|
Name |
Accession |
Description |
Interval |
E-value |
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
97-520 |
1.68e-154 |
|
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: 447.46 E-value: 1.68e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 97 LNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTTKVI 176
Cdd:COG5256 8 LNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 177 TLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVTQLAVAVNKMDQVNWQQERFQE 256
Cdd:COG5256 88 TIIDAPGHRDFVKNMITGASQADAAILVVSAKDG-------VMGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 257 ITGKLGHFLKQAGFKESDVGFIPTSGLSGENLITRSQSselTKWYKGLCLLEQIDSFKPPQRSIDKPFRLCVSDVFKDQG 336
Cdd:COG5256 161 VKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDN---MPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQDVYSISG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 337 SGFCITGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGM---DIIKINVgcifCGPK-VPIK 412
Cdd:COG5256 238 IGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVeknDIKRGDV----AGHPdNPPT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 413 ACTRFRARILIFNIEIPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKFLTKGQNALVELQTQRPIALELY 492
Cdd:COG5256 314 VAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEKF 393
|
410 420
....*....|....*....|....*...
gi 1393428226 493 KDFKELGRFMLRYGGSTIAAGVVTEIKE 520
Cdd:COG5256 394 KEFPQLGRFAIRDMGQTVAAGVVLDVKP 421
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
94-520 |
1.37e-147 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 429.73 E-value: 1.37e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 94 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTT 173
Cdd:PRK12317 4 KPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 174 KVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEfeaGFEtgGQTREHGLLVRSLGVTQLAVAVNKMDQVNWQQER 253
Cdd:PRK12317 84 YYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAG---GVM--PQTREHVFLARTLGINQLIVAINKMDAVNYDEKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 254 FQEITGKLGHFLKQAGFKESDVGFIPTSGLSGENLITRsqsSELTKWYKGLCLLEQIDSFKPPQRSIDKPFRLCVSDVFK 333
Cdd:PRK12317 159 YEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKK---SENMPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQDVYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 334 DQGSGFCITGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGM---DIIKINVgcifCGP-KV 409
Cdd:PRK12317 236 ISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVgkkDIKRGDV----CGHpDN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 410 PIKACTRFRARILIFNIEIPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKFLTKGQNALVELQTQRPIAL 489
Cdd:PRK12317 312 PPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVI 391
|
410 420 430
....*....|....*....|....*....|.
gi 1393428226 490 ELYKDFKELGRFMLRYGGSTIAAGVVTEIKE 520
Cdd:PRK12317 392 EKVKEIPQLGRFAIRDMGQTIAAGMVIDVKP 422
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
98-317 |
6.39e-142 |
|
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: 407.26 E-value: 6.39e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTTKVIT 177
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 178 LMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAGFETGGQTREHGLLVRSLGVTQLAVAVNKMDQV--NWQQERFQ 255
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393428226 256 EITGKLGHFLKQAGFKESDVGFIPTSGLSGENLItrsQSSELTKWYKGLCLLEQIDSFKPPQ 317
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLI---EKSENMPWYKGPTLLEALDSLEPPE 219
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
94-518 |
1.41e-138 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 407.60 E-value: 1.41e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 94 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTT 173
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 174 KVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAGFETGGQTREHGLLVRSLGVTQLAVAVNKMD--QVNWQQ 251
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 252 ERFQEITGKLGHFLKQAGFKESDVGFIPTSGLSGENLITRSQSselTKWYKGLCLLEQIDSFKPPQRSIDKPFRLCVSDV 331
Cdd:PTZ00141 165 ERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDN---MPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 332 FKDQGSGFCITGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFCGPKV-P 410
Cdd:PTZ00141 242 YKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNdP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 411 IKACTRFRARILIFNIEIPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKFLTKGQNALVELQTQRPIALE 490
Cdd:PTZ00141 322 AKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVE 401
|
410 420
....*....|....*....|....*...
gi 1393428226 491 LYKDFKELGRFMLRYGGSTIAAGVVTEI 518
Cdd:PTZ00141 402 VFNEYPPLGRFAVRDMKQTVAVGVIKSV 429
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
97-520 |
6.85e-105 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 321.27 E-value: 6.85e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 97 LNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVTMDVGMTKFETTTKVI 176
Cdd:PLN00043 8 INIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 177 TLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAGFETGGQTREHGLLVRSLGVTQLAVAVNKMDQVN--WQQERF 254
Cdd:PLN00043 88 TVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTpkYSKARY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 255 QEITGKLGHFLKQAGFKESDVGFIPTSGLSGENLITRSQSSEltkWYKGLCLLEQIDSFKPPQRSIDKPFRLCVSDVFKD 334
Cdd:PLN00043 168 DEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLD---WYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 335 QGSGFCITGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFCGPKV-PIKA 413
Cdd:PLN00043 245 GGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDdPAKE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 414 CTRFRARILIFNIEIPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKFLTKGQNALVELQTQRPIALELYK 493
Cdd:PLN00043 325 AANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVVETFS 404
|
410 420
....*....|....*....|....*..
gi 1393428226 494 DFKELGRFMLRYGGSTIAAGVVTEIKE 520
Cdd:PLN00043 405 EYPPLGRFAVRDMRQTVAVGVIKSVEK 431
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
82-517 |
5.40e-97 |
|
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: 300.47 E-value: 5.40e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 82 DVKAELEKRQGgKQLLNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQESKKAGKASFAYAWVLDETGEERERGVT 161
Cdd:COG2895 4 DIEAYLAQHEN-KDLLRFITCGSVDDGKSTLIGRLLYDTKSIFEDQLAALERDSKKRGTQEIDLALLTDGLQAEREQGIT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 162 MDVGMTKFETTT-KVItLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVA 240
Cdd:COG2895 83 IDVAYRYFSTPKrKFI-IADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 241 VNKMDQVNWQQERFQEITGKLGHFLKQAGFKesDVGFIPTSGLSGENLITRsqsSELTKWYKGLCLLEQIDSFKPPQRSI 320
Cdd:COG2895 155 VNKMDLVDYSEEVFEEIVADYRAFAAKLGLE--DITFIPISALKGDNVVER---SENMPWYDGPTLLEHLETVEVAEDRN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 321 DKPFRLCVSDVFKDQGS--GFCitGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVgmDIIKI 398
Cdd:COG2895 230 DAPFRFPVQYVNRPNLDfrGYA--GTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLE--DEIDI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 399 NVGCIFCGPKVPIKACTRFRARILIFNiEIPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEvtKKKPKFLTKGQNAL 478
Cdd:COG2895 306 SRGDVIVAADAPPEVADQFEATLVWMD-EEPLLPGRKYLLKHGTRTVRATVTAIKYRIDVNTLE--HEAADSLELNDIGR 382
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1393428226 479 VELQTQRPIALELYKDFKELGRFML--RYGGSTIAAGVVTE 517
Cdd:COG2895 383 VTLRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMIRG 423
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
82-516 |
2.79e-68 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 230.97 E-value: 2.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 82 DVKAELeKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQESKKAG--KASFAYAWVLDETGEERERG 159
Cdd:PRK05506 11 DILAYL-AQHERKSLLRFITCGSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 160 VTMDVGMTKFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAV 239
Cdd:PRK05506 90 ITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 240 AVNKMDQVNWQQERFQEITGKLGHFLKQAGFkeSDVGFIPTSGLSGENLITRsqsSELTKWYKGLCLLEQIDSFKPPQRS 319
Cdd:PRK05506 163 AVNKMDLVDYDQEVFDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTR---SARMPWYEGPSLLEHLETVEIASDR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 320 IDKPFRLCVSDVFKDQGS--GFCitGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVgmDIIK 397
