58.07 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMGhmlyLL-------GNVNKRTM---HKYEQESKKAGKASFAyawVL--DETGE--ERERGVTMD 322
Cdd:cd04165 1 RVAVVGNVDAGKSTLLG----VLtqgeldnGRGKARLNlfrHKHEVESGRTSSVSND---ILgfDSDGEvvNYPDNHLGE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 323 VGMTKFETTTKVITLMDAPGHKDFIPNMITG--AAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVTqLAVAV 400
Cdd:cd04165 74 LDVEICEKSSKVVTFIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAG-------IIGMTKEHLGLALALKVP-VFVVV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110611224 401 NKMDQVNwqQERFQEITGKLGHFLKQAGFKESDVaFIPTSG---LSGENLTARSQ 452
Cdd:cd04165 146 TKIDMTP--ANVLQETLKDLKRLLKSPGVRKLPV-PVKSKDdvvLSASNLSSGRV 197
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
257-369 |
2.23e-09 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 58.05 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMgHMLYLLGNVNKRTMHKYEQESKkagkasfaYawvLDETGEERERGVTMD-VGMTKFETTTK-- 333
Cdd:cd04167 2 NVCIAGHLHHGKTSLL-DMLIEQTHKRTPSVKLGWKPLR--------Y---TDTRKDEQERGISIKsNPISLVLEDSKgk 69
|
90 100 110
....*....|....*....|....*....|....*...
gi 110611224 334 --VITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRG 369
Cdd:cd04167 70 syLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEG 107
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
253-406 |
6.86e-09 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 59.19 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 253 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKR-TMHKyeqeskkaGKAsfayawVLDETGEERERGVTMdvgmtkFETT 331
Cdd:PRK13351 6 MQIRNIGILAHIDAGKTTLTERILFYTGKIHKMgEVED--------GTT------VTDWMPQEQERGITI------ESAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 332 TKV------ITLMDAPGHKDFIPNMITGAAQADVAVLVVDASrgefeAGFETggQTRehgLLVRSL---GVTQLAVaVNK 402
Cdd:PRK13351 66 TSCdwdnhrINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAV-----TGVQP--QTE---TVWRQAdryGIPRLIF-INK 134
|
....
gi 110611224 403 MDQV 406
Cdd:PRK13351 135 MDRV 138
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
260-369 |
7.31e-09 |
|
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: 57.22 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 260 VIGHVDAGKSTL------MGHMLYLLGNVnkrtmhkyeqESKKAGKASfayawVLDETGEERERG--VTMDVgMTkFETT 331
Cdd:cd04169 7 IISHPDAGKTTLteklllFGGAIQEAGAV----------KARKSRKHA-----TSDWMEIEKQRGisVTSSV-MQ-FEYK 69
|
90 100 110
....*....|....*....|....*....|....*...
gi 110611224 332 TKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRG 369
Cdd:cd04169 70 GCVINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
253-369 |
1.09e-08 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 58.52 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 253 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNkrtmhkyeqeSKKAGKASFayawvLDETGEERERGVT-------MDVGM 325
Cdd:PTZ00416 17 DQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS----------SKNAGDARF-----TDTRADEQERGITikstgisLYYEH 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 110611224 326 TKFETTTK---VITLMDAPGHKDFiPNMITGAAQ-ADVAVLVVDASRG 369
Cdd:PTZ00416 82 DLEDGDDKqpfLINLIDSPGHVDF-SSEVTAALRvTDGALVVVDCVEG 128
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
483-560 |
2.70e-08 |
|
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: 51.37 E-value: 2.70e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110611224 483 FRLCVSDVFKDQGSGFCVTGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINVG 560
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
253-369 |
6.01e-08 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 56.02 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 253 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTmhkyeqeskkAGKASFayawvLDETGEERERGVTMD---VGMT-KF 328
