|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
14-465 |
0e+00 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 854.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 14 LAKQDLDKVGVDNLNPLTEEVISRQATINIGTIGHVAHGKSTLVKAFSGVHTVKFKRELERNITIKLGYANAKIYRCsnQ 93
Cdd:PTZ00327 8 LAKQDLSKLDLDKLTPLTPEVISRQATINIGTIGHVAHGKSTVVKALSGVKTVRFKREKVRNITIKLGYANAKIYKC--P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 94 ECPRPGCYRSAGSSTPDRFPCEraGCGGEFTCVRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPCPQPQTSEHL 173
Cdd:PTZ00327 86 KCPRPTCYQSYGSSKPDNPPCP--GCGHKMTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQPQTSEHL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 174 AAVEIMQLNHLMILQNKVDIIKESQARENYEQIAGFVQGTVAENAPVIPISAQLKYNVDLVCEYLCKKIPVPVRDFKSPA 253
Cdd:PTZ00327 164 AAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKRDLTSPP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 254 RLIIIRSFDVNKPGSEVENLKGGVAGGTLTKGILRVGQEIEVRPGIVSKTATGQLQCRPIFSRIDSLFAEKNQLEYAVPG 333
Cdd:PTZ00327 244 RMIVIRSFDVNKPGEDIENLKGGVAGGSILQGVLKVGDEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNELQYAVPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 334 GLIGVGTKIDPTLCRGDRLVGHILGAVGTLPDIFIEIEISFYLLRRLLGVRTEGKKKGAKVQKLVKEETLLVNIGSLSTG 413
Cdd:PTZ00327 324 GLIGVGTTIDPTLTRADRLVGQVLGYPGKLPEVYAEIEIQYYLLRRLLGVKSQDGKKATKVAKLKKGESLMINIGSTTTG 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 17509919 414 GRVTAVKGDA-AKIRLNDPICTEVGEKIAMSRRFEKSWRLIGWGTIRKGQTVE 465
Cdd:PTZ00327 404 GRVVGIKDDGiAKLELTTPVCTSVGEKIALSRRVDKHWRLIGWGTIRKGVPVK 456
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
37-459 |
0e+00 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 525.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 37 RQATINIGTIGHVAHGKSTLVKAFSGVHTVKFKRELERNITIKLGYANAKIYRCSNqeCPRPGCYRSAGSstpdrfpCER 116
Cdd:PRK04000 6 VQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATIRKCPD--CEEPEAYTTEPK-------CPN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 117 agCGGEFTCVRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPCPQPQTSEHLAAVEIMQLNHLMILQNKVDIIKE 196
Cdd:PRK04000 77 --CGSETELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 197 SQARENYEQIAGFVQGTVAENAPVIPISAQLKYNVDLVCEYLCKKIPVPVRDFKSPARLIIIRSFDVNKPGSEVENLKGG 276
Cdd:PRK04000 155 ERALENYEQIKEFVKGTVAENAPIIPVSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTPPEKLKGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 277 VAGGTLTKGILRVGQEIEVRPGIVSKTaTGQLQCRPIFSRIDSLFAEKNQLEYAVPGGLIGVGTKIDPTLCRGDRLVGHI 356
Cdd:PRK04000 235 VIGGSLIQGVLKVGDEIEIRPGIKVEE-GGKTKWEPITTKIVSLRAGGEKVEEARPGGLVGVGTKLDPSLTKADALAGSV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 357 LGAVGTLPDIFIEIEISFYLLRRLLGVrtegkKKGAKVQKLVKEETLLVNIGSLSTGGRVTAVKGDAAKIRLNDPICTEV 436
Cdd:PRK04000 314 AGKPGTLPPVWESLTIEVHLLERVVGT-----KEELKVEPIKTGEPLMLNVGTATTVGVVTSARKDEAEVKLKRPVCAEE 388
|
410 420
....*....|....*....|...
gi 17509919 437 GEKIAMSRRFEKSWRLIGWGTIR 459
Cdd:PRK04000 389 GDRVAISRRVGGRWRLIGYGIIK 411
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
37-459 |
4.32e-180 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 509.76 E-value: 4.32e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 37 RQATINIGTIGHVAHGKSTLVKAFSGVHTVKFKRELERNITIKLGYANAKIYRCSNqeCPRPGCYrsagSSTPDrfpCER 116
Cdd:COG5257 2 KQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATFYKCPN--CEPPEAY----TTEPK---CPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 117 agCGGEFTCVRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPCPQPQTSEHLAAVEIMQLNHLMILQNKVDIIKE 196
Cdd:COG5257 73 --CGSETELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 197 SQARENYEQIAGFVQGTVAENAPVIPISAQLKYNVDLVCEYLCKKIPVPVRDFKSPARLIIIRSFDVNKPGSEVENLKGG 276
Cdd:COG5257 151 ERALENYEQIKEFVKGTVAENAPIIPVSAQHKVNIDALIEAIEEEIPTPERDLSKPPRMLVARSFDVNKPGTPPKDLKGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 277 VAGGTLTKGILRVGQEIEVRPGIvSKTATGQLQCRPIFSRIDSLFAEKNQLEYAVPGGLIGVGTKIDPTLCRGDRLVGHI 356
Cdd:COG5257 231 VIGGSLIQGVLKVGDEIEIRPGI-KVEKGGKTKYEPITTTVVSLRAGGEEVEEAKPGGLVAVGTKLDPSLTKSDSLVGSV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 357 LGAVGTLPDIFIEIEISFYLLRRLLGVRTEgkkkgAKVQKLVKEETLLVNIGSLSTGGRVTAVKGDAAKIRLNDPICTEV 436
Cdd:COG5257 310 AGKPGTLPPVLDSLTMEVHLLERVVGTKEE-----VKVEPIKTGEPLMLNVGTATTVGVVTSARKDEIEVKLKRPVCAEK 384
|
410 420
....*....|....*....|...