Cdd:PRK05506 238 NLKDFRFPVQYVNRPNLDfrGFA--GTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLA--DEID 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 398 INVGCIFCGPKVPIKACTRFRARILIFNiEIPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEvtKKKPKFLTKGQNA 477
Cdd:PRK05506 314 ISRGDMLARADNRPEVADQFDATVVWMA-EEPLLPGRPYLLKHGTRTVPASVAAIKYRVDVNTLE--RLAAKTLELNEIG 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1393428226 478 LVELQTQRPIALELYKDFKELGRFML--RYGGSTIAAGVVT 516
Cdd:PRK05506 391 RCNLSTDAPIAFDPYARNRTTGSFILidRLTNATVGAGMID 431
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
97-515 |
2.77e-65 |
|
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: 217.24 E-value: 2.77e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 97 LNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQESKKAGK--ASFAYAWVLDETGEERERGVTMDVGMTKFETTTK 174
Cdd:TIGR02034 1 LRFLTCGSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 175 VITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNWQQERF 254
Cdd:TIGR02034 81 KFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 255 QEITGKLGHFLKQAGFkeSDVGFIPTSGLSGENLITRSQSSEltkWYKGLCLLEQIDSFKPPQRSIDKPFRLCVSDVFKD 334
Cdd:TIGR02034 154 ENIKKDYLAFAEQLGF--RDVTFIPLSALKGDNVVSRSESMP---WYSGPTLLEILETVEVERDAQDLPLRFPVQYVNRP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 335 QGS--GFciTGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLvgMDIIKINVGCIFCGPKVPIK 412
Cdd:TIGR02034 229 NLDfrGY--AGTIASGSVHVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTL--DDEIDISRGDLLAAADSAPE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 413 ACTRFRARILIFNIEiPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEvtKKKPKFLTKGQNALVELQTQRPIALELY 492
Cdd:TIGR02034 305 VADQFAATLVWMAEE-PLLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLE--KGAAKSLELNEIGRVNLSLDEPIAFDPY 381
|
410 420
....*....|....*....|....*
gi 1393428226 493 KDFKELGRFML--RYGGSTIAAGVV 515
Cdd:TIGR02034 382 AENRTTGAFILidRLSNRTVGAGMI 406
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
94-316 |
6.25e-61 |
|
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: 198.52 E-value: 6.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 94 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQESkkagkasfayawVLDETGEERERGVTMDVGMTKFETTT 173
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 174 KVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVtQLAVAVNKMDQVNwqQER 253
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGV-PIIVFINKMDRVD--GAE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393428226 254 FQEITGKLGH-FLKQAGFKESDVGFIPTSGLSGENLITrsqsseltkwykglcLLEQIDSFKPP 316
Cdd:pfam00009 139 LEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT---------------LLDALDEYLPS 187
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
410-518 |
4.43e-60 |
|
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: 193.14 E-value: 4.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 410 PIKACTRFRARILIFNIEIPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKFLTKGQNALVELQTQRPIAL 489
Cdd:cd04093 1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80
|
90 100
....*....|....*....|....*....
gi 1393428226 490 ELYKDFKELGRFMLRYGGSTIAAGVVTEI 518
Cdd:cd04093 81 ETFKDNKELGRFVLRRGGETIAAGIVTEI 109
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
98-317 |
4.32e-59 |
|
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: 194.33 E-value: 4.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQeSKKAGKA--SFAYAWVLDETGEERERGVTMDVGMTKFETTTKV 175
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAALER-SKSSGTQgeKLDLALLVDGLQAEREQGITIDVAYRYFSTPKRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 176 ITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNWQQERFQ 255
Cdd:cd04166 80 FIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393428226 256 EITGKLGHFLKQAGFkeSDVGFIPTSGLSGENLITRsqsSELTKWYKGLCLLEQIDSFKPPQ 317
Cdd:cd04166 153 EIKADYLAFAASLGI--EDITFIPISALEGDNVVSR---SENMPWYKGPTLLEHLETVEIAS 209
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
41-520 |
7.20e-57 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 196.76 E-value: 7.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 41 SSDVLETASKSANPPHTIQASEEQSSTPAPVKKSGKLRQQIDVKAELEKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLL 120
Cdd:PLN03126 26 SSTFSFKSTSGKLKSLTLSSSFLSPFSTTTTSTSQRRRRSFTVRAARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 121 GNINKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMTKFETTTKVITLMDAPGHKDFIPNMITGAAQADV 200
Cdd:PLN03126 106 ASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 201 AVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNwQQERFQEITGKLGHFLKQAGFKESDVGFIPT 280
Cdd:PLN03126 171 AILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD-DEELLELVELEVRELLSSYEFPGDDIPIISG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 281 SGLSG-ENL-----ITRSQSSELTKWYKglcLLEQIDSFKP-PQRSIDKPFRLCVSDVFKDQGSGFCITGKIEAGYIQTG 353
Cdd:PLN03126 243 SALLAlEALmenpnIKRGDNKWVDKIYE---LMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 354 D--RLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFCGPKVpIKACTRFRARILIFNIE---- 427
Cdd:PLN03126 320 EtvDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGS-ITPHTKFEAIVYVLKKEeggr 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 428 -IPITKGFPVLLHYQTVSepaVIKRLISVLNKSTGEvtkkkPKFLTKGQNALVELQTQRPIALElykdfkELGRFMLRYG 506
Cdd:PLN03126 399 hSPFFAGYRPQFYMRTTD---VTGKVTSIMNDKDEE-----SKMVMPGDRVKMVVELIVPVACE------QGMRFAIREG 464
|
490
....*....|....
gi 1393428226 507 GSTIAAGVVTEIKE 520
Cdd:PLN03126 465 GKTVGAGVIQSIIE 478
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
88-520 |
2.92e-56 |
|
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: 193.07 E-value: 2.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 88 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMT 167
Cdd:TIGR00485 4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQ---------------IDNAPEEKARGITINTAHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 168 KFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 247
Cdd:TIGR00485 69 EYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 248 NwQQERFQEITGKLGHFLKQAGFKESDVGFIPTSGLS---GENlitrsqsseltKWY-KGLCLLEQIDSFKP-PQRSIDK 322
Cdd:TIGR00485 142 D-DEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKaleGDA-----------EWEaKILELMDAVDEYIPtPEREIDK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 323 PFRLCVSDVFKDQGSGFCITGKIEAGYIQTGDR--LLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINV 400
Cdd:TIGR00485 210 PFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEveIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIER 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 401 GCIFCGPKvPIKACTRFRARILIFNIE-----IPITKGFPVLLHYQTVSEPAVIKRLISVlnkstgevtkkkpKFLTKGQ 475
Cdd:TIGR00485 290 GMVLAKPG-SIKPHTKFEAEVYVLSKEeggrhTPFFSGYRPQFYFRTTDVTGTIELPEGV-------------EMVMPGD 355
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1393428226 476 NALVELQTQRPIALElykdfkELGRFMLRYGGSTIAAGVVTEIKE 520
Cdd:TIGR00485 356 NVKMTVELISPIALE------QGMRFAIREGGRTVGAGVVSKILE 394
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
94-520 |
1.25e-54 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 188.61 E-value: 1.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 94 KQLLNLVVIGHVDAGKSTLMGHMLYLLgninkrtmhkyeqeSKKAGKASFAYAWVlDETGEERERGVTMDVGMTKFETTT 173
Cdd:PRK12736 10 KPHVNIGTIGHVDHGKTTLTAAITKVL--------------AERGLNQAKDYDSI-DAAPEEKERGITINTAHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 174 KVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNwQQER 253
Cdd:PRK12736 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKVDLVD-DEEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 254 FQEITGKLGHFLKQAGFKESDVGFIPTSG---LSGENlitrsqsseltKWYKG-LCLLEQIDSFKP-PQRSIDKPFRLCV 328
Cdd:PRK12736 147 LELVEMEVRELLSEYDFPGDDIPVIRGSAlkaLEGDP-----------KWEDAiMELMDAVDEYIPtPERDTDKPFLMPV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 329 SDVFKDQGSGFCITGKIEAGYIQTGDR--LLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFCG 406
Cdd:PRK12736 216 EDVFTITGRGTVVTGRVERGTVKVGDEveIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 407 PKvPIKACTRFRARILIFNIEipitKG---FPVLLHYQtvsePAVIKRLISVlnksTGEVT-KKKPKFLTKGQNALVELQ 482
Cdd:PRK12736 296 PG-SIKPHTKFKAEVYILTKE----EGgrhTPFFNNYR----PQFYFRTTDV----TGSIElPEGTEMVMPGDNVTITVE 362
|
410 420 430
....*....|....*....|....*....|....*...
