|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-442 |
0e+00 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 924.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 1 MPKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDQRTIEKFEKESAEMGKGSFKYAWVLDNLKAERERGITIDISLWKF 80
Cdd:PTZ00141 1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 81 ETSKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEAGISKNGQTREHILLSYTLGVKQMIVGVNKMD--AI 158
Cdd:PTZ00141 81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 159 QYKQERYEEIKKEISAFLKKTGYNPDKIPFVPISGFQGDNMIEPSTNMPWYKGPTLIGALDSVTPPERPVDKPLRLPLQD 238
Cdd:PTZ00141 161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 239 VYKISGIGTVPCGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNVASDAKNQ 318
Cdd:PTZ00141 241 VYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKND 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 319 PAVGCEDFTAQVIVMNHPGQIRKGYTPVLDCHTSHIACKFEELLSKIDRRTGKSMEgGEPEYIKNGDSALVKIVPTKPLC 398
Cdd:PTZ00141 321 PAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLE-ENPKAIKSGDAAIVKMVPTKPMC 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 167385576 399 VEEFAKFPPLGRFAVRDMKQTVAVGVVKAVTPR---ASNAAAAGKKK 442
Cdd:PTZ00141 400 VEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKKegsGTKAAAKAKKK 446
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-432 |
0e+00 |
|
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: 706.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 1 MPKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDQRTIEKFEKESAEMGKGSFKYAWVLDNLKAERERGITIDISLWKF 80
Cdd:COG5256 1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 81 ETSKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEfeagiskNGQTREHILLSYTLGVKQMIVGVNKMDAIQY 160
Cdd:COG5256 81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 161 KQERYEEIKKEISAFLKKTGYNPDKIPFVPISGFQGDNMIEPSTNMPWYKGPTLIGALDSVTPPERPVDKPLRLPLQDVY 240
Cdd:COG5256 154 SEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQDVY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 241 KISGIGTVPCGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNVASDAKNQPA 320
Cdd:COG5256 234 SISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNPPT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 321 VGcEDFTAQVIVMNHPGQIRKGYTPVLDCHTSHIACKFEELLSKIDRRTGKSMEgGEPEYIKNGDSALVKIVPTKPLCVE 400
Cdd:COG5256 314 VA-EEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKE-ENPQFLKTGDAAIVKIKPTKPLVIE 391
|
410 420 430
....*....|....*....|....*....|..
gi 167385576 401 EFAKFPPLGRFAVRDMKQTVAVGVVKAVTPRA 432
Cdd:COG5256 392 KFKEFPQLGRFAIRDMGQTVAAGVVLDVKPKK 423
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
2-431 |
0e+00 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 695.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 2 PKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDQRTIEKFEKESAEMGKGSFKYAWVLDNLKAERERGITIDISLWKFE 81
Cdd:PRK12317 1 AKEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 82 TSKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAgtgefEAGISKNGQTREHILLSYTLGVKQMIVGVNKMDAIQYK 161
Cdd:PRK12317 81 TDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVNYD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 162 QERYEEIKKEISAFLKKTGYNPDKIPFVPISGFQGDNMIEPSTNMPWYKGPTLIGALDSVTPPERPVDKPLRLPLQDVYK 241
Cdd:PRK12317 156 EKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQDVYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 242 ISGIGTVPCGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNVASDAKNQPAV 321
Cdd:PRK12317 236 ISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDNPPTV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 322 GcEDFTAQVIVMNHPGQIRKGYTPVLDCHTSHIACKFEELLSKIDRRTGKSMEgGEPEYIKNGDSALVKIVPTKPLCVEE 401
Cdd:PRK12317 316 A-EEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAE-ENPQFIKTGDAAIVKIKPTKPLVIEK 393
|
410 420 430
....*....|....*....|....*....|
gi 167385576 402 FAKFPPLGRFAVRDMKQTVAVGVVKAVTPR 431
Cdd:PRK12317 394 VKEIPQLGRFAIRDMGQTIAAGMVIDVKPA 423
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-442 |
0e+00 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 676.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 1 MPKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDQRTIEKFEKESAEMGKGSFKYAWVLDNLKAERERGITIDISLWKF 80
Cdd:PLN00043 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 81 ETSKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEAGISKNGQTREHILLSYTLGVKQMIVGVNKMDAI-- 158
Cdd:PLN00043 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 159 QYKQERYEEIKKEISAFLKKTGYNPDKIPFVPISGFQGDNMIEPSTNMPWYKGPTLIGALDSVTPPERPVDKPLRLPLQD 238
Cdd:PLN00043 161 KYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 239 VYKISGIGTVPCGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNVASDAKNQ 318
Cdd:PLN00043 241 VYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 319 PAVGCEDFTAQVIVMNHPGQIRKGYTPVLDCHTSHIACKFEELLSKIDRRTGKSMEgGEPEYIKNGDSALVKIVPTKPLC 398
Cdd:PLN00043 321 PAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELE-KEPKFLKNGDAGFVKMIPTKPMV 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 167385576 399 VEEFAKFPPLGRFAVRDMKQTVAVGVVKAVTPRASNAA----AAGKKK 442
Cdd:PLN00043 400 VETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAkvtkAAAKKK 447
|
|
| EF-1_alpha |
TIGR00483 |
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ... |
1-431 |
0e+00 |
|
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: 671.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 1 MPKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDQRTIEKFEKESAEMGKGSFKYAWVLDNLKAERERGITIDISLWKF 80
Cdd:TIGR00483 1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 81 ETSKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagisKNGQTREHILLSYTLGVKQMIVGVNKMDAIQY 160
Cdd:TIGR00483 81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 161 KQERYEEIKKEISAFLKKTGYNPDKIPFVPISGFQGDNMIEPSTNMPWYKGPTLIGALDSVTPPERPVDKPLRLPLQDVY 240
Cdd:TIGR00483 157 DEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTLLEALDALEPPEKPTDKPLRIPIQDVY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 241 KISGIGTVPCGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNVASDAKNQPA 320
Cdd:TIGR00483 237 SITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPDNPPK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 321 VgCEDFTAQVIVMNHPGQIRKGYTPVLDCHTSHIACKFEELLSKIDRRTGKSMEgGEPEYIKNGDSALVKIVPTKPLCVE 400
Cdd:TIGR00483 317 V-AKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLE-ENPQFLKTGDAAIVKFKPTKPMVIE 394
|
410 420 430
....*....|....*....|....*....|.