gi 17509919 437 GEKIAMSRRFEKSWRLIGWGTIR 459
Cdd:COG5257 385 GSRVAISRRIGGRWRLIGWGIIK 407
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
37-459 |
1.82e-173 |
|
translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Pssm-ID: 274720 [Multi-domain] Cd Length: 406 Bit Score: 493.03 E-value: 1.82e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 37 RQATINIGTIGHVAHGKSTLVKAFSGVHTVKFKRELERNITIKLGYANAKIYRCsnQECPRPGCYRSAGSstpdrfpCER 116
Cdd:TIGR03680 1 RQPEVNIGMVGHVDHGKTTLTKALTGVWTDTHSEELKRGISIRLGYADAEIYKC--PECDGPECYTTEPV-------CPN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 117 agCGGEFTCVRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPCPQPQTSEHLAAVEIMQLNHLMILQNKVDIIKE 196
Cdd:TIGR03680 72 --CGSETELLRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPCPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 197 SQARENYEQIAGFVQGTVAENAPVIPISAQLKYNVDLVCEYLCKKIPVPVRDFKSPARLIIIRSFDVNKPGSEVENLKGG 276
Cdd:TIGR03680 150 EKALENYEEIKEFVKGTVAENAPIIPVSALHNANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNKPGTPPEKLKGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 277 VAGGTLTKGILRVGQEIEVRPGIvSKTATGQLQCRPIFSRIDSLFAEKNQLEYAVPGGLIGVGTKIDPTLCRGDRLVGHI 356
Cdd:TIGR03680 230 VIGGSLIQGKLKVGDEIEIRPGI-KVEKGGKTKWEPIYTEITSLRAGGYKVEEARPGGLVGVGTKLDPALTKADALAGQV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 357 LGAVGTLPDIFIEIEISFYLLRRLLGVRTEgkkkgAKVQKLVKEETLLVNIGSLSTGGRVTAVKGDAAKIRLNDPICTEV 436
Cdd:TIGR03680 309 VGKPGTLPPVWESLELEVHLLERVVGTEEE-----LKVEPIKTGEVLMLNVGTATTVGVVTSARKDEIEVKLKRPVCAEE 383
|
410 420
....*....|....*....|...
gi 17509919 437 GEKIAMSRRFEKSWRLIGWGTIR 459
Cdd:TIGR03680 384 GDRVAISRRVGGRWRLIGYGIIK 406
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
41-247 |
1.31e-138 |
|
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: 396.25 E-value: 1.31e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKAFSGVHTVKFKRELERNITIKLGYANAKIYRCSNQECPRPGcyrsagsstpDRFPCERAGCG 120
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWTVRHKEELKRNITIKLGYANAKIYKCPNCGCPRPY----------DTPECECPGCG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 121 GEFTCVRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPCPQPQTSEHLAAVEIMQLNHLMILQNKVDIIKESQAR 200
Cdd:cd01888 71 GETKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17509919 201 ENYEQIAGFVQGTVAENAPVIPISAQLKYNVDLVCEYLCKKIPVPVR 247
Cdd:cd01888 151 ENYEQIKEFVKGTIAENAPIIPISAQLKYNIDVLCEYIVKKIPTPPR 197
|
|
| eIF2_gamma_II |
cd03688 |
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily ... |
248-361 |
1.10e-63 |
|
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily represents domain II of the gamma subunit of eukaryotic translation initiation factor 2 (eIF2-gamma) found in eukaryota and archaea. eIF2 is a G protein that delivers the methionyl initiator tRNA to the small ribosomal subunit and releases it upon GTP hydrolysis after the recognition of the initiation codon. eIF2 is composed of three subunits, alpha, beta and gamma. Subunit gamma shows strongest conservation, and it confers both tRNA binding and GTP/GDP binding.
Pssm-ID: 293889 [Multi-domain] Cd Length: 113 Bit Score: 201.64 E-value: 1.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 248 DFKSPARLIIIRSFDVNKPGSEVENLKGGVAGGTLTKGILRVGQEIEVRPGIVSKTaTGQLQCRPIFSRIDSLFAEKNQL 327
Cdd:cd03688 1 DLDKPPRMIVIRSFDVNKPGTEVDDLKGGVIGGSLIQGVLKVGDEIEIRPGIVVKK-GGKTTCRPIFTKIVSLFAEGNDL 79
|
90 100 110
....*....|....*....|....*....|....
gi 17509919 328 EYAVPGGLIGVGTKIDPTLCRGDRLVGHILGAVG 361
Cdd:cd03688 80 EEAVPGGLIGVGTKLDPTLTKADRLVGQVVGEPG 113
|
|
| eIF2_gamma_III |
cd15490 |
Domain III of eukaryotic initiation factor eIF2 gamma; This family represents the C-terminal ... |
364-458 |
2.10e-44 |
|
Domain III of eukaryotic initiation factor eIF2 gamma; This family represents the C-terminal domain of the gamma subunit of eukaryotic translation initiation factor 2 (eIF2-gamma) found in eukaryotes and archaea. eIF2 is a G protein that delivers the methionyl initiator tRNA to the small ribosomal subunit and releases it upon GTP hydrolysis after the recognition of the initiation codon. eIF2 is composed three subunits, alpha, beta and gamma. Subunit gamma shows strongest conservation, and it confers both tRNA binding and GTP/GDP binding.
