|
Name |
Accession |
Description |
Interval |
E-value |
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
259-682 |
6.96e-148 |
|
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: 436.29 E-value: 6.96e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 259 LNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTTKVV 338
Cdd:COG5256 8 LNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 339 TLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVTQLAVAVNKMDQVNWQQERFQE 418
Cdd:COG5256 88 TIIDAPGHRDFVKNMITGASQADAAILVVSAKDG-------VMGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 419 ITGKLGHFLKQAGFKESDVAFIPTSGLSGENLTSRSQSsdlTKWYKGLCLLEQIDSFKPPQRSIDKPFRLCVSDVFKDQG 498
Cdd:COG5256 161 VKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDN---MPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQDVYSISG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 499 SGFCVTGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGM---DIIKINVgcifCGPKE-PIK 574
Cdd:COG5256 238 IGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVeknDIKRGDV----AGHPDnPPT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 575 ACTRFRARILIFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLTKGQNALVELQTQRPVALELY 654
Cdd:COG5256 314 VAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEKF 393
|
410 420
....*....|....*....|....*...
gi 1958644154 655 KDFKELGRFMLRYGGSTVAAGVVTEIKE 682
Cdd:COG5256 394 KEFPQLGRFAIRDMGQTVAAGVVLDVKP 421
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
260-479 |
4.93e-141 |
|
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: 410.73 E-value: 4.93e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTTKVVT 339
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 340 LMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAGFETGGQTREHGLLVRSLGVTQLAVAVNKMDQV--NWQQERFQ 417
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644154 418 EITGKLGHFLKQAGFKESDVAFIPTSGLSGENLTsrsQSSDLTKWYKGLCLLEQIDSFKPPQ 479
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLI---EKSENMPWYKGPTLLEALDSLEPPE 219
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
256-682 |
2.77e-140 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 417.02 E-value: 2.77e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 256 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTT 335
Cdd:PRK12317 4 KPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 336 KVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEfeaGFEtgGQTREHGLLVRSLGVTQLAVAVNKMDQVNWQQER 415
Cdd:PRK12317 84 YYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAG---GVM--PQTREHVFLARTLGINQLIVAINKMDAVNYDEKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 416 FQEITGKLGHFLKQAGFKESDVAFIPTSGLSGENLTSRsqsSDLTKWYKGLCLLEQIDSFKPPQRSIDKPFRLCVSDVFK 495
Cdd:PRK12317 159 YEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKK---SENMPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQDVYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 496 DQGSGFCVTGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGM---DIIKINVgcifCGPKE- 571
Cdd:PRK12317 236 ISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVgkkDIKRGDV----CGHPDn 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 572 PIKACTRFRARILIFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLTKGQNALVELQTQRPVAL 651
Cdd:PRK12317 312 PPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVI 391
|
410 420 430
....*....|....*....|....*....|.
gi 1958644154 652 ELYKDFKELGRFMLRYGGSTVAAGVVTEIKE 682
Cdd:PRK12317 392 EKVKEIPQLGRFAIRDMGQTIAAGMVIDVKP 422
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
256-680 |
1.06e-133 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 400.66 E-value: 1.06e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 256 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTT 335
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 336 KVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAGFETGGQTREHGLLVRSLGVTQLAVAVNKMD--QVNWQQ 413
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 414 ERFQEITGKLGHFLKQAGFKESDVAFIPTSGLSGENLTSRsqsSDLTKWYKGLCLLEQIDSFKPPQRSIDKPFRLCVSDV 493
Cdd:PTZ00141 165 ERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEK---SDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 494 FKDQGSGFCVTGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFCGPK-EP 572
Cdd:PTZ00141 242 YKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKnDP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 573 IKACTRFRARILIFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLTKGQNALVELQTQRPVALE 652
Cdd:PTZ00141 322 AKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVE 401
|
410 420
....*....|....*....|....*...
gi 1958644154 653 LYKDFKELGRFMLRYGGSTVAAGVVTEI 680
Cdd:PTZ00141 402 VFNEYPPLGRFAVRDMKQTVAVGVIKSV 429
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
259-682 |
7.96e-98 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 308.17 E-value: 7.96e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 259 LNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTTKVV 338
Cdd:PLN00043 8 INIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 339 TLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAGFETGGQTREHGLLVRSLGVTQLAVAVNKMDQVN--WQQERF 416
Cdd:PLN00043 88 TVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTpkYSKARY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 417 QEITGKLGHFLKQAGFKESDVAFIPTSGLSGENLTSRSQSSDltkWYKGLCLLEQIDSFKPPQRSIDKPFRLCVSDVFKD 496
Cdd:PLN00043 168 DEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLD---WYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 497 QGSGFCVTGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFCGPK-EPIKA 575
Cdd:PLN00043 245 GGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKdDPAKE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 576 CTRFRARILIFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLTKGQNALVELQTQRPVALELYK 655
Cdd:PLN00043 325 AANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVVETFS 404
|
410 420
....*....|....*....|....*..
gi 1958644154 656 DFKELGRFMLRYGGSTVAAGVVTEIKE 682
Cdd:PLN00043 405 EYPPLGRFAVRDMRQTVAVGVIKSVEK 431
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
251-679 |
2.67e-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: 298.15 E-value: 2.67e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 251 KRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTK 330
Cdd:COG2895 10 AQHENKDLLRFITCGSVDDGKSTLIGRLLYDTKSIFEDQLAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 331 FETTTKVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVN 410
Cdd:COG2895 90 FSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 411 WQQERFQEITGKLGHFLKQAGFKesDVAFIPTSGLSGENLTSRSQSsdlTKWYKGLCLLEQIDSFKPPQRSIDKPFRLCV 490
Cdd:COG2895 163 YSEEVFEEIVADYRAFAAKLGLE--DITFIPISALKGDNVVERSEN---MPWYDGPTLLEHLETVEVAEDRNDAPFRFPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 491 SDVFKDQGS--GFCvtGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVgmDIIKINVGCIFCG 568
Cdd:COG2895 238 QYVNRPNLDfrGYA--GTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLE--DEIDISRGDVIVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 569 PKEPIKACTRFRARILIFNiEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEvtkkKPKLLTKGQN--ALVELQTQ 646
Cdd:COG2895 314 ADAPPEVADQFEATLVWMD-EEPLLPGRKYLLKHGTRTVRATVTAIKYRIDVNTLE----HEAADSLELNdiGRVTLRLA 388
|
410 420 430
....*....|....*....|....*....|....*
gi 1958644154 647 RPVALELYKDFKELGRFML--RYGGSTVAAGVVTE 679
Cdd:COG2895 389 EPIAFDPYADNRATGSFILidRLTNATVGAGMIRG 423
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
244-678 |
1.99e-64 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 224.81 E-value: 1.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 244 DVKAGLeKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAG--KASFAYAWVLDETGEERERG 321
Cdd:PRK05506 11 DILAYL-AQHERKSLLRFITCGSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 322 VTMDVGMTKFETTTKVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAV 401
Cdd:PRK05506 90 ITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 402 AVNKMDQVNWQQERFQEITGKLGHFLKQAGFkeSDVAFIPTSGLSGENLTSRSQSsdlTKWYKGLCLLEQIDSFKPPQRS 481
Cdd:PRK05506 163 AVNKMDLVDYDQEVFDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSAR---MPWYEGPSLLEHLETVEIASDR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 482 IDKPFRLCVSDVFKDQGS--GFCvtGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVgmDIIK 559
Cdd:PRK05506 238 NLKDFRFPVQYVNRPNLDfrGFA--GTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLA--DEID 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 560 INVGCIFCGPKEPIKACTRFRARILIFNiEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEvtKKKPKLLTKGQNA 639
Cdd:PRK05506 314 ISRGDMLARADNRPEVADQFDATVVWMA-EEPLLPGRPYLLKHGTRTVPASVAAIKYRVDVNTLE--RLAAKTLELNEIG 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958644154 640 LVELQTQRPVALELYKDFKELGRFML--RYGGSTVAAGVVT 678
Cdd:PRK05506 391 RCNLSTDAPIAFDPYARNRTTGSFILidRLTNATVGAGMID 431
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
259-677 |
1.00e-62 |
|
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: 214.16 E-value: 1.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 259 LNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESKKAGK--ASFAYAWVLDETGEERERGVTMDVGMTKFETTTK 336
Cdd:TIGR02034 1 LRFLTCGSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 337 VVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNWQQERF 416
Cdd:TIGR02034 81 KFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 417 QEITGKLGHFLKQAGFkeSDVAFIPTSGLSGENLTSRSQSSDltkWYKGLCLLEQIDSFKPPQRSIDKPFRLCVSDVFKD 496
Cdd:TIGR02034 154 ENIKKDYLAFAEQLGF--RDVTFIPLSALKGDNVVSRSESMP---WYSGPTLLEILETVEVERDAQDLPLRFPVQYVNRP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 497 QGS--GFcvTGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLvgMDIIKINVGCIFCGPKEPIK 574
Cdd:TIGR02034 229 NLDfrGY--AGTIASGSVHVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTL--DDEIDISRGDLLAAADSAPE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 575 ACTRFRARILIFNiEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEvtkkKPKLLTKGQNA--LVELQTQRPVALE 652
Cdd:TIGR02034 305 VADQFAATLVWMA-EEPLLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLE----KGAAKSLELNEigRVNLSLDEPIAFD 379
|
410 420
....*....|....*....|....*..
