|
Name |
Accession |
Description |
Interval |
E-value |
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-435 |
3.71e-133 |
|
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: 389.68 E-value: 3.71e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMAKLQTKADEAGKSSFAFAFYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:COG5256 16 VDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDFVKNMITGASQADAGLLLVPAdgnfvtalakggKDEVQGSSRMHAQILKLIGCRQLMVGANKMDEkqAAWSQSASTRF 160
Cdd:COG5256 96 RDFVKNMITGASQADAAILVVSA------------KDGVMGQTREHAFLARTLGINQLIVAVNKMDA--VNYSEKRYEEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 161 SSEMKNVLLRTGWTkkqvDDEIPIIPYSGFAGDNLIKKSTNMPWWSGvdvhndaekvhvETILDCLSKFvRIPPRPVDKP 240
Cdd:COG5256 162 KEEVSKLLKMVGYK----VDKIPFIPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNL-KEPEKPVDKP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 241 GRVPISGLYSIKGVGDVLTGCCEQGTFKNGDEVVFLPTHTKalpclGKIFTMEAHHNKKEICMPGDNLGFNIKGLKKDNM 320
Cdd:COG5256 225 LRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVV-----GEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 321 pKVGDVMVKKSDCAGLArvKSFTAQIQCLQHPGELNVGYSPMGIVRTGRSAMRMTAIHWKVGKETGGTKLENPPNLKANE 400
Cdd:COG5256 300 -KRGDVAGHPDNPPTVA--EEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGD 376
|
410 420 430
....*....|....*....|....*....|....*
gi 193811884 401 MAQVEFEPTQPIFLEKFTDCEGLGRLACLESNQPI 435
Cdd:COG5256 377 AAIVKIKPTKPLVIEKFKEFPQLGRFAIRDMGQTV 411
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
1-427 |
3.78e-127 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 374.26 E-value: 3.78e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMAKLQTKADEAGKSSFAFAFYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:PRK12317 15 VDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIVDCPGH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDFVKNMITGASQADAGLLLVPADGnfvtalAKGgkdeVQGSSRMHAQILKLIGCRQLMVGANKMDekQAAWSQSASTRF 160
Cdd:PRK12317 95 RDFVKNMITGASQADAAVLVVAADD------AGG----VMPQTREHVFLARTLGINQLIVAINKMD--AVNYDEKRYEEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 161 SSEMKNVLLRTGWTkkqvDDEIPIIPYSGFAGDNLIKKSTNMPWWSGvdvhndaekvhvETILDCLSKFvRIPPRPVDKP 240
Cdd:PRK12317 163 KEEVSKLLKMVGYK----PDDIPFIPVSAFEGDNVVKKSENMPWYNG------------PTLLEALDNL-KPPEKPTDKP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 241 GRVPISGLYSIKGVGDVLTGCCEQGTFKNGDEVVFLPTHTkalpcLGKIFTMEAHHNKKEICMPGDNLGFNIKGLKKDNM 320
Cdd:PRK12317 226 LRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGV-----VGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 321 pKVGDVMVKKSDCAGLArvKSFTAQIQCLQHPGELNVGYSPMGIVRTGRSAMRMTAIHWKVGKETGGTKLENPPNLKANE 400
Cdd:PRK12317 301 -KRGDVCGHPDNPPTVA--EEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGD 377
|
410 420
....*....|....*....|....*..
gi 193811884 401 MAQVEFEPTQPIFLEKFTDCEGLGRLA 427
Cdd:PRK12317 378 AAIVKIKPTKPLVIEKVKEIPQLGRFA 404
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-427 |
7.56e-118 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 351.36 E-value: 7.56e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMAKLQTKADEAGKSSFAFAFYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:PTZ00141 16 VDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDFVKNMITGASQADAGLLLVPAD-GNFVTALAKggkdevQGSSRMHAQILKLIGCRQLMVGANKMDEKQAAWSQSASTR 159
Cdd:PTZ00141 96 RDFIKNMITGTSQADVAILVVASTaGEFEAGISK------DGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 160 FSSEMKNVLLRTGWTKkqvdDEIPIIPYSGFAGDNLIKKSTNMPWWSGvdvhndaekvhvETILDCLSKfVRIPPRPVDK 239
Cdd:PTZ00141 170 IKKEVSAYLKKVGYNP----EKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDT-LEPPKRPVDK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 240 PGRVPISGLYSIKGVGDVLTGCCEQGTFKNGDEVVFLPTHTKAlpclgKIFTMEAHHNKKEICMPGDNLGFNIKG----- 314
Cdd:PTZ00141 233 PLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTT-----EVKSVEMHHEQLAEAVPGDNVGFNVKNvsvkd 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 315 LKKDNMpkVGDVmvkKSDCAGLArvKSFTAQIQCLQHPGELNVGYSPMGIVRTGRSAMRMTAIHWKVGKETGGTKLENPP 394
Cdd:PTZ00141 308 IKRGYV--ASDS---KNDPAKEC--ADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPK 380
|
410 420 430
....*....|....*....|....*....|...