gi 167385576 401 EFAKFPPLGRFAVRDMKQTVAVGVVKAVTPR 431
Cdd:TIGR00483 395 AVKEIPPLGRFAIRDMGQTVAAGMIIDVDPT 425
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
9-225 |
5.60e-162 |
|
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: 455.03 E-value: 5.60e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDQRTIEKFEKESAEMGKGSFKYAWVLDNLKAERERGITIDISLWKFETSKYYFT 88
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 89 IIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEAGISKNGQTREHILLSYTLGVKQMIVGVNKMDAI--QYKQERYE 166
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 167385576 167 EIKKEISAFLKKTGYNPDKIPFVPISGFQGDNMIEPSTNMPWYKGPTLIGALDSVTPPE 225
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPTLLEALDSLEPPE 219
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
4-434 |
1.32e-115 |
|
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: 345.15 E-value: 1.32e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 4 EKTHINIVVIGHVDSGKSTTTGHLIYKCGGI--DQrtIEKFEKESAEMGKGSFKYAWVLDNLKAERERGITIDISLWKFE 81
Cdd:COG2895 14 NKDLLRFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 82 TSKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNKMDAIQYK 161
Cdd:COG2895 92 TPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 162 QERYEEIKKEISAFLKKTGYNPdkIPFVPISGFQGDNMIEPSTNMPWYKGPTLIGALDSVTPPERPVDKPLRLPLQDVYK 241
Cdd:COG2895 165 EEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWYDGPTLLEHLETVEVAEDRNDAPFRFPVQYVNR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 242 isgigtvP-------CGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVGfnvrnLTVK---DIKRGNV 311
Cdd:COG2895 243 -------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVT-----LTLEdeiDISRGDV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 312 ASDAKNQPAVGcEDFTAQVIVMN-HPGQIRKGYtpVLDCHTSHIACKFEELLSKIDRRTGKSMEGGEpeyIKNGDSALVK 390
Cdd:COG2895 311 IVAADAPPEVA-DQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNTLEHEAADS---LELNDIGRVT 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 167385576 391 IVPTKPLCVEEFAKFPPLGRFAV--RDMKQTVAVGVVKAVTPRASN 434
Cdd:COG2895 385 LRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMIRGALRRAAN 430
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
5-224 |
2.81e-78 |
|
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: 240.89 E-value: 2.81e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 5 KTHINIVVIGHVDSGKSTTTGHLIYKCGGIDQRTIEKFEKESaemgkgsfkyawVLDNLKAERERGITIDISLWKFETSK 84
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGefeagisKNGQTREHILLSYTLGVKqMIVGVNKMDAIqyKQER 164
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167385576 165 YEEIKKEIS-AFLKKTGYNPDKIPFVPISGFQGDNMiepstnmpwykgPTLIGALDSVTPP 224
Cdd:pfam00009 139 LEEVVEEVSrELLEKYGEDGEFVPVVPGSALKGEGV------------QTLLDALDEYLPS 187
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
14-434 |
4.17e-78 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 254.47 E-value: 4.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 14 GHVDSGKSTTTGHLIYKCGGI--DQrtIEKFEKESAEMG--KGSFKYAWVLDNLKAERERGITIDISLWKFETSKYYFTI 89
Cdd:PRK05506 31 GSVDDGKSTLIGRLLYDSKMIfeDQ--LAALERDSKKVGtqGDEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 90 IDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNKMDAIQYKQERYEEIK 169
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 170 KEISAFLKKTGYNpdKIPFVPISGFQGDNMIEPSTNMPWYKGPTLIGALDSVTPPERPVDKPLRLPLQDVYKisgigtvP 249
Cdd:PRK05506 182 ADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWYEGPSLLEHLETVEIASDRNLKDFRFPVQYVNR-------P 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 250 -------CGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVgfnvrNLTVKD---IKRGNVASDAKNQP 319
Cdd:PRK05506 253 nldfrgfAGTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAV-----TLTLADeidISRGDMLARADNRP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 320 AVGcEDFTAQVIVMN----HPGqirKGYtpVLDCHTSHIACKFEELLSKIDRRTgksMEGGEPEYIKNGDSALVKIVPTK 395
Cdd:PRK05506 328 EVA-DQFDATVVWMAeeplLPG---RPY--LLKHGTRTVPASVAAIKYRVDVNT---LERLAAKTLELNEIGRCNLSTDA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 167385576 396 PLCVEEFAKFPPLGRFAV--RDMKQTVAVGVVKAVTPRASN 434
Cdd:PRK05506 399 PIAFDPYARNRTTGSFILidRLTNATVGAGMIDFALRRATN 439
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
14-425 |
3.40e-75 |
|
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: 240.74 E-value: 3.40e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 14 GHVDSGKSTTTGHLIYKCGGIDQRTIEKFEKESAEMGK--GSFKYAWVLDNLKAERERGITIDISLWKFETSKYYFTIID 91
Cdd:TIGR02034 7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 92 APGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNKMDAIQYKQERYEEIKKE 171
Cdd:TIGR02034 87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 172 ISAFLKKTGYNPdkIPFVPISGFQGDNMIEPSTNMPWYKGPTLIGALDSVTPPERPVDKPLRLPLQDVYK----ISGI-G 246
Cdd:TIGR02034 160 YLAFAEQLGFRD--VTFIPLSALKGDNVVSRSESMPWYSGPTLLEILETVEVERDAQDLPLRFPVQYVNRpnldFRGYaG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 247 TVPCGRVEtgvlrPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVgfnvrNLTVK---DIKRGNVASDAKNQPAVGc 323
Cdd:TIGR02034 238 TIASGSVH-----VGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAV-----TLTLDdeiDISRGDLLAAADSAPEVA- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 324 EDFTAQVIVM-NHPgqIRKGYTPVLDCHTSHIACKFEELLSKIDRRTGKsmEGGEPEYIKNgDSALVKIVPTKPLCVEEF 402
Cdd:TIGR02034 307 DQFAATLVWMaEEP--LLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLE--KGAAKSLELN-EIGRVNLSLDEPIAFDPY 381
|
410 420
....*....|....*....|....*
gi 167385576 403 AKFPPLGRFAV--RDMKQTVAVGVV 425
Cdd:TIGR02034 382 AENRTTGAFILidRLSNRTVGAGMI 406
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
9-224 |
1.19e-72 |
|
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: 227.45 E-value: 1.19e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDQRTIEKFEK-ESAEMGKGSFKYAWVLDNLKAERERGITIDISLWKFETSKYYF 87
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAALERsKSSGTQGEKLDLALLVDGLQAEREQGITIDVAYRYFSTPKRKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 88 TIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNKMDAIQYKQERYEE 167
Cdd:cd04166 81 IIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 167385576 168 IKKEISAFLKKTGYNPdkIPFVPISGFQGDNMIEPSTNMPWYKGPTLIGALDSVTPP 224
Cdd:cd04166 154 IKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYKGPTLLEHLETVEIA 208
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
14-425 |
1.14e-71 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 233.65 E-value: 1.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 14 GHVDSGKSTTTGHL------IYKcggiDQrtIEKFEKESAEMGKGSFK--YAWVLDNLKAERERGITIDISLWKFETSKY 85
Cdd:PRK05124 34 GSVDDGKSTLIGRLlhdtkqIYE----DQ--LASLHNDSKRHGTQGEKldLALLVDGLQAEREQGITIDVAYRYFSTEKR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 86 YFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNKMDAIQYKQERY 165
Cdd:PRK05124 108 KFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 166 EEIKKEISAFLKKTGYNPDkIPFVPISGFQGDNMIEPSTNMPWYKGPTLIGALDSVTPPERPVDKPLRLPLQDVYKisgi 245
Cdd:PRK05124 181 ERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWYSGPTLLEVLETVDIQRVVDAQPFRFPVQYVNR---- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 246 gtvP-------CGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVgfnvrNLTVK---DIKRGNVASDA 315
Cdd:PRK05124 256 ---PnldfrgyAGTLASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAI-----TLVLEdeiDISRGDLLVAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 316 KNQPAVGcEDFTAQVIVMN-HPGQIRKGY--------TPVldchtshiacKFEELLSKIDRRTgksMEGGEPEYIKNGDS 386
Cdd:PRK05124 328 DEALQAV-QHASADVVWMAeQPLQPGQSYdikiagkkTRA----------RVDAIRYQVDINT---LTQREAENLPLNGI 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 167385576 387 ALVKIVPTKPLCVEEFAKFPPLGRFAV--RDMKQTVAVGVV 425
Cdd:PRK05124 394 GLVELTFDEPLVLDPYQQNRVTGGFIFidRLTNVTVGAGMV 434
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-425 |
5.25e-70 |
|
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: 226.96 E-value: 5.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 1 MPKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidqrtiekfeKESAEMGKGSFKYAWVLDNLKAERERGITIDI 75
Cdd:COG0050 1 MAKEkfertKPHVNIGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAKAKAYDQIDKAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 76 SLWKFETSKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNKM 155
Cdd:COG0050 66 SHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 156 DAIQyKQERYEEIKKEISAFLKKTGYNPDKIPFVPISGFQGdnmIEPSTNMPWYKGPT-LIGALDSVTP-PERPVDKPLR 233
Cdd:COG0050 139 DMVD-DEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKA---LEGDPDPEWEKKILeLMDAVDSYIPePERDTDKPFL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 234 LPLQDVYKISGIGTVPCGRVETGVLRPGT---IVQFAPSgVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGN 310
Cdd:COG0050 215 MPVEDVFSITGRGTVVTGRVERGIIKVGDeveIVGIRDT-QKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 311 VAsdAKNQPAVGCEDFTAQVIVMN-------HPgqIRKGYTPVLDCHTSHIackfeellskidrrTGKSMEGGEPEYIKN 383
Cdd:COG0050 294 VL--AKPGSITPHTKFEAEVYVLSkeeggrhTP--FFNGYRPQFYFRTTDV--------------TGVITLPEGVEMVMP 355
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 167385576 384 GDSALVKIVPTKPLCVEEfakfpplG-RFAVRDMKQTVAVGVV 425
Cdd:COG0050 356 GDNVTMTVELITPIAMEE-------GlRFAIREGGRTVGAGVV 391
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-311 |
1.29e-65 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 215.44 E-value: 1.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 1 MPKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidqrtiekfeKESAEMGKGSFK-YAWVlDNLKAERERGITID 74
Cdd:PRK00049 1 MAKEkfertKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAEAKaYDQI-DKAPEEKARGITIN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 75 ISLWKFETSKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNK 154
Cdd:PRK00049 65 TAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 155 MDAIQyKQERYEEIKKEISAFLKKTGYNPDKIPFVPISGFQGdnmIEPSTNMPWYKG-PTLIGALDSVTP-PERPVDKPL 232
Cdd:PRK00049 138 CDMVD-DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEKKiLELMDAVDSYIPtPERAIDKPF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 233 RLPLQDVYKISGIGTVPCGRVETGVLRPGT---IVQFAPSgVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRG 309
Cdd:PRK00049 214 LMPIEDVFSISGRGTVVTGRVERGIIKVGEeveIVGIRDT-QKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERG 292
|
..
