|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
3-410 |
0e+00 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 832.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 3 EKRKSRQAEVNIGMVGHVDHGKTTLTKALTGVWTDTHSEELRRGITIKIGFADAEIRRCPNCG---RYSTSPVCPYCGHE 79
Cdd:PRK04000 1 MMWEKVQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATIRKCPDCEepeAYTTEPKCPNCGSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 80 TEFVRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPCPRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKALEN 159
Cdd:PRK04000 81 TELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSKERALEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 160 YRQIKEFIEGTVAENAPIIPISALHGANIDVLVKAIEDFIPTPKRDPNKPPKMLVLRSFDVNKPGTPPEKLVGGVLGGSI 239
Cdd:PRK04000 161 YEQIKEFVKGTVAENAPIIPVSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTPPEKLKGGVIGGSL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 240 VQGKLKVGDEIEIRPGVPYEEHGRIKYEPITTEIVSLQAGGQFVEEAYPGGLVGVGTKLDPYLTKGDLMAGNVVGKPGKL 319
Cdd:PRK04000 241 IQGVLKVGDEIEIRPGIKVEEGGKTKWEPITTKIVSLRAGGEKVEEARPGGLVGVGTKLDPSLTKADALAGSVAGKPGTL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 320 PPVWDSLRLEVHLLERVVGTEQELKVEPIKRKEVLLLNVGTARTMGLVTGLGKDEIEVKLQIPVCAEPGDRVAISRQIGS 399
Cdd:PRK04000 321 PPVWESLTIEVHLLERVVGTKEELKVEPIKTGEPLMLNVGTATTVGVVTSARKDEAEVKLKRPVCAEEGDRVAISRRVGG 400
|
410
....*....|.
gi 499169315 400 RWRLIGYGIIK 410
Cdd:PRK04000 401 RWRLIGYGIIK 411
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
8-410 |
0e+00 |
|
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: 802.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 8 RQAEVNIGMVGHVDHGKTTLTKALTGVWTDTHSEELRRGITIKIGFADAEIRRCPNCG---RYSTSPVCPYCGHETEFVR 84
Cdd:TIGR03680 1 RQPEVNIGMVGHVDHGKTTLTKALTGVWTDTHSEELKRGISIRLGYADAEIYKCPECDgpeCYTTEPVCPNCGSETELLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 85 RVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPCPRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKALENYRQIK 164
Cdd:TIGR03680 81 RVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPCPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSKEKALENYEEIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 165 EFIEGTVAENAPIIPISALHGANIDVLVKAIEDFIPTPKRDPNKPPKMLVLRSFDVNKPGTPPEKLVGGVLGGSIVQGKL 244
Cdd:TIGR03680 161 EFVKGTVAENAPIIPVSALHNANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNKPGTPPEKLKGGVIGGSLIQGKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 245 KVGDEIEIRPGVPYEEHGRIKYEPITTEIVSLQAGGQFVEEAYPGGLVGVGTKLDPYLTKGDLMAGNVVGKPGKLPPVWD 324
Cdd:TIGR03680 241 KVGDEIEIRPGIKVEKGGKTKWEPIYTEITSLRAGGYKVEEARPGGLVGVGTKLDPALTKADALAGQVVGKPGTLPPVWE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 325 SLRLEVHLLERVVGTEQELKVEPIKRKEVLLLNVGTARTMGLVTGLGKDEIEVKLQIPVCAEPGDRVAISRQIGSRWRLI 404
Cdd:TIGR03680 321 SLELEVHLLERVVGTEEELKVEPIKTGEVLMLNVGTATTVGVVTSARKDEIEVKLKRPVCAEEGDRVAISRRVGGRWRLI 400
|
....*.
gi 499169315 405 GYGIIK 410
Cdd:TIGR03680 401 GYGIIK 406
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-411 |
0e+00 |
|
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: 793.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 8 RQAEVNIGMVGHVDHGKTTLTKALTGVWTDTHSEELRRGITIKIGFADAEIRRCPNCG---RYSTSPVCPYCGHETEFVR 84
Cdd:COG5257 2 KQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATFYKCPNCEppeAYTTEPKCPNCGSETELLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 85 RVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPCPRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKALENYRQIK 164
Cdd:COG5257 82 RVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSKERALENYEQIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 165 EFIEGTVAENAPIIPISALHGANIDVLVKAIEDFIPTPKRDPNKPPKMLVLRSFDVNKPGTPPEKLVGGVLGGSIVQGKL 244
Cdd:COG5257 162 EFVKGTVAENAPIIPVSAQHKVNIDALIEAIEEEIPTPERDLSKPPRMLVARSFDVNKPGTPPKDLKGGVIGGSLIQGVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 245 KVGDEIEIRPGVPYEEHGRIKYEPITTEIVSLQAGGQFVEEAYPGGLVGVGTKLDPYLTKGDLMAGNVVGKPGKLPPVWD 324
Cdd:COG5257 242 KVGDEIEIRPGIKVEKGGKTKYEPITTTVVSLRAGGEEVEEAKPGGLVAVGTKLDPSLTKSDSLVGSVAGKPGTLPPVLD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 325 SLRLEVHLLERVVGTEQELKVEPIKRKEVLLLNVGTARTMGLVTGLGKDEIEVKLQIPVCAEPGDRVAISRQIGSRWRLI 404
Cdd:COG5257 322 SLTMEVHLLERVVGTKEEVKVEPIKTGEPLMLNVGTATTVGVVTSARKDEIEVKLKRPVCAEKGSRVAISRRIGGRWRLI 401
|
....*..
gi 499169315 405 GYGIIKE 411
Cdd:COG5257 402 GWGIIKE 408
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
7-410 |
0e+00 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 515.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 7 SRQAEVNIGMVGHVDHGKTTLTKALTGVWTDTHSEELRRGITIKIGFADAEIRRCPNCGR------YSTS----PVCPYC 76
Cdd:PTZ00327 30 SRQATINIGTIGHVAHGKSTVVKALSGVKTVRFKREKVRNITIKLGYANAKIYKCPKCPRptcyqsYGSSkpdnPPCPGC 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 77 GHETEFVRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPCPRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKA 156
Cdd:PTZ00327 110 GHKMTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 157 LENYRQIKEFIEGTVAENAPIIPISALHGANIDVLVKAIEDFIPTPKRDPNKPPKMLVLRSFDVNKPGTPPEKLVGGVLG 236
Cdd:PTZ00327 190 QDQYEEIRNFVKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKRDLTSPPRMIVIRSFDVNKPGEDIENLKGGVAG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 237 GSIVQGKLKVGDEIEIRPG-VPYEEHGRIKYEPITTEIVSLQAGGQFVEEAYPGGLVGVGTKLDPYLTKGDLMAGNVVGK 315
Cdd:PTZ00327 270 GSILQGVLKVGDEIEIRPGiISKDSGGEFTCRPIRTRIVSLFAENNELQYAVPGGLIGVGTTIDPTLTRADRLVGQVLGY 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 316 PGKLPPVWDSLRLEVHLLERVVGTEQE-----LKVEPIKRKEVLLLNVGTARTMGLVTGLGKDEIE-VKLQIPVCAEPGD 389
Cdd:PTZ00327 350 PGKLPEVYAEIEIQYYLLRRLLGVKSQdgkkaTKVAKLKKGESLMINIGSTTTGGRVVGIKDDGIAkLELTTPVCTSVGE 429
|
410 420
....*....|....*....|.
gi 499169315 390 RVAISRQIGSRWRLIGYGIIK 410
Cdd:PTZ00327 430 KIALSRRVDKHWRLIGWGTIR 450
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
12-204 |
6.46e-131 |
|
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: 374.30 E-value: 6.46e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLTKALTGVWTDTHSEELRRGITIKIGFADAEIRRCPNCGRYS----TSPVCPYCGHETEFVRRVS 87
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWTVRHKEELKRNITIKLGYANAKIYKCPNCGCPRpydtPECECPGCGGETKLVRHVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 88 FIDAPGHEALMTTMLAGASLMDGAILVIAANEPCPRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKALENYRQIKEFI 167
Cdd:cd01888 81 FVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQALENYEQIKEFV 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 499169315 168 EGTVAENAPIIPISALHGANIDVLVKAIEDFIPTPKR 204
Cdd:cd01888 161 KGTIAENAPIIPISAQLKYNIDVLCEYIVKKIPTPPR 197
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
12-409 |
2.20e-79 |
|
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: 256.76 E-value: 2.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLTKALTGVWTDTHSEELRRGITIKIGFAdaeirrcpncgrYSTSPvcpyCGhetefvRRVSFIDA 91
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGIDTDRLKEEKKRGITIDLGFA------------YLPLP----DG------RRLGFVDV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 92 PGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKALENYRQIKEFIEGTV 171
Cdd:COG3276 59 PGHEKFIKNMLAGAGGIDLVLLVVAADEG-VMPQTREHLAILDLLGIKRGIVVLTKADLVDEEWLELVEEEIRELLAGTF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 172 AENAPIIPISALHGANIDVLVKAIEDFI-PTPKRDPNKPPKMLVLRSFDVnkpgtppeKLVGGVLGGSIVQGKLKVGDEI 250
Cdd:COG3276 138 LEDAPIVPVSAVTGEGIDELRAALDALAaAVPARDADGPFRLPIDRVFSI--------KGFGTVVTGTLLSGTVRVGDEL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 251 EIRPGvpyeehgrikyePITTEIVSLQAGGQFVEEAYPG-----GLVGVGtkldpyltKGDLMAGNVVGKPGKLPPvwdS 325
Cdd:COG3276 210 ELLPS------------GKPVRVRGIQVHGQPVEEAYAGqrvalNLAGVE--------KEEIERGDVLAAPGALRP---T 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 326 LRLEVHLleRVVGTEQelkvEPIKRKEVLLLNVGTARTMGLVTGLGKDEI--------EVKLQIPVCAEPGDRVaISRQI 397
Cdd:COG3276 267 DRIDVRL--RLLPSAP----RPLKHWQRVHLHHGTAEVLARVVLLDREELapgeealaQLRLEEPLVAARGDRF-ILRDY 339
|
410
....*....|..