gi 1958644154 653 LYKDFKELGRFML--RYGGSTVAAGVV 677
Cdd:TIGR02034 380 PYAENRTTGAFILidRLSNRTVGAGMI 406
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
256-478 |
5.99e-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: 199.29 E-value: 5.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 256 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQESkkagkasfayawVLDETGEERERGVTMDVGMTKFETTT 335
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 336 KVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVtQLAVAVNKMDQVNwqQER 415
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGV-PIIVFINKMDRVD--GAE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644154 416 FQEITGKLGH-FLKQAGFKESDVAFIPTSGLSGENLTSrsqssdltkwykglcLLEQIDSFKPP 478
Cdd:pfam00009 139 LEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT---------------LLDALDEYLPS 187
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
260-479 |
6.09e-58 |
|
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: 194.71 E-value: 6.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQeSKKAGKA--SFAYAWVLDETGEERERGVTMDVGMTKFETTTKV 337
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAALER-SKSSGTQgeKLDLALLVDGLQAEREQGITIDVAYRYFSTPKRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 338 VTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNWQQERFQ 417
Cdd:cd04166 80 FIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644154 418 EITGKLGHFLKQAGFkeSDVAFIPTSGLSGENLTSRSQSsdlTKWYKGLCLLEQIDSFKPPQ 479
Cdd:cd04166 153 EIKADYLAFAASLGI--EDITFIPISALEGDNVVSRSEN---MPWYKGPTLLEHLETVEIAS 209
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
199-682 |
2.30e-55 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 196.37 E-value: 2.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 199 SIASPNVPETGTPKSTAHPPS--LQTSEELGCTPTPLRKSGKLRQQIDVKAGLEKRQGGKQLLNLVVIGHVDAGKSTLMG 276
Cdd:PLN03126 20 SSSSPSSSTFSFKSTSGKLKSltLSSSFLSPFSTTTTSTSQRRRRSFTVRAARGKFERKKPHVNIGTIGHVDHGKTTLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 277 HMLYLLGNVNKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMTKFETTTKVVTLMDAPGHKDFIPNMITG 356
Cdd:PLN03126 100 ALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 357 AAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNwQQERFQEITGKLGHFLKQAGFKESD 436
Cdd:PLN03126 165 AAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD-DEELLELVELEVRELLSSYEFPGDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 437 VAFIPTSGLSG-ENLTS-----RSQSSDLTKWYKglcLLEQIDSFKP-PQRSIDKPFRLCVSDVFKDQGSGFCVTGKIEA 509
Cdd:PLN03126 237 IPIISGSALLAlEALMEnpnikRGDNKWVDKIYE---LMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 510 GYVQTGD--RLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFCGPKEpIKACTRFRARILIFN 587
Cdd:PLN03126 314 GTVKVGEtvDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGS-ITPHTKFEAIVYVLK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 588 IE-----VPITKGFPVLLHYQTVSepaVIKRLISVLNKSTGEvtkkkPKLLTKGQNALVELQTQRPVALElykdfkELGR 662
Cdd:PLN03126 393 KEeggrhSPFFAGYRPQFYMRTTD---VTGKVTSIMNDKDEE-----SKMVMPGDRVKMVVELIVPVACE------QGMR 458
|
490 500
....*....|....*....|
gi 1958644154 663 FMLRYGGSTVAAGVVTEIKE 682
Cdd:PLN03126 459 FAIREGGKTVGAGVIQSIIE 478
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
250-682 |
9.64e-55 |
|
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: 9.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 250 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMT 329
Cdd:TIGR00485 4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQ---------------IDNAPEEKARGITINTAHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 330 KFETTTKVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 409
Cdd:TIGR00485 69 EYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 410 NwQQERFQEITGKLGHFLKQAGFKESDVAFIPTSGLSGenLTSRSQSSDltkwyKGLCLLEQIDSFKP-PQRSIDKPFRL 488
Cdd:TIGR00485 142 D-DEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKA--LEGDAEWEA-----KILELMDAVDEYIPtPEREIDKPFLL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 489 CVSDVFKDQGSGFCVTGKIEAGYVQTGDR--LLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIF 566
Cdd:TIGR00485 214 PIEDVFSITGRGTVVTGRVERGIIKVGEEveIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 567 CGPKEpIKACTRFRARILIFNIE-----VPITKGFPVLLHYQTVSEPAVIKRLISVlnkstgevtkkkpKLLTKGQNALV 641
Cdd:TIGR00485 294 AKPGS-IKPHTKFEAEVYVLSKEeggrhTPFFSGYRPQFYFRTTDVTGTIELPEGV-------------EMVMPGDNVKM 359
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958644154 642 ELQTQRPVALElykdfkELGRFMLRYGGSTVAAGVVTEIKE 682
Cdd:TIGR00485 360 TVELISPIALE------QGMRFAIREGGRTVGAGVVSKILE 394
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
256-682 |
1.43e-54 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 191.70 E-value: 1.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 256 KQLLNLVVIGHVDAGKSTLMGHMLYLLgnvnkrtmhkyeqeSKKAGKASFAYAWVlDETGEERERGVTMDVGMTKFETTT 335
Cdd:PRK12736 10 KPHVNIGTIGHVDHGKTTLTAAITKVL--------------AERGLNQAKDYDSI-DAAPEEKERGITINTAHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 336 KVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNwQQER 415
Cdd:PRK12736 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKVDLVD-DEEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 416 FQEITGKLGHFLKQAGFKESDVAFIPTSGLSGenLTSRSqssdltKWYKG-LCLLEQIDSFKP-PQRSIDKPFRLCVSDV 493
Cdd:PRK12736 147 LELVEMEVRELLSEYDFPGDDIPVIRGSALKA--LEGDP------KWEDAiMELMDAVDEYIPtPERDTDKPFLMPVEDV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 494 FKDQGSGFCVTGKIEAGYVQTGDR--LLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFCGPKE 571
Cdd:PRK12736 219 FTITGRGTVVTGRVERGTVKVGDEveIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 572 pIKACTRFRARILIFNIE-----VPITKGFPVLLHYQTVSEPAVIKrlisvLNKSTGEVtkkkpkllTKGQNALVELQTQ 646
Cdd:PRK12736 299 -IKPHTKFKAEVYILTKEeggrhTPFFNNYRPQFYFRTTDVTGSIE-----LPEGTEMV--------MPGDNVTITVELI 364
|
410 420 430
....*....|....*....|....*....|....*.
