|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
13-452 |
0e+00 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 843.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 13 PHLSRQDLATLDVTKLTPLSREIISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLD 92
Cdd:PTZ00327 6 DGLAKQDLSKLDLDKLTPLTPEVISRQATINIGTIGHVAHGKSTVVKALSGVKTVRFKREKVRNITIKLGYANAKIYKCP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 93 DssCPRPECYRSCGSSTPDEFPSdiPGTKGNFRLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSE 172
Cdd:PTZ00327 86 K--CPRPTCYQSYGSSKPDNPPC--PGCGHKMTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQPQTSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 173 HLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPLRDFTS 252
Cdd:PTZ00327 162 HLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKRDLTS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 253 EPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDGEGKLMCKPIFSKIVSLFAEHNDLQYAA 332
Cdd:PTZ00327 242 PPRMIVIRSFDVNKPGEDIENLKGGVAGGSILQGVLKVGDEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNELQYAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 333 PGGLIGVGTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLS 412
Cdd:PTZ00327 322 PGGLIGVGTTIDPTLTRADRLVGQVLGYPGKLPEVYAEIEIQYYLLRRLLGVKSQDGKKATKVAKLKKGESLMINIGSTT 401
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1907207648 413 TGGRVSAVKAD-LGKIVLTNPVCTEVGEKIALSRRVEKHWR 452
Cdd:PTZ00327 402 TGGRVVGIKDDgIAKLELTTPVCTSVGEKIALSRRVDKHWR 442
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
38-452 |
0e+00 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 522.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 38 RQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLDDssCPRPECYRS------CGSSTpd 111
Cdd:PRK04000 6 VQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATIRKCPD--CEEPEAYTTepkcpnCGSET-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 112 efpsdipgtkgnfRLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNK 191
Cdd:PRK04000 82 -------------ELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 192 IDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPLRDFTSEPRLIVIRSFDVNKPGCEV 271
Cdd:PRK04000 149 IDLVSKERALENYEQIKEFVKGTVAENAPIIPVSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTPP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 272 DDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDGeGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRAD 351
Cdd:PRK04000 229 EKLKGGVIGGSLIQGVLKVGDEIEIRPGIKVEEG-GKTKWEPITTKIVSLRAGGEKVEEARPGGLVGVGTKLDPSLTKAD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 352 RMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEgdkkaAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTN 431
Cdd:PRK04000 308 ALAGSVAGKPGTLPPVWESLTIEVHLLERVVGTKEE-----LKVEPIKTGEPLMLNVGTATTVGVVTSARKDEAEVKLKR 382
|
410 420
....*....|....*....|.
gi 1907207648 432 PVCTEVGEKIALSRRVEKHWR 452
Cdd:PRK04000 383 PVCAEEGDRVAISRRVGGRWR 403
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
38-452 |
1.17e-177 |
|
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: 503.22 E-value: 1.17e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 38 RQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLDDssCPRPECY------RSCGSSTpd 111
Cdd:COG5257 2 KQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATFYKCPN--CEPPEAYttepkcPNCGSET-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 112 efpsdipgtkgnfRLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNK 191
Cdd:COG5257 78 -------------ELLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 192 IDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPLRDFTSEPRLIVIRSFDVNKPGCEV 271
Cdd:COG5257 145 IDLVSKERALENYEQIKEFVKGTVAENAPIIPVSAQHKVNIDALIEAIEEEIPTPERDLSKPPRMLVARSFDVNKPGTPP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 272 DDLKGGVAGGSILKGVLKVGQEIEVRPGI-VSKDGEGKLmcKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRA 350
Cdd:COG5257 225 KDLKGGVIGGSLIQGVLKVGDEIEIRPGIkVEKGGKTKY--EPITTTVVSLRAGGEEVEEAKPGGLVAVGTKLDPSLTKS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 351 DRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEgdkkaAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLT 430
Cdd:COG5257 303 DSLVGSVAGKPGTLPPVLDSLTMEVHLLERVVGTKEE-----VKVEPIKTGEPLMLNVGTATTVGVVTSARKDEIEVKLK 377
|
410 420
....*....|....*....|..
gi 1907207648 431 NPVCTEVGEKIALSRRVEKHWR 452
Cdd:COG5257 378 RPVCAEKGSRVAISRRIGGRWR 399
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
38-452 |
3.35e-172 |
|
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: 489.56 E-value: 3.35e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 38 RQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKldDSSCPRPECY------RSCGSSTpd 111
Cdd:TIGR03680 1 RQPEVNIGMVGHVDHGKTTLTKALTGVWTDTHSEELKRGISIRLGYADAEIYK--CPECDGPECYttepvcPNCGSET-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 112 efpsdipgtkgnfRLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNK 191
Cdd:TIGR03680 77 -------------ELLRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPCPQPQTKEHLMALEIIGIKNIVIVQNK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 192 IDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPLRDFTSEPRLIVIRSFDVNKPGCEV 271
Cdd:TIGR03680 144 IDLVSKEKALENYEEIKEFVKGTVAENAPIIPVSALHNANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNKPGTPP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 272 DDLKGGVAGGSILKGVLKVGQEIEVRPGI-VSKDGEGKLMckPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRA 350
Cdd:TIGR03680 224 EKLKGGVIGGSLIQGKLKVGDEIEIRPGIkVEKGGKTKWE--PIYTEITSLRAGGYKVEEARPGGLVGVGTKLDPALTKA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 351 DRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVrtegdKKAAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLT 430
Cdd:TIGR03680 302 DALAGQVVGKPGTLPPVWESLELEVHLLERVVGT-----EEELKVEPIKTGEVLMLNVGTATTVGVVTSARKDEIEVKLK 376
|
410 420
....*....|....*....|..