gi 499169315 398 GSRwRLIGYGII 409
Cdd:COG3276 340 SPR-RTIGGGRV 350
|
|
| eIF2_gamma_II |
cd03688 |
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily ... |
205-317 |
7.95e-64 |
|
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: 200.10 E-value: 7.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 205 DPNKPPKMLVLRSFDVNKPGTPPEKLVGGVLGGSIVQGKLKVGDEIEIRPGVPYEEHGRIKYEPITTEIVSLQAGGQFVE 284
Cdd:cd03688 1 DLDKPPRMIVIRSFDVNKPGTEVDDLKGGVIGGSLIQGVLKVGDEIEIRPGIVVKKGGKTTCRPIFTKIVSLFAEGNDLE 80
|
90 100 110
....*....|....*....|....*....|...
gi 499169315 285 EAYPGGLVGVGTKLDPYLTKGDLMAGNVVGKPG 317
Cdd:cd03688 81 EAVPGGLIGVGTKLDPTLTKADRLVGQVVGEPG 113
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
13-202 |
1.83e-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: 178.64 E-value: 1.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELRRGITIKIGFADAEIRRcpncgrystspvcpycghe 79
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTgaidrrgtrketfLDTLKEERERGITIKTGVVEFEWPK------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 80 tefvRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREHLMALQiIGQKNIIIAQNKIELVDKEKALEN 159
Cdd:cd00881 62 ----RRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEG-VEPQTREHLNIAL-AGGLPIIVAVNKIDRVGEEDFDEV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499169315 160 YRQIKEFIEGTVA-----ENAPIIPISALHGANIDVLVKAIEDFIPTP 202
Cdd:cd00881 136 LREIKELLKLIGFtflkgKDVPIIPISALTGEGIEELLDAIVEHLPPP 183
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-195 |
2.48e-51 |
|
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: 170.09 E-value: 2.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 14 IGMVGHVDHGKTTLTKALTGVWTDTHSEELRRGITIKIGFADAEIRRcpncgrystspvcpycghetefVRRVSFIDAPG 93
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGIETDRLPEEKKRGITIDLGFAYLDLPD----------------------GKRLGFIDVPG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 94 HEALMTTMLAGASLMDGAILVIAANEPCpRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKALENYRQIKEFIEGTVAE 173
Cdd:cd04171 60 HEKFVKNMLAGAGGIDAVLLVVAADEGI-MPQTREHLEILELLGIKKGLVVLTKADLVDEDRLELVEEEILELLAGTFLA 138
|
170 180
....*....|....*....|..
gi 499169315 174 NAPIIPISALHGANIDVLVKAI 195
Cdd:cd04171 139 DAPIFPVSSVTGEGIEELKNYL 160
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
12-391 |
1.62e-49 |
|
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: 176.22 E-value: 1.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLTKALTGVWTDTHSEELRRGITIKIGFAdaeirrcpncgrYSTSPvcpycghetefVRRVSFIDA 91
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAADRLPEEKKRGMTIDLGFA------------YFPLP-----------DYRLGFIDV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 92 PGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKALENYRQIKEFIEGTV 171
Cdd:TIGR00475 58 PGHEKFISNAIAGGGGIDAALLVVDADEG-VMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIKRTEMFMKQILNSYI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 172 -AENAPIIPISALHGANIDVLVKAIEDFIPTPK-RDPNKPPKMLVLRSFDVnkpgtppeKLVGGVLGGSIVQGKLKVGDE 249
Cdd:TIGR00475 137 fLKNAKIFKTSAKTGQGIGELKKELKNLLESLDiKRIQKPLRMAIDRAFKV--------KGAGTVVTGTAFSGEVKVGDN 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 250 IEIRP-GVPYeehgRIKyepitteivSLQAGGQFVEEAYPGGLVGVGTkldPYLTKGDLMAGNVVGKPgkLPPvwdSLRL 328
Cdd:TIGR00475 209 LRLLPiNHEV----RVK---------AIQAQNQDVEIAYAGQRIALNL---MDVEPESLKRGLLILTP--EDP---KLRV 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499169315 329 EVHLLERVvgteqelkvePIKRKEVLLLNVGTARTMGLVTGLGKDEIEVKLQIPVCAEPGDRV 391
Cdd:TIGR00475 268 VVKFIAEV----------PLLELQPYHIAHGMSVTTGKISLLDKGIALLTLDAPLILAKGDKL 320
|
|
| eIF2_gamma_III |
cd15490 |
Domain III of eukaryotic initiation factor eIF2 gamma; This family represents the C-terminal ... |
320-409 |
4.51e-47 |
|
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: 156.14 E-value: 4.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 320 PPVWDSLRLEVHLLERVVGTEQELKVEPIKRKEVLLLNVGTARTMGLVTGLGKDEIEVKLQIPVCAEPGDRVAISRQIGS 399
Cdd:cd15490 1 PPVYTELEIEYHLLERVVGVKEEIKVEKIKKGEVLMLNIGSATTGGVVTSVKKDEAEVELKRPVCAEIGERVAISRRIDG 80
|
90
....*....|
gi 499169315 400 RWRLIGYGII 409
Cdd:cd15490 81 RWRLIGWGII 90
|
|
| eIF2_C |
pfam09173 |
Initiation factor eIF2 gamma, C terminal; Members of this family, which are found in the ... |
324-409 |
1.91e-43 |
|
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: 146.50 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 324 DSLRLEVHLLERVVGTEQELKVEPIKRKEVLLLNVGTARTMGLVTGLGKDEIEVKLQIPVCAEPGDRVAISRQIGSRWRL 403
Cdd:pfam09173 1 TELEIEYHLLERVVGVKEEKKVEPIKKGEVLMLNVGTATTGGVVTSVKKDEAEVELKKPVCAEKGERVAISRRIGGRWRL 80
|
....*.
gi 499169315 404 IGYGII 409
Cdd:pfam09173 81 IGWGII 86
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
12-321 |
3.37e-41 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 150.09 E-value: 3.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLTKALTGVWTDTHS-------------EELRRGITIkigfadaeirrcpncgrySTSPVcpycGH 78
Cdd:PRK12736 13 VNIGTIGHVDHGKTTLTAAITKVLAERGLnqakdydsidaapEEKERGITI------------------NTAHV----EY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 79 ETEfVRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREH-LMALQiIGQKNIIIAQNKIELVDKEKAL 157
Cdd:PRK12736 71 ETE-KRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHiLLARQ-VGVPYLVVFLNKVDLVDDEELL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 158 ENYR-QIKEFIE--GTVAENAPIIPISALHG--------ANIDVLVKAIEDFIPTPKRDPNKPPKMLVLRSFDVNKPGTp 226
Cdd:PRK12736 148 ELVEmEVRELLSeyDFPGDDIPVIRGSALKAlegdpkweDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGT- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 227 peklvggVLGGSIVQGKLKVGDEIEIrpgvpyeehgrIKYEPITTEIVS-LQAGGQFVEEAYPGGLVGV---GTKLDpyl 302
Cdd:PRK12736 227 -------VVTGRVERGTVKVGDEVEI-----------VGIKETQKTVVTgVEMFRKLLDEGQAGDNVGVllrGVDRD--- 285
|
330
....*....|....*....
gi 499169315 303 tkgDLMAGNVVGKPGKLPP 321
Cdd:PRK12736 286 ---EVERGQVLAKPGSIKP 301
|
|
| tufA |
CHL00071 |
elongation factor Tu |
12-335 |
3.00e-40 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 147.80 E-value: 3.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLTKALTGVWT-------------DTHSEELRRGITIKigfadaeirrcpncgrysTSPVcpycGH 78
Cdd:CHL00071 13 VNIGTIGHVDHGKTTLTAAITMTLAakggakakkydeiDSAPEEKARGITIN------------------TAHV----EY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 79 ETEfVRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKALE 158
Cdd:CHL00071 71 ETE-NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 159 NYR-QIKEFIE--GTVAENAPIIPISAL-------------HGAN-----IDVLVKAIEDFIPTPKRDPNKPPKMLVLRS 217
Cdd:CHL00071 149 LVElEVRELLSkyDFPGDDIPIVSGSALlalealtenpkikRGENkwvdkIYNLMDAVDSYIPTPERDTDKPFLMAIEDV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 218 FDVNKPGTppeklvggVLGGSIVQGKLKVGDEIEIrpgVPYEEHGrikyepiTTEIVSLQAGGQFVEEAYPGGLVGVgtk 297
Cdd:CHL00071 229 FSITGRGT--------VATGRIERGTVKVGDTVEI---VGLRETK-------TTTVTGLEMFQKTLDEGLAGDNVGI--- 287
|
330 340 350
....*....|....*....|....*....|....*...
gi 499169315 298 LDPYLTKGDLMAGNVVGKPGKLPPvWDSLRLEVHLLER 335
Cdd:CHL00071 288 LLRGIQKEDIERGMVLAKPGTITP-HTKFEAQVYILTK 324
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
12-201 |
1.54e-39 |
|
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: 139.58 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLTKALT----------------GVWTDTHSEELRRGITIKIGFAdaeirrcpncgRYSTSPvcpy 75
Cdd:pfam00009 4 RNIGIIGHVDHGKTTLTDRLLyytgaiskrgevkgegEAGLDNLPEERERGITIKSAAV-----------SFETKD---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 76 cghetefvRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANE-PCprPQTREHLMALQIIGqKNIIIAQNKIELVDKE 154
Cdd:pfam00009 69 --------YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEgVM--PQTREHLRLARQLG-VPIIVFINKMDRVDGA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499169315 155 KALENYRQIK-EFIE--GTVAENAPIIPISALHGANIDVLVKAIEDFIPT 201
Cdd:pfam00009 138 ELEEVVEEVSrELLEkyGEDGEFVPVVPGSALKGEGVQTLLDALDEYLPS 187
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
12-321 |
3.28e-39 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 145.74 E-value: 3.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLTKALTGVWT-------------DTHSEELRRGITIkigfadaeirrcpncgrySTSPVcpycGH 78
Cdd:PLN03127 62 VNVGTIGHVDHGKTTLTAAITKVLAeegkakavafdeiDKAPEEKARGITI------------------ATAHV----EY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 79 ETEfVRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKALE 158
Cdd:PLN03127 120 ETA-KRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDG-PMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 159 ----NYRQIKEFIEGTvAENAPIIPISALH---------GAN-IDVLVKAIEDFIPTPKRDPNKPPKMLVLRSFDVNKPG 224
Cdd:PLN03127 198 lvemELRELLSFYKFP-GDEIPIIRGSALSalqgtndeiGKNaILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 225 TppeklvggVLGGSIVQGKLKVGDEIEIRpgvpyeehGRIKYEPITTEIVSLQAGGQFVEEAYPGGLVGVgtkLDPYLTK 304
Cdd:PLN03127 277 T--------VATGRVEQGTIKVGEEVEIV--------GLRPGGPLKTTVTGVEMFKKILDQGQAGDNVGL---LLRGLKR 337
|
330
....*....|....*..