gi 1958644154 647 RPVALElykdfkELGRFMLRYGGSTVAAGVVTEIKE 682
Cdd:PRK12736 365 HPIAME------QGLKFAIREGGRTVGAGTVTEILD 394
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
250-682 |
1.48e-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: 191.90 E-value: 1.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 250 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMT 329
Cdd:COG0050 4 EKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQ---------------IDKAPEEKERGITINTSHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 330 KFETTTKVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 409
Cdd:COG0050 69 EYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 410 NwQQERFQEITGKLGHFLKQAGFKESDVAFIPTSGLSGENltsrsqSSDLTKWYKG-LCLLEQIDSFKP-PQRSIDKPFR 487
Cdd:COG0050 142 D-DEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKALE------GDPDPEWEKKiLELMDAVDSYIPePERDTDKPFL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 488 LCVSDVFKDQGSGFCVTGKIEAGYVQTGDR--LLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCI 565
Cdd:COG0050 215 MPVEDVFSITGRGTVVTGRVERGIIKVGDEveIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 566 FCGPKEpIKACTRFRARILIFNIE-----VPITKGFPVLLHYQTVSEPAVIKrlisvLNKSTGEVtkkkpkllTKGQNAL 640
Cdd:COG0050 295 LAKPGS-ITPHTKFEAEVYVLSKEeggrhTPFFNGYRPQFYFRTTDVTGVIT-----LPEGVEMV--------MPGDNVT 360
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958644154 641 VELQTQRPVALElykdfKELgRFMLRYGGSTVAAGVVTEIKE 682
Cdd:COG0050 361 MTVELITPIAME-----EGL-RFAIREGGRTVGAGVVTKIIE 396
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
241-679 |
6.48e-53 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 189.35 E-value: 6.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 241 QQIDVKAGLE---KRQGGKQLLNLVVIGHVDAGKSTLMGHMLYllgnvnkRTMHKYE-------QESKKAGKASFA--YA 308
Cdd:PRK05124 7 QQIANEGGVEaylHAQQHKSLLRFLTCGSVDDGKSTLIGRLLH-------DTKQIYEdqlaslhNDSKRHGTQGEKldLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 309 WVLDETGEERERGVTMDVGMTKFETTTKVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHG 388
Cdd:PRK05124 80 LLVDGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 389 LLVRSLGVTQLAVAVNKMDQVNWQQERFQEITGKLGHFLKQAGfKESDVAFIPTSGLSGENLTSRSQSsdlTKWYKGLCL 468
Cdd:PRK05124 153 FIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLP-GNLDIRFVPLSALEGDNVVSQSES---MPWYSGPTL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 469 LEQIDSFKPPQRSIDKPFRLCVSDV------FKdqgsGFCvtGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWA 542
Cdd:PRK05124 229 LEVLETVDIQRVVDAQPFRFPVQYVnrpnldFR----GYA--GTLASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 543 AAGDHVSLTLvgMDIIKINVGCIFCGPKEPIKACTRFRARIlIFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKST 622
Cdd:PRK05124 303 FAGEAITLVL--EDEIDISRGDLLVAADEALQAVQHASADV-VWMAEQPLQPGQSYDIKIAGKKTRARVDAIRYQVDINT 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644154 623 GEvtkkKPKLLTKGQNA--LVELQTQRPVALELYKDFKELGRFML--RYGGSTVAAGVVTE 679
Cdd:PRK05124 380 LT----QREAENLPLNGigLVELTFDEPLVLDPYQQNRVTGGFIFidRLTNVTVGAGMVRE 436
|
|
| tufA |
CHL00071 |
elongation factor Tu |
250-680 |
1.23e-51 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 184.39 E-value: 1.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 250 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMT 329
Cdd:CHL00071 4 EKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDE---------------IDSAPEEKARGITINTAHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 330 KFETTTKVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 409
Cdd:CHL00071 69 EYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 410 NwQQERFQEITGKLGHFLKQAGFKESDVAFIPTSGLsgENLTSRSQSSDLT----KWY-KGLCLLEQIDSFKP-PQRSID 483
Cdd:CHL00071 142 D-DEELLELVELEVRELLSKYDFPGDDIPIVSGSAL--LALEALTENPKIKrgenKWVdKIYNLMDAVDSYIPtPERDTD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 484 KPFRLCVSDVFKDQGSGFCVTGKIEAGYVQTGD--RLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKIN 561
Cdd:CHL00071 219 KPFLMAIEDVFSITGRGTVATGRIERGTVKVGDtvEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 562 VGCIFCGPKEpIKACTRFRARILIFNIE-----VPITKGFpvllhyqtvsEPAVIKRLISVlnksTGEVTKKKPKLLTKG 636
Cdd:CHL00071 299 RGMVLAKPGT-ITPHTKFEAQVYILTKEeggrhTPFFPGY----------RPQFYVRTTDV----TGKIESFTADDGSKT 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1958644154 637 QNAL--------VELQTqrPVALElykdfKELgRFMLRYGGSTVAAGVVTEI 680
Cdd:CHL00071 364 EMVMpgdrikmtVELIY--PIAIE-----KGM-RFAIREGGRTVGAGVVSKI 407
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
250-682 |
2.88e-50 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 180.03 E-value: 2.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 250 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMT 329
Cdd:PRK12735 4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQ---------------IDNAPEEKARGITINTSHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 330 KFETTTKVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 409
Cdd:PRK12735 69 EYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 410 NwQQERFQEITGKLGHFLKQAGFKESDVAFIPTSGLSGENltsrsqSSDLTKWYKG-LCLLEQIDSFKP-PQRSIDKPFR 487
Cdd:PRK12735 142 D-DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALE------GDDDEEWEAKiLELMDAVDSYIPePERAIDKPFL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 488 LCVSDVFKDQGSGFCVTGKIEAGYVQTGD--RLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCI 565
Cdd:PRK12735 215 MPIEDVFSISGRGTVVTGRVERGIVKVGDevEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 566 FCGPKEpIKACTRFRARILIFNIE-----VPITKGFPVLLHYQTVSEPAVIKrlisvLNKSTGEVtkkkpkllTKGQNAL 640
Cdd:PRK12735 295 LAKPGS-IKPHTKFEAEVYVLSKEeggrhTPFFNGYRPQFYFRTTDVTGTIE-----LPEGVEMV--------MPGDNVK 360
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958644154 641 VELQTQRPVALElykdfKELgRFMLRYGGSTVAAGVVTEIKE 682
Cdd:PRK12735 361 MTVELIAPIAME-----EGL-RFAIREGGRTVGAGVVAKIIE 396
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
572-680 |
5.30e-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: 169.65 E-value: 5.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 572 PIKACTRFRARILIFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLTKGQNALVELQTQRPVAL 651
Cdd:cd04093 1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80
|
90 100
....*....|....*....|....*....