Cdd:PRK07560 18 EQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEEL----------AGEQLA-----LDFDEEEQARGITIKaanVSMVhEY 82
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 110611224 329 ETTTKVITLMDAPGHKDFiPNMITGAAQA-DVAVLVVDASRG 369
Cdd:PRK07560 83 EGKEYLINLIDTPGHVDF-GGDVTRAMRAvDGAIVVVDAVEG 123
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
102-479 |
7.84e-08 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 55.61 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 102 LKHKFDVQKALSVVLEQDGVQpwKEKSERAVCAGQPSKVISRSSQSESEIVPK---VAKMTVSGKKQTmgfevpglTSEE 178
Cdd:CHL00189 77 LKQKKKIKKKLHIDDDYDNFF--DSKNNSKQFAGPLAISLMRKPKPKTEKLKKkitVNKSTNKKKKKV--------LSSK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 179 NGLSVRAPHkgpPGDDVSVASP----------NIPETGTPKS------ALPPPSL-------QTSEELGSTPTPVRKSG- 234
Cdd:CHL00189 147 DELIKYDNN---KPKSISIHSPltiqelstllCIPETEIIKSlflkgiSVTVNQIidisiisQVADDFGINIISEEKNNi 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 235 -----KLRQQIDVKAELEKRQGgkqllNLVVIGHVDAGKSTLMghmlyllgnvnkrtmHKYEQeSKKAGKasfayawvld 309
Cdd:CHL00189 224 nektsNLDNTSAFTENSINRPP-----IVTILGHVDHGKTTLL---------------DKIRK-TQIAQK---------- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 310 ETGeererGVTMDVGMTKFE----TTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHG 385
Cdd:CHL00189 273 EAG-----GITQKIGAYEVEfeykDENQKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIEAI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 386 LLVRSLGVTqLAVAVNKMDQVNWQQERFQE-------ITGKLGhflkqagfkeSDVAFIPTSGLSGEN-------LTARS 451
Cdd:CHL00189 341 NYIQAANVP-IIVAINKIDKANANTERIKQqlakynlIPEKWG----------GDTPMIPISASQGTNidklletILLLA 409
|
410 420 430
....*....|....*....|....*....|..
gi 110611224 452 QSSDL----TTWYKGMCLLEQIDSFKPPQRSI 479
Cdd:CHL00189 410 EIEDLkadpTQLAQGIILEAHLDKTKGPVATI 441
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
483-549 |
1.01e-07 |
|
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: 49.87 E-value: 1.01e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110611224 483 FRLCVSDVFKDQGS--GFCvtGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTL 549
Cdd:cd03695 1 FRFPVQYVNRPNLDfrGYA--GTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTL 67
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
257-422 |
2.57e-07 |
|
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: 52.49 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMGHMLYLLGNVNKrtMHkyEQESKKAgkasfayawVLDETGEERERGVTMDVGMTKFETTTKVIT 336
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHK--IG--EVHGGGA---------TMDWMEQERERGITIQSAATTCFWKDHRIN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 337 LMDAPGHKDFIPNMITGAAQADVAVLVVDASrgefeAGFETggQT----REhgllVRSLGVTQLAVaVNKMDQVNWQQER 412
Cdd:cd01886 68 IIDTPGHVDFTIEVERSLRVLDGAVAVFDAV-----AGVQP--QTetvwRQ----ADRYGVPRIAF-VNKMDRTGADFYR 135
|
170
....*....|.
gi 110611224 413 -FQEITGKLGH 422
Cdd:cd01886 136 vVEQIREKLGA 146
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
259-447 |
9.14e-07 |
|
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: 49.38 E-value: 9.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 259 VVIGHVDAGKSTLMGHMLYllGNVNkrtmhkyeqeskkagkasfayawvldETGEERERGVTMDVGMTKFETTTKVITLM 338
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLG--GEVG--------------------------EVSDVPGTTRDPDVYVKELDKGKVKLVLV 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 339 DAPGHKDFIPNMITGAA-----QADVAVLVVDASRGEFEAgfetgGQTREHGLLVRSLGVTQLAVAvNKMDQVNWQQERF 413
Cdd:cd00882 53 DTPGLDEFGGLGREELArlllrGADLILLVVDSTDRESEE-----DAKLLILRRLRKEGIPIILVG-NKIDLLEEREVEE 126
|
170 180 190
....*....|....*....|....*....|....