gi 193811884 395 NLKANEMAQVEFEPTQPIFLEKFTDCEGLGRLA 427
Cdd:PTZ00141 381 AIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFA 413
|
|
| EF-1_alpha |
TIGR00483 |
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ... |
1-435 |
1.47e-109 |
|
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]
Pssm-ID: 129574 [Multi-domain] Cd Length: 426 Bit Score: 329.52 E-value: 1.47e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMAKLQTKADEAGKSSFAFAFYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:TIGR00483 16 VDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETDKYEVTIVDCPGH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDFVKNMITGASQADAGLLLVPADgnfvtalakGGKDEVQGSSRMHAQILKLIGCRQLMVGANKMDekQAAWSQSASTRF 160
Cdd:TIGR00483 96 RDFIKNMITGASQADAAVLVVAVG---------DGEFEVQPQTREHAFLARTLGINQLIVAINKMD--SVNYDEEEFEAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 161 SSEMKNVLLRTGWTKkqvdDEIPIIPYSGFAGDNLIKKSTNMPWWSGvdvhndaekvhvETILDCLSKFvRIPPRPVDKP 240
Cdd:TIGR00483 165 KKEVSNLIKKVGYNP----DTVPFIPISAWNGDNVIKKSENTPWYKG------------KTLLEALDAL-EPPEKPTDKP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 241 GRVPISGLYSIKGVGDVLTGCCEQGTFKNGDEVVFLPTHTKalpclGKIFTMEAHHNKKEICMPGDNLGFNIKGLKKDNm 320
Cdd:TIGR00483 228 LRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVS-----GEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKD- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 321 pkvgdvmVKKSDCAGLAR-----VKSFTAQIQCLQHPGELNVGYSPMGIVRTGRSAMRMTAIHWKVGKETGGTKLENPPN 395
Cdd:TIGR00483 302 -------IRRGDVCGHPDnppkvAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQF 374
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 193811884 396 LKANEMAQVEFEPTQPIFLEKFTDCEGLGRLACLESNQPI 435
Cdd:TIGR00483 375 LKTGDAAIVKFKPTKPMVIEAVKEIPPLGRFAIRDMGQTV 414
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
1-207 |
9.29e-89 |
|
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: 268.98 E-value: 9.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMAKLQTKADEAGKSSFAFAFYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:cd01883 8 VDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDFVKNMITGASQADAGLLLVPAD-GNFVTAlakggkDEVQGSSRMHAQILKLIGCRQLMVGANKMDEKQAAWSQSastR 159
Cdd:cd01883 88 RDFVKNMITGASQADVAVLVVSARkGEFEAG------FEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQE---R 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 193811884 160 F---SSEMKNVLLRTGWTKKQVddeiPIIPYSGFAGDNLIKKSTNMPWWSG 207
Cdd:cd01883 159 YdeiKKKVSPFLKKVGYNPKDV----PFIPISGFTGDNLIEKSENMPWYKG 205
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-435 |
1.66e-84 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 265.80 E-value: 1.66e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMAKLQTKADEAGKSSFAFAFYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:PLN00043 16 VDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDFVKNMITGASQADAGLLLVPA-DGNFVTALAKGGKdevqgsSRMHAQILKLIGCRQLMVGANKMDEKQAAWSQSASTR 159
Cdd:PLN00043 96 RDFIKNMITGTSQADCAVLIIDStTGGFEAGISKDGQ------TREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 160 FSSEMKNVLLRTGWTKkqvdDEIPIIPYSGFAGDNLIKKSTNMPWWSGvdvhndaekvhvETILDCLSKfVRIPPRPVDK 239
Cdd:PLN00043 170 IVKEVSSYLKKVGYNP----DKIPFVPISGFEGDNMIERSTNLDWYKG------------PTLLEALDQ-INEPKRPSDK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 240 PGRVPISGLYSIKGVGDVLTGCCEQGTFKNGDEVVFLPTHTKAlpclgKIFTMEAHHNKKEICMPGDNLGFNIKGLKKDN 319
Cdd:PLN00043 233 PLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTT-----EVKSVEMHHESLQEALPGDNVGFNVKNVAVKD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 320 MPKVGDVMVKKSDCAGLArvKSFTAQIQCLQHPGELNVGYSPMGIVRTGRSAMRMTAIHWKVGKETGGTKLENPPNLKAN 399
Cdd:PLN00043 308 LKRGYVASNSKDDPAKEA--ANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNG 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 193811884 400 EMAQVEFEPTQPIFLEKFTDCEGLGRLACLESNQPI 435
Cdd:PLN00043 386 DAGFVKMIPTKPMVVETFSEYPPLGRFAVRDMRQTV 421
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-426 |
1.28e-45 |
|
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: 163.33 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMAKLQTKADEAGKSSFAFAFYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:COG2895 26 VDDGKSTLIGRLLYDTKSIFEDQLAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPKRKFIIADTPGH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDFVKNMITGASQADAGLLLVPAdgnfvtalAKGgkdeVQGSSRMHAQILKLIGCRQLMVGANKMDekQAAWSQSASTRF 160
Cdd:COG2895 106 EQYTRNMVTGASTADLAILLIDA--------RKG----VLEQTRRHSYIASLLGIRHVVVAVNKMD--LVDYSEEVFEEI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 161 SSEMKNVLLRTGWTkkqvddEIPIIPYSGFAGDNLIKKSTNMPWWSGvdvhndaekvhvETILDCLSKfVRIPPRPVDKP 240
Cdd:COG2895 172 VADYRAFAAKLGLE------DITFIPISALKGDNVVERSENMPWYDG------------PTLLEHLET-VEVAEDRNDAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 241 GRVPISglYSIKGVGDV--LTGCCEQGTFKNGDEVVFLPTHTKAlpclgKIFTMEAHHNKKEICMPGDNLGFNikgLKKD 318
Cdd:COG2895 233 FRFPVQ--YVNRPNLDFrgYAGTIASGTVRVGDEVVVLPSGKTS-----TVKSIVTFDGDLEEAFAGQSVTLT---LEDE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 319 NMPKVGDVMVKKSDCAGLARvkSFTAQIqCLQHPGELNVG--YspmgIVRTG--RSAMRMTAIHWKVGKETGgtKLENPP 394
Cdd:COG2895 303 IDISRGDVIVAADAPPEVAD--QFEATL-VWMDEEPLLPGrkY----LLKHGtrTVRATVTAIKYRIDVNTL--EHEAAD 373
|
410 420 430
....*....|....*....|....*....|..
gi 193811884 395 NLKANEMAQVEFEPTQPIFLEKFTDCEGLGRL 426
Cdd:COG2895 374 SLELNDIGRVTLRLAEPIAFDPYADNRATGSF 405
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
1-195 |
9.88e-42 |
|
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: 146.13 E-value: 9.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMAKLQTKAdeagkssfafafYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:pfam00009 12 VDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDFVKNMITGASQADAGLLLVPADgnfvtalaKGgkdeVQGSSRMHAQILKLIGCRqLMVGANKMDEKQAAwsqsastRF 160
Cdd:pfam00009 80 VDFVKEVIRGLAQADGAILVVDAV--------EG----VMPQTREHLRLARQLGVP-IIVFINKMDRVDGA-------EL 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 193811884 161 S---SEMKNVLLRTGWTKKqvdDEIPIIPYSGFAGDNL 195
Cdd:pfam00009 140 EevvEEVSRELLEKYGEDG---EFVPVVPGSALKGEGV 174
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
1-220 |
5.70e-41 |
|
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: 144.63 E-value: 5.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMAKLQ--TKADEAGKSsFAFAFYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAP 78
Cdd:cd04166 8 VDDGKSTLIGRLLYDSKSIFEDQLAALErsKSSGTQGEK-LDLALLVDGLQAEREQGITIDVAYRYFSTPKRKFIIADTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 79 GHRDFVKNMITGASQADAGLLLVPAdgnfvtalAKGgkdeVQGSSRMHAQILKLIGCRQLMVGANKMDekQAAWSQSAST 158
Cdd:cd04166 87 GHEQYTRNMVTGASTADLAILLVDA--------RKG----VLEQTRRHSYIASLLGIRHVVVAVNKMD--LVDYDEEVFE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193811884 159 RFSSEMKNVLLRTGWTkkqvddEIPIIPYSGFAGDNLIKKSTNMPWWSGVDVHNDAEKVHVE 220
Cdd:cd04166 153 EIKADYLAFAASLGIE------DITFIPISALEGDNVVSRSENMPWYKGPTLLEHLETVEIA 208
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
337-435 |
1.29e-37 |
|
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: 132.32 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 337 ARVKSFTAQIQCLQHPGELNVGYSPMGIVRTGRSAMRMTAIHWKVGKETGGTKLENPPNLKANEMAQVEFEPTQPIFLEK 416
Cdd:cd03705 1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80
|
90
....*....|....*....