gi 167385576 310 NV 311
Cdd:PRK00049 293 QV 294
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-428 |
2.70e-64 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 212.11 E-value: 2.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 1 MPKE-----KTHINIVVIGHVDSGKSTTTGHLiykcggidqrtiekfEKESAEMGKGSFKYAWVLDNLKAERERGITIDI 75
Cdd:PRK12736 1 MAKEkfdrsKPHVNIGTIGHVDHGKTTLTAAI---------------TKVLAERGLNQAKDYDSIDAAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 76 SLWKFETSKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNKM 155
Cdd:PRK12736 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 156 DAIQyKQERYEEIKKEISAFLKKTGYNPDKIPFVPISGF---QGDNmiepstnmPWYKG-PTLIGALDSVTP-PERPVDK 230
Cdd:PRK12736 139 DLVD-DEELLELVEMEVRELLSEYDFPGDDIPVIRGSALkalEGDP--------KWEDAiMELMDAVDEYIPtPERDTDK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 231 PLRLPLQDVYKISGIGTVPCGRVETGVLRPGT---IVQFAPSgVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIK 307
Cdd:PRK12736 210 PFLMPVEDVFTITGRGTVVTGRVERGTVKVGDeveIVGIKET-QKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 308 RGNVAsdAKNQPAVGCEDFTAQVIVMNHPGQIR-----KGYTPVLDCHTSHIAckfeellSKIDRRTGKSMeggepeyIK 382
Cdd:PRK12736 289 RGQVL--AKPGSIKPHTKFKAEVYILTKEEGGRhtpffNNYRPQFYFRTTDVT-------GSIELPEGTEM-------VM 352
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 167385576 383 NGDSALVKIVPTKPLCVEEfakfpplG-RFAVRDMKQTVAVGVVKAV 428
Cdd:PRK12736 353 PGDNVTITVELIHPIAMEQ-------GlKFAIREGGRTVGAGTVTEI 392
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
321-425 |
5.89e-64 |
|
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: 201.27 E-value: 5.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 321 VGCEDFTAQVIVMNHPGQIRKGYTPVLDCHTSHIACKFEELLSKIDRRTGKSMEgGEPEYIKNGDSALVKIVPTKPLCVE 400
Cdd:cd03705 1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLE-ENPKFLKSGDAAIVKMVPTKPLCVE 79
|
90 100
....*....|....*....|....*
gi 167385576 401 EFAKFPPLGRFAVRDMKQTVAVGVV 425
Cdd:cd03705 80 TFSEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-311 |
6.79e-63 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 208.15 E-value: 6.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 1 MPKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidqrtiekfeKESAEMGKGSFKYAWVLDNLKAERERGITIDI 75
Cdd:PRK12735 1 MAKEkfertKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGGEAKAYDQIDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 76 SLWKFETSKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNKM 155
Cdd:PRK12735 66 SHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 156 DAIQyKQERYEEIKKEISAFLKKTGYNPDKIPFVPISGFQGdnmIEPSTNMPWYKG-PTLIGALDSVTP-PERPVDKPLR 233
Cdd:PRK12735 139 DMVD-DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEAKiLELMDAVDSYIPePERAIDKPFL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 234 LPLQDVYKISGIGTVPCGRVETGVLRPG---TIVQFAPSgVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGN 310
Cdd:PRK12735 215 MPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKET-QKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQ 293
|
.
gi 167385576 311 V 311
Cdd:PRK12735 294 V 294
|
|
| tufA |
CHL00071 |
elongation factor Tu |
3-425 |
4.91e-62 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 206.35 E-value: 4.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 3 KEKTHINIVVIGHVDSGKSTTTGHLIYKCggidqrtiekfekeSAEMGKGSFKYAWVlDNLKAERERGITIDISLWKFET 82
Cdd:CHL00071 8 RKKPHVNIGTIGHVDHGKTTLTAAITMTL--------------AAKGGAKAKKYDEI-DSAPEEKARGITINTAHVEYET 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 83 SKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNKMDAIQyKQ 162
Cdd:CHL00071 73 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQVD-DE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 163 ERYEEIKKEISAFLKKTGYNPDKIPFVPISGFQGDNMIEPSTNM-----PWY-KGPTLIGALDSVTP-PERPVDKPLRLP 235
Cdd:CHL00071 145 ELLELVELEVRELLSKYDFPGDDIPIVSGSALLALEALTENPKIkrgenKWVdKIYNLMDAVDSYIPtPERDTDKPFLMA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 236 LQDVYKISGIGTVPCGRVETGVLRPG---TIVQFAPSgVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNVA 312
Cdd:CHL00071 225 IEDVFSITGRGTVATGRIERGTVKVGdtvEIVGLRET-KTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 313 SDAKN-QPAVgceDFTAQVIVMNHPGQIR-----KGYTPVLDCHTSHIACKFEELlskidrrtgKSMEGGEPEYIKNGDS 386
Cdd:CHL00071 304 AKPGTiTPHT---KFEAQVYILTKEEGGRhtpffPGYRPQFYVRTTDVTGKIESF---------TADDGSKTEMVMPGDR 371
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 167385576 387 ALVKIVPTKPLCVEEfakfpplG-RFAVRDMKQTVAVGVV 425
Cdd:CHL00071 372 IKMTVELIYPIAIEK-------GmRFAIREGGRTVGAGVV 404
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
3-429 |
3.07e-58 |
|
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: 196.15 E-value: 3.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 3 KEKTHINIVVIGHVDSGKSTTTGHLIykcggidqrtiekfeKESAEMGKGSFKYAWVLDNLKAERERGITIDISLWKFET 82
Cdd:TIGR00485 8 RTKPHVNVGTIGHVDHGKTTLTAAIT---------------TVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYET 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 83 SKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNKMDAIQyKQ 162
Cdd:TIGR00485 73 ETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVD-DE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 163 ERYEEIKKEISAFLKKTGYNPDKIPFV---PISGFQGDNMIEPstnmpwyKGPTLIGALDSVTP-PERPVDKPLRLPLQD 238
Cdd:TIGR00485 145 ELLELVEMEVRELLSQYDFPGDDTPIIrgsALKALEGDAEWEA-------KILELMDAVDEYIPtPEREIDKPFLLPIED 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 239 VYKISGIGTVPCGRVETGVLRPG---TIVQFAPSGvSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNVAsdA 315
Cdd:TIGR00485 218 VFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTR-KTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVL--A 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 316 KNQPAVGCEDFTAQVIVMNHPGQIR-----KGYTPVLDCHTSHIackfeellskidrrTGKSMEGGEPEYIKNGDSALVK 390
Cdd:TIGR00485 295 KPGSIKPHTKFEAEVYVLSKEEGGRhtpffSGYRPQFYFRTTDV--------------TGTIELPEGVEMVMPGDNVKMT 360
|
410 420 430
....*....|....*....|....*....|....*....