gi 1393428226 483 TQRPIALElykdfkELGRFMLRYGGSTIAAGVVTEIKE 520
Cdd:PRK12736 363 LIHPIAME------QGLKFAIREGGRTVGAGTVTEILD 394
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
88-520 |
2.26e-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: 188.05 E-value: 2.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 88 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMT 167
Cdd:COG0050 4 EKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQ---------------IDKAPEEKERGITINTSHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 168 KFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 247
Cdd:COG0050 69 EYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 248 NwQQERFQEITGKLGHFLKQAGFKESDVGFIPTSGLSGENlitrsqSSELTKWYKG-LCLLEQIDSFKP-PQRSIDKPFR 325
Cdd:COG0050 142 D-DEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKALE------GDPDPEWEKKiLELMDAVDSYIPePERDTDKPFL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 326 LCVSDVFKDQGSGFCITGKIEAGYIQTGDR--LLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCI 403
Cdd:COG0050 215 MPVEDVFSITGRGTVVTGRVERGIIKVGDEveIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 404 FCGPKvPIKACTRFRARILIFNIE-----IPITKGFpvllhyqtvsEPAVIKRLISVlnksTGEVTkkkpkfLTK----- 473
Cdd:COG0050 295 LAKPG-SITPHTKFEAEVYVLSKEeggrhTPFFNGY----------RPQFYFRTTDV----TGVIT------LPEgvemv 353
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1393428226 474 --GQNALVELQTQRPIALElykdfKELgRFMLRYGGSTIAAGVVTEIKE 520
Cdd:COG0050 354 mpGDNVTMTVELITPIAME-----EGL-RFAIREGGRTVGAGVVTKIIE 396
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
79-517 |
2.89e-54 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 189.74 E-value: 2.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 79 QQIDVKAELEKRQGgKQLLNLVVIGHVDAGKSTLMGHMLYllgninkRTMHKYE-------QESKKAGKASFA--YAWVL 149
Cdd:PRK05124 11 NEGGVEAYLHAQQH-KSLLRFLTCGSVDDGKSTLIGRLLH-------DTKQIYEdqlaslhNDSKRHGTQGEKldLALLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 150 DETGEERERGVTMDVGMTKFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLV 229
Cdd:PRK05124 83 DGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 230 RSLGVTQLAVAVNKMDQVNWQQERFQEITGKLGHFLKQAGfKESDVGFIPTSGLSGENLITRSQSselTKWYKGLCLLEQ 309
Cdd:PRK05124 156 TLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLP-GNLDIRFVPLSALEGDNVVSQSES---MPWYSGPTLLEV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 310 IDSFKPPQRSIDKPFRLCVSDV------FKdqgsGFCitGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAG 383
Cdd:PRK05124 232 LETVDIQRVVDAQPFRFPVQYVnrpnldFR----GYA--GTLASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 384 DHVSLTLvgMDIIKINVGCIFCGPKVPIKACTRFRARIlIFNIEIPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEv 463
Cdd:PRK05124 306 EAITLVL--EDEIDISRGDLLVAADEALQAVQHASADV-VWMAEQPLQPGQSYDIKIAGKKTRARVDAIRYQVDINTLT- 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1393428226 464 tKKKPKFLTKGQNALVELQTQRPIALELYKDFKELGRFML--RYGGSTIAAGVVTE 517
Cdd:PRK05124 382 -QREAENLPLNGIGLVELTFDEPLVLDPYQQNRVTGGFIFidRLTNVTVGAGMVRE 436
|
|
| tufA |
CHL00071 |
elongation factor Tu |
88-518 |
3.38e-53 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 185.16 E-value: 3.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 88 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMT 167
Cdd:CHL00071 4 EKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDE---------------IDSAPEEKARGITINTAHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 168 KFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 247
Cdd:CHL00071 69 EYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 248 NwQQERFQEITGKLGHFLKQAGFKESDVGFIPTSGLsgENLITRSQSSELT----KWY-KGLCLLEQIDSFKP-PQRSID 321
Cdd:CHL00071 142 D-DEELLELVELEVRELLSKYDFPGDDIPIVSGSAL--LALEALTENPKIKrgenKWVdKIYNLMDAVDSYIPtPERDTD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 322 KPFRLCVSDVFKDQGSGFCITGKIEAGYIQTGD--RLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKIN 399
Cdd:CHL00071 219 KPFLMAIEDVFSITGRGTVATGRIERGTVKVGDtvEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 400 VGCIFCGPKVpIKACTRFRARILIFNIE-----IPITKGFpvllhyqtvsEPAVIKRLISVlnksTGEVTK------KKP 468
Cdd:CHL00071 299 RGMVLAKPGT-ITPHTKFEAQVYILTKEeggrhTPFFPGY----------RPQFYVRTTDV----TGKIESftaddgSKT 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1393428226 469 KFLTKGQNALVELQTQRPIALElykdfKELgRFMLRYGGSTIAAGVVTEI 518
Cdd:CHL00071 364 EMVMPGDRIKMTVELIYPIAIE-----KGM-RFAIREGGRTVGAGVVSKI 407
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
94-518 |
5.85e-51 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 180.41 E-value: 5.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 94 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMTKFETTT 173
Cdd:PLN03127 59 KPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDE---------------IDKAPEEKARGITIATAHVEYETAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 174 KVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNwQQER 253
Cdd:PLN03127 124 RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVD-DEEL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 254 FQEITGKLGHFLKQAGFKESDVGFIPTSGLSGenliTRSQSSELTKwYKGLCLLEQIDSFKP-PQRSIDKPFRLCVSDVF 332
Cdd:PLN03127 196 LELVEMELRELLSFYKFPGDEIPIIRGSALSA----LQGTNDEIGK-NAILKLMDAVDEYIPePVRVLDKPFLMPIEDVF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 333 KDQGSGFCITGKIEAGYIQTGDRL----LAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFCGPK 408
Cdd:PLN03127 271 SIQGRGTVATGRVEQGTIKVGEEVeivgLRPGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 409 vPIKACTRFRARILIFNIEiPITKGFPVLLHYQtvsePAVIKRLISVlnksTGEVT-KKKPKFLTKGQNALVELQTQRPI 487
Cdd:PLN03127 351 -SIKTYKKFEAEIYVLTKD-EGGRHTPFFSNYR----PQFYLRTADV----TGKVElPEGVKMVMPGDNVTAVFELISPV 420
|
410 420 430
....*....|....*....|....*....|.