gi 499169315 305 GDLMAGNVVGKPGKLPP 321
Cdd:PLN03127 338 EDVQRGQVICKPGSIKT 354
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
12-252 |
4.00e-39 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 144.56 E-value: 4.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLTKALTGVWTDTHS-------------EELRRGITIkigfadaeirrcpncgrySTSPVcpycGH 78
Cdd:PRK00049 13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGaeakaydqidkapEEKARGITI------------------NTAHV----EY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 79 ETEfVRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREH-LMALQiIGQKNIIIAQNKIELVDKEKAL 157
Cdd:PRK00049 71 ETE-KRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHiLLARQ-VGVPYIVVFLNKCDMVDDEELL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 158 enyrqikEFIEGTVAE----------NAPIIPISAL----------HGANIDVLVKAIEDFIPTPKRDPNKPPKMLVLRS 217
Cdd:PRK00049 148 -------ELVEMEVREllskydfpgdDTPIIRGSALkalegdddeeWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDV 220
|
250 260 270
....*....|....*....|....*....|....*
gi 499169315 218 FDVNKPGTppeklvggVLGGSIVQGKLKVGDEIEI 252
Cdd:PRK00049 221 FSISGRGT--------VVTGRVERGIIKVGEEVEI 247
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
12-321 |
3.64e-38 |
|
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: 141.83 E-value: 3.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLTKALTGVWTDTH-------------SEELRRGITIkigfadaeirrcpncgrySTSPVcpycGH 78
Cdd:COG0050 13 VNIGTIGHVDHGKTTLTAAITKVLAKKGgakakaydqidkaPEEKERGITI------------------NTSHV----EY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 79 ETEfVRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREH-LMALQiIGQKNIIIAQNKIELVDKEKAL 157
Cdd:COG0050 71 ETE-KRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHiLLARQ-VGVPYIVVFLNKCDMVDDEELL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 158 enyrqikEFIEGTVAE----------NAPIIPISAL----------HGANIDVLVKAIEDFIPTPKRDPNKPPKMLVLRS 217
Cdd:COG0050 148 -------ELVEMEVREllskygfpgdDTPIIRGSALkalegdpdpeWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 218 FDVNKPGTppeklvggVLGGSIVQGKLKVGDEIEIrpgvpyeehgrIKYEPITTEIV-SLQAGGQFVEEAYPGGLVGV-- 294
Cdd:COG0050 221 FSITGRGT--------VVTGRVERGIIKVGDEVEI-----------VGIRDTQKTVVtGVEMFRKLLDEGEAGDNVGLll 281
|
330 340
....*....|....*....|....*...
gi 499169315 295 -GTKLDpyltkgDLMAGNVVGKPGKLPP 321
Cdd:COG0050 282 rGIKRE------DVERGQVLAKPGSITP 303
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
3-321 |
5.40e-38 |
|
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: 141.45 E-value: 5.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 3 EKRKSRQAEVNIGMVGHVDHGKTTLTKALTGVWT-------------DTHSEELRRGITIkigfadaeirrcpncgryST 69
Cdd:TIGR00485 4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAkeggaaaraydqiDNAPEEKARGITI------------------NT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 70 SPVcpycGHETEfVRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREHLMALQIIGQKNIIIAQNKIE 149
Cdd:TIGR00485 66 AHV----EYETE-TRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGVPYIVVFLNKCD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 150 LVDKEKALENYR-QIKEFIE--GTVAENAPIIPISALH--------GANIDVLVKAIEDFIPTPKRDPNKPPKMLVLRSF 218
Cdd:TIGR00485 140 MVDDEELLELVEmEVRELLSqyDFPGDDTPIIRGSALKalegdaewEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 219 DVNKPGTppeklvggVLGGSIVQGKLKVGDEIEIrpgvpyeehgrIKYEPITTEIVS-LQAGGQFVEEAYPGGLVGV--- 294
Cdd:TIGR00485 220 SITGRGT--------VVTGRVERGIIKVGEEVEI-----------VGLKDTRKTTVTgVEMFRKELDEGRAGDNVGLllr 280
|
330 340
....*....|....*....|....*..
gi 499169315 295 GTKldpyltKGDLMAGNVVGKPGKLPP 321
Cdd:TIGR00485 281 GIK------REEIERGMVLAKPGSIKP 301
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
12-252 |
5.04e-37 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 138.82 E-value: 5.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLTKALTGVWTDTHS-------------EELRRGITIkigfadaeirrcpncgrySTSPVcpycGH 78
Cdd:PRK12735 13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGgeakaydqidnapEEKARGITI------------------NTSHV----EY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 79 ETEfVRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREH-LMALQiIGQKNIIIAQNKIELVDKEKAL 157
Cdd:PRK12735 71 ETA-NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHiLLARQ-VGVPYIVVFLNKCDMVDDEELL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 158 enyrqikEFIEGTVAE----------NAPIIPISALHGAN----------IDVLVKAIEDFIPTPKRDPNKPPKMLVLRS 217
Cdd:PRK12735 148 -------ELVEMEVREllskydfpgdDTPIIRGSALKALEgdddeeweakILELMDAVDSYIPEPERAIDKPFLMPIEDV 220
|
250 260 270
....*....|....*....|....*....|....*
gi 499169315 218 FDVNKPGTppeklvggVLGGSIVQGKLKVGDEIEI 252
Cdd:PRK12735 221 FSISGRGT--------VVTGRVERGIVKVGDEVEI 247
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
12-206 |
1.94e-36 |
|
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: 131.72 E-value: 1.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLTKALTGVWT----DTHSEELRRGITIKIGFADAEIRrcpncgrystSPVCPYCGHETEFVR-RV 86
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAStaafDKNPQSQERGITLDLGFSSFEVD----------KPKHLEDNENPQIENyQI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 87 SFIDAPGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREHLMALQIIgQKNIIIAQNKIELVD---KEKALENYRQ- 162
Cdd:cd01889 71 TLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-IQTQTAECLVIGELL-CKPLIVVLNKIDLIPeeeRKRKIEKMKKr 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499169315 163 IKEFIEGTVAENAPIIPISALHGANIDVLVKAIEDFIPTPKRDP 206
Cdd:cd01889 149 LQKTLEKTRLKDSPIIPVSAKPGEGEAELGGELKNLIVLPLINL 192
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
3-410 |
1.23e-32 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 128.19 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 3 EKRKSRQAEVNIGMVGHVDHGKTTLTKALTGVWT-------------DTHSEELRRGITIkigfadaeirrcpncgryST 69
Cdd:PLN03126 73 GKFERKKPHVNIGTIGHVDHGKTTLTAALTMALAsmggsapkkydeiDAAPEERARGITI------------------NT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 70 SPVcpycGHETEfVRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREHLMALQIIGQKNIIIAQNKIE 149
Cdd:PLN03126 135 ATV----EYETE-NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPNMVVFLNKQD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 150 LVDKEKALENYR-QIKEFIEG--TVAENAPIIPISAL-------------HGAN-----IDVLVKAIEDFIPTPKRDPNK 208
Cdd:PLN03126 209 QVDDEELLELVElEVRELLSSyeFPGDDIPIISGSALlalealmenpnikRGDNkwvdkIYELMDAVDSYIPIPQRQTDL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 209 PPKMLVLRSFDVNKPGTppeklvggVLGGSIVQGKLKVGDEIEIrPGVPyeehgrikyEPITTEIVSLQAGGQFVEEAYP 288
Cdd:PLN03126 289 PFLLAVEDVFSITGRGT--------VATGRVERGTVKVGETVDI-VGLR---------ETRSTTVTGVEMFQKILDEALA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 289 GGLVGVgtkLDPYLTKGDLMAGNVVGKPGKLPPvWDSLRLEVHLLERvvgtEQELKVEPIKRKEVLLLNVGTARTMGLVT 368
Cdd:PLN03126 351 GDNVGL---LLRGIQKADIQRGMVLAKPGSITP-HTKFEAIVYVLKK----EEGGRHSPFFAGYRPQFYMRTTDVTGKVT 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 499169315 369 GLGKDEIE--------------VKLQIPVCAEPGDRVAIsRQIGsrwRLIGYGIIK 410
Cdd:PLN03126 423 SIMNDKDEeskmvmpgdrvkmvVELIVPVACEQGMRFAI-REGG---KTVGAGVIQ 474
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
12-202 |