gi 167385576 391 IVPTKPLCVEEFAkfpplgRFAVRDMKQTVAVGVVKAVT 429
Cdd:TIGR00485 361 VELISPIALEQGM------RFAIREGGRTVGAGVVSKIL 393
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
3-428 |
4.38e-56 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 192.91 E-value: 4.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 3 KEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDQRTIEKFEKesaemgkgsfkyawvLDNLKAERERGITIDISLWKFET 82
Cdd:PLN03126 77 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYET 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 83 SKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNKMDAIQyKQ 162
Cdd:PLN03126 142 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD-DE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 163 ERYEEIKKEISAFLKKTGYNPDKIPFVPISGFQGDNMIEPSTNMP-----WY-KGPTLIGALDSVTP-PERPVDKPLRLP 235
Cdd:PLN03126 214 ELLELVELEVRELLSSYEFPGDDIPIISGSALLALEALMENPNIKrgdnkWVdKIYELMDAVDSYIPiPQRQTDLPFLLA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 236 LQDVYKISGIGTVPCGRVETGVLRPGTIVQFAPSGVSSEC--KSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNVAs 313
Cdd:PLN03126 294 VEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETRSTtvTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVL- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 314 dAKNQPAVGCEDFTAQVIVMNHPGQIR-----KGYTPVLDCHTSHIACKFEELLSKIDRrtgksmeggEPEYIKNGDSAL 388
Cdd:PLN03126 373 -AKPGSITPHTKFEAIVYVLKKEEGGRhspffAGYRPQFYMRTTDVTGKVTSIMNDKDE---------ESKMVMPGDRVK 442
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 167385576 389 VKIVPTKPLCVEEFAkfpplgRFAVRDMKQTVAVGVVKAV 428
Cdd:PLN03126 443 MVVELIVPVACEQGM------RFAIREGGKTVGAGVIQSI 476
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
3-428 |
2.84e-55 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 189.65 E-value: 2.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 3 KEKTHINIVVIGHVDSGKSTTTGHLIykcggidqrtiekfeKESAEMGKGSFKYAWVLDNLKAERERGITIDISLWKFET 82
Cdd:PLN03127 57 RTKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYET 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 83 SKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNKMDAIQyKQ 162
Cdd:PLN03127 122 AKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVD-DE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 163 ERYEEIKKEISAFLKKTGYNPDKIPFV---PISGFQGDN-MIEPSTNMpwykgpTLIGALDSVTP-PERPVDKPLRLPLQ 237
Cdd:PLN03127 194 ELLELVEMELRELLSFYKFPGDEIPIIrgsALSALQGTNdEIGKNAIL------KLMDAVDEYIPePVRVLDKPFLMPIE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 238 DVYKISGIGTVPCGRVETGVLRPG---TIVQFAPSG-VSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNVAs 313
Cdd:PLN03127 268 DVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPGGpLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVI- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 314 dAKNQPAVGCEDFTAQVIVMNHPGQIRkgYTPVLDCHTSHIACKFEELLSKIDRRTGKSMeggepeyIKNGDSALVKIVP 393
Cdd:PLN03127 347 -CKPGSIKTYKKFEAEIYVLTKDEGGR--HTPFFSNYRPQFYLRTADVTGKVELPEGVKM-------VMPGDNVTAVFEL 416
|
410 420 430
....*....|....*....|....*....|....*
gi 167385576 394 TKPLCVEefakfpPLGRFAVRDMKQTVAVGVVKAV 428
Cdd:PLN03127 417 ISPVPLE------PGQRFALREGGRTVGAGVVSKV 445
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
9-199 |
1.70e-54 |
|
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: 179.41 E-value: 1.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDQRTIEKFekesaemgkgsfkyaWVLDNLKAERERGITIDISLWKFETSKYYFT 88
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 89 IIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEfeagiskNGQTREHILLSyTLGVKQMIVGVNKMDAIqyKQERYEEI 168
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIA-LAGGLPIIVAVNKIDRV--GEEDFDEV 135
|
170 180 190
....*....|....*....|....*....|....
gi 167385576 169 KKEISAFLKKTGY---NPDKIPFVPISGFQGDNM 199
Cdd:cd00881 136 LREIKELLKLIGFtflKGKDVPIIPISALTGEGI 169
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
228-318 |
4.33e-54 |
|
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: 175.07 E-value: 4.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 228 VDKPLRLPLQDVYKISGIGTVPCGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIK 307
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
90
....*....|.
gi 167385576 308 RGNVASDAKNQ 318
Cdd:cd03693 81 RGDVAGDSKND 91
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
8-425 |
1.52e-45 |
|
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: 167.01 E-value: 1.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 8 INIVVIGHVDSGKSTttghLIYKCGGIDqrTiekfekesaemgkgsfkyawvlDNLKAERERGITIDISlwkfetskY-Y 86
Cdd:COG3276 1 MIIGTAGHIDHGKTT----LVKALTGID--T----------------------DRLKEEKKRGITIDLG--------FaY 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 87 FT--------IIDAPGHRDFIKNMITGTSQADVAILIVAAgtgefEAGISKngQTREHILLSYTLGVKQMIVGVNKMDAI 158
Cdd:COG3276 45 LPlpdgrrlgFVDVPGHEKFIKNMLAGAGGIDLVLLVVAA-----DEGVMP--QTREHLAILDLLGIKRGIVVLTKADLV 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 159 QykQERYEEIKKEISAFLKKTGYnpDKIPFVPISGFQGDNMiepstnmpwykgPTLIGALDSV--TPPERPVDKPLRLPL 236
Cdd:COG3276 118 D--EEWLELVEEEIRELLAGTFL--EDAPIVPVSAVTGEGI------------DELRAALDALaaAVPARDADGPFRLPI 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 237 QDVYKISGIGTVPCGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNVASDAk 316
Cdd:COG3276 182 DRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAP- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 317 nQPAVGCEDFTAQVIVMNHPGQIRKGYTPVLdCH--TSHIACKfeelLSKIDRrtgksmeggepEYIKNGDSALVKIVPT 394
Cdd:COG3276 261 -GALRPTDRIDVRLRLLPSAPRPLKHWQRVH-LHhgTAEVLAR----VVLLDR-----------EELAPGEEALAQLRLE 323
|
410 420 430
....*....|....*....|....*....|....