gi 1393428226 488 ALELYKdfkelgRFMLRYGGSTIAAGVVTEI 518
Cdd:PLN03127 421 PLEPGQ------RFALREGGRTVGAGVVSKV 445
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
88-520 |
2.16e-50 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 177.34 E-value: 2.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 88 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQeskkagkasfayawvLDETGEERERGVTMDVGMT 167
Cdd:PRK12735 4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQ---------------IDNAPEEKARGITINTSHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 168 KFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 247
Cdd:PRK12735 69 EYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 248 NwQQERFQEITGKLGHFLKQAGFKESDVGFIPTSGLSGENlitrsqSSELTKWYKG-LCLLEQIDSFKP-PQRSIDKPFR 325
Cdd:PRK12735 142 D-DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALE------GDDDEEWEAKiLELMDAVDSYIPePERAIDKPFL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 326 LCVSDVFKDQGSGFCITGKIEAGYIQTGD--RLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCI 403
Cdd:PRK12735 215 MPIEDVFSISGRGTVVTGRVERGIVKVGDevEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 404 FCGPKvPIKACTRFRARILIFNIE-----IPITKGFpvllhyqtvsEPAVIKRLISVlnksTGEVT-KKKPKFLTKGQNA 477
Cdd:PRK12735 295 LAKPG-SIKPHTKFEAEVYVLSKEeggrhTPFFNGY----------RPQFYFRTTDV----TGTIElPEGVEMVMPGDNV 359
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1393428226 478 LVELQTQRPIALElykdfKELgRFMLRYGGSTIAAGVVTEIKE 520
Cdd:PRK12735 360 KMTVELIAPIAME-----EGL-RFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
88-520 |
3.64e-49 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 174.22 E-value: 3.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 88 EKRQGGKQLLNLVVIGHVDAGKSTLMGHMLYLLgninkrtmhkyeqeSKKAGKASFAYAWVlDETGEERERGVTMDVGMT 167
Cdd:PRK00049 4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITKVL--------------AKKGGAEAKAYDQI-DKAPEEKARGITINTAHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 168 KFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQV 247
Cdd:PRK00049 69 EYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 248 NwQQERFQEITGKLGHFLKQAGFKESDVGFIPTSGLSGENlitrsqSSELTKWYKG-LCLLEQIDSFKP-PQRSIDKPFR 325
Cdd:PRK00049 142 D-DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALE------GDDDEEWEKKiLELMDAVDSYIPtPERAIDKPFL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 326 LCVSDVFKDQGSGFCITGKIEAGYIQTGD--RLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCI 403
Cdd:PRK00049 215 MPIEDVFSISGRGTVVTGRVERGIIKVGEevEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 404 FCGPKvPIKACTRFRARILIFNIE-----IPITKGFpvllhyqtvsEPAVIKRLISVlnksTGEVTkkkpkfLTKGQ--- 475
Cdd:PRK00049 295 LAKPG-SITPHTKFEAEVYVLSKEeggrhTPFFNGY----------RPQFYFRTTDV----TGVIE------LPEGVemv 353
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1393428226 476 ----NALVELQTQRPIALElykdfKELgRFMLRYGGSTIAAGVVTEIKE 520
Cdd:PRK00049 354 mpgdNVEMTVELIAPIAME-----EGL-RFAIREGGRTVGAGVVTKIIE 396
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
323-405 |
1.33e-48 |
|
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: 162.30 E-value: 1.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 323 PFRLCVSDVFKDQGSGFCITGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGC 402
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
...
gi 1393428226 403 IFC 405
Cdd:cd16267 81 ILC 83
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
103-518 |
1.27e-44 |
|
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: 166.24 E-value: 1.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 103 GHVDAGKSTLMghmlyllgninkrtmhkyeqeskKA--GKASfayawvlDETGEERERGVTMDVGMTKFETTT-KVITLM 179
Cdd:COG3276 7 GHIDHGKTTLV-----------------------KAltGIDT-------DRLKEEKKRGITIDLGFAYLPLPDgRRLGFV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 180 DAPGHKDFIPNMITGAAQADVAVLVVDASrgefeagfEtgG---QTREHGLLVRSLGVTQLAVAVNKMDQVNwqQERFQE 256
Cdd:COG3276 57 DVPGHEKFIKNMLAGAGGIDLVLLVVAAD--------E--GvmpQTREHLAILDLLGIKRGIVVLTKADLVD--EEWLEL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 257 ITGKLGHFLKQAGFKESDVgfIPTSGLSGENLitrsqsSELtkwykglclLEQIDSF--KPPQRSIDKPFRLCVSDVFKD 334
Cdd:COG3276 125 VEEEIRELLAGTFLEDAPI--VPVSAVTGEGI------DEL---------RAALDALaaAVPARDADGPFRLPIDRVFSI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 335 QGSGFCITGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFCGPKvPIKAC 414
Cdd:COG3276 188 KGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPG-ALRPT 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 415 TRFRARI-LIFNIEIPITKGFPVLLHYQTvSEpaVIKRlISVLNKSTgevtkkkpkfLTKGQNALVELQTQRPIALeLYK 493
Cdd:COG3276 267 DRIDVRLrLLPSAPRPLKHWQRVHLHHGT-AE--VLAR-VVLLDREE----------LAPGEEALAQLRLEEPLVA-ARG 331
|
410 420
....*....|....*....|....*..
gi 1393428226 494 DfkelgRFMLRYGGS--TIAAGVVTEI 518
Cdd:COG3276 332 D-----RFILRDYSPrrTIGGGRVLDP 353
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
97-474 |
1.16e-42 |
|
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: 160.04 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 97 LNLVVIGHVDAGKSTLmghmLYLLGNINKrtmhkyeqeskkagkasfayawvlDETGEERERGVTMDVGMTKFETTTKVI 176
Cdd:TIGR00475 1 MIIATAGHVDHGKTTL----LKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 177 TLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVTQLAVAVNKMDQVNwqQERFQE 256
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEG-------VMTQTGEHLAVLDLLGIPHTIVVITKADRVN--EEEIKR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 257 ITGKLGHFLKQAGF-KESDVgfIPTSGLSGENLitrsqsSELTKWYKGlcLLEQIDSfkppqRSIDKPFRLCVSDVFKDQ 335
Cdd:TIGR00475 124 TEMFMKQILNSYIFlKNAKI--FKTSAKTGQGI------GELKKELKN--LLESLDI-----KRIQKPLRMAIDRAFKVK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 336 GSGFCITGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFCGPKVPikact 415
Cdd:TIGR00475 189 GAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDP----- 263
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1393428226 416 rFRARILIFNIEIPITKGFPVLLHYQTvsepAVIKRLISVLNKSTGEVTKKKPKFLTKG 474
Cdd:TIGR00475 264 -KLRVVVKFIAEVPLLELQPYHIAHGM----SVTTGKISLLDKGIALLTLDAPLILAKG 317
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
98-286 |
8.72e-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: 145.13 E-value: 8.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYeqeskkagkasfayaWVLDETGEERERGVTMDVGMTKFETTTKVIT 177
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 178 LMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEfeagfetGGQTREHgLLVRSLGVTQLAVAVNKMDQVNwqQERFQEI 257
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREH-LNIALAGGLPIIVAVNKIDRVG--EEDFDEV 135
|
170 180 190
....*....|....*....|....*....|..
gi 1393428226 258 TGKLGHFLKQAGF---KESDVGFIPTSGLSGE 286
Cdd:cd00881 136 LREIKELLKLIGFtflKGKDVPIIPISALTGE 167
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
97-316 |
3.20e-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: 122.31 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 97 LNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQEskkagkasfayawvlDETGEERERGVTMDVGMTKFETTTKVI 176
Cdd:cd01884 3 VNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEI---------------DKAPEEKARGITINTAHVEYETANRHY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 177 TLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNwQQERFQE 256
Cdd:cd01884 68 AHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD-DEELLEL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393428226 257 ITGKLGHFLKQAGFKESDVGFIPTSGLSG-ENLITrsqsselTKWYKG-LCLLEQIDSFKPP 316
Cdd:cd01884 140 VEMEVRELLSKYGFDGDDTPIVRGSALKAlEGDDP-------NKWVDKiLELLDALDSYIPT 194
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
412-518 |
1.08e-29 |
|
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: 112.26 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 412 KACTRFRARILIfnIEIP---ITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKFLTKGQNALVELQTQRPIA 488
Cdd:cd03704 1 PVVTEFEAQIVI--LDLLksiITAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPIC 78
|
90 100 110
....*....|....*....|....*....|
gi 1393428226 489 LELYKDFKELGRFMLRYGGSTIAAGVVTEI 518
Cdd:cd03704 79 LETFKDFPQLGRFTLRDEGKTIAIGKVLKL 108
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
410-518 |
5.33e-29 |
|
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: 110.43 E-value: 5.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 410 PIKACTRFRARILIFNIE-----IPITKGFPVLLHYQTVSEPAVIKRLISVLNksTGEVTKKkPKFLTKGQNALVELQTQ 484
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEeggrhTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|....