gi 1958644154 652 ELYKDFKELGRFMLRYGGSTVAAGVVTEI 680
Cdd:cd04093 81 ETFKDNKELGRFVLRRGGETIAAGIVTEI 109
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
256-680 |
6.69e-49 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 177.71 E-value: 6.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 256 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMTKFETTT 335
Cdd:PLN03127 59 KPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDE---------------IDKAPEEKARGITIATAHVEYETAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 336 KVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNwQQER 415
Cdd:PLN03127 124 RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVD-DEEL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 416 FQEITGKLGHFLKQAGFKESDVAFIPTSGLSGENLTSRSQSSDltkwyKGLCLLEQIDSFKP-PQRSIDKPFRLCVSDVF 494
Cdd:PLN03127 196 LELVEMELRELLSFYKFPGDEIPIIRGSALSALQGTNDEIGKN-----AILKLMDAVDEYIPePVRVLDKPFLMPIEDVF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 495 KDQGSGFCVTGKIEAGYVQTGDRL----LAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFCGPK 570
Cdd:PLN03127 271 SIQGRGTVATGRVEQGTIKVGEEVeivgLRPGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 571 EpIKACTRFRARILIFNIEVPiTKGFPVLLHYQtvsePAVIKRLISVlnksTGEVTKKKPKLLTK-GQNALVELQTQRPV 649
Cdd:PLN03127 351 S-IKTYKKFEAEIYVLTKDEG-GRHTPFFSNYR----PQFYLRTADV----TGKVELPEGVKMVMpGDNVTAVFELISPV 420
|
410 420 430
....*....|....*....|....*....|.
gi 1958644154 650 ALELYKdfkelgRFMLRYGGSTVAAGVVTEI 680
Cdd:PLN03127 421 PLEPGQ------RFALREGGRTVGAGVVSKV 445
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
250-682 |
1.47e-48 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 175.38 E-value: 1.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 250 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLgnvnkrtmhkyeqeSKKAGKASFAYAWVlDETGEERERGVTMDVGMT 329
Cdd:PRK00049 4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITKVL--------------AKKGGAEAKAYDQI-DKAPEEKARGITINTAHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 330 KFETTTKVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 409
Cdd:PRK00049 69 EYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 410 NwQQERFQEITGKLGHFLKQAGFKESDVAFIPTSGLSGENltsrsqSSDLTKWYKG-LCLLEQIDSFKP-PQRSIDKPFR 487
Cdd:PRK00049 142 D-DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALE------GDDDEEWEKKiLELMDAVDSYIPtPERAIDKPFL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 488 LCVSDVFKDQGSGFCVTGKIEAGYVQTGD--RLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCI 565
Cdd:PRK00049 215 MPIEDVFSISGRGTVVTGRVERGIIKVGEevEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 566 FCGPKEpIKACTRFRARILIFNIE-----VPITKGFPVLLHYQTVSEPAVIKrlisvLNKSTGEVtkkkpkllTKGQNAL 640
Cdd:PRK00049 295 LAKPGS-ITPHTKFEAEVYVLSKEeggrhTPFFNGYRPQFYFRTTDVTGVIE-----LPEGVEMV--------MPGDNVE 360
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958644154 641 VELQTQRPVALElykdfKELgRFMLRYGGSTVAAGVVTEIKE 682
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 ... |
485-567 |
3.13e-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: 161.14 E-value: 3.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 485 PFRLCVSDVFKDQGSGFCVTGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGC 564
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
...
gi 1958644154 565 IFC 567
Cdd:cd16267 81 ILC 83
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
265-680 |
2.87e-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: 2.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 265 GHVDAGKSTLMghmlyllgnvnkrtmhkyeqeskKA--GKASfayawvlDETGEERERGVTMDVGMTKFETTT-KVVTLM 341
Cdd:COG3276 7 GHIDHGKTTLV-----------------------KAltGIDT-------DRLKEEKKRGITIDLGFAYLPLPDgRRLGFV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 342 DAPGHKDFIPNMITGAAQADVAVLVVDASrgefeagfEtgG---QTREHGLLVRSLGVTQLAVAVNKMDQVN--WQQERF 416
Cdd:COG3276 57 DVPGHEKFIKNMLAGAGGIDLVLLVVAAD--------E--GvmpQTREHLAILDLLGIKRGIVVLTKADLVDeeWLELVE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 417 QEITGKL-GHFLKQAgfkesdvAFIPTSGLSGENLTSrsqssdltkwykglcLLEQIDSF--KPPQRSIDKPFRLCVSDV 493
Cdd:COG3276 127 EEIRELLaGTFLEDA-------PIVPVSAVTGEGIDE---------------LRAALDALaaAVPARDADGPFRLPIDRV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 494 FKDQGSGFCVTGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFCGPkEPI 573
Cdd:COG3276 185 FSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAP-GAL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 574 KACTRFRARI-LIFNIEVPITKGFPVLLHYQTvSEpaVIKRlISVLNKSTgevtkkkpklLTKGQNALVELQTQRPVALe 652
Cdd:COG3276 264 RPTDRIDVRLrLLPSAPRPLKHWQRVHLHHGT-AE--VLAR-VVLLDREE----------LAPGEEALAQLRLEEPLVA- 328
|
410 420 430
....*....|....*....|....*....|
gi 1958644154 653 LYKDfkelgRFMLRYGGS--TVAAGVVTEI 680
Cdd:COG3276 329 ARGD-----RFILRDYSPrrTIGGGRVLDP 353
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
260-448 |
6.87e-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: 147.44 E-value: 6.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYeqeskkagkasfayaWVLDETGEERERGVTMDVGMTKFETTTKVVT 339
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 340 LMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEfeagfetGGQTREHgLLVRSLGVTQLAVAVNKMDQVNwqQERFQEI 419
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREH-LNIALAGGLPIIVAVNKIDRVG--EEDFDEV 135
|
170 180 190
....*....|....*....|....*....|..
gi 1958644154 420 TGKLGHFLKQAGF---KESDVAFIPTSGLSGE 448
Cdd:cd00881 136 LREIKELLKLIGFtflKGKDVPIIPISALTGE 167
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
259-625 |
1.04e-40 |
|
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: 157.34 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 259 LNLVVIGHVDAGKSTLmghmLYLLGNVNKrtmhkyeqeskkagkasfayawvlDETGEERERGVTMDVGMTKFETTTKVV 338
Cdd:TIGR00475 1 MIIATAGHVDHGKTTL----LKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 339 TLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVTQLAVAVNKMDQVNwqQERFQE 418
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEG-------VMTQTGEHLAVLDLLGIPHTIVVITKADRVN--EEEIKR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 419 ITGKLGHFLKQAGFKESDVAFIpTSGLSGENLtsrsqsSDLTKWYKGlcLLEQIDSfkppqRSIDKPFRLCVSDVFKDQG 498
Cdd:TIGR00475 124 TEMFMKQILNSYIFLKNAKIFK-TSAKTGQGI------GELKKELKN--LLESLDI-----KRIQKPLRMAIDRAFKVKG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 499 SGFCVTGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFCGPKEPikactr 578
Cdd:TIGR00475 190 AGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDP------ 263
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958644154 579 FRARILIFNIEVPITKGFPVLLHYQTvsepAVIKRLISVLNKSTGEV 625
Cdd:TIGR00475 264 KLRVVVKFIAEVPLLELQPYHIAHGM----SVTTGKISLLDKGIALL 306
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
259-478 |
5.59e-32 |
|
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: 122.69 E-value: 5.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 259 LNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHKYEQEskkagkasfayawvlDETGEERERGVTMDVGMTKFETTTKVV 338
Cdd:cd01884 3 VNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEI---------------DKAPEEKARGITINTAHVEYETANRHY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 339 TLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNwQQERFQE 418
Cdd:cd01884 68 AHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD-DEELLEL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644154 419 ITGKLGHFLKQAGFKESDVAFIPTSGLSG-ENLTSrsqssdlTKWYKG-LCLLEQIDSFKPP 478
Cdd:cd01884 140 VEMEVRELLSKYGFDGDDTPIVRGSALKAlEGDDP-------NKWVDKiLELLDALDSYIPT 194
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
265-563 |
1.02e-25 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 112.45 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 265 GHVDAGKSTLmghmLYLLGNVNKrtmhkyeqeskkagkasfayawvlDETGEERERGVTMDVGMTKF-ETTTKVVTLMDA 343
Cdd:PRK10512 7 GHVDHGKTTL----LQAITGVNA------------------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 344 PGHKDFIPNMITGAAQADVAVLVVDASRGEFeagfetgGQTREHGLLVRSLGVTQLAVAVNKMDQVNwqQERFQEITGKL 423
Cdd:PRK10512 59 PGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHLAILQLTGNPMLTVALTKADRVD--EARIAEVRRQV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 424 GHFLKQAGFkeSDVAFIPTSGLSGENLTSrsqssdltkwykglcLLEQIDSFKPPQRSIDKPFRLCVSDVFKDQGSGFCV 503
Cdd:PRK10512 130 KAVLREYGF--AEAKLFVTAATEGRGIDA---------------LREHLLQLPEREHAAQHRFRLAIDRAFTVKGAGLVV 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644154 504 TGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGmDIIK--INVG 563
Cdd:PRK10512 193 TGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAG-DAEKeqINRG 253
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
572-680 |
1.74e-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: 98.11 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 572 PIKACTRFRARILIFNIEV-----PITKGFPVLLHYQTVSEPAVIKRLISVLNksTGEVTKKKPKLLTkGQNALVELQTQ 646
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEggrhtPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSENPEFVMP-GDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|....