gi 167385576 395 KPLCVEEfakfpplG-RFAVRDM--KQTVAVGVV 425
Cdd:COG3276 324 EPLVAAR-------GdRFILRDYspRRTIGGGRV 350
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
6-224 |
1.55e-42 |
|
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: 148.50 E-value: 1.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 6 THINIVVIGHVDSGKSTTTGHLIykcggidqrtiekfeKESAEMGKGSFKYAWVLDNLKAERERGITIDISLWKFETSKY 85
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 86 YFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNKMDAIQyKQERY 165
Cdd:cd01884 66 HYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD-DEELL 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 166 EEIKKEISAFLKKTGYNPDKIPFVPISGFqgdNMIEPSTNMPWYKG-PTLIGALDSVTPP 224
Cdd:cd01884 138 ELVEMEVRELLSKYGFDGDDTPIVRGSAL---KALEGDDPNKWVDKiLELLDALDSYIPT 194
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
8-365 |
5.44e-35 |
|
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: 136.93 E-value: 5.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 8 INIVVIGHVDSGKSTttghLIYKCGGIDQrtiekfekesaemgkgsfkyawvlDNLKAERERGITIDISLWKFETSKYYF 87
Cdd:TIGR00475 1 MIIATAGHVDHGKTT----LLKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 88 TIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVGVNKMDAIQykQERYEE 167
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEGVMT-------QTGEHLAVLDLLGIPHTIVVITKADRVN--EEEIKR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 168 IKKEISAFLKKTGYNPDKIPFVpISGFQGDNMIEPSTNMpwykgPTLIGALDSvtppeRPVDKPLRLPLQDVYKISGIGT 247
Cdd:TIGR00475 124 TEMFMKQILNSYIFLKNAKIFK-TSAKTGQGIGELKKEL-----KNLLESLDI-----KRIQKPLRMAIDRAFKVKGAGT 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 248 VPCGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNVAsdakNQPavgcEDFT 327
Cdd:TIGR00475 193 VVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLI----LTP----EDPK 264
|
330 340 350
....*....|....*....|....*....|....*...
gi 167385576 328 AQVIVmnhpgqIRKGYTPVLDCHTSHIACKFEELLSKI 365
Cdd:TIGR00475 265 LRVVV------KFIAEVPLLELQPYHIAHGMSVTTGKI 296
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
319-428 |
5.57e-33 |
|
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: 120.06 E-value: 5.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 319 PAVGCEDFTAQVIVMNH-----PGQIRKGYTPVLDCHTSHIACKFEELLSKIDrrTGKSMEggEPEYIKNGDSALVKIVP 393
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSE--NPEFVMPGDNVIVTVEL 76
|
90 100 110
....*....|....*....|....*....|....*
gi 167385576 394 TKPLCVEEFAkfpplgRFAVRDMKQTVAVGVVKAV 428
Cdd:pfam03143 77 IKPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
321-425 |
3.77e-29 |
|
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: 109.79 E-value: 3.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 321 VGCEDFTAQVIVMNHPGQIRKGYTPVLDCHTSHIACKFEELLSKIDRRTGksmEGGEPEYIKNGDSALVKIVPTKPLCVE 400
Cdd:cd01513 1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTK---EKKPPDSLQPGENGTVEVELQKPVVLE 77
|
90 100
....*....|....*....|....*
gi 167385576 401 EFAKFPPLGRFAVRDMKQTVAVGVV 425
Cdd:cd01513 78 RGKEFPTLGRFALRDGGRTVGAGLI 102
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
10-196 |
7.19e-26 |
|
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: 103.07 E-value: 7.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 10 IVVIGHVDSGKSTttghLIYKCGGIDQrtiekfekesaemgkgsfkyawvlDNLKAERERGITIDISL--WKFETSKYyF 87
Cdd:cd04171 2 IGTAGHIDHGKTT----LIKALTGIET------------------------DRLPEEKKRGITIDLGFayLDLPDGKR-L 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 88 TIIDAPGHRDFIKNMITGTSQADVAILIVAAgtgefEAGISKngQTREHILLSYTLGVKQMIVGVNKMDAIQykQERYEE 167
Cdd:cd04171 53 GFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLVD--EDRLEL 123
|
170 180
....*....|....*....|....*....
gi 167385576 168 IKKEISAFLKKTGYNPDKIPFVPISGFQG 196
Cdd:cd04171 124 VEEEILELLAGTFLADAPIFPVSSVTGEG 152
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
323-425 |
1.37e-21 |
|
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: 89.15 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 323 CEDFTAQVIVMNHPGQI-RKGYTPVLDCHTSHIACKFEELLSKIDRRTGKSMEGgEPEYIKNGDSALVKIVPTKPLCVEE 401
Cdd:cd03704 3 VTEFEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKK-KPKFVKSGQVVIARLETARPICLET 81
|
90 100
....*....|....*....|....
gi 167385576 402 FAKFPPLGRFAVRDMKQTVAVGVV 425
Cdd:cd03704 82 FKDFPQLGRFTLRDEGKTIAIGKV 105
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
1-234 |
4.96e-20 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 91.45 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 1 MPKEKTH--INIVVIGHVDSGKSTTTGHLiykcggidqrTIEKFEKESAEMgkgsfkyawvldnlkaerERGITI----- 73
Cdd:PRK04000 1 MMWEKVQpeVNIGMVGHVDHGKTTLVQAL----------TGVWTDRHSEEL------------------KRGITIrlgya 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 74 DISLWK---FETSKYYFT------------------IIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEAgiskngQ 132
Cdd:PRK04000 53 DATIRKcpdCEEPEAYTTepkcpncgsetellrrvsFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------Q 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 133 TREHILLSYTLGVKQMIVGVNKMDAIQYKQ--ERYEEIKKeisaFLKktGYNPDKIPFVPISGFQGDNMiepstnmpwyk 210
Cdd:PRK04000 127 TKEHLMALDIIGIKNIVIVQNKIDLVSKERalENYEQIKE----FVK--GTVAENAPIIPVSALHKVNI----------- 189
|
250 260
....*....|....*....|....*
gi 167385576 211 gPTLIGALDSVTP-PERPVDKPLRL 234
Cdd:PRK04000 190 -DALIEAIEEEIPtPERDLDKPPRM 213
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
319-428 |
1.94e-19 |
|
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: 83.36 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 319 PAVGCEDFTAQVIVMNHPGQIRKGYTPVLDCHTSHIACKFEELLSKIDRRTGKsMEGGEPEYIKNGDSALVKIVPTKPLC 398
Cdd:cd04093 1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGE-VIKKKPRCLGKNQSAVVEIELERPIP 79
|
90 100 110
....*....|....*....|....*....|
gi 167385576 399 VEEFAKFPPLGRFAVRDMKQTVAVGVVKAV 428
Cdd:cd04093 80 LETFKDNKELGRFVLRRGGETIAAGIVTEI 109
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
8-196 |
4.98e-18 |
|
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: 81.64 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 8 INIVVIGHVDSGKSTTTGHLIykcggidqrtiekfEKESAEmgkgsfkyawVLDNLKAERERGITIDISLWKF------- 80
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALS--------------EIASTA----------AFDKNPQSQERGITLDLGFSSFevdkpkh 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 81 -------ETSKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGefeagisKNGQTREHILLSYTLGvKQMIVGVN 153
Cdd:cd01889 57 lednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQTAECLVIGELLC-KPLIVVLN 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 167385576 154 KMDAIQ--YKQERYEEIKKEISAFLKKTgyNPDKIPFVPISGFQG 196
Cdd:cd01889 129 KIDLIPeeERKRKIEKMKKRLQKTLEKT--RLKDSPIIPVSAKPG 171
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
8-200 |
5.23e-18 |
|
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: 81.93 E-value: 5.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 8 INIVVIGHVDSGKSTTTGHLiykcGGIdqrtiekfekesaemgkgsfkyaWVlDNLKAERERGITI-----DISLWKFET 82
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKAL----SGV-----------------------WT-VRHKEELKRNITIklgyaNAKIYKCPN 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 83 SKYY----------------------FTIIDAPGHRDFIKNMITGTSQADVAILIVAAgtgefeagiskN-----GQTRE 135
Cdd:cd01888 53 CGCPrpydtpececpgcggetklvrhVSFVDCPGHEILMATMLSGAAVMDGALLLIAA-----------NepcpqPQTSE 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167385576 136 HILLSYTLGVKQMIVGVNKMDAIQYKQ--ERYEEIKKeisaFLKKTGYnpDKIPFVPISGFQGDNMI 200
Cdd:cd01888 122 HLAALEIMGLKHIIILQNKIDLVKEEQalENYEQIKE----FVKGTIA--ENAPIIPISAQLKYNID 182
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
9-201 |
1.27e-17 |
|
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: 81.90 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDQRtiekfekesaemgkGSfkyawV------LDNLKAERERGITIDISLWKFET 82
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIREL--------------GS-----VdkgttrTDSMELERQRGITIFSAVASFQW 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 83 SKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGefeagisKNGQTRehILLSyTLgvKQM----IVGVNKMDAI 158
Cdd:cd04168 62 EDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTR--ILFR-LL--RKLniptIIFVNKIDRA 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 167385576 159 QYKQER-YEEIKKEISAFLKKTgYNPDKIPFVPISGFQGDNMIE 201
Cdd:cd04168 130 GADLEKvYQEIKEKLSPDIVPM-QKVGLYPNICDTNNIDDEQIE 172
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
232-311 |
3.20e-16 |
|
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: 73.07 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 232 LRLPLQDVYKISGIGTVPCGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVGFNVRNltVKDIKRGNV 311
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
234-313 |
3.73e-15 |
|
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: 70.24 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 234 LPLQDVYKISGIGTVPCGRVETGVLRPG---TIVQFAPSgVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGN 310
Cdd:cd03697 3 MPIEDVFSIPGRGTVVTGRIERGVIKVGdevEIVGFKET-LKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGM 81
|
...