Pssm-ID: 294011 [Multi-domain] Cd Length: 90 Bit Score: 150.36 E-value: 2.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 364 PDIFIEIEISFYLLRRLLGVRTEgkkkgAKVQKLVKEETLLVNIGSLSTGGRVTAVKGDAAKIRLNDPICTEVGEKIAMS 443
Cdd:cd15490 1 PPVYTELEIEYHLLERVVGVKEE-----IKVEKIKKGEVLMLNIGSATTGGVVTSVKKDEAEVELKRPVCAEIGERVAIS 75
|
90
....*....|....*
gi 17509919 444 RRFEKSWRLIGWGTI 458
Cdd:cd15490 76 RRIDGRWRLIGWGII 90
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
41-440 |
3.95e-43 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 160.85 E-value: 3.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKAFSGVHTVKFKRELERNITIKLGYANAKIyrcsnqecprpgcyrsagsstPDrfpceragcg 120
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGIDTDRLKEEKKRGITIDLGFAYLPL---------------------PD---------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 121 geftcVRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEHLAAVEIMQLNHLMILQNKVDIIKESQAR 200
Cdd:COG3276 50 -----GRRLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAADEG-VMPQTREHLAILDLLGIKRGIVVLTKADLVDEEWLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 201 ENYEQIAGFVQGTVAENAPVIPISAQLKYNVDLVCEYLCKKI-PVPVRDFKSPARLIIIRSFdvnkpgseveNLKG-G-V 277
Cdd:COG3276 124 LVEEEIRELLAGTFLEDAPIVPVSAVTGEGIDELRAALDALAaAVPARDADGPFRLPIDRVF----------SIKGfGtV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 278 AGGTLTKGILRVGQEIEVRPGivsktatgqlqcrPIFSRIDSLFAEKNQLEYAVPG-----GLIGVGTKidpTLCRGDrl 352
Cdd:COG3276 194 VTGTLLSGTVRVGDELELLPS-------------GKPVRVRGIQVHGQPVEEAYAGqrvalNLAGVEKE---EIERGD-- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 353 vghILGAVGTLPdIFIEIEISFYLL---RRLLGVRTEgkkkgakvqklvkeetLLVNIGSLSTGGRVTAVKGDA------ 423
Cdd:COG3276 256 ---VLAAPGALR-PTDRIDVRLRLLpsaPRPLKHWQR----------------VHLHHGTAEVLARVVLLDREElapgee 315
|
410
....*....|....*....
gi 17509919 424 --AKIRLNDPICTEVGEKI 440
Cdd:COG3276 316 alAQLRLEEPLVAARGDRF 334
|
|
| eIF2_C |
pfam09173 |
Initiation factor eIF2 gamma, C terminal; Members of this family, which are found in the ... |
368-458 |
2.60e-39 |
|
Initiation factor eIF2 gamma, C terminal; Members of this family, which are found in the initiation factors eIF2 and EF-Tu, adopt a structure consisting of a beta barrel with Greek key topology. They are required for formation of the ternary complex with GTP and initiator tRNA.
Pssm-ID: 462703 [Multi-domain] Cd Length: 86 Bit Score: 136.87 E-value: 2.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 368 IEIEISFYLLRRLLGVRTEgkkkgAKVQKLVKEETLLVNIGSLSTGGRVTAVKGDAAKIRLNDPICTEVGEKIAMSRRFE 447
Cdd:pfam09173 1 TELEIEYHLLERVVGVKEE-----KKVEPIKKGEVLMLNVGTATTGGVVTSVKKDEAEVELKKPVCAEKGERVAISRRIG 75
|
90
....*....|.
gi 17509919 448 KSWRLIGWGTI 458
Cdd:pfam09173 76 GRWRLIGWGII 86
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
43-225 |
4.08e-33 |
|
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: 123.10 E-value: 4.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 43 IGTIGHVAHGKSTLVKAFSGVHTVKFKRELERNITIKLGYANAkiyrcsnqecprpgcyrsagsstpdrfpceragcggE 122
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGIETDRLPEEKKRGITIDLGFAYL------------------------------------D 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 123 FTCVRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPCpQPQTSEHLAAVEIMQLNHLMILQNKVDIIKESQAREN 202
Cdd:cd04171 46 LPDGKRLGFIDVPGHEKFVKNMLAGAGGIDAVLLVVAADEGI-MPQTREHLEILELLGIKKGLVVLTKADLVDEDRLELV 124
|
170 180
....*....|....*....|...