gi 1958644154 647 RPVALELYKdfkelgRFMLRYGGSTVAAGVVTEI 680
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
265-450 |
6.19e-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: 6.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 265 GHVDAGKSTLMghmlyllgnvnkrtmhkyeqeskKA--GKASfayawvlDETGEERERGVTMDVGMTKFE-TTTKVVTLM 341
Cdd:cd04171 6 GHIDHGKTTLI-----------------------KAltGIET-------DRLPEEKKRGITIDLGFAYLDlPDGKRLGFI 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 342 DAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNwqQERFQEITG 421
Cdd:cd04171 56 DVPGHEKFVKNMLAGAGGIDAVLLVVAADEGIMP-------QTREHLEILELLGIKKGLVVLTKADLVD--EDRLELVEE 126
|
170 180
....*....|....*....|....*....
gi 1958644154 422 KLGHFLKQAGFKESDVafIPTSGLSGENL 450
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 ... |
45-125 |
1.46e-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: 91.88 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 45 RDNPEEEYGYEDLKESsnsllNHQLSEIDQARLYSCLDHMREVLGDAVPDDILTEAILKHKFDVQKALSVVLEQDGVQTL 124
Cdd:pfam08938 1 DDYDDEEEEEEEEEEA-----DDELSDEDQELLNSCLPQVREVLGDSITDKQIKEALWHYYFDVEKAVDYLLNKFKKKKP 75
|
.
gi 1958644154 125 K 125
Cdd:pfam08938 76 K 76
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
574-680 |
1.89e-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: 92.62 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 574 KACTRFRARILIfnIEVP---ITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLTKGQNALVELQTQRPVA 650
Cdd:cd03704 1 PVVTEFEAQIVI--LDLLksiITAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPIC 78
|
90 100 110
....*....|....*....|....*....|
gi 1958644154 651 LELYKDFKELGRFMLRYGGSTVAAGVVTEI 680
Cdd:cd03704 79 LETFKDFPQLGRFTLRDEGKTIAIGKVLKL 108
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
574-677 |
6.11e-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: 6.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 574 KACTRFRARILIFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLtkGQNALVELQTQRPVALEL 653
Cdd:cd01513 1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEKKPPDSLQP--GENGTVEVELQKPVVLER 78
|
90 100
....*....|....*....|....
gi 1958644154 654 YKDFKELGRFMLRYGGSTVAAGVV 677
Cdd:cd01513 79 GKEFPTLGRFALRDGGRTVGAGLI 102
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
260-448 |
5.35e-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: 79.72 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMghmlyllgnvnkrtmhkyEQESKKAGKASFayawvlDETGEERERGVTMDVGMTKFETTTKV-- 337
Cdd:cd01889 2 NVGLLGHVDSGKTSLA------------------KALSEIASTAAF------DKNPQSQERGITLDLGFSSFEVDKPKhl 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 338 ------------VTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRgefeaGFETggQTREHgLLVRSLGVTQLAVAVNK 405
Cdd:cd01889 58 ednenpqienyqITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKK-----GIQT--QTAEC-LVIGELLCKPLIVVLNK 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958644154 406 MD--QVNWQQERFQEITGKLGHFLKQAGFKesDVAFIPTSGLSGE 448
Cdd:cd01889 130 IDliPEEERKRKIEKMKKRLQKTLEKTRLK--DSPIIPVSAKPGE 172
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
260-423 |
2.01e-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: 76.12 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMGHMLYLLGNVNKRTmhkyeqeSKKAGKASfayawvLDETGEERERGVTMDVGMTKFETTTKVVT 339
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELG-------SVDKGTTR------TDSMELERQRGITIFSAVASFQWEDTKVN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 340 LMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVTQLaVAVNKMDQVNWQQER-FQE 418
Cdd:cd04168 68 IIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTRILFRLLRKLNIPTI-IFVNKIDRAGADLEKvYQE 139
|
....*
gi 1958644154 419 ITGKL 423
Cdd:cd04168 140 IKEKL 144
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
485-567 |
2.15e-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: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 485 PFRLCVSDVFKDQGSgfCVTGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGC 564
Cdd:cd04089 1 PLRMPILDKYKDMGT--VVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78
|
...
gi 1958644154 565 IFC 567
Cdd:cd04089 79 VLC 81
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
485-567 |
8.23e-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: 67.14 E-value: 8.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 485 PFRLCVSDVFKDQgSGFCVTGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEP-VDWAAAGDHVSLTLVGMDIIKINVG 563
Cdd:cd03698 1 PFRLSIDDKYKSP-RGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEeTDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....
gi 1958644154 564 CIFC 567
Cdd:cd03698 80 DILS 83
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
263-450 |
1.10e-13 |
|
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: 69.42 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 263 VIGHVDAGKSTLMGHMlyllgnvnkrtmhkyeQESKKAGKasfayawvldETGeererGVTMDVGMTKFETTTKV--VTL 340
Cdd:cd01887 5 VMGHVDHGKTTLLDKI----------------RKTNVAAG----------EAG-----GITQHIGAYQVPIDVKIpgITF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 341 MDAPGHKDFIpNMIT-GAAQADVAVLVVDASRGeFEAgfetggQTREHGLLVRSLGVtQLAVAVNKMDQVNWQQ---ERF 416
Cdd:cd01887 54 IDTPGHEAFT-NMRArGASVTDIAILVVAADDG-VMP------QTIEAINHAKAANV-PIIVAINKIDKPYGTEadpERV 124
|
170 180 190
....*....|....*....|....*....|....