gi 167385576 311 VAS 313
Cdd:cd03697 82 VLA 84
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
232-311 |
7.66e-15 |
|
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: 69.48 E-value: 7.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 232 LRLPLQDVYKISGIGTVPCGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNV 311
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
9-189 |
2.25e-14 |
|
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: 71.03 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDQRtiekfekesaEMgkgsfkYAWVLDNLKAERERGITID---ISL-WKFETSK 84
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSER----------EM------KEQVLDSMDLERERGITIKaqaVRLfYKAKDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 85 -YYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGeFEAgiskngQTREHILLSYTLGVKqMIVGVNKMDAiqyKQE 163
Cdd:cd01890 66 eYLLNLIDTPGHVDFSYEVSRSLAACEGALLVVDATQG-VEA------QTLANFYLALENNLE-IIPVINKIDL---PAA 134
|
170 180
....*....|....*....|....*.
gi 167385576 164 RYEEIKKEISAFLkktGYNPDKIPFV 189
Cdd:cd01890 135 DPDRVKQEIEDVL---GLDASEAILV 157
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
9-118 |
3.90e-14 |
|
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: 71.11 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDQRTIekfekesaemgkGSFKYawvLDNLKAERERGITID---ISLwKFETSK- 84
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGIISEKLA------------GKARY---LDTREDEQERGITIKssaISL-YFEYEEe 65
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 167385576 85 ------YYFTIIDAPGHRDFIKNMITGTSQADVAILIVAA 118
Cdd:cd01885 66 kmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDA 105
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
9-260 |
6.83e-14 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 73.59 E-value: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDQRTiekfekESAEMgkgsfkyawVLDNLKAERERGITIDISLWKFETSKYYFT 88
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA------ETQER---------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 89 IIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEagiskngQTREHILLSYTLGVKQMIVgVNKMDAIQYKQERYEEI 168
Cdd:PRK10218 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 169 KKEISAFLKKTGYNPDkIPFV------PISGFQGDNMIEPSTnmPWYKgptliGALDSVTPPERPVDKPLRLPLQDVYKI 242
Cdd:PRK10218 144 VFDLFVNLDATDEQLD-FPIVyasalnGIAGLDHEDMAEDMT--PLYQ-----AIVDHVPAPDVDLDGPFQMQISQLDYN 215
|
250
....*....|....*...
gi 167385576 243 SGIGTVPCGRVETGVLRP 260
Cdd:PRK10218 216 SYVGVIGIGRIKRGKVKP 233
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
10-261 |
3.32e-13 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 71.62 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 10 IVVIGHVDSGKSTttghLIYKCGGIDQrtiekfekesaemgkgsfkyawvlDNLKAERERGITIDI--SLWKFETSKYyF 87
Cdd:PRK10512 3 IATAGHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWPQPDGRV-L 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 88 TIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFeagisknGQTREHILLSYTLGVKQMIVGVNKMDAIQykQERYEE 167
Cdd:PRK10512 54 GFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHLAILQLTGNPMLTVALTKADRVD--EARIAE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 168 IKKEISAFLKKTGYnpDKIPFVPISGFQGDNMiepstnmpwykgPTLIGALDSVTPPERPVDKPLRLPLQDVYKISGIGT 247
Cdd:PRK10512 125 VRRQVKAVLREYGF--AEAKLFVTAATEGRGI------------DALREHLLQLPEREHAAQHRFRLAIDRAFTVKGAGL 190
|
250
....*....|....
gi 167385576 248 VPCGRVETGVLRPG 261
Cdd:PRK10512 191 VVTGTALSGEVKVG 204
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
7-320 |
1.07e-12 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 70.05 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 7 HI-NIVVIGHVDSGKSTTTGHLIYKCGGIDQRtiekfekesaEMGkgsfkyAWVLDNLKAERERGITID---ISL-WKFE 81
Cdd:COG0481 5 NIrNFSIIAHIDHGKSTLADRLLELTGTLSER----------EMK------EQVLDSMDLERERGITIKaqaVRLnYKAK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 82 TSK-YYFTIIDAPGHRDFIknmitgtsqADV---------AILIVAAGTGeFEAgiskngQTREHILLSYTLGVKqmIVG 151
Cdd:COG0481 69 DGEtYQLNLIDTPGHVDFS---------YEVsrslaacegALLVVDASQG-VEA------QTLANVYLALENDLE--IIP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 152 V-NKMD---AiqykqeRYEEIKKEISAFLkktGYNPDKIpfVPISGFQGDNMIEpstnmpwykgptLIGAL-DSVTPPER 226
Cdd:COG0481 131 ViNKIDlpsA------DPERVKQEIEDII---GIDASDA--ILVSAKTGIGIEE------------ILEAIvERIPPPKG 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 227 PVDKPLRlPL-----QDVYKisgiGTVPCGRVETGVLRPGTIVQFAPSGVSSECKSV---EMHHTALAQAIPGDnVGFNV 298
Cdd:COG0481 188 DPDAPLQ-ALifdswYDSYR----GVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVgvfTPKMTPVDELSAGE-VGYII 261
|
330 340
....*....|....*....|...
gi 167385576 299 RNL-TVKDIKRGNVASDAKNqPA 320
Cdd:COG0481 262 AGIkDVRDARVGDTITLAKN-PA 283
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
10-199 |
1.22e-12 |
|
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: 65.57 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 10 IVVIGHVDSGKSTttghliykcggidqrtiekfekesaemgkgsfkyawVLDNLK----AERE-RGITIDISLWKFETSK 84
Cdd:cd01887 3 VTVMGHVDHGKTT------------------------------------LLDKIRktnvAAGEaGGITQHIGAYQVPIDV 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 85 YY--FTIIDAPGHRDFiKNMIT-GTSQADVAILIVAAGTGeFEAgiskngQTREHILLSYTLGVKqMIVGVNKMDAIQYK 161
Cdd:cd01887 47 KIpgITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------QTIEAINHAKAANVP-IIVAINKIDKPYGT 117
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 167385576 162 QERYEEIKKEISAF----LKKTGYnpdkIPFVPISGFQGDNM 199
Cdd:cd01887 118 EADPERVKNELSELglvgEEWGGD----VSIVPISAKTGEGI 155
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
9-156 |
1.52e-12 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 69.60 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDQR-TIEKFEKESaemgkgsfkyawvlDNLKAERERGITIDISL----WKfets 83
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKIHKMgEVEDGTTVT--------------DWMPQEQERGITIESAAtscdWD---- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167385576 84 KYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGeFEAgiskngQTREHILLSYTLGVKQMIVgVNKMD 156
Cdd:PRK13351 72 NHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTG-VQP------QTETVWRQADRYGIPRLIF-INKMD 136
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
9-206 |
3.73e-12 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 64.92 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDQRtiekfeKESAEMgkgsfkyawVLDNLKAERERGITIdisLWKfETSKYY-- 86
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGTFREN------EEVGER---------VMDSNDLERERGITI---LAK-NTAITYkd 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 87 --FTIIDAPGHRDF------IKNMitgtsqADVAILIVAAGTGEFEagiskngQTRehILLSYTL--GVKqMIVGVNKMD 156
Cdd:cd01891 65 tkINIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP-------QTR--FVLKKALeaGLK-PIVVINKID 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 167385576 157 AiqyKQERYEEIKKEISAFLKKTGYNPDKIPFvPI------SGFQGDNMIEPSTNM 206
Cdd:cd01891 129 R---PDARPEEVVDEVFDLFLELNATDEQLDF-PIvyasakNGWASLNLDDPSEDL 180
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
13-157 |
1.15e-11 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 66.69 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 13 IGHVDSGKSTTTGHLIYKCGGIDQR-TIEkfEKESaemgkgsfkyawVLDNLKAERERGITIDISLWKFETSKYYFTIID 91
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIgEVE--DGTT------------TMDFMPEERERGISITSAATTCEWKGHKINLID 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167385576 92 APGHRDFIKNMITGTSQADVAILIVAAGTGefeagisKNGQTRehILLSYT--LGVKQMIVgVNKMDA 157
Cdd:PRK12740 67 TPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TVWRQAekYGVPRIIF-VNKMDR 124
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
246-311 |
1.38e-11 |
|
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: 59.97 E-value: 1.38e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167385576 246 GTVPCGRVETGVLRPGTIVQFAPSGVS-----SECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNV 311
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGkkkivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
231-314 |
1.42e-11 |
|
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: 60.22 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 231 PLRLPLQDVYKISGIGTVPCGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGN 310
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
....