gi 17509919 203 YEQIAGFVQGTVAENAPVIPISA 225
Cdd:cd04171 125 EEEILELLAGTFLADAPIFPVSS 147
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
41-440 |
1.08e-28 |
|
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: 119.21 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKAFSGVHTVKFKRELERNITIKLGYANakiyrcsnqecprpgcyrsagsstpdrFPCERagcg 120
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAADRLPEEKKRGMTIDLGFAY---------------------------FPLPD---- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 121 geftcvRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEHLAAVEIMQLNHLMILQNKVDIIKESQAR 200
Cdd:TIGR00475 50 ------YRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDADEG-VMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 201 ENYEQIAGFVQGTV-AENAPVIPISAQLKYNVDLVCEYLcKKIP--VPVRDFKSPARLIIIRSFDVNKPGSevenlkggV 277
Cdd:TIGR00475 123 RTEMFMKQILNSYIfLKNAKIFKTSAKTGQGIGELKKEL-KNLLesLDIKRIQKPLRMAIDRAFKVKGAGT--------V 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 278 AGGTLTKGILRVGQEIEVRPgivsktaTGQLqcrpifSRIDSLFAEKNQLEYAVPGGLIGVG-TKIDPT-LCRGdrlvgh 355
Cdd:TIGR00475 194 VTGTAFSGEVKVGDNLRLLP-------INHE------VRVKAIQAQNQDVEIAYAGQRIALNlMDVEPEsLKRG------ 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 356 ilgavgtlpdiFIEIEISFYLLRRLLGVRTEGK-KKGAKVQklvkeetllVNIGSLSTGGRVTAVKGDAAKIRLNDPICT 434
Cdd:TIGR00475 255 -----------LLILTPEDPKLRVVVKFIAEVPlLELQPYH---------IAHGMSVTTGKISLLDKGIALLTLDAPLIL 314
|
....*.
gi 17509919 435 EVGEKI 440
Cdd:TIGR00475 315 AKGDKL 320
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
42-245 |
2.77e-28 |
|
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: 110.46 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 42 NIGTIGHVAHGKSTLVK-------AFSGVHTVKF------KRELERNITIKLGYANAKiyrcsnqecprpgcyrsagssT 108
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGsllyqtgAIDRRGTRKEtfldtlKEERERGITIKTGVVEFE---------------------W 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 109 PDRfpceragcggeftcvrHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEHLAAVEIMQLnHLMILQ 188
Cdd:cd00881 60 PKR----------------RINFIDTPGHEDFSKETVRGLAQADGALLVVDANEG-VEPQTREHLNIALAGGL-PIIVAV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17509919 189 NKVDIIKESQARENYEQIAGFVQGTVA-----ENAPVIPISAQLKYNVDLVCEYLCKKIPVP 245
Cdd:cd00881 122 NKIDRVGEEDFDEVLREIKELLKLIGFtflkgKDVPIIPISALTGEGIEELLDAIVEHLPPP 183
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
41-225 |
5.86e-24 |
|
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: 98.59 E-value: 5.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKAFSGVHTV----KFKRELERNITIKLGYAnakiyrcsnqecprpGCYRSAGSSTPDRFpcer 116
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIASTaafdKNPQSQERGITLDLGFS---------------SFEVDKPKHLEDNE---- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 117 agcGGEFTCVRhVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEHLAAVEIMQlNHLMILQNKVDIIKE 196
Cdd:cd01889 62 ---NPQIENYQ-ITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-IQTQTAECLVIGELLC-KPLIVVLNKIDLIPE 135
|
170 180 190
....*....|....*....|....*....|...
gi 17509919 197 SQARENYEQIAGFVQGTVA----ENAPVIPISA 225
Cdd:cd01889 136 EERKRKIEKMKKRLQKTLEktrlKDSPIIPVSA 168
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
41-306 |
2.12e-21 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 95.78 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKA-------FSGVHTVKFKR------ELERNITIKLG---YANAKiyrcsnqecprpgcyrsa 104
Cdd:PRK12736 13 VNIGTIGHVDHGKTTLTAAitkvlaeRGLNQAKDYDSidaapeEKERGITINTAhveYETEK------------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 105 gsstpdrfpceragcggeftcvRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEHLAAVEIMQLNHL 184
Cdd:PRK12736 75 ----------------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVPYL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 185 MILQNKVDIIKEsqarenyEQIAGFVQGTVAE----------NAPVIPISA------------QLKYNVDLVCEYlckkI 242
Cdd:PRK12736 132 VVFLNKVDLVDD-------EELLELVEMEVREllseydfpgdDIPVIRGSAlkalegdpkwedAIMELMDAVDEY----I 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17509919 243 PVPVRDFKSPARLIIIRSFDVNKpgsevenlKGGVAGGTLTKGILRVGQEIEV---RPgIVSKTATG 306
Cdd:PRK12736 201 PTPERDTDKPFLMPVEDVFTITG--------RGTVVTGRVERGTVKVGDEVEIvgiKE-TQKTVVTG 258
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
41-295 |
5.99e-21 |
|
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: 94.46 E-value: 5.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKAFSGVHTvkfkrelernitiKLGYANAKIYrcsnqecprpgcyrsagsSTPDRFPCERA--- 117