gi 193811884 417 FTDCEGLGRLACLESNQPI 435
Cdd:cd03705 81 FSEYPPLGRFAVRDMRQTV 99
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
1-193 |
2.30e-34 |
|
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: 126.26 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMAKLQtkadeagkssfafafYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:cd00881 8 VDHGKTTLTGSLLYQTGAIDRRGTRKET---------------FLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDFVKNMITGASQADAGLLLVPADgnfvtalakggkDEVQGSSRMHAQILKLiGCRQLMVGANKMDEkqaawsqSASTRF 160
Cdd:cd00881 73 EDFSKETVRGLAQADGALLVVDAN------------EGVEPQTREHLNIALA-GGLPIIVAVNKIDR-------VGEEDF 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 193811884 161 SS---EMKNVLLRTGWTkKQVDDEIPIIPYSGFAGD 193
Cdd:cd00881 133 DEvlrEIKELLKLIGFT-FLKGKDVPIIPISALTGE 167
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
1-349 |
1.77e-33 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 130.72 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGrlifelggiseremAKLQTKADEAGKSSFAFAfYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:PLN03127 70 VDHGKTTLTA--------------AITKVLAEEGKAKAVAFD-EIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDFVKNMITGASQADAGLLLVPAdgnfvtalakggKDEVQGSSRMHAQILKLIGCRQLMVGANKMDekqAAWSQSASTRF 160
Cdd:PLN03127 135 ADYVKNMITGAAQMDGGILVVSA------------PDGPMPQTKEHILLARQVGVPSLVVFLNKVD---VVDDEELLELV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 161 SSEMKNVLLrtgwTKKQVDDEIPIIPYSGFAGdnliKKSTNmpwwsgvdvhndaEKVHVETIL---DCLSKFVRIPPRPV 237
Cdd:PLN03127 200 EMELRELLS----FYKFPGDEIPIIRGSALSA----LQGTN-------------DEIGKNAILklmDAVDEYIPEPVRVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 238 DKPGRVPISGLYSIKGVGDVLTGCCEQGTFKNGDEVVFL---PTHTKALPCLGkiftMEAHHNKKEICMPGDNLGFNIKG 314
Cdd:PLN03127 259 DKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVglrPGGPLKTTVTG----VEMFKKILDQGQAGDNVGLLLRG 334
|
330 340 350
....*....|....*....|....*....|....*
gi 193811884 315 LKKDNMPKvGDVMVKKSDCaglARVKSFTAQIQCL 349
Cdd:PLN03127 335 LKREDVQR-GQVICKPGSI---KTYKKFEAEIYVL 365
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
1-277 |
6.41e-32 |
|
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: 125.56 E-value: 6.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMAKLQTKADEAGKS--SFAFAFYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAP 78
Cdd:TIGR02034 9 VDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTQggEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVADTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 79 GHRDFVKNMITGASQADAGLLLVPAdgnfvtalAKGgkdeVQGSSRMHAQILKLIGCRQLMVGANKMDEKQaaWSQSAST 158
Cdd:TIGR02034 89 GHEQYTRNMATGASTADLAVLLVDA--------RKG----VLEQTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 159 RFSSEMKnvllrtGWTKKQVDDEIPIIPYSGFAGDNLIKKSTNMPWWSGVDVHNDAEKVHVETILDclSKFVRIPPRPVD 238
Cdd:TIGR02034 155 NIKKDYL------AFAEQLGFRDVTFIPLSALKGDNVVSRSESMPWYSGPTLLEILETVEVERDAQ--DLPLRFPVQYVN 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 193811884 239 KPGrvpisglYSIKGvgdvLTGCCEQGTFKNGDEVVFLP 277
Cdd:TIGR02034 227 RPN-------LDFRG----YAGTIASGSVHVGDEVVVLP 254
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
1-278 |
1.21e-31 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 127.35 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMAKLQTKADEAGKSS--FAFAFYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAP 78
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGTQGdeIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVADTP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 79 GHRDFVKNMITGASQADAGLLLVPAdgnfvtalAKGgkdeVQGSSRMHAQILKLIGCRQLMVGANKMDEKQaaWSQSAST 158
Cdd:PRK05506 113 GHEQYTRNMVTGASTADLAIILVDA--------RKG----VLTQTRRHSFIASLLGIRHVVLAVNKMDLVD--YDQEVFD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 159 RFSSEMKNVLLRTGWTkkqvddEIPIIPYSGFAGDNLIKKSTNMPWWSGVDVHNDAEKVHVETilDCLSKFVRIPPRPVD 238
Cdd:PRK05506 179 EIVADYRAFAAKLGLH------DVTFIPISALKGDNVVTRSARMPWYEGPSLLEHLETVEIAS--DRNLKDFRFPVQYVN 250
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 193811884 239 KPGRvpisglySIKGVgdvlTGCCEQGTFKNGDEVVFLPT 278
Cdd:PRK05506 251 RPNL-------DFRGF----AGTVASGVVRPGDEVVVLPS 279
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
1-385 |
7.18e-30 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 120.88 E-value: 7.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISeremAKLQTKADEagkssfafafyMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:PLN03126 90 VDHGKTTLTAALTMALASMG----GSAPKKYDE-----------IDAAPEERARGITINTATVEYETENRHYAHVDCPGH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDFVKNMITGASQADAGLLLVpadgnfvtalakGGKDEVQGSSRMHAQILKLIGCRQLMVGANKMDEKQaawSQSASTRF 160
Cdd:PLN03126 155 ADYVKNMITGAAQMDGAILVV------------SGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVD---DEELLELV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 161 SSEMKNVLLRTGWTkkqvDDEIPIIPYSGFAG------DNLIKKSTNmPWwsgVDvhndaekvHVETILDCLSKFVRIPP 234
Cdd:PLN03126 220 ELEVRELLSSYEFP----GDDIPIISGSALLAlealmeNPNIKRGDN-KW---VD--------KIYELMDAVDSYIPIPQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 235 RPVDKPGRVPISGLYSIKGVGDVLTGCCEQGTFKNGDEVVFLP-THTKALPCLGkiftMEAHHNKKEICMPGDNLGFNIK 313
Cdd:PLN03126 284 RQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGlRETRSTTVTG----VEMFQKILDEALAGDNVGLLLR 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193811884 314 GLKKDNMPKvGDVMVKKSDCAGLARvksFTAQIQCLQHP-----GELNVGYSPMGIVRTGRSAMRMTAIHWKVGKET 385
Cdd:PLN03126 360 GIQKADIQR-GMVLAKPGSITPHTK---FEAIVYVLKKEeggrhSPFFAGYRPQFYMRTTDVTGKVTSIMNDKDEES 432
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
1-424 |
1.36e-29 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 120.02 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMAKLQTkaDEAGKSS----FAFAFYMDTCAEEQARGITIQCNTKEFHTENYRYSIID 76
Cdd:PRK05124 36 VDDGKSTLIGRLLHDTKQIYEDQLASLHN--DSKRHGTqgekLDLALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIAD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 77 APGHRDFVKNMITGASQADAGLLLVPAdgnfvtalAKGgkdeVQGSSRMHAQILKLIGCRQLMVGANKMDekQAAWSQSA 156
Cdd:PRK05124 114 TPGHEQYTRNMATGASTCDLAILLIDA--------RKG----VLDQTRRHSFIATLLGIKHLVVAVNKMD--LVDYSEEV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 157 STRFSSEMKNVLLRTGwtkkqVDDEIPIIPYSGFAGDNLIKKSTNMPWWSG---VDVhndAEKVHVETILDclSKFVRIP 233
Cdd:PRK05124 180 FERIREDYLTFAEQLP-----GNLDIRFVPLSALEGDNVVSQSESMPWYSGptlLEV---LETVDIQRVVD--AQPFRFP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 234 PRPVDKPGrvpisglYSIKGVGDVLTGcceqGTFKNGDEVVFLPThtkalpclGKIFTMeahhnKKEICMPGDnLGFNIK 313
Cdd:PRK05124 250 VQYVNRPN-------LDFRGYAGTLAS----GVVKVGDRVKVLPS--------GKESNV-----ARIVTFDGD-LEEAFA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 314 G------LKKDNMPKVGDVMVKKSdcAGLARVKSFTAQIQCLQhPGELNVGYSPMGIVRTGRSAMRMTAIHWKVGKETGG 387
Cdd:PRK05124 305 GeaitlvLEDEIDISRGDLLVAAD--EALQAVQHASADVVWMA-EQPLQPGQSYDIKIAGKKTRARVDAIRYQVDINTLT 381
|
410 420 430
....*....|....*....|....*....|....*..