gi 167385576 311 VASD 314
Cdd:cd16267 81 ILCD 84
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
9-157 |
1.44e-11 |
|
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: 64.54 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDQrtiekfeKESAEMGKGsfkyawVLDNLKAERERGITIDISLWKFETSKYYFT 88
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDR-------LGRVEDGNT------VSDYDPEEKKRKMSIETSVAPLEWNGHKIN 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167385576 89 IIDAPGHRDFIKNMITGTSQADVAILIVAAGTGefeagisKNGQTREHILLSYTLGVKQMIVgVNKMDA 157
Cdd:cd04170 68 LIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWEFLDDAKLPRIIF-INKMDR 128
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
9-121 |
2.10e-11 |
|
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: 65.84 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDQrtIEKFEKESAEMgkgsfkyawvlDNLKAERERGITIDISLWKFETSKYYFT 88
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHR--IGEVHDGNTVM-----------DWMPEEQERGITITSAATTCEWKGHKIN 77
|
90 100 110
....*....|....*....|....*....|...
gi 167385576 89 IIDAPGHRDFIKNMITGTSQADVAILIVAAGTG 121
Cdd:COG0480 78 IIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG 110
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
9-156 |
3.75e-11 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 62.29 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 9 NIVVIGHVDSGKSTTTGHLIYKcggidqrtIEKFEKESAEMGKgSFKYawvLDNLKAERERGITID---ISLwKFETSK- 84
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQ--------THKRTPSVKLGWK-PLRY---TDTRKDEQERGISIKsnpISL-VLEDSKg 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167385576 85 --YYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTgefeaGISKNgqTREHILLSYTLGVKqMIVGVNKMD 156
Cdd:cd04167 69 ksYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTSV--TERLIRHAIQEGLP-MVLVINKID 134
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
9-98 |
5.02e-10 |
|
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: 59.81 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDqrtiekfekesaEMG----KGSfkyawVLDNLKAERERGITID---ISL-WKf 80
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIH------------KIGevhgGGA-----TMDWMEQERERGITIQsaaTTCfWK- 62
|
90
....*....|....*...
gi 167385576 81 etsKYYFTIIDAPGHRDF 98
Cdd:cd01886 63 ---DHRINIIDTPGHVDF 77
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
8-199 |
1.41e-09 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 59.63 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 8 INIVVIGHVDSGKSTT--------------------TGHL------IYKCggidqrtiEKFEKESAEMGKGSFKyawvLD 61
Cdd:PTZ00327 35 INIGTIGHVAHGKSTVvkalsgvktvrfkrekvrniTIKLgyanakIYKC--------PKCPRPTCYQSYGSSK----PD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 62 NLKAERERGITidislwkfeTSKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGefeagiSKNGQTREHILLSY 141
Cdd:PTZ00327 103 NPPCPGCGHKM---------TLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANES------CPQPQTSEHLAAVE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 142 TLGVKQMIVGVNKMDAI--QYKQERYEEIKKeisaFLKKTgyNPDKIPFVPISGFQGDNM 199
Cdd:PTZ00327 168 IMKLKHIIILQNKIDLVkeAQAQDQYEEIRN----FVKGT--IADNAPIIPISAQLKYNI 221
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
232-311 |
2.83e-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: 53.72 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 232 LRLPLQDVYKISGIGTVPCGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVGfnvrnLTVK---DIKR 308
Cdd:cd03695 1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVT-----LTLEdeiDVSR 75
|
...
gi 167385576 309 GNV 311
Cdd:cd03695 76 GDL 78
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
9-264 |
3.23e-09 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 58.88 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDQRtiekfeKESAEMgkgsfkyawVLDNLKAERERGITIdisLWKfETSKYY-- 86
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQSGTFREN------QEVAER---------VMDSNDLERERGITI---LAK-NTAVRYkg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 87 --FTIIDAPGHRDF------IKNMitgtsqADVAILIVAAgtgeFEagisknG---QTR-------EhillsytLGVKqM 148
Cdd:COG1217 69 vkINIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlkkalE-------LGLK-P 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 149 IVGVNKMDaiqyKQE-RYEEIKKEISAFLKKTGYNPDKIPFvPI------SGFQGDNMIEPSTNM-PWYKgptLIgaLDS 220
Cdd:COG1217 125 IVVINKID----RPDaRPDEVVDEVFDLFIELGATDEQLDF-PVvyasarNGWASLDLDDPGEDLtPLFD---TI--LEH 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 167385576 221 VTPPERPVDKPLRlpLQ------DVYkisgIGTVPCGRVETGVLRPGTIV 264
Cdd:COG1217 195 VPAPEVDPDGPLQ--MLvtnldySDY----VGRIAIGRIFRGTIKKGQQV 238
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
12-121 |
9.37e-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: 56.07 E-value: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 12 VIGHVDSGKSTTTGHLIYKCGGIdqrtiekfeKESAEM-GKGSFKYAwVLDNLKAERERGITIDISLWKFETSKYYFTII 90
Cdd:cd04169 7 IISHPDAGKTTLTEKLLLFGGAI---------QEAGAVkARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76
|
90 100 110
....*....|....*....|....*....|.
gi 167385576 91 DAPGHRDFIKNMITGTSQADVAILIVAAGTG 121
Cdd:cd04169 77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
231-314 |
1.74e-08 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 51.35 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 231 PLRLPLQDVYKiSGIGTVPCGRVETGVLRPGTIVQFAPSGVSSECKSVEMH-HTALAQAIPGDNVGFNVRNLTVKDIKRG 309
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....*
gi 167385576 310 NVASD 314
Cdd:cd03698 80 DILSS 84
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
10-199 |
2.07e-08 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 56.38 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 10 IVVIGHVDSGKsTTTGHLIYK-------CGGIDQRtIEKFEKEsaemgkgsFKYawvldnlkaerergitidislwKFET 82
Cdd:CHL00189 247 VTILGHVDHGK-TTLLDKIRKtqiaqkeAGGITQK-IGAYEVE--------FEY----------------------KDEN 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 83 SKYYFtiIDAPGHRDFIKNMITGTSQADVAILIVAAGTGefeagisKNGQTREHIllSYTLGVK-QMIVGVNKMDAIQYK 161
Cdd:CHL00189 295 QKIVF--LDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIEAI--NYIQAANvPIIVAINKIDKANAN 363
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 167385576 162 QERyeeIKKEISAflkktgYN--PDK----IPFVPISGFQGDNM 199
Cdd:CHL00189 364 TER---IKQQLAK------YNliPEKwggdTPMIPISASQGTNI 398
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
3-98 |
3.89e-08 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 55.64 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 3 KEKTHI-NIVVIGHVDSGKSTTTGHLIYKCGGIDQRTiekfekesaeMGKgsfkyAWVLDNLKAERERGITID---ISLW 78
Cdd:PRK07560 15 KNPEQIrNIGIIAHIDHGKTTLSDNLLAGAGMISEEL----------AGE-----QLALDFDEEEQARGITIKaanVSMV 79
|
90 100
....*....|....*....|.