Cdd:TIGR00485 13 VNVGTIGHVDHGKTTLTAAITTVLA-------------KEGGAAARAY------------------DQIDNAPEEKArgi 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 118 ---GCGGEF-TCVRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEHLAAVEIMQLNHLMILQNKVDI 193
Cdd:TIGR00485 62 tinTAHVEYeTETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGVPYIVVFLNKCDM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 194 IKEsqarenyEQIAGFVQGTVAE----------NAPVIPISAQLKYN------------VDLVCEYlckkIPVPVRDFKS 251
Cdd:TIGR00485 141 VDD-------EELLELVEMEVREllsqydfpgdDTPIIRGSALKALEgdaeweakilelMDAVDEY----IPTPEREIDK 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 17509919 252 PARLIIIRSFDVNKpgsevenlKGGVAGGTLTKGILRVGQEIEV 295
Cdd:TIGR00485 210 PFLLPIEDVFSITG--------RGTVVTGRVERGIIKVGEEVEI 245
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
41-243 |
8.70e-21 |
|
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: 89.51 E-value: 8.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLV---------------KAFSGVHTV-KFKRELERNITIKLgyANAKIYrcsnqecprpgcyrsa 104
Cdd:pfam00009 4 RNIGIIGHVDHGKTTLTdrllyytgaiskrgeVKGEGEAGLdNLPEERERGITIKS--AAVSFE---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 105 gssTPDRfpceragcggeftcvrHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEHLAAVEIMQLNHL 184
Cdd:pfam00009 66 ---TKDY----------------LINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-VMPQTREHLRLARQLGVPII 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17509919 185 MILqNKVDIIKESQARENYEQIA---GFVQGTVAENAPVIPISAQLKYNVDLVCEYLCKKIP 243
Cdd:pfam00009 126 VFI-NKMDRVDGAELEEVVEEVSrelLEKYGEDGEFVPVVPGSALKGEGVQTLLDALDEYLP 186
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
41-295 |
8.34e-20 |
|
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: 90.98 E-value: 8.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKAFSGV----HTVKFK---------RELERNITIKLgyanakiyrcSNQEcprpgcYRSAGss 107
Cdd:COG0050 13 VNIGTIGHVDHGKTTLTAAITKVlakkGGAKAKaydqidkapEEKERGITINT----------SHVE------YETEK-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 108 tpdrfpceragcggeftcvRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEHLAAVEIMQLNHLMIL 187
Cdd:COG0050 75 -------------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 188 QNKVDIIK--------ESQARENYEQiagfvQGTVAENAPVIPISAQLKYNVDLVCEYlCKK-----------IPVPVRD 248
Cdd:COG0050 135 LNKCDMVDdeellelvEMEVRELLSK-----YGFPGDDTPIIRGSALKALEGDPDPEW-EKKilelmdavdsyIPEPERD 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17509919 249 FKSPARLiiirsfdvnkPgseVENL-----KGGVAGGTLTKGILRVGQEIEV 295
Cdd:COG0050 209 TDKPFLM----------P---VEDVfsitgRGTVVTGRVERGIIKVGDEVEI 247
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
41-460 |
1.71e-19 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 90.65 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKAFSGV-------HTVKFKR------ELERNITIklgyANAKI-YRCSNqecprpgcyrsags 106
Cdd:PLN03127 62 VNVGTIGHVDHGKTTLTAAITKVlaeegkaKAVAFDEidkapeEKARGITI----ATAHVeYETAK-------------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 107 stpdrfpceragcggeftcvRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEHLAAVEIMQLNHLMI 186
Cdd:PLN03127 124 --------------------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDG-PMPQTKEHILLARQVGVPSLVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 187 LQNKVDIIKESQARENYEQ------------------IAGFVQGTVAENAPVIPISAQLKYnVDLVCEYlckkIPVPVRD 248
Cdd:PLN03127 183 FLNKVDVVDDEELLELVEMelrellsfykfpgdeipiIRGSALSALQGTNDEIGKNAILKL-MDAVDEY----IPEPVRV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 249 FKSPARLIIIRSFDVNKpgsevenlKGGVAGGTLTKGILRVGQEIEVrpgivsktaTGQLQCRPIFSRIDSLFAEKNQLE 328
Cdd:PLN03127 258 LDKPFLMPIEDVFSIQG--------RGTVATGRVEQGTIKVGEEVEI---------VGLRPGGPLKTTVTGVEMFKKILD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 329 YAVPG---GLIGVGTKidptlcRGDRLVGHILGAVGTLpDIFIEIEISFYLLRRLLGVRTEGKKKGAKVQKLVKEE---- 401
Cdd:PLN03127 321 QGQAGdnvGLLLRGLK------REDVQRGQVICKPGSI-KTYKKFEAEIYVLTKDEGGRHTPFFSNYRPQFYLRTAdvtg 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17509919 402 --TLLVNIGSLSTGGRVTAVkgdaakIRLNDPICTEVGEKIAMsrrfEKSWRLIGWGTIRK 460
Cdd:PLN03127 394 kvELPEGVKMVMPGDNVTAV------FELISPVPLEPGQRFAL----REGGRTVGAGVVSK 444
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
41-301 |
4.46e-19 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 89.21 E-value: 4.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKAF---SGV---HTVK----------------------FKRELERNITIKLgyANAKIyrcsn 92