gi 110611224 414 QEITGKLghflkqagFKESDVAFIPTSGLSGENL 447
Cdd:cd00882 127 LLRLEEL--------AKILGVPVFEVSAKTGEGV 152
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
497-564 |
3.35e-06 |
|
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: 45.33 E-value: 3.35e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110611224 497 GFCVTGKIEAGYIQTGDRLLAMPP-----NETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINVGCIFC 564
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
335-513 |
7.45e-06 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 48.85 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 335 ITLMDAPGHKDFIPNMITGAAQADVAVLVVdasrgefeAGFET--GGQTREHGLLVRSLGVTQLAVAVNKMDQVNWQ--Q 410
Cdd:PTZ00327 119 VSFVDCPGHDILMATMLNGAAVMDAALLLI--------AANEScpQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAqaQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 411 ERFQEITgklgHFLKqaGFKESDVAFIPTSGLSGENLTarsqssdlttwykgmCLLEQIDSFKP-PQRSIDKPFRLCVS- 488
Cdd:PTZ00327 191 DQYEEIR----NFVK--GTIADNAPIIPISAQLKYNID---------------VVLEYICTQIPiPKRDLTSPPRMIVIr 249
|
170 180 190
....*....|....*....|....*....|..
gi 110611224 489 --DVFK-----DQGSGFCVTGKIEAGYIQTGD 513
Cdd:PTZ00327 250 sfDVNKpgediENLKGGVAGGSILQGVLKVGD 281
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
483-560 |
2.18e-05 |
|
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: 43.02 E-value: 2.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110611224 483 FRLCVSDVFKDQGSGFCVTGKIEAGYIQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDhvNLTLVGMDIIKINVG 560
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGD--IVGIGILGVKDILTG 76
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
257-449 |
3.68e-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: 44.67 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMGHMLYllgnvNKRTMHKYEQeskkagkasfayawvldetgeererGVTMDVGMTKFET--TTKV 334
Cdd:TIGR00231 3 KIVIVGHPNVGKSTLLNSLLG-----NKGSITEYYP-------------------------GTTRNYVTTVIEEdgKTYK 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 335 ITLMDAPGHKDF-------IPNMITGAAQADVAVLVVDASRGEFEagfetggQTREhglLVRSL--GVTQLaVAVNKMDQ 405
Cdd:TIGR00231 53 FNLLDTAGQEDYdairrlyYPQVERSLRVFDIVILVLDVEEILEK-------QTKE---IIHHAdsGVPII-LVGNKIDL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 110611224 406 VnwqQERFQEitgKLGHFLKQAGFKesdvAFIPTSGLSGENLTA 449
Cdd:TIGR00231 122 K---DADLKT---HVASEFAKLNGE----PIIPLSAETGKNIDS 155
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
259-447 |
5.16e-05 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 44.16 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 259 VVIGHVDAGKSTLM----GHMLYLLGNVNKRTMHKYeqeskkagkasfAYAWVLDETGEerergvtmdvgmtkfetttkv 334
Cdd:cd00880 1 AIFGRPNVGKSSLLnallGQNVGIVSPIPGTTRDPV------------RKEWELLPLGP--------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 335 ITLMDAPG-------HKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSlGVTQLAVAvNKMDQVN 407
Cdd:cd00880 48 VVLIDTPGldeegglGRERVEEARQVADRADLVLLVVDSDLTPVE-------EEAKLGLLRER-GKPVLLVL-NKIDLVP 118
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110611224 408 WQQERFQEITGKLGHFLkqagfkesDVAFIPTSGLSGENL 447
Cdd:cd00880 119 ESEEEELLRERKLELLP--------DLPVIAVSALPGEGI 150
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
241-369 |
1.25e-04 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 45.12 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 241 DVKAELEKRQggkqllNLVVIGHVDAGKSTLMGHMLyLLGNVnkrtmhkyEQE-----SKKAGKasfaYA---WVldetg 312