4.31e-32 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 120.38 E-value: 4.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLTKALTGVWTDTHS-------------EELRRGITIkigfadaeirrcpncgrySTSPVcpycGH 78
Cdd:cd01884 3 VNVGTIGHVDHGKTTLTAAITKVLAKKGGakakkydeidkapEEKARGITI------------------NTAHV----EY 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 79 ETEfVRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKALE 158
Cdd:cd01884 61 ETA-NRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDG-PMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLE 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499169315 159 NYRQ-IKEFIE--GTVAENAPIIPISALHG----------ANIDVLVKAIEDFIPTP 202
Cdd:cd01884 139 LVEMeVRELLSkyGFDGDDTPIVRGSALKAlegddpnkwvDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
12-333 |
2.06e-31 |
|
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: 123.89 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLTKAL---TGV------------------------WT-DTHSEELRRGITIKIGFADAEIRRcpn 63
Cdd:COG5256 8 LNLVVIGHVDHGKSTLVGRLlyeTGAidehiiekyeeeaekkgkesfkfaWVmDRLKEERERGVTIDLAHKKFETDK--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 64 cgRYSTspvcpycghetefvrrvsFIDAPGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREHLMALQIIGQKNIII 143
Cdd:COG5256 85 --YYFT------------------IIDAPGHRDFVKNMITGASQADAAILVVSAKDG-VMGQTREHAFLARTLGINQLIV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 144 AQNKIELVDKEKalENYRQIKEFIE------GTVAENAPIIPISALHGANI------------DVLVKAIEDFIPTPKRD 205
Cdd:COG5256 144 AVNKMDAVNYSE--KRYEEVKEEVSkllkmvGYKVDKIPFIPVSAWKGDNVvkksdnmpwyngPTLLEALDNLKEPEKPV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 206 pNKPPKMLVLrsfDV-NKPGtppeklVGGVLGGSIVQGKLKVGDEIEIRPgvpyeehgrikyEPITTEIVSLQAGGQFVE 284
Cdd:COG5256 222 -DKPLRIPIQ---DVySISG------IGTVPVGRVETGVLKVGDKVVFMP------------AGVVGEVKSIEMHHEELE 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 499169315 285 EAYPGGLVGVGTKldpYLTKGDLMAGNVVGKPGKLPPVWDSLRLEVHLL 333
Cdd:COG5256 280 QAEPGDNIGFNVR---GVEKNDIKRGDVAGHPDNPPTVAEEFTAQIVVL 325
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
14-248 |
8.06e-31 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 124.39 E-value: 8.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 14 IGMVGHVDHGKTTLTKALTGVWTDTHSEELRRGITIKIGFAdaeirrcpncgrYSTSPVCpycghetefvRRVSFIDAPG 93
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYA------------YWPQPDG----------RVLGFIDVPG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 94 HEALMTTMLAGASLMDGAILVIAANEPCpRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKALENYRQIKEFIEGTVAE 173
Cdd:PRK10512 61 HEKFLSNMLAGVGGIDHALLVVACDDGV-MAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRRQVKAVLREYGFA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499169315 174 NAPIIPISALHGANIDVLVKAIEDFIPTPkRDPNKPPKMLVLRSFDVnkpgtppeKLVGGVLGGSIVQGKLKVGD 248
Cdd:PRK10512 140 EAKLFVTAATEGRGIDALREHLLQLPERE-HAAQHRFRLAIDRAFTV--------KGAGLVVTGTALSGEVKVGD 205
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
12-334 |
2.15e-30 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 121.19 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLTKAL---TGV------------------------WT-DTHSEELRRGITIKIGFADAEIRRcpn 63
Cdd:PRK12317 7 LNLAVIGHVDHGKSTLVGRLlyeTGAidehiieelreeakekgkesfkfaWVmDRLKEERERGVTIDLAHKKFETDK--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 64 cgRYSTspvcpycghetefvrrvsFIDAPGHEALMTTMLAGASLMDGAILVIAANEP-CPRPQTREHLMALQIIGQKNII 142
Cdd:PRK12317 84 --YYFT------------------IVDCPGHRDFVKNMITGASQADAAVLVVAADDAgGVMPQTREHVFLARTLGINQLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 143 IAQNKIELVDKEKalENYRQIKEFIE------GTVAENAPIIPISALHGANI------------DVLVKAIEDFIPTPKR 204
Cdd:PRK12317 144 VAINKMDAVNYDE--KRYEEVKEEVSkllkmvGYKPDDIPFIPVSAFEGDNVvkksenmpwyngPTLLEALDNLKPPEKP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 205 DpNKPPKMLVLRSFDVNKPGTPPeklVGGVlggsiVQGKLKVGDEIEIRP-GVpyeehgrikyepiTTEIVSLQAGGQFV 283
Cdd:PRK12317 222 T-DKPLRIPIQDVYSISGVGTVP---VGRV-----ETGVLKVGDKVVFMPaGV-------------VGEVKSIEMHHEEL 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 499169315 284 EEAYPGGLVGVGTKldpYLTKGDLMAGNVVGKPGKLPPVWDSLRLEVHLLE 334
Cdd:PRK12317 280 PQAEPGDNIGFNVR---GVGKKDIKRGDVCGHPDNPPTVAEEFTAQIVVLQ 327
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
3-323 |
2.54e-25 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 107.71 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 3 EKRKSRQAEVNIGMVGHVDHGKTTLTKAL-TG----------VWTDTHSEELRRGITIKI-----GFADAEIRRCPNCGR 66
Cdd:COG5258 114 EGKEKDPEHIVVGVAGHVDHGKSTLVGTLvTGklddgnggtrSFLDVQPHEVERGLSADLsyavyGFDDDGPVRMKNPLR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 67 YStspvcpycgHETEFV----RRVSFIDAPGHEALMTTMLAG--ASLMDGAILVIAANEPcPRPQTREHLmALQIIGQKN 140
Cdd:COG5258 194 KT---------DRARVVeesdKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDG-PTHTTREHL-GILLAMDLP 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 141 IIIAQNKIELVDKEKALENYRQIKEF-----------------------IEGTVaenAPIIPISALHGANIDVLVKAIED 197
Cdd:COG5258 263 VIVAITKIDKVDDERVEEVEREIENLlrivgrtplevesrhdvdaaieeINGRV---VPILKTSAVTGEGLDLLDELFER 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 198 fIPTPKRDPNKPPKMLVLRSFDVnkpgtppeKLVGGVLGGSIVQGKLKVGDEIEIRPgvpyEEHGRIKyepiTTEIVSLQ 277
Cdd:COG5258 340 -LPKRATDEDEPFLMYIDRIYNV--------TGVGTVVSGTVKSGKVEAGDELLIGP----TKDGSFR----EVEVKSIE 402
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 499169315 278 AGGQFVEEAYPGGLVGVGTKldpYLTKGDLMAGNVVGKPGKLP-PVW 323
Cdd:COG5258 403 MHYHRVDKAEAGRIVGIALK---GVEEEELERGMVLLPRDADPkAVR 446
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
14-265 |
2.15e-23 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 102.60 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 14 IGMVGHVDHGKTTLTKALTGvwTDTHSEELRrGITIKIGFADAEIrrcpncgrystspvcPYCGHEtefvRRVSFIDAPG 93
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRK--TQIAQKEAG-GITQKIGAYEVEF---------------EYKDEN----QKIVFLDTPG 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 94 HEALMTTMLAGASLMDGAILVIAANEPCpRPQTREhlmALQIIGQKN--IIIAQNKIelvDKEKA--------LENYRQI 163
Cdd:CHL00189 305 HEAFSSMRSRGANVTDIAILIIAADDGV-KPQTIE---AINYIQAANvpIIVAINKI---DKANAnterikqqLAKYNLI 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 164 KEFIEGTVaenaPIIPISALHGANIDVLVKAI------EDFiptpKRDPNKPPKMLVLRSFdVNKPGTPPEKLvggvlgg 237
Cdd:CHL00189 378 PEKWGGDT----PMIPISASQGTNIDKLLETIlllaeiEDL----KADPTQLAQGIILEAH-LDKTKGPVATI------- 441
|
250 260
....*....|....*....|....*....
gi 499169315 238 sIVQ-GKLKVGDEIeirpgVPYEEHGRIK 265
Cdd:CHL00189 442 -LVQnGTLHIGDII-----VIGTSYAKIR 464
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
18-195 |
6.47e-23 |
|
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: 94.46 E-value: 6.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 18 GHVDHGKTTLTKALTGvwTDTHSEELRrGITIKIGfadaeirrcpncgrystspvcPYCGHETEFVRRVSFIDAPGHEAL 97
Cdd:cd01887 7 GHVDHGKTTLLDKIRK--TNVAAGEAG-GITQHIG---------------------AYQVPIDVKIPGITFIDTPGHEAF 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 98 mTTMLA-GASLMDGAILVIAANEpCPRPQTREhlmALQIIGQKN--IIIAQNKIELVDKEKALEN--YRQIKEFieGTVA 172
Cdd:cd01887 63 -TNMRArGASVTDIAILVVAADD-GVMPQTIE---AINHAKAANvpIIVAINKIDKPYGTEADPErvKNELSEL--GLVG 135
|
170 180
....*....|....*....|....*..