gi 1958644154 417 QEITGKLGHFLKQAGfkeSDVAFIPTSGLSGENL 450
Cdd:cd01887 125 KNELSELGLVGEEWG---GDVSIVPISAKTGEGI 155
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
260-419 |
2.27e-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: 70.70 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMGHMLYLLGNVNKRtmhkyeqESKKAGKAsfayawVLDETGEERERGVTMDVGMTKFETTTKVVT 339
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRL-------GRVEDGNT------VSDYDPEEKKRKMSIETSVAPLEWNGHKIN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 340 LMDAPGHKDFIPNMITGAAQADVAVLVVDAsrgefEAGFEtgGQTREHGLLVRSLGVTQLaVAVNKMDQVNwqqERFQEI 419
Cdd:cd04170 68 LIDTPGYADFVGETLSALRAVDAALIVVEA-----QSGVE--VGTEKVWEFLDDAKLPRI-IFINKMDRAR---ADFDKT 136
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
260-490 |
2.29e-13 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 72.58 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLmghmlyllgnVNKRTmhkyeqeskkaGKasfayaWVlDETGEERERGVTMDVGMTKFE------- 332
Cdd:PRK04000 11 NIGMVGHVDHGKTTL----------VQALT-----------GV------WT-DRHSEELKRGITIRLGYADATirkcpdc 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 333 ------TTTKV-------------VTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAgfetggQTREHGLLVRS 393
Cdd:PRK04000 63 eepeayTTEPKcpncgsetellrrVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEHLMALDI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 394 LGVTQLAVAVNKMDQVNWQQ--ERFQEITGklghFLKqaGFKESDVAFIPTSGLSGENLtsrsqssDLtkwykglcLLEQ 471
Cdd:PRK04000 137 IGIKNIVIVQNKIDLVSKERalENYEQIKE----FVK--GTVAENAPIIPVSALHKVNI-------DA--------LIEA 195
|
250 260
....*....|....*....|
gi 1958644154 472 IDSF-KPPQRSIDKPFRLCV 490
Cdd:PRK04000 196 IEEEiPTPERDLDKPPRMYV 215
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
256-570 |
3.60e-13 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 72.82 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 256 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTmhkyEQESKkagkasfayawVLDETGEERERGVTMDVGMTKFETTT 335
Cdd:PRK10218 3 EKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRA----ETQER-----------VMDSNDLEKERGITILAKNTAIKWND 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 336 KVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAGFETGGQTREHGLlvrslgvtQLAVAVNKMD----QVNW 411
Cdd:PRK10218 68 YRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGL--------KPIVVINKVDrpgaRPDW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 412 QQERFQEITGKLghflkQAGFKESDVAFIPTSGLSG-ENLTSRSQSSDLTKWYKGLclleqIDSFKPPQRSIDKPFRLCV 490
Cdd:PRK10218 140 VVDQVFDLFVNL-----DATDEQLDFPIVYASALNGiAGLDHEDMAEDMTPLYQAI-----VDHVPAPDVDLDGPFQMQI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 491 SDVFKDQGSGFCVTGKIEAGYVQTGDRLLAMpPNETCTAKG--------ITLHDEPVDWAAAGDHVSLTLVGmdiiKINV 562
Cdd:PRK10218 210 SQLDYNSYVGVIGIGRIKRGKVKPNQQVTII-DSEGKTRNAkvgkvlghLGLERIETDLAEAGDIVAITGLG----ELNI 284
|
....*...
gi 1958644154 563 GCIFCGPK 570
Cdd:PRK10218 285 SDTVCDTQ 292
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
260-478 |
3.61e-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: 65.25 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMGHMLYLLGNVNKRTMHkyEQeskkagkasfayawVLDETGEERERGVTMD---VGM--TKFETT 334
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSEREMK--EQ--------------VLDSMDLERERGITIKaqaVRLfyKAKDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 335 TKVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGeFEAgfetggQTREHGLLVRSLGVTQLAVaVNKMDQVNWQQE 414
Cdd:cd01890 66 EYLLNLIDTPGHVDFSYEVSRSLAACEGALLVVDATQG-VEA------QTLANFYLALENNLEIIPV-INKIDLPAADPD 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644154 415 RF-QEITGKLghflkqaGFKESDVafIPTSGLSGENLTSrsqssdltkwykglcLLEQI-DSFKPP 478
Cdd:cd01890 138 RVkQEIEDVL-------GLDASEA--ILVSAKTGLGVED---------------LLEAIvERIPPP 179
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
260-410 |
3.71e-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: 69.69 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMGHMLYLLGNVNKrtMHKYEqeskkAGKAsfayawVLDETGEERERGVTMDVGMTKFETTTKVVT 339
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHR--IGEVH-----DGNT------VMDWMPEEQERGITITSAATTCEWKGHKIN 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644154 340 LMDAPGHKDFIPNMITGAAQADVAVLVVDASRGeFEAGFET-GGQTREHGLLVrslgvtqlAVAVNKMDQVN 410
Cdd:COG0480 78 IIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG-VEPQTETvWRQADKYGVPR--------IVFVNKMDREG 140
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
264-410 |
1.05e-10 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 64.76 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 264 IGHVDAGKSTLMGHMLYLLGNVNKrtMHKYEqeskkaGKASfayawVLDETGEERERGVTMDVGMTKFETTTKVVTLMDA 343
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHR--IGEVE------DGTT-----TMDFMPEERERGISITSAATTCEWKGHKINLIDT 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644154 344 PGHKDFIPNMITGAAQADVAVLVVDASRGEfEAGFETG-GQTREHGLLVrslgvtqlAVAVNKMDQVN 410
Cdd:PRK12740 68 PGHVDFTGEVERALRVLDGAVVVVCAVGGV-EPQTETVwRQAEKYGVPR--------IIFVNKMDRAG 126
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
574-677 |
3.47e-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: 57.59 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 574 KACTRFRARILIFNIEVPITKGF-PVLlHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLTKGQNALVELQTQRPVALE 652
Cdd:cd03705 1 KEAKSFTAQVIILNHPGQIKAGYtPVL-DCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVE 79
|
90 100
....*....|....*....|....*
gi 1958644154 653 LYKDFKELGRFMLRYGGSTVAAGVV 677
Cdd:cd03705 80 TFSEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
259-450 |
6.90e-10 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 59.20 E-value: 6.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 259 LNLVVIGHVDAGKSTLmghmLYLLGNVnkRTM-HKYEQESKKAGKASFAYAWV-----------LDETGEERERGVtmdv 326
Cdd:cd01888 1 INIGTIGHVAHGKTTL----VKALSGV--WTVrHKEELKRNITIKLGYANAKIykcpncgcprpYDTPECECPGCG---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 327 GMTKFEtttKVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASrgefeagfET--GGQTREHGLLVRSLGVTQLAVAVN 404
Cdd:cd01888 71 GETKLV---RHVSFVDCPGHEILMATMLSGAAVMDGALLLIAAN--------EPcpQPQTSEHLAALEIMGLKHIIILQN 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958644154 405 KMDQVnwQQERFQEitgklgHFLKQAGFKESDVA----FIPTSGLSGENL 450
Cdd:cd01888 140 KIDLV--KEEQALE------NYEQIKEFVKGTIAenapIIPISAQLKYNI 181
|
|
| CysN_NoDQ_III |
cd04095 |
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of ... |
578-677 |
1.06e-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: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 578 RFRARILIFNiEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEvtkkKPKLLTKGQN--ALVELQTQRPVALELYK 655
Cdd:cd04095 5 QFEATLVWMD-EKPLQPGRRYLLKHGTRTVRARVTEIDYRIDVNTLE----REPADTLALNdiGRVTLRLAEPLAFDPYA 79
|
90 100
....*....|....*....|....
gi 1958644154 656 DFKELGRFML--RYGGSTVAAGVV 677
Cdd:cd04095 80 ENRATGSFILidRLTNATVAAGMI 103
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
482-572 |
1.06e-09 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 55.66 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 482 IDKPFRLCVSDVFKDQGSGFCVTGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKIN 561
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
90
....*....|.