gi 193811884 388 TKleNPPNLKANEMAQVEFEPTQPIFLEKFTDCEGLG 424
Cdd:PRK05124 382 QR--EAENLPLNGIGLVELTFDEPLVLDPYQQNRVTG 416
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-367 |
2.97e-29 |
|
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: 117.96 E-value: 2.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTgrlifelggiseremAKLQTKADEAGKSSFAFAFYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:TIGR00485 21 VDHGKTTLT---------------AAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDFVKNMITGASQADAGLLLVPAdgnfvtalakggKDEVQGSSRMHAQILKLIGCRQLMVGANKMDEkqaawsqsASTRF 160
Cdd:TIGR00485 86 ADYVKNMITGAAQMDGAILVVSA------------TDGPMPQTREHILLARQVGVPYIVVFLNKCDM--------VDDEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 161 SSEMKNVLLRTGWTKKQVD-DEIPIIPYSGfagdnlIKKSTNMPWWSgvdvhndaEKVHveTILDCLSKFVRIPPRPVDK 239
Cdd:TIGR00485 146 LLELVEMEVRELLSQYDFPgDDTPIIRGSA------LKALEGDAEWE--------AKIL--ELMDAVDEYIPTPEREIDK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 240 PGRVPISGLYSIKGVGDVLTGCCEQGTFKNGDEVVFLpthtkALPCLGKIFTMEAHHNKKEI--CMPGDNLGFNIKGLKK 317
Cdd:TIGR00485 210 PFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIV-----GLKDTRKTTVTGVEMFRKELdeGRAGDNVGLLLRGIKR 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 193811884 318 DNMPKvGDVMVKKSDCAGLarvKSFTAQIQCLQ------HPGELNvGYSPMGIVRT 367
Cdd:TIGR00485 285 EEIER-GMVLAKPGSIKPH---TKFEAEVYVLSkeeggrHTPFFS-GYRPQFYFRT 335
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
237-332 |
1.49e-27 |
|
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: 104.96 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 237 VDKPGRVPISGLYSIKGVGDVLTGCCEQGTFKNGDEVVFLPTHtkalpCLGKIFTMEAHHNKKEICMPGDNLGFNIKGLK 316
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAG-----VTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVS 75
|
90
....*....|....*.
gi 193811884 317 KdNMPKVGDVMVKKSD 332
Cdd:cd03693 76 V-KDIKRGDVAGDSKN 90
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-329 |
2.58e-27 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 112.35 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTgrlifelggiseremAKLQTKADEAGKSSF-AFAfYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPG 79
Cdd:PRK12736 21 VDHGKTTLT---------------AAITKVLAERGLNQAkDYD-SIDAAPEEKERGITINTAHVEYETEKRHYAHVDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 80 HRDFVKNMITGASQADAGLLLVPAdgnfvtalakggKDEVQGSSRMHAQILKLIGCRQLMVGANKMDEKQAAwsqsastr 159
Cdd:PRK12736 85 HADYVKNMITGAAQMDGAILVVAA------------TDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDE-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 160 fssEMKNVL---LRTGWTKKQVD-DEIPIIPYSGFA---GDnlikkstnmPWWSGVdvhndaekvhVETILDCLSKFVRI 232
Cdd:PRK12736 145 ---ELLELVemeVRELLSEYDFPgDDIPVIRGSALKaleGD---------PKWEDA----------IMELMDAVDEYIPT 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 233 PPRPVDKPGRVPISGLYSIKGVGDVLTGCCEQGTFKNGDEVVFLPTH-TKALPCLGkiftMEAHHNKKEICMPGDNLGFN 311
Cdd:PRK12736 203 PERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIKeTQKTVVTG----VEMFRKLLDEGQAGDNVGVL 278
|
330
....*....|....*...