gi 1393428226 485 RPIALELYKdfkelgRFMLRYGGSTIAAGVVTEI 518
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
103-401 |
6.19e-26 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 111.68 E-value: 6.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 103 GHVDAGKSTLmghmLYLLGNINKrtmhkyeqeskkagkasfayawvlDETGEERERGVTMDVGMTKF-ETTTKVITLMDA 181
Cdd:PRK10512 7 GHVDHGKTTL----LQAITGVNA------------------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 182 PGHKDFIPNMITGAAQADVAVLVVDASRGEFeagfetgGQTREHGLLVRSLGVTQLAVAVNKMDQVNwqQERFQEITGKL 261
Cdd:PRK10512 59 PGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHLAILQLTGNPMLTVALTKADRVD--EARIAEVRRQV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 262 GHFLKQAGFkeSDVGFIPTSGLSGENLITrsqsseltkwykglcLLEQIDSFKPPQRSIDKPFRLCVSDVFKDQGSGFCI 341
Cdd:PRK10512 130 KAVLREYGF--AEAKLFVTAATEGRGIDA---------------LREHLLQLPEREHAAQHRFRLAIDRAFTVKGAGLVV 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393428226 342 TGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGmDIIK--INVG 401
Cdd:PRK10512 193 TGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAG-DAEKeqINRG 253
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
103-288 |
1.50e-22 |
|
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: 94.59 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 103 GHVDAGKSTLmghmLYLLGNINKrtmhkyeqeskkagkasfayawvlDETGEERERGVTMDVGMTKFE-TTTKVITLMDA 181
Cdd:cd04171 6 GHIDHGKTTL----IKALTGIET------------------------DRLPEEKKRGITIDLGFAYLDlPDGKRLGFIDV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 182 PGHKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSLGVTQLAVAVNKMDQVNwqQERFQEITGKL 261
Cdd:cd04171 58 PGHEKFVKNMLAGAGGIDAVLLVVAADEGIMP-------QTREHLEILELLGIKKGLVVLTKADLVD--EDRLELVEEEI 128
|
170 180
....*....|....*....|....*..
gi 1393428226 262 GHFLKQAGFKESDVgfIPTSGLSGENL 288
Cdd:cd04171 129 LELLAGTFLADAPI--FPVSSVTGEGI 153
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
412-515 |
3.25e-22 |
|
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: 91.30 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 412 KACTRFRARILIFNIEIPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEvtKKKPKFLTKGQNALVELQTQRPIALEL 491
Cdd:cd01513 1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE--KKPPDSLQPGENGTVEVELQKPVVLER 78
|
90 100
....*....|....*....|....
gi 1393428226 492 YKDFKELGRFMLRYGGSTIAAGVV 515
Cdd:cd01513 79 GKEFPTLGRFALRDGGRTVGAGLI 102
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
323-405 |
2.14e-16 |
|
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: 74.06 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 323 PFRLCVSDVFKDQGSgfCITGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGC 402
Cdd:cd04089 1 PLRMPILDKYKDMGT--VVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78
|
...
gi 1393428226 403 IFC 405
Cdd:cd04089 79 VLC 81
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
98-286 |
2.66e-16 |
|
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: 77.02 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMghmlyllgninkrtmhkyEQESKKAGKASFayawvlDETGEERERGVTMDVGMTKFETTTKV-- 175
Cdd:cd01889 2 NVGLLGHVDSGKTSLA------------------KALSEIASTAAF------DKNPQSQERGITLDLGFSSFEVDKPKhl 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 176 ------------ITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRgefeaGFETggQTREHgLLVRSLGVTQLAVAVNK 243
Cdd:cd01889 58 ednenpqienyqITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKK-----GIQT--QTAEC-LVIGELLCKPLIVVLNK 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1393428226 244 MD--QVNWQQERFQEITGKLGHFLKQAGFKESDVgfIPTSGLSGE 286
Cdd:cd01889 130 IDliPEEERKRKIEKMKKRLQKTLEKTRLKDSPI--IPVSAKPGE 172
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
98-261 |
1.24e-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: 76.51 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGHMLYLLGNINKRTmhkyeqeSKKAGKASfayawvLDETGEERERGVTMDVGMTKFETTTKVIT 177
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELG-------SVDKGTTR------TDSMELERQRGITIFSAVASFQWEDTKVN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 178 LMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVTQLaVAVNKMDQVNWQQER-FQE 256
Cdd:cd04168 68 IIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTRILFRLLRKLNIPTI-IFVNKIDRAGADLEKvYQE 139
|
....*
gi 1393428226 257 ITGKL 261
Cdd:cd04168 140 IKEKL 144
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
323-405 |
5.39e-15 |
|
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: 70.22 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 323 PFRLCVSDVFKDQgSGFCITGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEP-VDWAAAGDHVSLTLVGMDIIKINVG 401
Cdd:cd03698 1 PFRLSIDDKYKSP-RGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEeTDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....
gi 1393428226 402 CIFC 405
Cdd:cd03698 80 DILS 83
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
98-257 |
1.84e-14 |
|
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: 73.40 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGHMLYLLGNINKRtmhkyeqESKKAGKAsfayawVLDETGEERERGVTMDVGMTKFETTTKVIT 177
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRL-------GRVEDGNT------VSDYDPEEKKRKMSIETSVAPLEWNGHKIN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 178 LMDAPGHKDFIPNMITGAAQADVAVLVVDAsrgefEAGFEtgGQTREHGLLVRSLGVTQLaVAVNKMDQVNwqqERFQEI 257
Cdd:cd04170 68 LIDTPGYADFVGETLSALRAVDAALIVVEA-----QSGVE--VGTEKVWEFLDDAKLPRI-IFINKMDRAR---ADFDKT 136
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
412-515 |
2.28e-14 |
|
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: 69.14 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 412 KACTRFRARILIFNIEIPITKGF-PVLlHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKFLTKGQNALVELQTQRPIALE 490
Cdd:cd03705 1 KEAKSFTAQVIILNHPGQIKAGYtPVL-DCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVE 79
|
90 100
....*....|....*....|....*
gi 1393428226 491 LYKDFKELGRFMLRYGGSTIAAGVV 515
Cdd:cd03705 80 TFSEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
98-248 |
1.95e-13 |
|
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: 72.77 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGHMLYLLGNINKrtMHKYEqeskkAGKAsfayawVLDETGEERERGVTMDVGMTKFETTTKVIT 177
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHR--IGEVH-----DGNT------VMDWMPEEQERGITITSAATTCEWKGHKIN 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393428226 178 LMDAPGHKDFIPNMITGAAQADVAVLVVDASRGeFEAGFET-GGQTREHGLLVrslgvtqlAVAVNKMDQVN 248
Cdd:COG0480 78 IIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG-VEPQTETvWRQADKYGVPR--------IVFVNKMDREG 140
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
101-288 |
4.30e-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: 67.11 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 101 VIGHVDAGKSTLMGHMlyllgninkrtmhkyeQESKKAGKasfayawvldETGeererGVTMDVGMTKFETTTKV--ITL 178
Cdd:cd01887 5 VMGHVDHGKTTLLDKI----------------RKTNVAAG----------EAG-----GITQHIGAYQVPIDVKIpgITF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 179 MDAPGHKDFIpNMIT-GAAQADVAVLVVDASRGeFEAgfetggQTREHGLLVRSLGVtQLAVAVNKMDQVNWQQ---ERF 254
Cdd:cd01887 54 IDTPGHEAFT-NMRArGASVTDIAILVVAADDG-VMP------QTIEAINHAKAANV-PIIVAINKIDKPYGTEadpERV 124
|
170 180 190
....*....|....*....|....*....|....
gi 1393428226 255 QEITGKLGHFLKQAGfkeSDVGFIPTSGLSGENL 288
Cdd:cd01887 125 KNELSELGLVGEEWG---GDVSIVPISAKTGEGI 155
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
94-408 |
2.10e-12 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 69.35 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 94 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNINKRTmhkyEQESKkagkasfayawVLDETGEERERGVTMDVGMTKFETTT 173
Cdd:PRK10218 3 EKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRA----ETQER-----------VMDSNDLEKERGITILAKNTAIKWND 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 174 KVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAGFETGGQTREHGLlvrslgvtQLAVAVNKMD----QVNW 249
Cdd:PRK10218 68 YRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGL--------KPIVVINKVDrpgaRPDW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 250 QQERFQEITGKLghflkQAGFKESDVGFIPTSGLSG-ENLITRSQSSELTKWYKGLclleqIDSFKPPQRSIDKPFRLCV 328
Cdd:PRK10218 140 VVDQVFDLFVNL-----DATDEQLDFPIVYASALNGiAGLDHEDMAEDMTPLYQAI-----VDHVPAPDVDLDGPFQMQI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 329 SDVFKDQGSGFCITGKIEAGYIQTGDRLLAMpPNETCTVKG--------ITLHDEPVDWAAAGDHVSLTLVGmdiiKINV 400
Cdd:PRK10218 210 SQLDYNSYVGVIGIGRIKRGKVKPNQQVTII-DSEGKTRNAkvgkvlghLGLERIETDLAEAGDIVAITGLG----ELNI 284
|
....*...