gi 1958644154 562 VGCIFCGPKEP 572
Cdd:cd03693 81 RGDVAGDSKND 91
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
260-455 |
1.31e-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: 58.84 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMGhmlyLL-------GNVNKRTM---HKYEQESKKAGKASFAyawVL--DETGE--ERERGVTMD 325
Cdd:cd04165 1 RVAVVGNVDAGKSTLLG----VLtqgeldnGRGKARLNlfrHKHEVESGRTSSVSND---ILgfDSDGEvvNYPDNHLGE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 326 VGMTKFETTTKVVTLMDAPGHKDFIPNMITG--AAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVTqLAVAV 403
Cdd:cd04165 74 LDVEICEKSSKVVTFIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAG-------IIGMTKEHLGLALALKVP-VFVVV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958644154 404 NKMDQVnwQQERFQEITGKLGHFLKQAGFKESDVaFIPTSG---LSGENLTSRSQ 455
Cdd:cd04165 146 TKIDMT--PANVLQETLKDLKRLLKSPGVRKLPV-PVKSKDdvvLSASNLSSGRV 197
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
260-372 |
2.54e-09 |
|
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: 57.22 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMGHMLYLLG------NVNKRTMHKYEQeskkagkasfayawvldetgeERERGVTMDVGMTKFET 333
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGtfreneEVGERVMDSNDL---------------------ERERGITILAKNTAITY 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1958644154 334 TTKVVTLMDAPGHKDF------IPNMitgaaqADVAVLVVDASRG 372
Cdd:cd01891 63 KDTKINIIDTPGHADFggeverVLSM------VDGVLLLVDASEG 101
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
260-372 |
3.50e-09 |
|
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: 57.63 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMGHMLYLLGNVNkrtmhkyeqeSKKAGKASFayawvLDETGEERERGVTMD---VGMtKFETTTK 336
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGIIS----------EKLAGKARY-----LDTREDEQERGITIKssaISL-YFEYEEE 65
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958644154 337 -------VVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRG 372
Cdd:cd01885 66 kmdgndyLINLIDSPGHVDFSSEVTAALRLTDGALVVVDAVEG 108
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
260-372 |
4.41e-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: 56.89 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMgHMLYLLGNVNKRTMHKYEQESKkagkasfaYawvLDETGEERERGVTMD-VGMTKFETTTK-- 336
Cdd:cd04167 2 NVCIAGHLHHGKTSLL-DMLIEQTHKRTPSVKLGWKPLR--------Y---TDTRKDEQERGISIKsNPISLVLEDSKgk 69
|
90 100 110
....*....|....*....|....*....|....*...
gi 1958644154 337 --VVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRG 372
Cdd:cd04167 70 syLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEG 107
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
486-563 |
9.26e-09 |
|
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: 52.53 E-value: 9.26e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644154 486 FRLCVSDVFKDQGSGFCVTGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVG 563
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
263-372 |
1.60e-08 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 56.07 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 263 VIGHVDAGKSTL------MGHMLYLLGNVnkrtmhkyeqESKKAGKASfayawVLDETGEERERG--VTMDVgMTkFETT 334
Cdd:cd04169 7 IISHPDAGKTTLteklllFGGAIQEAGAV----------KARKSRKHA-----TSDWMEIEKQRGisVTSSV-MQ-FEYK 69
|
90 100 110
....*....|....*....|....*....|....*...
gi 1958644154 335 TKVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRG 372
Cdd:cd04169 70 GCVINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
256-409 |
3.45e-08 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 56.88 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 256 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKR-TMHKyeqeskkaGKAsfayawVLDETGEERERGVTMdvgmtkFETT 334
Cdd:PRK13351 6 MQIRNIGILAHIDAGKTTLTERILFYTGKIHKMgEVED--------GTT------VTDWMPQEQERGITI------ESAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 335 TKV------VTLMDAPGHKDFIPNMITGAAQADVAVLVVDASrgefeAGFETggQTRehgLLVRSL---GVTQLAVaVNK 405
Cdd:PRK13351 66 TSCdwdnhrINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAV-----TGVQP--QTE---TVWRQAdryGIPRLIF-INK 134
|
....
gi 1958644154 406 MDQV 409
Cdd:PRK13351 135 MDRV 138
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
486-552 |
3.56e-08 |
|
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: 51.03 E-value: 3.56e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644154 486 FRLCVSDVFKDQGS--GFCvtGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTL 552
Cdd:cd03695 1 FRFPVQYVNRPNLDfrGYA--GTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTL 67
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
256-372 |
4.56e-08 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 56.60 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 256 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNkrtmhkyeqeSKKAGKASFayawvLDETGEERERGVT-------MDVGM 328
Cdd:PTZ00416 17 DQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS----------SKNAGDARF-----TDTRADEQERGITikstgisLYYEH 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958644154 329 TKFETTTK---VVTLMDAPGHKDFiPNMITGAAQ-ADVAVLVVDASRG 372
Cdd:PTZ00416 82 DLEDGDDKqpfLINLIDSPGHVDF-SSEVTAALRvTDGALVVVDCVEG 128
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
256-372 |
2.88e-07 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 53.71 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 256 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNVNKRTmhkyeqeskkAGKASFayawvLDETGEERERGVTMD---VGMT-KF 331
Cdd:PRK07560 18 EQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEEL----------AGEQLA-----LDFDEEEQARGITIKaanVSMVhEY 82
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958644154 332 ETTTKVVTLMDAPGHKDFiPNMITGAAQA-DVAVLVVDASRG 372
Cdd:PRK07560 83 EGKEYLINLIDTPGHVDF-GGDVTRAMRAvDGAIVVVDAVEG 123
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
263-482 |
5.35e-07 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 52.91 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 263 VIGHVDAGKSTLMghmlyllgnvnkrtmHKYEQeSKKAGKasfayawvldETGeererGVTMDVGMTKFE----TTTKVV 338
Cdd:CHL00189 249 ILGHVDHGKTTLL---------------DKIRK-TQIAQK----------EAG-----GITQKIGAYEVEfeykDENQKI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 339 TLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVTqLAVAVNKMDQVNWQQERFQE 418
Cdd:CHL00189 298 VFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIEAINYIQAANVP-IIVAINKIDKANANTERIKQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 419 -------ITGKLGhflkqagfkeSDVAFIPTSGLSGEN-------LTSRSQSSDL----TKWYKGLCLLEQIDSFKPPQR 480
Cdd:CHL00189 370 qlakynlIPEKWG----------GDTPMIPISASQGTNidklletILLLAEIEDLkadpTQLAQGIILEAHLDKTKGPVA 439
|
..
gi 1958644154 481 SI 482
Cdd:CHL00189 440 TI 441
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
500-567 |
8.98e-07 |
|
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: 46.87 E-value: 8.98e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644154 500 GFCVTGKIEAGYVQTGDRLLAMPP-----NETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFC 567
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
260-425 |
1.02e-06 |
|
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: 50.57 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMGHMLYLLGNVNKrtMHkyEQESKKAgkasfayawVLDETGEERERGVTMDVGMTKFETTTKVVT 339
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHK--IG--EVHGGGA---------TMDWMEQERERGITIQSAATTCFWKDHRIN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 340 LMDAPGHKDFIPNMITGAAQADVAVLVVDASrgefeAGFETggQT----REhgllVRSLGVTQLAVaVNKMDQVNWQQER 415
Cdd:cd01886 68 IIDTPGHVDFTIEVERSLRVLDGAVAVFDAV-----AGVQP--QTetvwRQ----ADRYGVPRIAF-VNKMDRTGADFYR 135
|
170
....*....|.
gi 1958644154 416 -FQEITGKLGH 425
Cdd:cd01886 136 vVEQIREKLGA 146
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
262-450 |
1.23e-06 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 48.99 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 262 VVIGHVDAGKSTLMGHMLYllGNVNkrtmhkyeqeskkagkasfayawvldETGEERERGVTMDVGMTKFETTTKVVTLM 341
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLG--GEVG--------------------------EVSDVPGTTRDPDVYVKELDKGKVKLVLV 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 342 DAPGHKDFIPNMITGAA-----QADVAVLVVDASRGEFEAgfetgGQTREHGLLVRSLGVTQLAVAvNKMDQVNWQQERF 416
Cdd:cd00882 53 DTPGLDEFGGLGREELArlllrGADLILLVVDSTDRESEE-----DAKLLILRRLRKEGIPIILVG-NKIDLLEEREVEE 126
|
170 180 190
....*....|....*....|....*....|....