gi 193811884 312 IKGLKKDNMPKvGDVMVK 329
Cdd:PRK12736 279 LRGVDRDEVER-GQVLAK 295
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-367 |
8.53e-27 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 111.20 E-value: 8.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGrlifelgGISereMAkLQTKADEAGKSsfafafY--MDTCAEEQARGITIqcNTK--EFHTENYRYSIID 76
Cdd:CHL00071 21 VDHGKTTLTA-------AIT---MT-LAAKGGAKAKK------YdeIDSAPEEKARGITI--NTAhvEYETENRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 77 APGHRDFVKNMITGASQADAGLLLVP-ADGNFvtalakggkdevqGSSRMHAQILKLIGCRQLMVGANKMDekqaawsQS 155
Cdd:CHL00071 82 CPGHADYVKNMITGAAQMDGAILVVSaADGPM-------------PQTKEHILLAKQVGVPNIVVFLNKED-------QV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 156 ASTRFSS----EMKNVLLRTGWTkkqvDDEIPIIPYSGF-AGDNLIKKST----NMPWwsgVDvhndaeKVHveTILDCL 226
Cdd:CHL00071 142 DDEELLElvelEVRELLSKYDFP----GDDIPIVSGSALlALEALTENPKikrgENKW---VD------KIY--NLMDAV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 227 SKFVRIPPRPVDKPGRVPISGLYSIKGVGDVLTGCCEQGTFKNGD--EVV-FLPTHTKalpclgKIFTMEAHHNKKEICM 303
Cdd:CHL00071 207 DSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDtvEIVgLRETKTT------TVTGLEMFQKTLDEGL 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193811884 304 PGDNLGFNIKGLKKDNMpKVGdvMVkksdcagLARVKS------FTAQIQCL------QHPGeLNVGYSPMGIVRT 367
Cdd:CHL00071 281 AGDNVGILLRGIQKEDI-ERG--MV-------LAKPGTitphtkFEAQVYILtkeeggRHTP-FFPGYRPQFYVRT 345
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-318 |
3.74e-26 |
|
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: 109.08 E-value: 3.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGrlifelggiseremAKLQTKADEAGKSSFAFAfYMDTCAEEQARGITIqcNTK--EFHTENYRYSIIDAP 78
Cdd:COG0050 21 VDHGKTTLTA--------------AITKVLAKKGGAKAKAYD-QIDKAPEEKERGITI--NTShvEYETEKRHYAHVDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 79 GHRDFVKNMITGASQADAGLLLVPADgnfvtalakggkDEVQGSSRMHAQILKLIGCRQLMVGANKMD-----------E 147
Cdd:COG0050 84 GHADYVKNMITGAAQMDGAILVVSAT------------DGPMPQTREHILLARQVGVPYIVVFLNKCDmvddeellelvE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 148 kqaawsqsastrfsSEMKNVLlrtgwTKKQVD-DEIPIIPYSGFAGdnlikkstnmpwwsgvdVHNDAEKVHVETI---L 223
Cdd:COG0050 152 --------------MEVRELL-----SKYGFPgDDTPIIRGSALKA-----------------LEGDPDPEWEKKIlelM 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 224 DCLSKFVRIPPRPVDKPGRVPISGLYSIKGVGDVLTGCCEQGTFKNGDEV--VFLpTHTKALPCLGkiftMEAHHNKKEI 301
Cdd:COG0050 196 DAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVeiVGI-RDTQKTVVTG----VEMFRKLLDE 270
|
330
....*....|....*..
gi 193811884 302 CMPGDNLGFNIKGLKKD 318
Cdd:COG0050 271 GEAGDNVGLLLRGIKRE 287
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-329 |
6.71e-26 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 108.35 E-value: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGrlifelggiseremAKLQTKADEAGKSSFAFAfYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:PRK00049 21 VDHGKTTLTA--------------AITKVLAKKGGAEAKAYD-QIDKAPEEKARGITINTAHVEYETEKRHYAHVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDFVKNMITGASQADAGLLLVPADgnfvtalakggkDEVQGSSRMHAQILKLIGCRQLMVGANKMDekqaawsqsastrf 160
Cdd:PRK00049 86 ADYVKNMITGAAQMDGAILVVSAA------------DGPMPQTREHILLARQVGVPYIVVFLNKCD-------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 161 ssemknvllrtgwtkkQVDDE-----------------------IPIIPYSGFAGdnlikkstnmpwwsgvdVHNDAEKV 217
Cdd:PRK00049 140 ----------------MVDDEellelvemevrellskydfpgddTPIIRGSALKA-----------------LEGDDDEE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 218 HVETIL---DCLSKFVRIPPRPVDKPGRVPISGLYSIKGVGDVLTGCCEQGTFKNGDEV--VFLPTHTKALpCLGkiftM 292
Cdd:PRK00049 187 WEKKILelmDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVeiVGIRDTQKTT-VTG----V 261
|
330 340 350
....*....|....*....|....*....|....*..
gi 193811884 293 EAHHNKKEICMPGDNLGFNIKGLKKDNMPKvGDVMVK 329
Cdd:PRK00049 262 EMFRKLLDEGQAGDNVGALLRGIKREDVER-GQVLAK 297
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
46-330 |
1.09e-25 |
|
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: 109.62 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 46 DTCAEEQARGITIqcntkE--F-HTE---NYRYSIIDAPGHRDFVKNMITGASQADAGLLLVPADgnfvtalakggkDEV 119
Cdd:COG3276 26 DRLKEEKKRGITI-----DlgFaYLPlpdGRRLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAAD------------EGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 120 QGSSRMHAQILKLIGCRQLMVGANKMDEKQAAWSQSASTrfssEMKNVLLRTGWtkkqvdDEIPIIPYSGFAGDNLikks 199
Cdd:COG3276 89 MPQTREHLAILDLLGIKRGIVVLTKADLVDEEWLELVEE----EIRELLAGTFL------EDAPIVPVSAVTGEGI---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 200 tnmpwwsgvdvhnDAEKVHVETILDclskfvRIPPRPVDKPGRVPISGLYSIKGVGDVLTGCCEQGTFKNGDEVVFLPTH 279
Cdd:COG3276 155 -------------DELRAALDALAA------AVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSG 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 193811884 280 TKAlpclgKIFTMEAHHNKKEICMPGDNLGFNIKGLKKDNMPKvGDVMVKK 330
Cdd:COG3276 216 KPV-----RVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIER-GDVLAAP 260
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-329 |
2.11e-24 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 104.15 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLifelggiseremAKLQTKADEAGKSSFAfafYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:PRK12735 21 VDHGKTTLTAAI------------TKVLAKKGGGEAKAYD---QIDNAPEEKARGITINTSHVEYETANRHYAHVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDFVKNMITGASQADAGLLLVPADgnfvtalakggkDEVQGSSRMHAQILKLIGCRQLMVGANKMD--------Ekqaaw 152
Cdd:PRK12735 86 ADYVKNMITGAAQMDGAILVVSAA------------DGPMPQTREHILLARQVGVPYIVVFLNKCDmvddeellE----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 153 sqsastrfSSEMKnvlLRTGWTKKQVD-DEIPIIPYSGFAGDNlikkstnmpwwsgvdvhNDAEKVHVETIL---DCLSK 228
Cdd:PRK12735 149 --------LVEME---VRELLSKYDFPgDDTPIIRGSALKALE-----------------GDDDEEWEAKILelmDAVDS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 229 FVRIPPRPVDKPGRVPISGLYSIKGVGDVLTGCCEQGTFKNGDEV--VFLpTHTKALPCLGkiftMEAHHNKKEICMPGD 306
Cdd:PRK12735 201 YIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVeiVGI-KETQKTTVTG----VEMFRKLLDEGQAGD 275
|
330 340
....*....|....*....|...