Cdd:PRK12317 7 LNLAVIGHVDHGKSTLVGRLlyeTGAideHIIEelreeakekgkesfkfawvmdrLKEERERGVTIDL--AHKKF----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 93 qecprpgcyrsagsSTPDRFpceragcggeFTcvrhvsFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEP-CPQPQTSE 171
Cdd:PRK12317 80 --------------ETDKYY----------FT------IVDCPGHRDFVKNMITGASQADAAVLVVAADDAgGVMPQTRE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 172 HLAAVEIMQLNHLMILQNKVDIIKESQARenYEQIAGFVQ------GTVAENAPVIPISAQLK------------YNVDL 233
Cdd:PRK12317 130 HVFLARTLGINQLIVAINKMDAVNYDEKR--YEEVKEEVSkllkmvGYKPDDIPFIPVSAFEGdnvvkksenmpwYNGPT 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 234 VCEYLcKKIPVPVRDFKSPARLiiirsfdvnkPGSEVENLK--GGVAGGTLTKGILRVGQEIEVRPGIVS 301
Cdd:PRK12317 208 LLEAL-DNLKPPEKPTDKPLRI----------PIQDVYSISgvGTVPVGRVETGVLKVGDKVVFMPAGVV 266
|
|
| tufA |
CHL00071 |
elongation factor Tu |
41-399 |
3.29e-18 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 86.16 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKAfsgvhtvkfkrelernITIKL---GYANAKIYrcsnqecprpgcyrsagsSTPDRFPCERA 117
Cdd:CHL00071 13 VNIGTIGHVDHGKTTLTAA----------------ITMTLaakGGAKAKKY------------------DEIDSAPEEKA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 118 -GCG-----GEF-TCVRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEHLAAVEIMQLNHLMILQNK 190
Cdd:CHL00071 59 rGITintahVEYeTENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTKEHILLAKQVGVPNIVVFLNK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 191 VDIIKEsqarenyEQIAGFVQGTVAE----------NAPVIPISAQLK---------------------YN-VDLVCEYl 238
Cdd:CHL00071 138 EDQVDD-------EELLELVELEVREllskydfpgdDIPIVSGSALLAlealtenpkikrgenkwvdkiYNlMDAVDSY- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 239 ckkIPVPVRDFKSPARLIIIRSFDVnkPGsevenlKGGVAGGTLTKGILRVGQEIEVRPGIVSKTATgqlqcrpifsrID 318
Cdd:CHL00071 210 ---IPTPERDTDKPFLMAIEDVFSI--TG------RGTVATGRIERGTVKVGDTVEIVGLRETKTTT-----------VT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 319 SLFAEKNQLEYAVPGGLIGVgtkidptLCRG----DRLVGHILGAVGTLpDIFIEIEISFYLLRRLLGVRTEGKKKGAKV 394
Cdd:CHL00071 268 GLEMFQKTLDEGLAGDNVGI-------LLRGiqkeDIERGMVLAKPGTI-TPHTKFEAQVYILTKEEGGRHTPFFPGYRP 339
|
....*
gi 17509919 395 QKLVK 399
Cdd:CHL00071 340 QFYVR 344
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
41-295 |
7.28e-18 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 85.28 E-value: 7.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKAFSGVHTVKFK-------------RELERNITIKLgyanakiyrcSNQEcprpgcYRSAgss 107
Cdd:PRK12735 13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGgeakaydqidnapEEKARGITINT----------SHVE------YETA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 108 tpdrfpceragcggeftcVRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEHLAAVEIMQLNHLMIL 187
Cdd:PRK12735 74 ------------------NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 188 QNKVDIIKESQAREnyeqiagFVQGTVAE----------NAPVIPISAQLKYNVDLVCEYlCKK-----------IPVPV 246
Cdd:PRK12735 135 LNKCDMVDDEELLE-------LVEMEVREllskydfpgdDTPIIRGSALKALEGDDDEEW-EAKilelmdavdsyIPEPE 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17509919 247 RDFKSPARLIIIRSFDVNKpgsevenlKGGVAGGTLTKGILRVGQEIEV 295
Cdd:PRK12735 207 RAIDKPFLMPIEDVFSISG--------RGTVVTGRVERGIVKVGDEVEI 247
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
41-295 |
1.42e-17 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 85.05 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKAfsgvhtvkfkrelernITIKLGyanakiyrcsnqecprpgcyrSAGSSTPDRF------PC 114
Cdd:PLN03126 82 VNIGTIGHVDHGKTTLTAA----------------LTMALA---------------------SMGGSAPKKYdeidaaPE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 115 ERA-GCGGEFTCV------RHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEHLAAVEIMQLNHLMIL 187
Cdd:PLN03126 125 ERArGITINTATVeyetenRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPNMVVF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 188 QNKVDIIKEsqarenyEQIAGFVQGTVAE----------NAPVIPISAQLKYN---------------VDLVCEYL---C 239
Cdd:PLN03126 204 LNKQDQVDD-------EELLELVELEVREllssyefpgdDIPIISGSALLALEalmenpnikrgdnkwVDKIYELMdavD 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17509919 240 KKIPVPVRDFKSPARLIIIRSFDVNKpgsevenlKGGVAGGTLTKGILRVGQEIEV 295
Cdd:PLN03126 277 SYIPIPQRQTDLPFLLAVEDVFSITG--------RGTVATGRVERGTVKVGETVDI 324
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
41-295 |
1.46e-17 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 84.08 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKAFSGVHTVKFK-------------RELERNITIKLgyanakiyrcSNQEcprpgcYRSAGss 107