gi 499169315 173 EN----APIIPISALHGANIDVLVKAI 195
Cdd:cd01887 136 EEwggdVSIVPISAKTGEGIDDLLEAI 162
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
13-190 |
8.37e-23 |
|
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: 95.64 E-value: 8.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLTKAL---TGV------------------------WT-DTHSEELRRGITIKIGFADaeirrcpnc 64
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLlykLGGvdkrtiekyekeakemgkesfkyaWVlDKLKEERERGVTIDVGLAK--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 65 grystspvcpycgHETEfVRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPC------PRPQTREHLMALQIIGQ 138
Cdd:cd01883 72 -------------FETE-KYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEfeagfeKGGQTREHALLARTLGV 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499169315 139 KNIIIAQNKIELVDKEKALENYRQIKE----FIE--GTVAENAPIIPISALHGANIDV 190
Cdd:cd01883 138 KQLIVAVNKMDDVTVNWSQERYDEIKKkvspFLKkvGYNPKDVPFIPISGFTGDNLIE 195
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
9-322 |
4.75e-22 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 97.51 E-value: 4.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 9 QAEVNIGMVGHVDHGKTTLTKALT----GV-----------------------WT-DTHSEELRRGITIKIGFADAEirr 60
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHLIykcgGIdkrtiekfekeaaemgkgsfkyaWVlDKLKAERERGITIDIALWKFE--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 61 cpnCGRYStspvcpycghetefvrrVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEP------CPRPQTREHLMALQ 134
Cdd:PTZ00141 82 ---TPKYY-----------------FTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGefeagiSKDGQTREHALLAF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 135 IIGQKNIIIAQNKIELVDKEKALENYRQIKEFIE------GTVAENAPIIPISALHGANI------------DVLVKAIE 196
Cdd:PTZ00141 142 TLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSaylkkvGYNPEKVPFIPISGWQGDNMieksdnmpwykgPTLLEALD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 197 DFIPtPKRDPNKPpkmLVLRSFDVNKPGTppeklVGGVLGGSIVQGKLKVGDEIEIRPGvpyeehgrikyePITTEIVSL 276
Cdd:PTZ00141 222 TLEP-PKRPVDKP---LRLPLQDVYKIGG-----IGTVPVGRVETGILKPGMVVTFAPS------------GVTTEVKSV 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499169315 277 QAGGQFVEEAYPGGLVGVGTKldpYLTKGDLMAGNVVGKPGKLPPV 322
Cdd:PTZ00141 281 EMHHEQLAEAVPGDNVGFNVK---NVSVKDIKRGYVASDSKNDPAK 323
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
17-399 |
2.18e-20 |
|
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: 92.46 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 17 VGHVDHGKTTL-------TKALT--------------GVW-------TDTHSEELRRGITIKIGFadaeirrcpncgRY- 67
Cdd:COG2895 23 CGSVDDGKSTLigrllydTKSIFedqlaalerdskkrGTQeidlallTDGLQAEREQGITIDVAY------------RYf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 68 STSpvcpycghetefvRRvSFI--DAPGHEALMTTMLAGASLMDGAILVIAANEPCpRPQTREHLMALQIIGQKNIIIAQ 145
Cdd:COG2895 91 STP-------------KR-KFIiaDTPGHEQYTRNMVTGASTADLAILLIDARKGV-LEQTRRHSYIASLLGIRHVVVAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 146 NKIELVD-KEKAlenYRQIK----EFIEGTVAENAPIIPISALHGANI------------DVLVKAIEDfIPTPKRDPNK 208
Cdd:COG2895 156 NKMDLVDySEEV---FEEIVadyrAFAAKLGLEDITFIPISALKGDNVversenmpwydgPTLLEHLET-VEVAEDRNDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 209 PPKMLVLrsfDVNKP-----GtppeklvggvLGGSIVQGKLKVGDEIEIRPGvpyeehGRikyepiTTEIVSLQAGGQFV 283
Cdd:COG2895 232 PFRFPVQ---YVNRPnldfrG----------YAGTIASGTVRVGDEVVVLPS------GK------TSTVKSIVTFDGDL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 284 EEAYPGGLVGVGTKLDPYLTKGDLMAgnvvgKPGKLPPVwdSLRLEVHLL---ER--VVGTEQELK---------VEPIK 349
Cdd:COG2895 287 EEAFAGQSVTLTLEDEIDISRGDVIV-----AADAPPEV--ADQFEATLVwmdEEplLPGRKYLLKhgtrtvratVTAIK 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 499169315 350 RKevllLNVGT-----ARTMGLvTGLGkdEIEVKLQIPVCAEPGDRvaiSRQIGS 399
Cdd:COG2895 360 YR----IDVNTleheaADSLEL-NDIG--RVTLRLAEPIAFDPYAD---NRATGS 404
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
17-188 |
6.44e-19 |
|
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: 84.54 E-value: 6.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 17 VGHVDHGKTTL-------TKALT----------------------GVWTDTHSEELRRGITIKIGFadaeirrcpncgRY 67
Cdd:cd04166 5 CGSVDDGKSTLigrllydSKSIFedqlaalerskssgtqgekldlALLVDGLQAEREQGITIDVAY------------RY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 68 STSPvcpycghetefvRRvSFI--DAPGHEALMTTMLAGASLMDGAILVIAANEPCpRPQTREHLMALQIIGQKNIIIAQ 145
Cdd:cd04166 73 FSTP------------KR-KFIiaDTPGHEQYTRNMVTGASTADLAILLVDARKGV-LEQTRRHSYIASLLGIRHVVVAV 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499169315 146 NKIELVDKEKalENYRQIK----EFIEGTVAENAPIIPISALHGANI 188
Cdd:cd04166 139 NKMDLVDYDE--EVFEEIKadylAFAASLGIEDITFIPISALEGDNV 183
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
18-265 |
1.82e-17 |
|
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: 83.91 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 18 GHVDHGKTTLTKAL--TGVwtdTHSEElrRGITIKIGfadAeirrcpncgrYSTspvcpycghETEfVRRVSFIDAPGHE 95
Cdd:COG0532 11 GHVDHGKTSLLDAIrkTNV---AAGEA--GGITQHIG---A----------YQV---------ETN-GGKITFLDTPGHE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 96 ALmTTMLA-GASLMDGAILVIAANEpCPRPQTRE---HLMALQIigqkNIIIAQNKIelvDKEKAleNYRQIK-EFIE-G 169
Cdd:COG0532 63 AF-TAMRArGAQVTDIVILVVAADD-GVMPQTIEainHAKAAGV----PIIVAINKI---DKPGA--NPDRVKqELAEhG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 170 TVAE----NAPIIPISALHGANIDVLVKAI------EDFiptpKRDPNKPPKMLVLRSF-DVNKpgtppeklvgGVLGGS 238
Cdd:COG0532 132 LVPEewggDTIFVPVSAKTGEGIDELLEMIllqaevLEL----KANPDRPARGTVIEAKlDKGR----------GPVATV 197
|
250 260
....*....|....*....|....*...
gi 499169315 239 IVQ-GKLKVGDEIeirpgVPYEEHGRIK 265
Cdd:COG0532 198 LVQnGTLKVGDIV-----VAGTAYGRVR 220
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
2-288 |
8.64e-15 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 75.96 E-value: 8.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 2 GEKRKSRQAEVNIgmVGHVDHGKTTLTKAL--TGVwtdTHSEElrRGITIKIGfadaeirrcpncgRYSTspvcpycghE 79
Cdd:TIGR00487 80 GDLLVERPPVVTI--MGHVDHGKTSLLDSIrkTKV---AQGEA--GGITQHIG-------------AYHV---------E 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 80 TEFVRRVSFIDAPGHEALmTTMLA-GASLMDGAILVIAANEPCpRPQTRE---HLMALQIigqkNIIIAQNKIelvDKEK 155
Cdd:TIGR00487 131 NEDGKMITFLDTPGHEAF-TSMRArGAKVTDIVVLVVAADDGV-MPQTIEaisHAKAANV----PIIVAINKI---DKPE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 156 ALENyRQIKEFIE-GTVAE----NAPIIPISALHGANIDVLVKAI--EDFIPTPKRDPNKPPKMLVLRSFdvnkpgtpPE 228
Cdd:TIGR00487 202 ANPD-RVKQELSEyGLVPEdwggDTIFVPVSALTGDGIDELLDMIllQSEVEELKANPNGQASGVVIEAQ--------LD 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 229 KLVGGVLGGSIVQGKLKVGDEIEIRPgvpyeEHGRIKyePITTEIvslqagGQFVEEAYP 288
Cdd:TIGR00487 273 KGRGPVATVLVQSGTLRVGDIVVVGA-----AYGRVR--AMIDEN------GKSVKEAGP 319
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
13-198 |
6.45e-14 |
|
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: 70.73 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLTKAL---TGV------------WTDTHSEELRRGITIKIGFADAEIRRCpncgrystspvcpycg 77
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytSGAirelgsvdkgttRTDSMELERQRGITIFSAVASFQWEDT---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 78 hetefvrRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPCpRPQTREHLMALQIIgqkNI--IIAQNKI--ELVDK 153
Cdd:cd04168 65 -------KVNIIDTPGHMDFIAEVERSLSVLDGAILVISAVEGV-QAQTRILFRLLRKL---NIptIIFVNKIdrAGADL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499169315 154 EKAlenYRQIKE------FIEGTVAENAPIIPISALHGANIDVLVKAIEDF 198
Cdd:cd04168 134 EKV---YQEIKEklspdiVPMQKVGLYPNICDTNNIDDEQIETVAEGNDEL 181
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
210-314 |
1.00e-12 |
|
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: 63.05 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 210 PKMLVLRSFDVNKpgtppeklVGGVLGGSIVQGKLKVGDEIEIRPgvpyeehgrikyEPITTEIVSLQAGGQFVEEAYPG 289
Cdd:cd01342 1 LVMQVFKVFYIPG--------RGRVAGGRVESGTLKVGDEIRILP------------KGITGRVTSIERFHEEVDEAKAG 60
|
90 100
....*....|....*....|....*
gi 499169315 290 GLVGVGTKLDpyltkGDLMAGNVVG 314
Cdd:cd01342 61 DIVGIGILGV-----KDILTGDTLT 80
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
12-297 |
1.13e-12 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 69.35 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 12 VNIGMVGHVDHGKTTLT---------------------------KALTGVWT-DTHSEELRRGITIKIGFADAEIRRCpn 63
Cdd:PLN00043 8 INIVVIGHVDSGKSTTTghliyklggidkrvierfekeaaemnkRSFKYAWVlDKLKAERERGITIDIALWKFETTKY-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 64 cgrystspvcpYCghetefvrrvSFIDAPGHEALMTTMLAGASLMDGAILVIAANEP------CPRPQTREHLMALQIIG 137
Cdd:PLN00043 86 -----------YC----------TVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagiSKDGQTREHALLAFTLG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 138 QKNIIIAQNKIELVDKEKALENYRQIKEFIE------GTVAENAPIIPISALHGANI------------DVLVKAIeDFI 199
Cdd:PLN00043 145 VKQMICCCNKMDATTPKYSKARYDEIVKEVSsylkkvGYNPDKIPFVPISGFEGDNMierstnldwykgPTLLEAL-DQI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 200 PTPKRDPNKPpkmLVLRSFDVNKpgtppeklVGGVlgGSIVQGKLKVGdeiEIRPGVpyeehgRIKYEP--ITTEIVSLQ 277
Cdd:PLN00043 224 NEPKRPSDKP---LRLPLQDVYK--------IGGI--GTVPVGRVETG---VIKPGM------VVTFGPtgLTTEVKSVE 281
|
330 340
....*....|....*....|
gi 499169315 278 AGGQFVEEAYPGGLVGVGTK 297
Cdd:PLN00043 282 MHHESLQEALPGDNVGFNVK 301
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
13-294 |
1.47e-12 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 69.25 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLTKAL---TGVWT----------DTHSEELRRGITIkigFADAEIRRCPNCgrystspvcpycghe 79
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALlkqSGTFRaneavaervmDSNDLERERGITI---LAKNTAIRYNGT--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 80 tefvrRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANEPcPRPQTREHLMALQIIGQKNIIIAqNKIelvDKEKAlen 159
Cdd:TIGR01394 65 -----KINIVDTPGHADFGGEVERVLGMVDGVLLLVDASEG-PMPQTRFVLKKALELGLKPIVVI-NKI---DRPSA--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 160 yrQIKEFIEGT----VAENA-------PIIPISALHG----------ANIDVLVKAIEDFIPTPKRDPNKPPKMLVlRSF 218
Cdd:TIGR01394 132 --RPDEVVDEVfdlfAELGAddeqldfPIVYASGRAGwasldlddpsDNMAPLFDAIVRHVPAPKGDLDEPLQMLV-TNL 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499169315 219 DVNkpgtppeKLVGGVLGGSIVQGKLKVGDEIEI--RPGVpyEEHGRIKyEPITTEIVSLQAggqfVEEAYPGGLVGV 294
Cdd:TIGR01394 209 DYD-------EYLGRIAIGRVHRGTVKKGQQVALmkRDGT--IENGRIS-KLLGFEGLERVE----IDEAGAGDIVAV 272
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
11-196 |
2.57e-12 |
|
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: 64.32 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 11 EVNIGMVGHVDHGKTTLTKALTGvwtdTHSEELRRGITIkigfadaeirrcpncGRYSTSPVCPYCGHETEFvrrvSFID 90
Cdd:TIGR00231 1 DIKIVIVGHPNVGKSTLLNSLLG----NKGSITEYYPGT---------------TRNYVTTVIEEDGKTYKF----NLLD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 91 APGHEAL-------MTTMLAGASLMDGAILVIAANEPcPRPQTREhlmalqIIGQKN----IIIAQNKIELVDkEKALEN 159
Cdd:TIGR00231 58 TAGQEDYdairrlyYPQVERSLRVFDIVILVLDVEEI-LEKQTKE------IIHHADsgvpIILVGNKIDLKD-ADLKTH 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 499169315 160 YRQIKEFIEGtvaenAPIIPISALHGANIDVLVKAIE 196
Cdd:TIGR00231 130 VASEFAKLNG-----EPIIPLSAETGKNIDSAFKIVE 161
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
13-169 |
9.57e-12 |
|
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: 64.17 E-value: 9.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLTKAL-------------TGVWTDTHSEELRRGITIKigfadaeirrcpncgrySTSpVCPYCGHE 79
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLlasagiiseklagKARYLDTREDEQERGITIK-----------------SSA-ISLYFEYE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 80 TEFVRRVSF----IDAPGHEALMTTMLAGASLMDGAILVIAANEPCpRPQTRehlMALQIIGQKNI--IIAQNKIELVDK 153
Cdd:cd01885 64 EEKMDGNDYlinlIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGV-CVQTE---TVLRQALEERVkpVLVINKIDRLIL 139
|
170
....*....|....*....