gi 1393428226 401 GCIFCGPK 408
Cdd:PRK10218 285 SDTVCDTQ 292
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
98-287 |
2.96e-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: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHkyEQeskkagkasfayawVLDETGEERERGVTMD---VGM--TKFETT 172
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSEREMK--EQ--------------VLDSMDLERERGITIKaqaVRLfyKAKDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 173 TKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGeFEAgfetggQTREHGLLVRSLGVTQLAVaVNKMDQVNWQQE 252
Cdd:cd01890 66 EYLLNLIDTPGHVDFSYEVSRSLAACEGALLVVDATQG-VEA------QTLANFYLALENNLEIIPV-INKIDLPAADPD 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 1393428226 253 RF-QEITGKLghflkqaGFKESDVgfIPTSGLSGEN 287
Cdd:cd01890 138 RVkQEIEDVL-------GLDASEA--ILVSAKTGLG 164
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
98-354 |
3.64e-12 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 67.95 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLmghmlyllgninkrtmhkyeqeskkagkasfAYA----WVlDETGEERERGVTMDVGMTKFE--- 170
Cdd:PRK04000 11 NIGMVGHVDHGKTTL-------------------------------VQAltgvWT-DRHSEELKRGITIRLGYADATirk 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 171 ----------TTTKV-------------ITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGEFEAgfetggQTREHGL 227
Cdd:PRK04000 59 cpdceepeayTTEPKcpncgsetellrrVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEHLM 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 228 LVRSLGVTQLAVAVNKMDQVNWQQ--ERFQEITGklghFLKqaGFKESDVGFIPTSGLSGENLITrsqsseltkwykglc 305
Cdd:PRK04000 133 ALDIIGIKNIVIVQNKIDLVSKERalENYEQIKE----FVK--GTVAENAPIIPVSALHKVNIDA--------------- 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1393428226 306 LLEQIDSF-KPPQRSIDKPFRLCVS---DVFK-----DQGSGFCITGKIEAGYIQTGD 354
Cdd:PRK04000 192 LIEAIEEEiPTPERDLDKPPRMYVArsfDVNKpgtppEKLKGGVIGGSLIQGVLKVGD 249
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
102-248 |
4.71e-12 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 68.61 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 102 IGHVDAGKSTLMGHMLYLLGNINKrtMHKYEqeskkaGKASfayawVLDETGEERERGVTMDVGMTKFETTTKVITLMDA 181
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHR--IGEVE------DGTT-----TMDFMPEERERGISITSAATTCEWKGHKINLIDT 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393428226 182 PGHKDFIPNMITGAAQADVAVLVVDASRGEfEAGFETG-GQTREHGLLVrslgvtqlAVAVNKMDQVN 248
Cdd:PRK12740 68 PGHVDFTGEVERALRVLDGAVVVVCAVGGV-EPQTETVwRQAEKYGVPR--------IIFVNKMDRAG 126
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
98-210 |
7.55e-11 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 61.86 E-value: 7.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGHMLYLLGNINkrtmhkyeqeSKKAGKASFayawvLDETGEERERGVTMD---VGMtKFETTTK 174
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGIIS----------EKLAGKARY-----LDTREDEQERGITIKssaISL-YFEYEEE 65
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1393428226 175 -------VITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRG 210
Cdd:cd01885 66 kmdgndyLINLIDSPGHVDFSSEVTAALRLTDGALVVVDAVEG 108
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
320-408 |
1.56e-10 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 57.58 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 320 IDKPFRLCVSDVFKDQGSGFCITGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKIN 399
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
....*....
gi 1393428226 400 VGCIFCGPK 408
Cdd:cd03693 81 RGDVAGDSK 89
|
|
| CysN_NoDQ_III |
cd04095 |
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of ... |
416-515 |
5.07e-10 |
|
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: 56.68 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 416 RFRARILIFNiEIPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEvtKKKPKFLTKGQNALVELQTQRPIALELYKDF 495
Cdd:cd04095 5 QFEATLVWMD-EKPLQPGRRYLLKHGTRTVRARVTEIDYRIDVNTLE--REPADTLALNDIGRVTLRLAEPLAFDPYAEN 81
|
90 100
....*....|....*....|..
gi 1393428226 496 KELGRFML--RYGGSTIAAGVV 515
Cdd:cd04095 82 RATGSFILidRLTNATVAAGMI 103
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
98-410 |
6.14e-10 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 61.57 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGHMLYLLGninkrTMHKYEQESKKagkasfayawVLDETGEERERGVTM-------DVGMTKfe 170
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQSG-----TFRENQEVAER----------VMDSNDLERERGITIlakntavRYKGVK-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 171 tttkvITLMDAPGHKDF------IPNMitgaaqADVAVLVVDAsrgeFEagfetgG---QTR-------EHGLLVrslgv 234
Cdd:COG1217 71 -----INIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlkkalELGLKP----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 235 tqlAVAVNKMDQ--------VNWQQERFQEitgkLGHFLKQAGFKesdvgFIPTSGLSG---ENLITRSQSseLTkwykg 303
Cdd:COG1217 125 ---IVVINKIDRpdarpdevVDEVFDLFIE----LGATDEQLDFP-----VVYASARNGwasLDLDDPGED--LT----- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 304 lCLLEQI-DSFKPPQRSIDKPFRLCVSDVFKDQGSGFCITGKIEAGYIQTGDRLLAMPPNETcTVKG-IT-------LHD 374
Cdd:COG1217 186 -PLFDTIlEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALIKRDGK-VEKGkITklfgfegLER 263
|
330 340 350
....*....|....*....|....*....|....*.
gi 1393428226 375 EPVDWAAAGDHVSLTlvGMDiiKINVGCIFCGPKVP 410
Cdd:COG1217 264 VEVEEAEAGDIVAIA--GIE--DINIGDTICDPENP 295
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
324-390 |
1.10e-09 |
|
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: 54.88 E-value: 1.10e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393428226 324 FRLCVSDVFKDQGS--GFCitGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTL 390
Cdd:cd03695 1 FRFPVQYVNRPNLDfrGYA--GTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTL 67
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
94-247 |
1.33e-09 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 60.74 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 94 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNINKR-TMHKyeqeskkaGKAsfayawVLDETGEERERGVTMdvgmtkFETT 172
Cdd:PRK13351 6 MQIRNIGILAHIDAGKTTLTERILFYTGKIHKMgEVED--------GTT------VTDWMPQEQERGITI------ESAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 173 TKV------ITLMDAPGHKDFIPNMITGAAQADVAVLVVDASrgefeAGFETggQTRehgLLVRSL---GVTQLAVaVNK 243
Cdd:PRK13351 66 TSCdwdnhrINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAV-----TGVQP--QTE---TVWRQAdryGIPRLIF-INK 134
|
....
gi 1393428226 244 MDQV 247
Cdd:PRK13351 135 MDRV 138
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
98-245 |
1.56e-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: 57.60 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGHMLYLLGNINKRTmHKYEQeskkagkasfayawVLDETGEERERGVTMDVGMTKFETTTKVIT 177
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGTFRENE-EVGER--------------VMDSNDLERERGITILAKNTAITYKDTKIN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 178 LMDAPGHKDF------IPNMitgaaqADVAVLVVDASRGEFEagfetggQTR-------EHGLLVrslgvtqlAVAVNKM 244
Cdd:cd01891 69 IIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP-------QTRfvlkkalEAGLKP--------IVVINKI 127
|
.