gi 193811884 307 NLGFNIKGLKKDNMPKvGDVMVK 329
Cdd:PRK12735 276 NVGVLLRGTKREDVER-GQVLAK 297
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
1-146 |
6.84e-19 |
|
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: 84.17 E-value: 6.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGrlifelggiseremAKLQTKADEAGKSSFAFAfYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:cd01884 11 VDHGKTTLTA--------------AITKVLAKKGGAKAKKYD-EIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGH 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193811884 81 RDFVKNMITGASQADAGLLLVPADgnfvtalakggkDEVQGSSRMHAQILKLIGCRQLMVGANKMD 146
Cdd:cd01884 76 ADYIKNMITGAAQMDGAILVVSAT------------DGPMPQTREHLLLARQVGVPYIVVFLNKAD 129
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
35-152 |
1.20e-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 bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 77.26 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 35 GKSSFAFA---FYMDTCAEEQARGITIQCNTKEFH-TENYRYSIIDAPGHRDFVKNMITGASQADAGLLLVPADgnfvta 110
Cdd:cd04171 11 GKTTLIKAltgIETDRLPEEKKRGITIDLGFAYLDlPDGKRLGFIDVPGHEKFVKNMLAGAGGIDAVLLVVAAD------ 84
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 193811884 111 lakggkDEVQGSSRMHAQILKLIGCRQLMVGANKMDEKQAAW 152
Cdd:cd04171 85 ------EGIMPQTREHLEILELLGIKKGLVVLTKADLVDEDR 120
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
1-127 |
1.02e-11 |
|
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: 64.57 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISERemaklqTKADEaGKSsfafafYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:cd04168 8 VDAGKTTLTESLLYTSGAIREL------GSVDK-GTT------RTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGH 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 193811884 81 RDFVKNMITGASQADAGLLLVPAdgnfvtalakggKDEVQGSSR--MHA 127
Cdd:cd04168 75 MDFIAEVERSLSVLDGAILVISA------------VEGVQAQTRilFRL 111
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
242-320 |
1.36e-11 |
|
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: 60.23 E-value: 1.36e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193811884 242 RVPISGLYSIKGVGDVLTGCCEQGTFKNGDEVVFLPTHTKAlpclgKIFTMEAHHNKKEICMPGDNLGFNIKGLKKDNM 320
Cdd:cd03696 2 RLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEV-----RVRSIQVHDKPVEEAKAGDRVALNLTGVDAKEL 75
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
50-271 |
2.58e-10 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 62.38 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 50 EEQARGITIQCNtkefhtenYRY---------SIIDAPGHRDFVKNMITGASQADAGLLLVPADgnfvtalakggkDEVQ 120
Cdd:PRK10512 30 EEKKRGMTIDLG--------YAYwpqpdgrvlGFIDVPGHEKFLSNMLAGVGGIDHALLVVACD------------DGVM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 121 GSSRMHAQILKLIGCRQLMVGANKMDEKQAAWSQSAstrfSSEMKNVLLRTGWTkkqvddEIPIIPYSGFAGDNLikkst 200
Cdd:PRK10512 90 AQTREHLAILQLTGNPMLTVALTKADRVDEARIAEV----RRQVKAVLREYGFA------EAKLFVTAATEGRGI----- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193811884 201 nmpwwsgvdvhnDAEKVHVETILDclskfvriPPRPVDKPGRVPISGLYSIKGVGDVLTGCCEQGTFKNGD 271
Cdd:PRK10512 155 ------------DALREHLLQLPE--------REHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGD 205
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
1-103 |
3.49e-10 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 59.55 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREmaklqtkadeAGKssfafAFYMDTCAEEQARGITI---------QCNTKEFHTENYR 71
Cdd:cd01885 9 VDHGKTTLSDSLLASAGIISEKL----------AGK-----ARYLDTREDEQERGITIkssaislyfEYEEEKMDGNDYL 73
|
90 100 110
....*....|....*....|....*....|..
gi 193811884 72 YSIIDAPGHRDFVKNMITGASQADAGLLLVPA 103
Cdd:cd01885 74 INLIDSPGHVDFSSEVTAALRLTDGALVVVDA 105
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
1-83 |
6.71e-10 |
|
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: 57.93 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMaKLQtkadeagkssfafafYMDTCAEEQARGITIQCNT-----KEFHTENYRYSII 75
Cdd:cd01890 9 IDHGKSTLADRLLELTGTVSEREM-KEQ---------------VLDSMDLERERGITIKAQAvrlfyKAKDGEEYLLNLI 72
|
....*...
gi 193811884 76 DAPGHRDF 83
Cdd:cd01890 73 DTPGHVDF 80
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
1-83 |
1.45e-09 |
|
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: 58.66 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFeLGGISER--EMAKLQTKADeagkssfafafYMDtcaEEQARGITIQCNTKEFHTENYRYSIIDAP 78
Cdd:cd01886 8 IDAGKTTTTERILY-YTGRIHKigEVHGGGATMD-----------WME---QERERGITIQSAATTCFWKDHRINIIDTP 72
|
....*
gi 193811884 79 GHRDF 83
Cdd:cd01886 73 GHVDF 77
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
1-83 |
4.00e-09 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 58.81 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISER-EMAKLQTKADeagkssfafafYMdtcAEEQARGITIQCNTKEFHTENYRYSIIDAPG 79
Cdd:PRK13351 17 IDAGKTTLTERILFYTGKIHKMgEVEDGTTVTD-----------WM---PQEQERGITIESAATSCDWDNHRINLIDTPG 82
|
....
gi 193811884 80 HRDF 83
Cdd:PRK13351 83 HIDF 86
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
1-105 |
4.22e-09 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 58.60 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREmaklqtkADEAGKSsfafafYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:PRK12740 4 SGAGKTTLTEAILFYTGAIHRIG-------EVEDGTT------TMDFMPEERERGISITSAATTCEWKGHKINLIDTPGH 70
|
90 100
....*....|....*....|....*
gi 193811884 81 RDFVKNMITGASQADAGLLLVPADG 105
Cdd:PRK12740 71 VDFTGEVERALRVLDGAVVVVCAVG 95
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
1-83 |
1.48e-08 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 56.80 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEremaklqtkaDEAGKssfafAFYMDTCAEEQARGITI-QCN---TKEFHTENYRYSIID 76
Cdd:PRK07560 29 IDHGKTTLSDNLLAGAGMISE----------ELAGE-----QLALDFDEEEQARGITIkAANvsmVHEYEGKEYLINLID 93
|
....*..
gi 193811884 77 APGHRDF 83
Cdd:PRK07560 94 TPGHVDF 100
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-101 |
3.11e-08 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 55.82 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREmaklqtkadeAGKssfafAFYMDTCAEEQARGITIQCNTKEFHTEN----------Y 70
Cdd:PTZ00416 28 VDHGKSTLTDSLVCKAGIISSKN----------AGD-----ARFTDTRADEQERGITIKSTGISLYYEHdledgddkqpF 92
|
90 100 110
....*....|....*....|....*....|.