gi 499169315 154 EKAL---ENYRQIKEFIEG 169
Cdd:cd01885 140 ELKLspeEAYQRLLRIVED 158
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
13-250 |
1.92e-11 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 65.81 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLTKAL---TGVWTD-THSEEL--------R-RGITI--KigfadaeirrcpNCGrystspvCPYCG 77
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALlkqSGTFREnQEVAERvmdsndleReRGITIlaK------------NTA-------VRYKG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 78 HetefvrRVSFIDAPGH-------EALMttmlagaSLMDGAILVIAANEPcPRPQTREHLM-ALQiIGQKnIIIAQNKIe 149
Cdd:COG1217 69 V------KINIVDTPGHadfggevERVL-------SMVDGVLLLVDAFEG-PMPQTRFVLKkALE-LGLK-PIVVINKI- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 150 lvDKEKAlenyrQIKE--------FIE-GTVAE--NAPIIPISALHG----------ANIDVLVKAIEDFIPTPKRDPNK 208
Cdd:COG1217 132 --DRPDA-----RPDEvvdevfdlFIElGATDEqlDFPVVYASARNGwasldlddpgEDLTPLFDTILEHVPAPEVDPDG 204
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 499169315 209 PPKMLVLrSFDVNkpgtppeKLVGGVLGGSIVQGKLKVGDEI 250
Cdd:COG1217 205 PLQMLVT-NLDYS-------DYVGRIAIGRIFRGTIKKGQQV 238
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
87-254 |
2.95e-11 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 64.93 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 87 SFI--DAPGHEALMTTMLAGASLMDGAILVIAAnepcpR----PQTREHLMALQIIGQKNIIIAQNKIELVDKEKalENY 160
Cdd:PRK05124 108 KFIiaDTPGHEQYTRNMATGASTCDLAILLIDA-----RkgvlDQTRRHSFIATLLGIKHLVVAVNKMDLVDYSE--EVF 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 161 RQIK-EFIEgtVAENAP------IIPISALHGANI------------DVLVKAIEDfIPTPKRDPNKPPKMLVLRsfdVN 221
Cdd:PRK05124 181 ERIReDYLT--FAEQLPgnldirFVPLSALEGDNVvsqsesmpwysgPTLLEVLET-VDIQRVVDAQPFRFPVQY---VN 254
|
170 180 190
....*....|....*....|....*....|...
gi 499169315 222 KPGTPPEKLVGGVLGGSIvqgklKVGDEIEIRP 254
Cdd:PRK05124 255 RPNLDFRGYAGTLASGVV-----KVGDRVKVLP 282
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
17-195 |
3.02e-11 |
|
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: 61.32 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 17 VGHVDHGKTTLTKALTGVWTDTHSEElrRGITIKIGFADAEIRrcpncgrystspvcpycghetEFVRRVSFIDAPGH-- 94
Cdd:cd00882 3 VGRGGVGKSSLLNALLGGEVGEVSDV--PGTTRDPDVYVKELD---------------------KGKVKLVLVDTPGLde 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 95 ------EALMTTMLAGAslmDGAILVIAANEPCPRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKALENYRQIKEFIE 168
Cdd:cd00882 60 fgglgrEELARLLLRGA---DLILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKI 136
|
170 180
....*....|....*....|....*..
gi 499169315 169 gtvaENAPIIPISALHGANIDVLVKAI 195
Cdd:cd00882 137 ----LGVPVFEVSAKTGEGVDELFEKL 159
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
13-202 |
1.90e-10 |
|
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: 59.91 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLTKAL---TGVWT----------DTHSEELRRGITIkigfadaeirrcpncgrysTSPVCPYCGHE 79
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALlkqSGTFReneevgervmDSNDLERERGITI-------------------LAKNTAITYKD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 80 TefvrRVSFIDAPGH-------EALMttmlagaSLMDGAILVIAANEPcPRPQTREHLM-ALQiIGQKnIIIAQNKIelv 151
Cdd:cd01891 65 T----KINIIDTPGHadfggevERVL-------SMVDGVLLLVDASEG-PMPQTRFVLKkALE-AGLK-PIVVINKI--- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499169315 152 DKEKAlenyrQIKEFIEGT----VAENA-------PIIPISALHG----------ANIDVLVKAIEDFIPTP 202
Cdd:cd01891 128 DRPDA-----RPEEVVDEVfdlfLELNAtdeqldfPIVYASAKNGwaslnlddpsEDLDPLFETIIEHVPAP 194
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
88-200 |
1.90e-10 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 61.16 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 88 FIDAPG--------HEALMTTMLAGASLMDGAILVIAANEPcprpQTREHLMALQIIGQKN--IIIAQNKIELVDKEKAL 157
Cdd:COG1159 55 FVDTPGihkpkrklGRRMNKAAWSALEDVDVILFVVDATEK----IGEGDEFILELLKKLKtpVILVINKIDLVKKEELL 130
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 499169315 158 ENYRQIKEFiegtvAENAPIIPISALHGANIDVLVKAIEDFIP 200
Cdd:COG1159 131 PLLAEYSEL-----LDFAEIVPISALKGDNVDELLDEIAKLLP 168
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
13-202 |
1.21e-09 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 57.16 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLTKAL---TGVWTDTHSE---------ELRRGITIKigfadaeirrcpncgrySTSPVCPY-CGHE 79
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSEREMKeqvldsmdlERERGITIK-----------------AQAVRLFYkAKDG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 80 TEFVrrVSFIDAPGH-----EalmttmlAGASLM--DGAILVIAANEPCpRPQTREHL-MALqiigQKN--IIIAQNKIE 149
Cdd:cd01890 65 EEYL--LNLIDTPGHvdfsyE-------VSRSLAacEGALLVVDATQGV-EAQTLANFyLAL----ENNleIIPVINKID 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499169315 150 LV--DKEKALEnyrQIKEFIeGTVAENApiIPISALHGANIDVLVKAIEDFIPTP 202
Cdd:cd01890 131 LPaaDPDRVKQ---EIEDVL-GLDASEA--ILVSAKTGLGVEDLLEAIVERIPPP 179
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
88-188 |
1.24e-09 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 59.94 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 88 FI--DAPGHEALMTTMLAGASLMDGAILVIAAnepcpR----PQTREHLMALQIIGQKNIIIAQNKIELVDKEKAL---- 157
Cdd:PRK05506 106 FIvaDTPGHEQYTRNMVTGASTADLAIILVDA-----RkgvlTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVfdei 180
|
90 100 110
....*....|....*....|....*....|..
gi 499169315 158 -ENYRQIKEFIEgtVAENAPiIPISALHGANI 188
Cdd:PRK05506 181 vADYRAFAAKLG--LHDVTF-IPISALKGDNV 209
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
88-198 |
1.39e-09 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 56.70 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 88 FIDAPG----HEALMTTMLAGA-SLMDGA---ILVIAANEPCprpqTREHLMALQIIGQKN--IIIAQNKIELV-DKEKA 156
Cdd:cd04163 55 FVDTPGihkpKKKLGERMVKAAwSALKDVdlvLFVVDASEWI----GEGDEFILELLKKSKtpVILVLNKIDLVkDKEDL 130
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 499169315 157 LENYRQIKEFIEGtvaenAPIIPISALHGANIDVLVKAIEDF 198
Cdd:cd04163 131 LPLLEKLKELHPF-----AEIFPISALKGENVDELLEYIVEY 167
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
88-200 |
3.38e-09 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 57.36 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 88 FIDAPG--------HEALMTTMLAGASLMDGAILVIAANEPcPRPQTREHLMALQIIGqKNIIIAQNKIELV-DKEKALE 158
Cdd:PRK00089 57 FVDTPGihkpkralNRAMNKAAWSSLKDVDLVLFVVDADEK-IGPGDEFILEKLKKVK-TPVILVLNKIDLVkDKEELLP 134
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 499169315 159 NYRQIKEFIEgtvaeNAPIIPISALHGANIDVLVKAIEDFIP 200
Cdd:PRK00089 135 LLEELSELMD-----FAEIVPISALKGDNVDELLDVIAKYLP 171
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
232-314 |
1.40e-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: 51.11 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 232 GGVLGGSIVQGKLKVGDEIEIRPgvpyeehGRIKYEPITTEIVSLQAGGQFVEEAYPGGLVGVGTKLDPYltkGDLMAGN 311
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILP-------NGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGL---EDIRVGD 70
|
...