gi 1958644154 417 QEITGKLghflkqagFKESDVAFIPTSGLSGENL 450
Cdd:cd00882 127 LLRLEEL--------AKILGVPVFEVSAKTGEGV 152
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
338-516 |
8.99e-06 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 48.85 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 338 VTLMDAPGHKDFIPNMITGAAQADVAVLVVdasrgefeAGFET--GGQTREHGLLVRSLGVTQLAVAVNKMDQVNWQ--Q 413
Cdd:PTZ00327 119 VSFVDCPGHDILMATMLNGAAVMDAALLLI--------AANEScpQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAqaQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 414 ERFQEITgklgHFLKqaGFKESDVAFIPTSGLSGENLTsrsqssdltkwykglCLLEQIDSFKP-PQRSIDKPFRLCVS- 491
Cdd:PTZ00327 191 DQYEEIR----NFVK--GTIADNAPIIPISAQLKYNID---------------VVLEYICTQIPiPKRDLTSPPRMIVIr 249
|
170 180 190
....*....|....*....|....*....|..
gi 1958644154 492 --DVFK-----DQGSGFCVTGKIEAGYVQTGD 516
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 ... |
486-560 |
2.47e-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: 2.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644154 486 FRLCVSDVFKDQGSGFCVTGKIEAGYVQTGDRLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKI 560
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGVKDILT 75
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
260-452 |
3.37e-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: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMGHMLYllgnvNKRTMHKYEQeskkagkasfayawvldetgeererGVTMDVGMTKFET--TTKV 337
Cdd:TIGR00231 3 KIVIVGHPNVGKSTLLNSLLG-----NKGSITEYYP-------------------------GTTRNYVTTVIEEdgKTYK 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 338 VTLMDAPGHKDF-------IPNMITGAAQADVAVLVVDASRGEFEagfetggQTREhglLVRSL--GVTQLaVAVNKMDQ 408
Cdd:TIGR00231 53 FNLLDTAGQEDYdairrlyYPQVERSLRVFDIVILVLDVEEILEK-------QTKE---IIHHAdsGVPII-LVGNKIDL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958644154 409 VnwqQERFQEitgKLGHFLKQAGFKesdvAFIPTSGLSGENLTS 452
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 ... |
262-450 |
5.19e-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: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 262 VVIGHVDAGKSTLM----GHMLYLLGNVNKRTMHKYeqeskkagkasfAYAWVLDETGEerergvtmdvgmtkfetttkv 337
Cdd:cd00880 1 AIFGRPNVGKSSLLnallGQNVGIVSPIPGTTRDPV------------RKEWELLPLGP--------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 338 VTLMDAPG-------HKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSlGVTQLAVAvNKMDQVN 410
Cdd:cd00880 48 VVLIDTPGldeegglGRERVEEARQVADRADLVLLVVDSDLTPVE-------EEAKLGLLRER-GKPVLLVL-NKIDLVP 118
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958644154 411 WQQERFQEITGKLGHFLkqagfkesDVAFIPTSGLSGENL 450
Cdd:cd00880 119 ESEEEELLRERKLELLP--------DLPVIAVSALPGEGI 150
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
259-450 |
1.96e-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: 42.42 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 259 LNLVVIGHVDAGKSTLMGHMLyllgnvnkrtmhkyeqeskkagkasfayawvldetGEER-----ERGVTMDVGMTKFET 333
Cdd:cd01895 3 IKIAIIGRPNVGKSSLLNALL-----------------------------------GEERvivsdIAGTTRDSIDVPFEY 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 334 TTKVVTLMDAPG---------HKDFIPNMITGAA--QADVAVLVVDASRGEFEAGFETGGQTREHGL-LVrslgvtqlaV 401
Cdd:cd01895 48 DGQKYTLIDTAGirkkgkvteGIEKYSVLRTLKAieRADVVLLVLDASEGITEQDLRIAGLILEEGKaLI---------I 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958644154 402 AVNKMDQVNWQQERFQEITGKLGHFLKQAGFkeSDVAFIptSGLSGENL 450
Cdd:cd01895 119 VVNKWDLVEKDEKTMKEFEKELRRKLPFLDY--APIVFI--SALTGQGV 163
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
263-372 |
4.43e-04 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 43.20 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 263 VIGHVDAGKSTLMGHMLyLLGNVnkrtmhkyEQE-----SKKAGKasfaYA---WVldetgE-ERERG--VTMDVgMtKF 331
Cdd:PRK00741 15 IISHPDAGKTTLTEKLL-LFGGA--------IQEagtvkGRKSGR----HAtsdWM-----EmEKQRGisVTSSV-M-QF 74
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958644154 332 ETTTKVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRG 372
Cdd:PRK00741 75 PYRDCLINLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKG 115
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
486-569 |
4.91e-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: 39.42 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 486 FRLCVSDVFKDQGSGFCVTGKIEAGYVQTGD--RLLAMPPNETCTAKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVG 563
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDevEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*.
gi 1958644154 564 CIFCGP 569
Cdd:cd03697 81 MVLAKP 86
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
260-372 |
8.41e-04 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 42.79 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 260 NLVVIGHVDAGKSTLMGHMLYLLGNVNkrtmhkyeqeSKKAGKASFAyawvlDETGEERERGVTM-DVGMTKFETTTK-- 336
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTDSLVAAAGIIA----------QEVAGDVRMT-----DTRADEAERGITIkSTGISLYYEMTDes 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958644154 337 -------------VVTLMDAPGHKDFiPNMITGAAQ-ADVAVLVVDASRG 372
Cdd:PLN00116 86 lkdfkgerdgneyLINLIDSPGHVDF-SSEVTAALRiTDGALVVVDCIEG 134
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
326-448 |
6.34e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 39.87 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 326 VGMTKFETTTKVVTLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGeFEAgfetggQTREHGLLVRSLGvTQLAVAVNK 405
Cdd:PRK14845 516 LKLLKAEIKIPGLLFIDTPGHEAFTSLRKRGGSLADLAVLVVDINEG-FKP------QTIEAINILRQYK-TPFVVAANK 587
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644154 406 MDQV-NWQQE----------------------RFQEITGKLGHFLKQAGFKE------SDVAFIPTSGLSGE 448
Cdd:PRK14845 588 IDLIpGWNISedepfllnfneqdqhalteleiKLYELIGKLYELGFDADRFDrvqdftRTVAIVPVSAKTGE 659
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
262-448 |
9.79e-03 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 39.01 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 262 VVIGHVDAGKSTLmghmlylLGNVNKRTMHKYEqeskkAGkasfayawvldetgeererGVTMDVGMT------------ 329
Cdd:PRK04004 10 VVLGHVDHGKTTL-------LDKIRGTAVAAKE-----AG-------------------GITQHIGATevpidviekiag 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 330 ----KFETTTKVVTLM--DAPGHKDFiPNMIT-GAAQADVAVLVVDASRGeFEAgfetggQTREHGLLVRSLGvTQLAVA 402
Cdd:PRK04004 59 plkkPLPIKLKIPGLLfiDTPGHEAF-TNLRKrGGALADIAILVVDINEG-FQP------QTIEAINILKRRK-TPFVVA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644154 403 VNKMDQVN-W--------------QQERFQ--------EITGKlghfLKQAGFkESD-----------VAFIPTSGLSGE 448
Cdd:PRK04004 130 ANKIDRIPgWkstedapflesiekQSQRVQqeleeklyELIGQ----LSELGF-SADrfdrvkdftktVAIVPVSAKTGE 204
|
|
| |