gi 167385576 79 -KFETSKYYFTIIDAPGHRDF 98
Cdd:PRK07560 80 hEYEGKEYLINLIDTPGHVDF 100
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-98 |
7.04e-08 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 54.73 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 1 MPKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDQrtiekfekESAemgkGSFKYAwvlDNLKAERERGITID---ISL 77
Cdd:PLN00116 13 MDKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGIIAQ--------EVA----GDVRMT---DTRADEAERGITIKstgISL 77
|
90 100 110
....*....|....*....|....*....|....
gi 167385576 78 W-------------KFETSKYYFTIIDAPGHRDF 98
Cdd:PLN00116 78 YyemtdeslkdfkgERDGNEYLINLIDSPGHVDF 111
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-98 |
7.99e-08 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 54.67 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 1 MPKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIdqrtiekfekESAEMGKGSFkyawvLDNLKAERERGITID---ISL 77
Cdd:PTZ00416 13 MDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGII----------SSKNAGDARF-----TDTRADEQERGITIKstgISL 77
|
90 100
....*....|....*....|....*...
gi 167385576 78 ---WKFETSK----YYFTIIDAPGHRDF 98
Cdd:PTZ00416 78 yyeHDLEDGDdkqpFLINLIDSPGHVDF 105
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
11-201 |
1.65e-07 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 50.53 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 11 VVIGHVDSGKSTTTGHLIYKcggidqrtieKFEKESAEMGKgsfkyawvldnlkaerergiTIDISL--WKFETSKYYFT 88
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGG----------EVGEVSDVPGT--------------------TRDPDVyvKELDKGKVKLV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 89 IIDAPGHRDFIKNMITGT-----SQADVAILIVAAGTGEFEAgiskngQTREHILLSYTLGVKQMIVGVNKMDAIQYKQE 163
Cdd:cd00882 51 LVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRESEE------DAKLLILRRLRKEGIPIILVGNKIDLLEEREV 124
|
170 180 190
....*....|....*....|....*....|....*...
gi 167385576 164 RYEEIKKEISAFLkktgynpdKIPFVPISGFQGDNMIE 201
Cdd:cd00882 125 EELLRLEELAKIL--------GVPVFEVSAKTGEGVDE 154
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
231-311 |
3.80e-07 |
|
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: 47.48 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 231 PLRLPLQDVYKisGIGTVPCGRVETGVLRPGTIVQFAPSGVSSECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGN 310
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78
|
.
gi 167385576 311 V 311
Cdd:cd04089 79 V 79
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
238-311 |
1.38e-06 |
|
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: 46.06 E-value: 1.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167385576 238 DVYKISGIGTVPCGRVETGVLRPGTIVQFAPSGVSS----ECKSVEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNV 311
Cdd:cd03694 7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKfrpvTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
321-428 |
1.52e-05 |
|
Domain III of the GP-1 family of GTPases; This family 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 the 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: 294007 [Multi-domain] Cd Length: 87 Bit Score: 43.28 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 321 VGCEDFTAQVIVMNHPGQIRKGYTPVLDCHTSHIACKFEellsKIDRrtgksmeggepEYIKNGDSALVKIvptkplcve 400
Cdd:cd03708 1 RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARII----SIDK-----------EVLRTGDRALVRF--------- 56
|
90 100 110
....*....|....*....|....*....|..
gi 167385576 401 EFAKFP----PLGRFAVRDMKqTVAVGVVKAV 428
Cdd:cd03708 57 RFLYRPeylrEGQRLIFREGR-TKGIGTVTKV 87
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
8-201 |
6.61e-05 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 43.13 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 8 INIVVIGHVDSGKSTTTGHLIYKCGGIDqrtiekfekesaEMGKGSFKYAWVLdnlkAERERGITidislwkfetskYYF 87
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSIT------------EYYPGTTRNYVTT----VIEEDGKT------------YKF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 88 TIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEAGISKNGQTREhILLSYTLGVKqMIVGVNKMDAIQYKQERYEE 167
Cdd:TIGR00231 54 NLLDTAGQEDYDAIRRLYYPQVERSLRVFDIVILVLDVEEILEKQTKE-IIHHADSGVP-IILVGNKIDLKDADLKTHVA 131
|
170 180 190
....*....|....*....|....*....|....
gi 167385576 168 IKKEISAFlkktgynpdkIPFVPISGFQGDNMIE 201
Cdd:TIGR00231 132 SEFAKLNG----------EPIIPLSAETGKNIDS 155
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
70-199 |
6.88e-04 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 41.92 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 70 GITIDISLWKFETSKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAgtgefeagisKNG---QTREHILLSYTLGVK 146
Cdd:COG0532 36 GITQHIGAYQVETNGGKITFLDTPGHEAFTAMRARGAQVTDIVILVVAA----------DDGvmpQTIEAINHAKAAGVP 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 167385576 147 qMIVGVNKMDAIQYKQERyeeIKKEISAFlkktGYNPD----KIPFVPISGFQGDNM 199
Cdd:COG0532 106 -IIVAINKIDKPGANPDR---VKQELAEH----GLVPEewggDTIFVPVSAKTGEGI 154
|
|
| CysN_NoDQ_III |
cd04095 |
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of ... |
325-425 |
2.89e-03 |
|
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: 37.03 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 325 DFTAQVIVMNH-PGQIRKGYtpVLDCHTSHIACKFEELLSKIDRRTGKSMEGgePEYIKNgDSALVKIVPTKPLCVEEFA 403
Cdd:cd04095 5 QFEATLVWMDEkPLQPGRRY--LLKHGTRTVRARVTEIDYRIDVNTLEREPA--DTLALN-DIGRVTLRLAEPLAFDPYA 79
|
90 100
....*....|....*....|....
gi 167385576 404 KFPPLGRFAV--RDMKQTVAVGVV 425
Cdd:cd04095 80 ENRATGSFILidRLTNATVAAGMI 103
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
12-98 |
4.85e-03 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 39.35 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 12 VIGHVDSGKSTTTGHLIYKCGGIDQRTIEKfekesaemGKGSFKYA---WvldnLKAERERGITIDISLWKFETSKYYFT 88
Cdd:PRK00741 15 IISHPDAGKTTLTEKLLLFGGAIQEAGTVK--------GRKSGRHAtsdW----MEMEKQRGISVTSSVMQFPYRDCLIN 82
|
90
....*....|
gi 167385576 89 IIDAPGHRDF 98
Cdd:PRK00741 83 LLDTPGHEDF 92
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
326-425 |
6.82e-03 |
|
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: 35.67 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167385576 326 FTAQVIVMN------HPGqIRKGYTPVLDCHTSHIACKFEELLSKidrrtgksmeggepEYIKNGDSALVKIVPTKPLCV 399
Cdd:cd03706 6 FEAQVYLLSkeeggrHKP-FTSGFQQQMFSKTWDCACRIDLPEGK--------------EMVMPGEDTSVKLTLLKPMVL 70
|
90 100
....*....|....*....|....*..
gi 167385576 400 EEfakfpplG-RFAVRDMKQTVAVGVV 425
Cdd:cd03706 71 EK-------GqRFTLREGGRTIGTGVV 90
|
|
| |