gi 499169315 312 VVG 314
Cdd:pfam03144 71 TLT 73
|
|
| Nop10 |
COG2260 |
rRNA maturation protein Nop10, contains Zn-ribbon domain [Translation, ribosomal structure and ... |
57-81 |
1.90e-08 |
|
rRNA maturation protein Nop10, contains Zn-ribbon domain [Translation, ribosomal structure and biogenesis]; rRNA maturation protein Nop10, contains Zn-ribbon domain is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 441861 [Multi-domain] Cd Length: 51 Bit Score: 50.28 E-value: 1.90e-08
10 20
....*....|....*....|....*
gi 499169315 57 EIRRCPNCGRYSTSPVCPYCGHETE 81
Cdd:COG2260 4 LIRKCPSCGRYTLKDTCPVCGGPTV 28
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
84-196 |
3.57e-08 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 52.63 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 84 RRVSFIDAPG-----HEALMTTMLAGASLM--DGAILVIAANEPCPRPQTREHLMALQiigQKNIIIAQNKIELV--DKE 154
Cdd:cd00880 46 GPVVLIDTPGldeegGLGRERVEEARQVADraDLVLLVVDSDLTPVEEEAKLGLLRER---GKPVLLVLNKIDLVpeSEE 122
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 499169315 155 KALENYRQIKEFIEgtvaenAPIIPISALHGANIDVLVKAIE 196
Cdd:cd00880 123 EELLRERKLELLPD------LPVIAVSALPGEGIDELRKKIA 158
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
13-119 |
5.18e-08 |
|
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: 53.04 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLT--------KALTGVW--------TDTHSEELRRGITIK-----IGFADAEirrcpncgrySTSp 71
Cdd:cd04167 2 NVCIAGHLHHGKTSLLdmlieqthKRTPSVKlgwkplryTDTRKDEQERGISIKsnpisLVLEDSK----------GKS- 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 499169315 72 vcpycghetefvRRVSFIDAPGHEALMTTMLAGASLMDGAILVIAANE 119
Cdd:cd04167 71 ------------YLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE 106
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
13-127 |
9.50e-08 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 54.19 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLTKAL---TGVW------------TDTHSEELRRGITIKigfadaeirrcpncgrySTSPVCPYCG 77
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIlfyTGKIhkmgevedgttvTDWMPQEQERGITIE-----------------SAATSCDWDN 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 499169315 78 HetefvrRVSFIDAPGHEALmtTMLAGASL--MDGAILVIAANEPCpRPQTR 127
Cdd:PRK13351 73 H------RINLIDTPGHIDF--TGEVERSLrvLDGAVVVFDAVTGV-QPQTE 115
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
13-117 |
1.52e-07 |
|
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: 53.51 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLTKAL---TGV------------WTDTHSEELRRGITIkigfadaeirrcpncgrySTSPV-CPYC 76
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERIlfyTGAihrigevhdgntVMDWMPEEQERGITI------------------TSAATtCEWK 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 499169315 77 GHetefvrRVSFIDAPGH-----EALmttmlagASLM--DGAILVIAA 117
Cdd:COG0480 73 GH------KINIIDTPGHvdftgEVE-------RSLRvlDGAVVVFDA 107
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
134-199 |
1.76e-07 |
|
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.
Pssm-ID: 206685 [Multi-domain] Cd Length: 170 Bit Score: 50.50 E-value: 1.76e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499169315 134 QIIGQKNIIIAQNKIELVDKEKALEnyrQIKEFIEGTvaENAPIIPISALHGANIDVLVKAIEDFI 199
Cdd:cd01898 110 PGLAEKPRIVVLNKIDLLDAEERFE---KLKELLKEL--KGKKVFPISALTGEGLDELLKKLAKLL 170
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
13-126 |
4.01e-07 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 52.17 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLTKALTG-------------VWTDTHSEELRRGITIKigfaDAEIrrcpncgrystSPVCPYCGhe 79
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDNLLAgagmiseelageqLALDFDEEEQARGITIK----AANV-----------SMVHEYEG-- 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499169315 80 TEFVrrVSFIDAPGHEAL--MTT--MLAgaslMDGAILVIAANEPcPRPQT 126
Cdd:PRK07560 85 KEYL--INLIDTPGHVDFggDVTraMRA----VDGAIVVVDAVEG-VMPQT 128
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
13-119 |
4.95e-07 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 51.97 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLTKAL---TGV----------WTDTHSEELRRGITIKigfadaeirrcpncgrySTS-------PV 72
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTDSLvckAGIissknagdarFTDTRADEQERGITIK-----------------STGislyyehDL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 499169315 73 CPYCGHEtEFVrrVSFIDAPGHEALMTTMLAGASLMDGAILVIAANE 119
Cdd:PTZ00416 84 EDGDDKQ-PFL--INLIDSPGHVDFSSEVTAALRVTDGALVVVDCVE 127
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
13-115 |
5.10e-07 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 52.03 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLTKAL---TGV----------WTDTHSEELRRGITIK-------IGFADAEIRRCPNcgrystspv 72
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTDSLvaaAGIiaqevagdvrMTDTRADEAERGITIKstgislyYEMTDESLKDFKG--------- 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 499169315 73 cpyCGHETEFVrrVSFIDAPGHEALMTTMLAGASLMDGAILVI 115
Cdd:PLN00116 92 ---ERDGNEYL--INLIDSPGHVDFSSEVTAALRITDGALVVV 129
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
18-151 |
5.69e-07 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 51.72 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 18 GHVDHGKTTLTKALTGvwTDTHSEElRRGITIKIG--FADAEIRRcpncgRYSTSPVCPYCGHETefVRRVSFIDAPGHE 95
Cdd:PRK04004 13 GHVDHGKTTLLDKIRG--TAVAAKE-AGGITQHIGatEVPIDVIE-----KIAGPLKKPLPIKLK--IPGLLFIDTPGHE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 499169315 96 ALmTTMLA-GASLMDGAILVIAANEPCpRPQTREhlmALQIIGQKNI--IIAQNKIELV 151
Cdd:PRK04004 83 AF-TNLRKrGGALADIAILVVDINEGF-QPQTIE---AINILKRRKTpfVVAANKIDRI 136
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
133-197 |
1.69e-06 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 50.02 E-value: 1.69e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499169315 133 LQIIGQ-----KNIIIAQNKIELVDKE-KALENY-RQIKE---FIEGtvaenAPIIPISALHGANIDVLVKAIED 197
Cdd:COG1160 276 LKIAGLaleagKALVIVVNKWDLVEKDrKTREELeKEIRRrlpFLDY-----APIVFISALTGQGVDKLLEAVDE 345
|
|
| obgE |
PRK12299 |
GTPase CgtA; Reviewed |
138-205 |
3.33e-06 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 48.53 E-value: 3.33e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499169315 138 QKNIIIAQNKIELVDKEKALENyrQIKEFIEgtvAENAPIIPISALHGANIDVLVKAIEDFIPTPKRD 205
Cdd:PRK12299 271 DKPRILVLNKIDLLDEEEEREK--RAALELA---ALGGPVFLISAVTGEGLDELLRALWELLEEARRE 333
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
210-294 |
4.81e-06 |
|
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: 44.44 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 210 PKMLVLRSFDVNKPGTppeklvggVLGGSIVQGKLKVGDEIEIrpgVPYEEHGRIKyepitteivSLQAGGQFVEEAYPG 289
Cdd:cd03696 1 FRLPIDHVFSIKGAGT--------VVTGTVLSGKVKVGDELEI---PPLGKEVRVR---------SIQVHDKPVEEAKAG 60
|
....*
gi 499169315 290 GLVGV 294
Cdd:cd03696 61 DRVAL 65
|
|
| PRK13130 |
PRK13130 |
RNA-protein complex protein Nop10; |
58-81 |
1.04e-05 |
|
RNA-protein complex protein Nop10;
Pssm-ID: 237287 [Multi-domain] Cd Length: 56 Bit Score: 42.69 E-value: 1.04e-05
|
| Nop10p |
pfam04135 |
Nucleolar RNA-binding protein, Nop10p family; Nop10p is a nucleolar protein that is ... |
58-81 |
1.30e-05 |
|
Nucleolar RNA-binding protein, Nop10p family; Nop10p is a nucleolar protein that is specifically associated with H/ACA snoRNAs. It is essential for normal 18S rRNA production and rRNA pseudouridylation by the ribonucleoprotein particles containing H/ACA snoRNAs (H/ACA snoRNPs). Nop10p is probably necessary for the stability of these RNPs.
Pssm-ID: 427735 [Multi-domain] Cd Length: 51 Bit Score: 42.17 E-value: 1.30e-05
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
133-197 |
1.98e-05 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 44.73 E-value: 1.98e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499169315 133 LQIIGQ-----KNIIIAQNKIELVDK-EKALENY-RQIKE---FIEGtvaenAPIIPISALHGANIDVLVKAIED 197
Cdd:cd01895 103 LRIAGLileegKALIIVVNKWDLVEKdEKTMKEFeKELRRklpFLDY-----APIVFISALTGQGVDKLFDAIKE 172
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
88-192 |
2.23e-05 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 46.80 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 88 FIDAPGHEALMTTMLAGASLMDGAILVIAANEPCpRPQTREhlmALQIIGQKN--IIIAQNKIELVD------------- 152
Cdd:PRK14845 530 FIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGF-KPQTIE---AINILRQYKtpFVVAANKIDLIPgwnisedepflln 605
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499169315 153 -KEKA------LEN--YRQIKEFIE-----------GTVAENAPIIPISALHGANI-DVLV 192
Cdd:PRK14845 606 fNEQDqhalteLEIklYELIGKLYElgfdadrfdrvQDFTRTVAIVPVSAKTGEGIpELLM 666
|
|
| Obg_like |
cd01881 |
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
15-195 |
4.24e-05 |
|
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified.