gi 1393428226 245 D 245
Cdd:cd01891 128 D 128
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
98-293 |
1.72e-09 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 58.07 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGhmlyLL-------GNINKRTM---HKYEQESKKAGKASFAyawVL--DETGE--ERERGVTMD 163
Cdd:cd04165 1 RVAVVGNVDAGKSTLLG----VLtqgeldnGRGKARLNlfrHKHEVESGRTSSVSND---ILgfDSDGEvvNYPDNHLGE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 164 VGMTKFETTTKVITLMDAPGHKDFIPNMITG--AAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVTqLAVAV 241
Cdd:cd04165 74 LDVEICEKSSKVVTFIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAG-------IIGMTKEHLGLALALKVP-VFVVV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1393428226 242 NKMDQVnwQQERFQEITGKLGHFLKQAGFKESDVgFIPTSG---LSGENLITRSQ 293
Cdd:cd04165 146 TKIDMT--PANVLQETLKDLKRLLKSPGVRKLPV-PVKSKDdvvLSASNLSSGRV 197
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
94-210 |
1.72e-09 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 60.45 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 94 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNINkrtmhkyeqeSKKAGKASFayawvLDETGEERERGVT-------MDVGM 166
Cdd:PTZ00416 17 DQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS----------SKNAGDARF-----TDTRADEQERGITikstgisLYYEH 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1393428226 167 TKFETTTK---VITLMDAPGHKDFiPNMITGAAQ-ADVAVLVVDASRG 210
Cdd:PTZ00416 82 DLEDGDDKqpfLINLIDSPGHVDF-SSEVTAALRvTDGALVVVDCVEG 128
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
98-210 |
1.87e-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: 57.66 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGhmlYLLGNInkrtmHKYEQESKKAGKASFAYawvlDETGEERERGVTMD-VGMTKFETTTK-- 174
Cdd:cd04167 2 NVCIAGHLHHGKTSLLD---MLIEQT-----HKRTPSVKLGWKPLRYT----DTRKDEQERGISIKsNPISLVLEDSKgk 69
|
90 100 110
....*....|....*....|....*....|....*...
gi 1393428226 175 --VITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRG 210
Cdd:cd04167 70 syLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEG 107
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
101-210 |
2.38e-09 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 58.38 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 101 VIGHVDAGKSTLMGHMLYLLGNINKRTMHKyeqeSKKAGKASfayawVLDETGEERERG--VTMDVgMTkFETTTKVITL 178
Cdd:cd04169 7 IISHPDAGKTTLTEKLLLFGGAIQEAGAVK----ARKSRKHA-----TSDWMEIEKQRGisVTSSV-MQ-FEYKGCVINL 75
|
90 100 110
....*....|....*....|....*....|..
gi 1393428226 179 MDAPGHKDFIPNMITGAAQADVAVLVVDASRG 210
Cdd:cd04169 76 LDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
324-401 |
3.72e-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: 53.30 E-value: 3.72e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393428226 324 FRLCVSDVFKDQGSGFCITGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVG 401
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
94-210 |
7.44e-09 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 58.34 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 94 KQLLNLVVIGHVDAGKSTLMGHMLYLLGNINKRTmhkyeqeskkAGKASFayawvLDETGEERERGVTMD---VGMT-KF 169
Cdd:PRK07560 18 EQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEEL----------AGEQLA-----LDFDEEEQARGITIKaanVSMVhEY 82
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1393428226 170 ETTTKVITLMDAPGHKDFiPNMITGAAQA-DVAVLVVDASRG 210
Cdd:PRK07560 83 EGKEYLINLIDTPGHVDF-GGDVTRAMRAvDGAIVVVDAVEG 123
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
97-289 |
1.33e-08 |
|
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: 54.97 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 97 LNLVVIGHVDAGKSTLmghmLYLLGNInkRTM-HKYEQESKKAGKASFAYAWV-----------LDETGEERERGVtmdv 164
Cdd:cd01888 1 INIGTIGHVAHGKTTL----VKALSGV--WTVrHKEELKRNITIKLGYANAKIykcpncgcprpYDTPECECPGCG---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 165 GMTKFEtttKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASrgefeagfET--GGQTREHGLLVRSLGVTQLAVAVN 242
Cdd:cd01888 71 GETKLV---RHVSFVDCPGHEILMATMLSGAAVMDGALLLIAAN--------EPcpQPQTSEHLAALEIMGLKHIIILQN 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1393428226 243 KMDQV--NWQQERFQEITGklghFLKqaGFKESDVGFIPTSGLSGENLI 289
Cdd:cd01888 140 KIDLVkeEQALENYEQIKE----FVK--GTIAENAPIIPISAQLKYNID 182
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
98-263 |
3.89e-08 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 54.42 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGHMLYLLGNINKrtMHkyEQESKKAgkasfayawVLDETGEERERGVTMDVGMTKFETTTKVIT 177
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHK--IG--EVHGGGA---------TMDWMEQERERGITIQSAATTCFWKDHRIN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 178 LMDAPGHKDFIPNMITGAAQADVAVLVVDASrgefeAGFETggQT----REhgllVRSLGVTQLAVaVNKMDQVNWQQER 253
Cdd:cd01886 68 IIDTPGHVDFTIEVERSLRVLDGAVAVFDAV-----AGVQP--QTetvwRQ----ADRYGVPRIAF-VNKMDRTGADFYR 135
|
170
....*....|.
gi 1393428226 254 -FQEITGKLGH 263
Cdd:cd01886 136 vVEQIREKLGA 146
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
338-405 |
1.72e-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: 48.42 E-value: 1.72e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393428226 338 GFCITGKIEAGYIQTGDRLLAMPP-----NETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKINVGCIFC 405
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
100-288 |
1.17e-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: 48.61 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 100 VVIGHVDAGKSTLmghmlyllgnINkrtmhkyeqeskkagkaSFAYAWVLdETGEERERGVTMDVGMTKFETTTKVITLM 179
Cdd:cd00882 1 VVVGRGGVGKSSL----------LN-----------------ALLGGEVG-EVSDVPGTTRDPDVYVKELDKGKVKLVLV 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 180 DAPGHKDFIPNMITGAA-----QADVAVLVVDASRGEFEAgfetgGQTREHGLLVRSLGVTQLAVAvNKMDQVNWQQERF 254
Cdd:cd00882 53 DTPGLDEFGGLGREELArlllrGADLILLVVDSTDRESEE-----DAKLLILRRLRKEGIPIILVG-NKIDLLEEREVEE 126
|
170 180 190
....*....|....*....|....*....|....
gi 1393428226 255 QEITGKLghflkqagFKESDVGFIPTSGLSGENL 288
Cdd:cd00882 127 LLRLEEL--------AKILGVPVFEVSAKTGEGV 152
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
101-288 |
2.75e-06 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 50.22 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 101 VIGHVDAGKSTLmghmlylLGNINKrtmhkyeqeSKKAGKasfayawvldETGeererGVTMDVGMTKFE----TTTKVI 176
Cdd:CHL00189 249 ILGHVDHGKTTL-------LDKIRK---------TQIAQK----------EAG-----GITQKIGAYEVEfeykDENQKI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 177 TLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGefeagfeTGGQTREHGLLVRSLGVTqLAVAVNKMDQVNWQQERFQE 256
Cdd:CHL00189 298 VFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIEAINYIQAANVP-IIVAINKIDKANANTERIKQ 369
|
170 180 190
....*....|....*....|....*....|....*....