Cdd:PRK00049 13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGaeakaydqidkapEEKARGITINT----------AHVE------YETEK-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 108 tpdrfpceragcggeftcvRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEHLAAVEIMQLNHLMIL 187
Cdd:PRK00049 75 -------------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 188 QNKVDIIK--------ESQARE---NYEqiagFvqgtVAENAPVIPISAQLKYNVDLVCEYlCKK-----------IPVP 245
Cdd:PRK00049 135 LNKCDMVDdeellelvEMEVREllsKYD----F----PGDDTPIIRGSALKALEGDDDEEW-EKKilelmdavdsyIPTP 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17509919 246 VRDFKSPARLIIIRSFDVnkPGsevenlKGGVAGGTLTKGILRVGQEIEV 295
Cdd:PRK00049 206 ERAIDKPFLMPIEDVFSI--SG------RGTVVTGRVERGIIKVGEEVEI 247
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
41-231 |
1.97e-17 |
|
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: 84.21 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKAF---SGV---HTVK----------------------FKRELERNITIKLgyANAKIyrcsn 92
Cdd:COG5256 8 LNLVVIGHVDHGKSTLVGRLlyeTGAideHIIEkyeeeaekkgkesfkfawvmdrLKEERERGVTIDL--AHKKF----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 93 qecprpgcyrsagsSTPDRFpceragcggeFTcvrhvsFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEH 172
Cdd:COG5256 81 --------------ETDKYY----------FT------IIDAPGHRDFVKNMITGASQADAAILVVSAKDG-VMGQTREH 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17509919 173 LAAVEIMQLNHLMILQNKVDIIKESQARenYEQIAGFVQ------GTVAENAPVIPISAQLKYNV 231
Cdd:COG5256 130 AFLARTLGINQLIVAVNKMDAVNYSEKR--YEEVKEEVSkllkmvGYKVDKIPFIPVSAWKGDNV 192
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
41-225 |
1.53e-16 |
|
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: 77.62 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLVKAfsgvhtvkfkrelernITI---KLGYANAKIYrcsnqecprpgcyrsagsSTPDRFPCERA 117
Cdd:cd01884 3 VNVGTIGHVDHGKTTLTAA----------------ITKvlaKKGGAKAKKY------------------DEIDKAPEEKA 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 118 ------GCGGEF-TCVRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPcPQPQTSEHLAAVEIMQLNHLMILQNK 190
Cdd:cd01884 49 rgitinTAHVEYeTANRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDG-PMPQTREHLLLARQVGVPYIVVFLNK 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17509919 191 VDIIK--------ESQARENYEQIaGFvQGtvaENAPVIPISA 225
Cdd:cd01884 128 ADMVDdeellelvEMEVRELLSKY-GF-DG---DDTPIVRGSA 165
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
43-290 |
1.70e-16 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 82.02 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 43 IGTIGHVAHGKSTLVKAFSGVHTVKFKRELERNITIKLGYAnakiYrcsnqeCPRP-Gcyrsagsstpdrfpceragcgg 121
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYA----Y------WPQPdG---------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 122 eftcvRHVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPCpQPQTSEHLAaveIMQLN---HLMILQNKVDIIKESQ 198
Cdd:PRK10512 51 -----RVLGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGV-MAQTREHLA---ILQLTgnpMLTVALTKADRVDEAR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 199 ARENYEQIagfvQGTVAE----NAPVIPISAQLKYNVDLVCEYLCK---KIPVPVRDFkspaRLIIIRSFDVNkpGSeve 271
Cdd:PRK10512 122 IAEVRRQV----KAVLREygfaEAKLFVTAATEGRGIDALREHLLQlpeREHAAQHRF----RLAIDRAFTVK--GA--- 188
|
250
....*....|....*....
gi 17509919 272 nlkGGVAGGTLTKGILRVG 290
Cdd:PRK10512 189 ---GLVVTGTALSGEVKVG 204
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
41-297 |
1.15e-08 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 57.25 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 41 INIGTIGHVAHGKSTLV---------------KAFSGVHtvkfKRELERNITIKLGYA-----NAKIYRCSNqecprpgc 100
Cdd:COG5258 123 IVVGVAGHVDHGKSTLVgtlvtgklddgnggtRSFLDVQ----PHEVERGLSADLSYAvygfdDDGPVRMKN-------- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 101 yrsagsstPDRfPCERAGCGGEftCVRHVSFVDCPGHDILMATMLNG--AAVMDAAFLLVAGNEPcPQPQTSEHLAAVEI 178
Cdd:COG5258 191 --------PLR-KTDRARVVEE--SDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDG-PTHTTREHLGILLA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 179 MQLNhLMILQNKVDIIKESQARENYEQIAGF---VQGTV--------AENA---------PVIPISAQLKYNVDLVCEYL 238
Cdd:COG5258 259 MDLP-VIVAITKIDKVDDERVEEVEREIENLlriVGRTPlevesrhdVDAAieeingrvvPILKTSAVTGEGLDLLDELF 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 17509919 239 cKKIPVPVRDFKSPARLIIIRSFDVnkpgSEVenlkGGVAGGTLTKGILRVGQEIEVRP 297
Cdd:COG5258 338 -ERLPKRATDEDEPFLMYIDRIYNV----TGV----GTVVSGTVKSGKVEAGDELLIGP 387
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