Pssm-ID: 206668 [Multi-domain] Cd Length: 167 Bit Score: 43.54 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 15 GMVGHVDHGKTTLTKALTGvwtdthseelrrgitikigfADAEIrrcpncGRYSTSPVCPYCGH-ETEFVRRVSFIDAPG 93
Cdd:cd01881 1 GLVGLPNVGKSTLLSALTS--------------------AKVEI------ASYPFTTLEPNVGVfEFGDGVDIQIIDLPG 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 94 -------HEALMTTMLAGASLMDGAILVIAANEPCPRPQTREHLMALQIIG-------QKNIIIAQNKIELVDKEkalen 159
Cdd:cd01881 55 lldgaseGRGLGEQILAHLYRSDLILHVIDASEDCVGDPLEDQKTLNEEVSgsflflkNKPEMIVANKIDMASEN----- 129
|
170 180 190
....*....|....*....|....*....|....*.
gi 499169315 160 yrQIKEFIEGTVAENAPIIPISALHGANIDVLVKAI 195
Cdd:cd01881 130 --NLKRLKLDKLKRGIPVVPTSALTRLGLDRVIRTI 163
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
133-203 |
6.04e-05 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 45.04 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 133 LQIIGQ-----KNIIIAQNKIELVDKEKALENYRQIKE---FIEGtvaenAPIIPISALHGANIDVLVKAIEDF------ 198
Cdd:PRK00093 274 LRIAGLaleagRALVIVVNKWDLVDEKTMEEFKKELRRrlpFLDY-----APIVFISALTGQGVDKLLEAIDEAyenanr 348
|
....*.
gi 499169315 199 -IPTPK 203
Cdd:PRK00093 349 rISTSV 354
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
84-199 |
6.99e-05 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 43.30 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 84 RRVSFIDAPG-------HEALMTTMLagaSLMDGAILVIAANepcpRPQTREHLMALQIIGQ---KNIIIAQNKIELVDK 153
Cdd:cd09912 46 KGVVLVDTPGlnstiehHTEITESFL---PRADAVIFVLSAD----QPLTESEREFLKEILKwsgKKIFFVLNKIDLLSE 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499169315 154 EKALEN--YRQIKEFIEGTVAENAPIIPISA--------------LHGANIDVLVKAIEDFI 199
Cdd:cd09912 119 EELEEVleYSREELGVLELGGGEPRIFPVSAkealearlqgdeelLEQSGFEELEEHLEEFL 180
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
17-117 |
7.61e-05 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 44.73 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 17 VGHVDHGKTTLTKAL---TGV------------WTDTHSEELRRGITIkigfadaeirrcpncgrySTSPV-CPYCGHet 80
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfyTGAihrigevedgttTMDFMPEERERGISI------------------TSAATtCEWKGH-- 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 499169315 81 efvrRVSFIDAPGH-----EALmttmlagASLM--DGAILVIAA 117
Cdd:PRK12740 61 ----KINLIDTPGHvdftgEVE-------RALRvlDGAVVVVCA 93
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
88-199 |
8.53e-05 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 42.88 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 88 FIDAPG-------------HEALMTTMLAGASLMDGAILVIAANepcpRPQTREHLMALQIIGQKNI--IIAQNKIELVD 152
Cdd:cd01876 49 LVDLPGygyakvskevrekWGKLIEEYLENRENLKGVVLLIDAR----HGPTPIDLEMLEFLEELGIpfLIVLTKADKLK 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 499169315 153 KEKALENYRQIKEFIEGtVAENAPIIPISALHGANIDVLVKAIEDFI 199
Cdd:cd01876 125 KSELAKVLKKIKEELNL-FNILPPVILFSSKKGTGIDELRALIAEWL 170
|
|
| obgE |
PRK12297 |
GTPase CgtA; Reviewed |
138-212 |
9.72e-05 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237046 [Multi-domain] Cd Length: 424 Bit Score: 44.32 E-value: 9.72e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499169315 138 QKNIIIAQNKIELVDkekALENYRQIKEFIEgtvaenAPIIPISALHGANIDVLVKAIEDFIPTPKRDPNKPPKM 212
Cdd:PRK12297 274 ERPQIVVANKMDLPE---AEENLEEFKEKLG------PKVFPISALTGQGLDELLYAVAELLEETPEFPLEEEEV 339
|
|
| COG2888 |
COG2888 |
Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 ... |
56-81 |
4.41e-04 |
|
Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 family [General function prediction only];
Pssm-ID: 442134 [Multi-domain] Cd Length: 52 Bit Score: 37.79 E-value: 4.41e-04
10 20
....*....|....*....|....*..
gi 499169315 56 AEIRRCPNCGRYSTSP-VCPYCGHETE 81
Cdd:COG2888 26 ALIIRCPKCRKQSNALyFCPKCGFEGP 52
|
|
| PolC_DP2 |
pfam03833 |
DNA polymerase II large subunit DP2; |
40-85 |
4.69e-04 |
|
DNA polymerase II large subunit DP2;
Pssm-ID: 427537 Cd Length: 866 Bit Score: 42.52 E-value: 4.69e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 499169315 40 SEELRRGITIKIGFadaeiRRCPNCGRYSTSPVCPYCGHETEFVRR 85
Cdd:pfam03833 607 YAENKGEIEVEIGR-----RRCPNCGKETFENRCPDCGAHTEPVYV 647
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
13-163 |
6.43e-04 |
|
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: 41.04 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 13 NIGMVGHVDHGKTTLTKAL---TGV------------WTDTHSEELRRGITIKIGFADAEirrcpncgrystspvcpYCG 77
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALlyaTGAidrlgrvedgntVSDYDPEEKKRKMSIETSVAPLE-----------------WNG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 78 HetefvrRVSFIDAPG-----HEALmtTMLAGAslmDGAILVIAAnEPCPRPQTREHLMALQiigQKNI--IIAQNKIEL 150
Cdd:cd04170 64 H------KINLIDTPGyadfvGETL--SALRAV---DAALIVVEA-QSGVEVGTEKVWEFLD---DAKLprIIFINKMDR 128
|
170
....*....|....*
gi 499169315 151 --VDKEKALENYRQI 163
Cdd:cd04170 129 arADFDKTLAALREA 143
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
112-199 |
6.49e-04 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 40.17 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 112 ILVIAANEPcprpQTREHLMALQIIGQKNIIIAQNKIELVDKEKALENyrqikefiegtvAENAPIIPISALHGANIDVL 191
Cdd:cd04164 87 LLVVDASEG----LDEEDLEILELPAKKPVIVVLNKSDLLSDAEGISE------------LNGKPIIAISAKTGEGIDEL 150
|
....*...
gi 499169315 192 VKAIEDFI 199
Cdd:cd04164 151 KEALLELA 158
|
|
| PRK04023 |
PRK04023 |
DNA polymerase II large subunit; Validated |
50-85 |
8.67e-04 |
|
DNA polymerase II large subunit; Validated
Pssm-ID: 235202 [Multi-domain] Cd Length: 1121 Bit Score: 41.82 E-value: 8.67e-04
10 20 30
....*....|....*....|....*....|....*...
gi 499169315 50 KIGFADAEI--RRCPNCGRYSTSPVCPYCGHETEFVRR 85
Cdd:PRK04023 616 YKGTIEVEIgrRKCPSCGKETFYRRCPFCGTHTEPVYR 653
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
109-197 |
1.14e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.07 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 109 DGAILVIAANEPCPRPqtreHLM--ALQIIGQKNI--IIAQNKIELVDKEKA---LENYRQIkefiegtvaeNAPIIPIS 181
Cdd:cd01854 4 DQVLIVFSLKEPFFNL----RLLdrYLVAAEASGIepVIVLNKADLVDDEELeelLEIYEKL----------GYPVLAVS 69
|
90
....*....|....*.
gi 499169315 182 ALHGANIDVLVKAIED 197
Cdd:cd01854 70 AKTGEGLDELRELLKG 85
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
232-317 |
1.53e-03 |
|
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: 37.50 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 232 GGVLGGSIVQGKLKVGDEIEIrpgVPYEehgrikyEPITTEIVSLQAGGQFVEEAYPGGLVGV---GTKLDpyltkgDLM 308
Cdd:cd03697 15 GTVVTGRIERGVIKVGDEVEI---VGFK-------ETLKTTVTGIEMFRKTLDEAEAGDNVGVllrGVKKE------DVE 78
|
....*....
gi 499169315 309 AGNVVGKPG 317
Cdd:cd03697 79 RGMVLAKPG 87
|
|
| YlqF |
cd01856 |
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ... |
124-216 |
2.07e-03 |
|
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).
Pssm-ID: 206749 [Multi-domain] Cd Length: 171 Bit Score: 38.66 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 124 PQTREHLMALQIIGQKNIIIAQNKIELVDKEKalenYRQIKEFIEGtvaENAPIIPISALHGANIDVLVKAIEDFIPTPK 203
Cdd:cd01856 32 PLSSRNPDLDKILGNKPRLIVLNKADLADPAK----TKKWLKYFKS---QGEPVLFVNAKNGKGVKKLLKKAKKLLKENE 104
|
90
....*....|...
gi 499169315 204 RDPNKPPKMLVLR 216
Cdd:cd01856 105 KLKAKGLLPRPLR 117
|
|
| YqeH |
cd01855 |
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
132-205 |
2.16e-03 |
|
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.
Pssm-ID: 206748 [Multi-domain] Cd Length: 191 Bit Score: 38.78 E-value: 2.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499169315 132 ALQIIGQKNIIIAQNKIELVDKEKaleNYRQIKEFIEGTVAENAP----IIPISALHGANIDVLVKAIEDFIPtPKRD 205
Cdd:cd01855 54 LAELIGAKPVILVGNKIDLLPKDV---KPNRLKQWVKKRLKIGGLkikdVILVSAKKGWGVEELIEEIKKLAK-YRGD 127
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
231-317 |
2.32e-03 |
|
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: 37.17 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499169315 231 VGGVLGGSIVQGKLKVGDEIEIRPGvpyeehgrikyePITTEIVSLQAGGQFVEEAYPGGLVGVGTKLdpyLTKGDLMAG 310
Cdd:cd03693 18 IGTVPVGRVETGILKPGMVVTFAPA------------GVTGEVKSVEMHHEPLEEAIPGDNVGFNVKG---VSVKDIKRG 82
|
....*..
gi 499169315 311 NVVGKPG 317
Cdd:cd03693 83 DVAGDSK 89
|
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| PRK14714 |
PRK14714 |
DNA-directed DNA polymerase II large subunit; |
52-85 |
3.03e-03 |
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DNA-directed DNA polymerase II large subunit;
Pssm-ID: 237798 [Multi-domain] Cd Length: 1337 Bit Score: 40.06 E-value: 3.03e-03
10 20 30
....*....|....*....|....*....|....*.
gi 499169315 52 GFADAEI--RRCPNCGRYSTSPVCPYCGHETEFVRR 85
Cdd:PRK14714 659 GVIEVEVgrRRCPSCGTETYENRCPDCGTHTEPVYV 694
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