gi 193811884 71 RYSIIDAPGHRDFvKNMITGASQADAGLLLV 101
Cdd:PTZ00416 93 LINLIDSPGHVDF-SSEVTAALRVTDGALVV 122
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
255-328 |
5.59e-08 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 49.57 E-value: 5.59e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193811884 255 GDVLTGCCEQGTFKNGDEVVFLPTHTKALPCLGKIFTMEAHHNKKEICMPGDNLGFNIKGLKKDNMpKVGDVMV 328
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDI-RVGDTLT 73
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-105 |
7.10e-08 |
|
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: 54.67 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISeremaKLQTKADeaGKSsfafafYMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:COG0480 18 IDAGKTTLTERILFYTGAIH-----RIGEVHD--GNT------VMDWMPEEQERGITITSAATTCEWKGHKINIIDTPGH 84
|
90 100
....*....|....*....|....*
gi 193811884 81 RDFVKNMITGASQADAGLLLVPADG 105
Cdd:COG0480 85 VDFTGEVERSLRVLDGAVVVFDAVA 109
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
244-329 |
8.53e-08 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 49.44 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 244 PISGLYSIKGVGDVLTGCCEQGTFKNGDEV--VFLPTHTKAlpclgKIFTMEAHHNKKEICMPGDNLGFNIKGLKKDNMp 321
Cdd:cd03697 4 PIEDVFSIPGRGTVVTGRIERGVIKVGDEVeiVGFKETLKT-----TVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDV- 77
|
....*...
gi 193811884 322 KVGDVMVK 329
Cdd:cd03697 78 ERGMVLAK 85
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
46-277 |
8.56e-08 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 54.09 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 46 DTCAEEQARGITI-------------QCNTKEFHTENY-------------RYSIIDAPGHRDFVKNMITGASQADAGLL 99
Cdd:PRK04000 35 DRHSEELKRGITIrlgyadatirkcpDCEEPEAYTTEPkcpncgsetellrRVSFVDAPGHETLMATMLSGAALMDGAIL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 100 LVPADgnfvtalakggKDEVQGSSRMHAQILKLIGCRQLMVGANKMD---EKQAawsqsastrfsseMKNVLLRTGWTKK 176
Cdd:PRK04000 115 VIAAN-----------EPCPQPQTKEHLMALDIIGIKNIVIVQNKIDlvsKERA-------------LENYEQIKEFVKG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 177 QVDDEIPIIPYSGFAGDNLikkstnmpwwsgvdvhnDAekvhvetILDCLSKFVRIPPRPVDKPGRV------------- 243
Cdd:PRK04000 171 TVAENAPIIPVSALHKVNI-----------------DA-------LIEAIEEEIPTPERDLDKPPRMyvarsfdvnkpgt 226
|
250 260 270
....*....|....*....|....*....|....
gi 193811884 244 PISGLysikgVGDVLTGCCEQGTFKNGDEVVFLP 277
Cdd:PRK04000 227 PPEKL-----KGGVIGGSLIQGVLKVGDEIEIRP 255
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
1-202 |
8.84e-08 |
|
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: 52.21 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISERemaklQTKADEAgkssfafafyMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:cd01891 11 VDHGKTTLVDALLKQSGTFREN-----EEVGERV----------MDSNDLERERGITILAKNTAITYKDTKINIIDTPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 81 RDF------VKNMITGAsqadagLLLVPA-DG-----NFVT--ALAKGgkdevqgssrmhaqiLKLIgcrqlmVGANKMD 146
Cdd:cd01891 76 ADFggeverVLSMVDGV------LLLVDAsEGpmpqtRFVLkkALEAG---------------LKPI------VVINKID 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 147 EKQAawsqsASTRFSSEMKNVLLRTGWTKKQVDdeIPIIpY----SGFAGDNLIKKSTNM 202
Cdd:cd01891 129 RPDA-----RPEEVVDEVFDLFLELNATDEQLD--FPIV-YasakNGWASLNLDDPSEDL 180
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
341-435 |
2.51e-07 |
|
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).
Pssm-ID: 275447 [Multi-domain] Cd Length: 102 Bit Score: 48.54 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 341 SFTAQIQCLQHPGELNVGYSPMGIVRTGRSAMRMTAIhwkVGKETGGTKLENPPN-LKANEMAQVEFEPTQPIFLEKFTD 419
Cdd:cd01513 5 KFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKL---LSKEDGKTKEKKPPDsLQPGENGTVEVELQKPVVLERGKE 81
|
90
....*....|....*.
gi 193811884 420 CEGLGRLACLESNQPI 435
Cdd:cd01513 82 FPTLGRFALRDGGRTV 97
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
4-103 |
1.35e-06 |
|
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: 48.80 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 4 GKSTTTGRLIFElggisEREMAKLQTKADEAGKssfafafYMDTCAEEQARGITIQCNTKEFHTENYRY-----SIIDAP 78
Cdd:cd04167 12 GKTSLLDMLIEQ-----THKRTPSVKLGWKPLR-------YTDTRKDEQERGISIKSNPISLVLEDSKGksyliNIIDTP 79
|
90 100
....*....|....*....|....*
gi 193811884 79 GHRDFVKNMITGASQADAGLLLVPA 103
Cdd:cd04167 80 GHVNFMDEVAAALRLCDGVVLVVDV 104
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
1-83 |
1.47e-06 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 50.40 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEREMaKLQtkadeagkssfafafYMDTCAEEQARGITIQCNT-----KEFHTENYRYSII 75
Cdd:COG0481 15 IDHGKSTLADRLLELTGTLSEREM-KEQ---------------VLDSMDLERERGITIKAQAvrlnyKAKDGETYQLNLI 78
|
....*...
gi 193811884 76 DAPGHRDF 83
Cdd:COG0481 79 DTPGHVDF 86
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
35-146 |
3.14e-06 |
|
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: 47.65 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 35 GKSSFAFAF---YMDTCAEEQARGITI---------------QCNTKEFHTENYR------------YSIIDAPGHRDFV 84
Cdd:cd01888 12 GKTTLVKALsgvWTVRHKEELKRNITIklgyanakiykcpncGCPRPYDTPECECpgcggetklvrhVSFVDCPGHEILM 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193811884 85 KNMITGASQADAGLLLVPADGNFvtalakggkdeVQGSSRMHAQILKLIGCRQLMVGANKMD 146
Cdd:cd01888 92 ATMLSGAAVMDGALLLIAANEPC-----------PQPQTSEHLAALEIMGLKHIIILQNKID 142
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
73-305 |
3.61e-06 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 48.85 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 73 SIIDAPGHRDFVKNMITGASQADAGLLLVPADGNFvtalakggkdeVQGSSRMHAQILKLIGCRQLMVGANKMD--EKQA 150
Cdd:PTZ00327 120 SFVDCPGHDILMATMLNGAAVMDAALLLIAANESC-----------PQPQTSEHLAAVEIMKLKHIIILQNKIDlvKEAQ 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 151 AWSQsastrfSSEMKNVLLRTgwtkkqVDDEIPIIPYSGfagdnlikkstnmpwwsgvdvhndAEKVHVETILDCLSKFV 230
Cdd:PTZ00327 189 AQDQ------YEEIRNFVKGT------IADNAPIIPISA------------------------QLKYNIDVVLEYICTQI 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 231 RIPPRP--------------VDKPGrvpisglYSIKGV-GDVLTGCCEQGTFKNGDEVVFLP--------THTKALPCLG 287
Cdd:PTZ00327 233 PIPKRDltspprmivirsfdVNKPG-------EDIENLkGGVAGGSILQGVLKVGDEIEIRPgiiskdsgGEFTCRPIRT 305
|
250
....*....|....*...