42-225 |
2.28e-08 |
|
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: 54.42 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 42 NIGTIGHVAHGKSTLVKAF---SGV---HTV-KFKR---------------------ELERNITIKLGYAnakiyrcsnq 93
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLlykLGGvdkRTIeKYEKeakemgkesfkyawvldklkeERERGVTIDVGLA---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 94 ecprpgcyrsagsstpdRFPCERagcggeftcvRHVSFVDCPGHDILMATMLNGAAVMDAAFLLV--------AGNEPcp 165
Cdd:cd01883 71 -----------------KFETEK----------YRFTIIDAPGHRDFVKNMITGASQADVAVLVVsarkgefeAGFEK-- 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17509919 166 QPQTSEHLAAVEIMQLNHLMILQNKVDIIKE--SQARenYEQI----AGFVQ--GTVAENAPVIPISA 225
Cdd:cd01883 122 GGQTREHALLARTLGVKQLIVAVNKMDDVTVnwSQER--YDEIkkkvSPFLKkvGYNPKDVPFIPISG 187
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
45-231 |
3.97e-08 |
|
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: 53.34 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 45 TIGHVAHGKSTLV-------------KAFSGVHTVKFKR----------------ELERNITIKLGYanakIYrcsnqec 95
Cdd:cd04166 4 TCGSVDDGKSTLIgrllydsksifedQLAALERSKSSGTqgekldlallvdglqaEREQGITIDVAY----RY------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 96 prpgcyrsagSSTPDRfpceragcggeftcvrhvSFV--DCPGHDILMATMLNGAAVMDAAFLLVAGNEPCpQPQTSEHL 173
Cdd:cd04166 73 ----------FSTPKR------------------KFIiaDTPGHEQYTRNMVTGASTADLAILLVDARKGV-LEQTRRHS 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17509919 174 AAVEIMQLNHLMILQNKVDIIKESQARenYEQIAG----FVQGTVAENAPVIPISAQLKYNV 231
Cdd:cd04166 124 YIASLLGIRHVVVAVNKMDLVDYDEEV--FEEIKAdylaFAASLGIEDITFIPISALEGDNV 183
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
25-332 |
5.25e-08 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 55.22 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 25 DNLNPLTEEVISRQATINIgtIGHVAHGKSTLVKAfsgVHTVKFKRELERNITIKLG-YANAKIYRCSNQEcprpgcyrs 103
Cdd:CHL00189 231 DNTSAFTENSINRPPIVTI--LGHVDHGKTTLLDK---IRKTQIAQKEAGGITQKIGaYEVEFEYKDENQK--------- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 104 agsstpdrfpceragcggeftcvrhVSFVDCPGHDILMATMLNGAAVMDAAFLLVAGNEPCpQPQTSEHLAAVEIMQLNh 183
Cdd:CHL00189 297 -------------------------IVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGV-KPQTIEAINYIQAANVP- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 184 LMILQNKVD-----IIKESQARENYEQIAGFVQGTVaenaPVIPISAQLKYNVDLVCEYLC--------KKIPvpvrdfK 250
Cdd:CHL00189 350 IIVAINKIDkananTERIKQQLAKYNLIPEKWGGDT----PMIPISASQGTNIDKLLETILllaeiedlKADP------T 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 251 SPARLIIIRSFdvnkpgseVENLKGGVAGGTLTKGILRVGqEIevrpgIVSKTATGQlqcrpIFSRIDSLfaeKNQLEYA 330
Cdd:CHL00189 420 QLAQGIILEAH--------LDKTKGPVATILVQNGTLHIG-DI-----IVIGTSYAK-----IRGMINSL---GNKINLA 477
|
..
gi 17509919 331 VP 332
Cdd:CHL00189 478 TP 479
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
275-358 |
7.84e-08 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 49.19 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 275 GGVAGGTLTKGILRVGQEIEVRPGIVSKTatgqlqcrPIFSRIDSLFAEKNQLEYAVPGGLIGVGTKIDPtlcRGDRLVG 354
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKK--------KIVTRVTSLLMFHAPLREAVAGDNAGLILAGVG---LEDIRVG 69
|
....
gi 17509919 355 HILG 358
Cdd:pfam03144 70 DTLT 73
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
272-353 |
1.07e-06 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 46.49 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 272 NLKGGVAGGTLTKGILRVGQEIEVRPGivsktatgqlqcrPIFSRIDSLFAEKNQLEYAVPGGLIGVGTKIDPTLCRGDR 351
Cdd:cd01342 12 PGRGRVAGGRVESGTLKVGDEIRILPK-------------GITGRVTSIERFHEEVDEAKAGDIVGIGILGVKDILTGDT 78
|
..
gi 17509919 352 LV 353
Cdd:cd01342 79 LT 80
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
46-240 |
4.14e-03 |
|
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: 37.82 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 46 IGHVAHGKSTLVKAFSGvhtvkfkreleRNITIKLgyanakiyrcsnqecPRPGCyrsagSSTPDRFPCERAGCGGEFTc 125
Cdd:cd00882 3 VGRGGVGKSSLLNALLG-----------GEVGEVS---------------DVPGT-----TRDPDVYVKELDKGKVKLV- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509919 126 vrhvsFVDCPGHD--------ILMATMLNGAavmDAAFLLVAGNEPcpqpQTSEHLAAVEIMQL---NHLMIL-QNKVDI 193
Cdd:cd00882 51 -----LVDTPGLDefgglgreELARLLLRGA---DLILLVVDSTDR----ESEEDAKLLILRRLrkeGIPIILvGNKIDL 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17509919 194 IKESQARENYEQIAGFVQgtvaENAPVIPISAQLKYNVDLVCEYLCK 240
Cdd:cd00882 119 LEEREVEELLRLEELAKI----LGVPVFEVSAKTGEGVDELFEKLIE 161
|
|
| |