gi 1393428226 257 -------ITGKLGhflkqagfkeSDVGFIPTSGLSGENL 288
Cdd:CHL00189 370 qlakynlIPEKWG----------GDTPMIPISASQGTNI 398
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
324-398 |
6.50e-06 |
|
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: 44.18 E-value: 6.50e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393428226 324 FRLCVSDVFKDQGSGFCITGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTLVGMDIIKI 398
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGVKDILT 75
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
82-210 |
1.55e-05 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 47.44 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 82 DVKAELEKRQggkqllNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKyeqeSKKAGKasfaYA---WVldetgE-ERE 157
Cdd:PRK00741 2 ELAQEVAKRR------TFAIISHPDAGKTTLTEKLLLFGGAIQEAGTVK----GRKSGR----HAtsdWM-----EmEKQ 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1393428226 158 RG--VTMDVgMtKFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRG 210
Cdd:PRK00741 63 RGisVTSSV-M-QFPYRDCLINLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKG 115
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
98-210 |
6.43e-05 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 45.87 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGHMLYLLGNINkrtmhkyeqeSKKAGKASFAyawvlDETGEERERGVTM-DVGMTKFETTTK-- 174
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTDSLVAAAGIIA----------QEVAGDVRMT-----DTRADEAERGITIkSTGISLYYEMTDes 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1393428226 175 -------------VITLMDAPGHKDFiPNMITGAAQ-ADVAVLVVDASRG 210
Cdd:PLN00116 86 lkdfkgerdgneyLINLIDSPGHVDF-SSEVTAALRiTDGALVVVDCIEG 134
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
176-354 |
7.55e-05 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 45.38 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 176 ITLMDAPGHKDFIPNMITGAAQADVAVLVVdasrgefeAGFET--GGQTREHGLLVRSLGVTQLAVAVNKMDQVNWQ--Q 251
Cdd:PTZ00327 119 VSFVDCPGHDILMATMLNGAAVMDAALLLI--------AANEScpQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAqaQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 252 ERFQEITgklgHFLKqaGFKESDVGFIPTSGLSGENLItrsqsseltkwykglCLLEQIDSFKP-PQRSIDKPFRLCVS- 329
Cdd:PTZ00327 191 DQYEEIR----NFVK--GTIADNAPIIPISAQLKYNID---------------VVLEYICTQIPiPKRDLTSPPRMIVIr 249
|
170 180 190
....*....|....*....|....*....|..
gi 1393428226 330 --DVFK-----DQGSGFCITGKIEAGYIQTGD 354
Cdd:PTZ00327 250 sfDVNKpgediENLKGGVAGGSILQGVLKVGD 281
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
100-288 |
1.20e-04 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 42.62 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 100 VVIGHVDAGKSTLM----GHMLYLLGNINKRTMHKYeqeskkagkasfAYAWVLDETGEerergvtmdvgmtkfetttkv 175
Cdd:cd00880 1 AIFGRPNVGKSSLLnallGQNVGIVSPIPGTTRDPV------------RKEWELLPLGP--------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 176 ITLMDAPG-------HKDFIPNMITGAAQADVAVLVVDASRGEFEagfetggQTREHGLLVRSlGVTQLAVAvNKMDQVN 248
Cdd:cd00880 48 VVLIDTPGldeegglGRERVEEARQVADRADLVLLVVDSDLTPVE-------EEAKLGLLRER-GKPVLLVL-NKIDLVP 118
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1393428226 249 WQQERfqeitgKLGHFLKQAGFKESDVgfIPTSGLSGENL 288
Cdd:cd00880 119 ESEEE------ELLRERKLELLPDLPV--IAVSALPGEGI 150
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
98-290 |
1.72e-04 |
|
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: 42.36 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 98 NLVVIGHVDAGKSTLMGHMLYllgniNKRTMHKYEQeskkagkasfayawvldetgeererGVTMDVGMTKFET--TTKV 175
Cdd:TIGR00231 3 KIVIVGHPNVGKSTLLNSLLG-----NKGSITEYYP-------------------------GTTRNYVTTVIEEdgKTYK 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 176 ITLMDAPGHKDF-------IPNMITGAAQADVAVLVVDASRGEFEagfetggQTREhglLVRSL-GVTQLAVAVNKMDQV 247
Cdd:TIGR00231 53 FNLLDTAGQEDYdairrlyYPQVERSLRVFDIVILVLDVEEILEK-------QTKE---IIHHAdSGVPIILVGNKIDLK 122
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1393428226 248 nwqQERFQEitgKLGHFLKQAGFKEsdvgFIPTSGLSGENLIT 290
Cdd:TIGR00231 123 ---DADLKT---HVASEFAKLNGEP----IIPLSAETGKNIDS 155
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
412-518 |
2.49e-04 |
|
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.
Pssm-ID: 294005 [Multi-domain] Cd Length: 93 Bit Score: 40.29 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 412 KACTRFRARILIFNIE-----IPITKGFPVLLHYQTVSEPAvikRLISVLNKStgevtkkkpkFLTKGQNALVELQTQRP 486
Cdd:cd03706 1 KMHNHFEAQVYLLSKEeggrhKPFTSGFQQQMFSKTWDCAC---RIDLPEGKE----------MVMPGEDTSVKLTLLKP 67
|
90 100 110
....*....|....*....|....*....|..
gi 1393428226 487 IALElykdfkELGRFMLRYGGSTIAAGVVTEI 518
Cdd:cd03706 68 MVLE------KGQRFTLREGGRTIGTGVVTKL 93
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
97-288 |
4.58e-04 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 41.26 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 97 LNLVVIGHVDAGKSTLMGHMLyllgninkrtmhkyeqeskkagkasfayawvldetGEER-----ERGVTMDVGMTKFET 171
Cdd:cd01895 3 IKIAIIGRPNVGKSSLLNALL-----------------------------------GEERvivsdIAGTTRDSIDVPFEY 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 172 TTKVITLMDAPG---------HKDFIPNMITGAA--QADVAVLVVDASRGEFEAGFETGGQTREHGL-LVrslgvtqlaV 239
Cdd:cd01895 48 DGQKYTLIDTAGirkkgkvteGIEKYSVLRTLKAieRADVVLLVLDASEGITEQDLRIAGLILEEGKaLI---------I 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1393428226 240 AVNKMDQVNWQQERFQEITGKLGHFLKQAGFkesdVGFIPTSGLSGENL 288
Cdd:cd01895 119 VVNKWDLVEKDEKTMKEFEKELRRKLPFLDY----APIVFISALTGQGV 163
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
100-286 |
3.91e-03 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 39.78 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 100 VVIGHVDAGKSTLmghmlylLGNINKRTMHKYEqeskkAGkasfayawvldetgeererGVTMDVGMT------------ 167
Cdd:PRK04004 10 VVLGHVDHGKTTL-------LDKIRGTAVAAKE-----AG-------------------GITQHIGATevpidviekiag 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 168 ----KFETTTKVITLM--DAPGHKDFiPNMIT-GAAQADVAVLVVDASRGeFEAgfetggQTREHGLLVRSLGvTQLAVA 240
Cdd:PRK04004 59 plkkPLPIKLKIPGLLfiDTPGHEAF-TNLRKrGGALADIAILVVDINEG-FQP------QTIEAINILKRRK-TPFVVA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 241 VNKMDQVN-W--------------QQERFQ--------EITGKlghfLKQAGFkESD-----------VGFIPTSGLSGE 286
Cdd:PRK04004 130 ANKIDRIPgWkstedapflesiekQSQRVQqeleeklyELIGQ----LSELGF-SADrfdrvkdftktVAIVPVSAKTGE 204
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
101-245 |
5.20e-03 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 39.23 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 101 VIGHVDAGKSTLmghmlylLGNINKrtmhkyeqeSKKAGKasfayawvldETGeererGVTMDVGMTKFETTTKVITLMD 180
Cdd:COG0532 9 VMGHVDHGKTSL-------LDAIRK---------TNVAAG----------EAG-----GITQHIGAYQVETNGGKITFLD 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393428226 181 APGHKDFipnmiT-----GAAQADVAVLVVDASRGEFEagfetggQTRE---HgllVRSLGVTqLAVAVNKMD 245
Cdd:COG0532 58 TPGHEAF-----TamrarGAQVTDIVILVVAADDGVMP-------QTIEainH---AKAAGVP-IIVAINKID 114
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
164-253 |
7.92e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 39.10 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428226 164 VGMTKFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASRGeFEAgfetggQTREHGLLVRSLGvTQLAVAVNK 243
Cdd:PRK14845 516 LKLLKAEIKIPGLLFIDTPGHEAFTSLRKRGGSLADLAVLVVDINEG-FKP------QTIEAINILRQYK-TPFVVAANK 587
|
90
....*....|.
gi 1393428226 244 MDQV-NWQQER 253
Cdd:PRK14845 588 IDLIpGWNISE 598
|
|
| |