gi 193811884 288 KIFTMEAHHNKKEICMPG 305
Cdd:PTZ00327 306 RIVSLFAENNELQYAVPG 323
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
45-274 |
9.72e-06 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 47.71 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 45 MDTCAEEQARGITIQC-NTKeFHTENYRYSIIDAPGHRDF------VKNMITGAsqadagLLLVPA-DG-----NFVT-- 109
Cdd:COG1217 44 MDSNDLERERGITILAkNTA-VRYKGVKINIVDTPGHADFggeverVLSMVDGV------LLLVDAfEGpmpqtRFVLkk 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 110 ALAKGgkdevqgssrmhaqiLKLIgcrqlmVGANKMDEKQA--AWSQsastrfsSEMKNVLLRTGWTKKQVDdeIPIIpY 187
Cdd:COG1217 117 ALELG---------------LKPI------VVINKIDRPDArpDEVV-------DEVFDLFIELGATDEQLD--FPVV-Y 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 188 ----SGFAGDNLIKKSTNMpwwsgvdvhndaeKVHVETILDclskfvRIPPRPVD--KPGRVPISGL-YSiKGVGDVLTG 260
Cdd:COG1217 166 asarNGWASLDLDDPGEDL-------------TPLFDTILE------HVPAPEVDpdGPLQMLVTNLdYS-DYVGRIAIG 225
|
250
....*....|....
gi 193811884 261 CCEQGTFKNGDEVV 274
Cdd:COG1217 226 RIFRGTIKKGQQVA 239
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
245-328 |
1.02e-05 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 43.75 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 245 ISGLYSIKGVGDVLTGCCEQGTFKNGDEVV--------FLPTHTKALpclgkiftmeaHHNKKEICM--PGDNLGFNIKG 314
Cdd:cd03694 5 IDDIYSVPGVGTVVSGTVSKGVIREGDTLLlgpdadgkFRPVTVKSI-----------HRNRQPVDRarAGQSASFALKK 73
|
90
....*....|....
gi 193811884 315 LKKDNMPKvGDVMV 328
Cdd:cd03694 74 IKRESLRK-GMVLV 86
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
1-116 |
1.06e-05 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 47.78 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISERemAKLQTKAdeagkssfafafyMDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGH 80
Cdd:PRK10218 14 VDHGKTTLVDKLLQQSGTFDSR--AETQERV-------------MDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGH 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 193811884 81 RDFVKNMITGASQADAGLLLVPA-DG-----NFVT--ALAKGGK 116
Cdd:PRK10218 79 ADFGGEVERVMSMVDSVLLVVDAfDGpmpqtRFVTkkAFAYGLK 122
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
2-146 |
1.65e-05 |
|
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: 46.05 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 2 DAGKSTTTGRLIFELGGISEREMaklqTKADEAGKssFAFAFYMDTcaeEQARGITIQCNTKEFHTENYRYSIIDAPGHR 81
Cdd:cd04169 12 DAGKTTLTEKLLLFGGAIQEAGA----VKARKSRK--HATSDWMEI---EKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193811884 82 DFVKNMITGASQADAGLLLVPAdgnfvtalAKGgkdevqgssrMHAQILKLIG-CRqlMVGA------NKMD 146
Cdd:cd04169 83 DFSEDTYRTLTAVDSAVMVIDA--------AKG----------VEPQTRKLFEvCR--LRGIpiitfiNKLD 134
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-101 |
2.13e-05 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 47.03 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 1 VDAGKSTTTGRLIFELGGISEremaklqtkaDEAGKssfafAFYMDTCAEEQARGITIQCN----------------TKE 64
Cdd:PLN00116 28 VDHGKSTLTDSLVAAAGIIAQ----------EVAGD-----VRMTDTRADEAERGITIKSTgislyyemtdeslkdfKGE 92
|
90 100 110
....*....|....*....|....*....|....*..
gi 193811884 65 FHTENYRYSIIDAPGHRDFvKNMITGASQADAGLLLV 101
Cdd:PLN00116 93 RDGNEYLINLIDSPGHVDF-SSEVTAALRITDGALVV 128
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
242-317 |
2.63e-05 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 42.25 E-value: 2.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193811884 242 RVPISGLYSIKGVGDVLTGCCEQGTFKNGDEVVFLPTHTKalpclGKIFTMEAHHNKKEICMPGDNLGFNIKGLKK 317
Cdd:cd01342 2 VMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGIT-----GRVTSIERFHEEVDEAKAGDIVGIGILGVKD 72
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
336-425 |
2.97e-05 |
|
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: 42.92 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 336 LARVKSFTAQIQCLQHPGELNVGYsPMGIVRTGRS-AMRMTAIHWKVGKETGGTKLENPPNLKANEMAQVEFEPTQPIFL 414
Cdd:cd04093 2 VATTSKFEARIVTFDLQVPILKGT-PVVLHRHSLSePATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80
|
90
....*....|.
gi 193811884 415 EKFTDCEGLGR 425
Cdd:cd04093 81 ETFKDNKELGR 91
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
339-417 |
2.46e-04 |
|
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: 40.33 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 339 VKSFTAQIQCLQH-----PGELNVGYSPMGIVRTGRSAMRMTAIHWKVgkETGGtKLENPPNLKANEMAQVEFEPTQPIF 413
Cdd:pfam03143 5 HTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKL--DPGG-VSENPEFVMPGDNVIVTVELIKPIA 81
|
....
gi 193811884 414 LEKF 417
Cdd:pfam03143 82 LEKG 85
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
339-425 |
4.21e-04 |
|
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: 39.46 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 339 VKSFTAQIQCLQHPGEL-NVGYSPMGIVRTGRSAMRMTAIHWKVGKETGGTKLENPPNLKANEMAQVEFEPTQPIFLEKF 417
Cdd:cd03704 3 VTEFEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETF 82
|
....*...
gi 193811884 418 TDCEGLGR 425
Cdd:cd03704 83 KDFPQLGR 90
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
45-146 |
3.95e-03 |
|
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: 38.73 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193811884 45 MDTCAEEQARGITIQCNTKEFHTENYRYSIIDAPGHRDFVKNMITGASQADAGLLLVPADgnfvtalakggkDEVQGSSR 124
Cdd:cd04170 39 SDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGETLSALRAVDAALIVVEAQ------------SGVEVGTE 106
|
90 100
....*....|....*....|...
gi 193811884 125 MHAQILKLIG-CRqlMVGANKMD 146
Cdd:cd04170 107 KVWEFLDDAKlPR--IIFINKMD 127
|
|
| |