Cdd:PRK00741 2 ELAQEVAKRR------TFAIISHPDAGKTTLTEKLL-LFGGA--------IQEagtvkGRKSGR----HAtsdWM----- 57
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 313 E-ERERG--VTMDVgMtKFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRG 369
Cdd:PRK00741 58 EmEKQRGisVTSSV-M-QFPYRDCLINLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKG 115
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
256-447 |
1.74e-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: 42.80 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 256 LNLVVIGHVDAGKSTLMGHMLyllgnvnkrtmhkyeqeskkagkasfayawvldetGEER-----ERGVTMDVGMTKFET 330
Cdd:cd01895 3 IKIAIIGRPNVGKSSLLNALL-----------------------------------GEERvivsdIAGTTRDSIDVPFEY 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 331 TTKVITLMDAPG---------HKDFIPNMITGAA--QADVAVLVVDASRGEFEAGFETGGQTREHGL-LVrslgvtqlaV 398
Cdd:cd01895 48 DGQKYTLIDTAGirkkgkvteGIEKYSVLRTLKAieRADVVLLVLDASEGITEQDLRIAGLILEEGKaLI---------I 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 110611224 399 AVNKMDQVNWQQERFQEITGKLGHFLKQAGFkeSDVAFIptSGLSGENL 447
Cdd:cd01895 119 VVNKWDLVEKDEKTMKEFEKELRRKLPFLDY--APIVFI--SALTGQGV 163
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
257-369 |
3.35e-04 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 43.94 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 257 NLVVIGHVDAGKSTLMGHMLYLLGNVNkrtmhkyeqeSKKAGKASFAyawvlDETGEERERGVTM-DVGMTKFETTTK-- 333
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTDSLVAAAGIIA----------QEVAGDVRMT-----DTRADEAERGITIkSTGISLYYEMTDes 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 110611224 334 -------------VITLMDAPGHKDFiPNMITGAAQ-ADVAVLVVDASRG 369
Cdd:PLN00116 86 lkdfkgerdgneyLINLIDSPGHVDF-SSEVTAALRiTDGALVVVDCIEG 134
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
483-566 |
3.68e-04 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 39.81 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 483 FRLCVSDVFKDQGSGFCVTGKIEAGYIQTGD--RLLAMPPNETCTAKGITLHDEPVDWAAAGDHVNLTLVGMDIIKINVG 560
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDevEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*.
gi 110611224 561 CIFCGP 566
Cdd:cd03697 81 MVLAKP 86
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
323-445 |
5.23e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 40.25 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 323 VGMTKFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGeFEAgfetggQTREHGLLVRSLGvTQLAVAVNK 402
Cdd:PRK14845 516 LKLLKAEIKIPGLLFIDTPGHEAFTSLRKRGGSLADLAVLVVDINEG-FKP------QTIEAINILRQYK-TPFVVAANK 587
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110611224 403 MDQV-NWQQE----------------------RFQEITGKLGHFLKQAGFKE------SDVAFIPTSGLSGE 445
Cdd:PRK14845 588 IDLIpGWNISedepfllnfneqdqhalteleiKLYELIGKLYELGFDADRFDrvqdftRTVAIVPVSAKTGE 659
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
329-447 |
7.98e-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: 39.23 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611224 329 ETTTKVITLMDAPGHKDFipnmiT-----GAAQADVAVLVVDASRGEFEagfetggQTRE---HgllVRSLGVTqLAVAV 400
Cdd:COG0532 47 ETNGGKITFLDTPGHEAF-----TamrarGAQVTDIVILVVAADDGVMP-------QTIEainH---AKAAGVP-IIVAI 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 110611224 401 NKMDQVNWQQERF-QEITgklghflkQAGF-KES---DVAFIPTSGLSGENL 447
Cdd:COG0532 111 NKIDKPGANPDRVkQELA--------EHGLvPEEwggDTIFVPVSAKTGEGI 154
|
|
| |