gi 1907207648 431 NPVCTEVGEKIALSRRVEKHWR 452
Cdd:TIGR03680 377 RPVCAEEGDRVAISRRVGGRWR 398
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
42-248 |
3.20e-136 |
|
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: 389.70 E-value: 3.20e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKlddssCPRPECYRSCgsstpDEFPSDIPGTK 121
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWTVRHKEELKRNITIKLGYANAKIYK-----CPNCGCPRPY-----DTPECECPGCG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 122 GNFRLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAK 201
Cdd:cd01888 71 GETKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907207648 202 EQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPLR 248
Cdd:cd01888 151 ENYEQIKEFVKGTIAENAPIIPISAQLKYNIDVLCEYIVKKIPTPPR 197
|
|
| eIF2_gamma_II |
cd03688 |
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily ... |
249-362 |
2.86e-68 |
|
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: 213.20 E-value: 2.86e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 249 DFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDGeGKLMCKPIFSKIVSLFAEHNDL 328
Cdd:cd03688 1 DLDKPPRMIVIRSFDVNKPGTEVDDLKGGVIGGSLIQGVLKVGDEIEIRPGIVVKKG-GKTTCRPIFTKIVSLFAEGNDL 79
|
90 100 110
....*....|....*....|....*....|....
gi 1907207648 329 QYAAPGGLIGVGTKIDPTLCRADRMVGQVLGAVG 362
Cdd:cd03688 80 EEAVPGGLIGVGTKLDPTLTKADRLVGQVVGEPG 113
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
42-299 |
1.50e-44 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 164.70 E-value: 1.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIyklddsscprpecyrscgsstpdefPSDipgtk 121
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGIDTDRLKEEKKRGITIDLGFAYLPL-------------------------PDG----- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 122 gnfrlvRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAK 201
Cdd:COG3276 51 ------RRLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAADEG-VMPQTREHLAILDLLGIKRGIVVLTKADLVDEEWLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 202 EQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKI-PVPLRDFTSEPRLIVIRSFDVnkpgcevddlKG-G-V 278
Cdd:COG3276 124 LVEEEIRELLAGTFLEDAPIVPVSAVTGEGIDELRAALDALAaAVPARDADGPFRLPIDRVFSI----------KGfGtV 193
|
250 260
....*....|....*....|.
gi 1907207648 279 AGGSILKGVLKVGQEIEVRPG 299
Cdd:COG3276 194 VTGTLLSGTVRVGDELELLPS 214
|
|
| eIF2_gamma_III |
cd15490 |
Domain III of eukaryotic initiation factor eIF2 gamma; This family represents the C-terminal ... |
365-452 |
5.50e-42 |
|
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: 143.81 E-value: 5.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 365 PEIFTELEISYFLLRRLLGVRTEgdkkaAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALS 444
Cdd:cd15490 1 PPVYTELEIEYHLLERVVGVKEE-----IKVEKIKKGEVLMLNIGSATTGGVVTSVKKDEAEVELKRPVCAEIGERVAIS 75
|
....*...
gi 1907207648 445 RRVEKHWR 452
Cdd:cd15490 76 RRIDGRWR 83
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
44-239 |
4.70e-39 |
|
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: 138.89 E-value: 4.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 44 IGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAkiyklddsscprpecyrscgsstpdEFPSDipgtkgn 123
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGIETDRLPEEKKRGITIDLGFAYL-------------------------DLPDG------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 124 frlvRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQ 203
Cdd:cd04171 50 ----KRLGFIDVPGHEKFVKNMLAGAGGIDAVLLVVAADEGI-MPQTREHLEILELLGIKKGLVVLTKADLVDEDRLELV 124
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907207648 204 YEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYI 239
Cdd:cd04171 125 EEEILELLAGTFLADAPIFPVSSVTGEGIEELKNYL 160
|
|
| eIF2_C |
pfam09173 |
Initiation factor eIF2 gamma, C terminal; Members of this family, which are found in the ... |
369-452 |
9.95e-37 |
|
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: 129.93 E-value: 9.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 369 TELEISYFLLRRLLGVRTEgdkkaAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALSRRVE 448
Cdd:pfam09173 1 TELEIEYHLLERVVGVKEE-----KKVEPIKKGEVLMLNVGTATTGGVVTSVKKDEAEVELKKPVCAEKGERVAISRRIG 75
|
....
gi 1907207648 449 KHWR 452
Cdd:pfam09173 76 GRWR 79
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
43-246 |
2.64e-29 |
|
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: 113.16 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 43 NIGTIGHVAHGKSTVVKAISGV-------HTVRF------KNELERNITIKLGYANAKIYKlddsscprpecyrscgsst 109
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQtgaidrrGTRKEtfldtlKEERERGITIKTGVVEFEWPK------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 110 pdefpsdipgtkgnfrlvRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKhILILQ 189
Cdd:cd00881 62 ------------------RRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEG-VEPQTREHLNIALAGGLP-IIVAV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907207648 190 NKIDLVKESQAKEQYEQILAFVQGTVA-----EGAPIIPISAQLKYNIEVVCEYIVKKIPVP 246
Cdd:cd00881 122 NKIDRVGEEDFDEVLREIKELLKLIGFtflkgKDVPIIPISALTGEGIEELLDAIVEHLPPP 183
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
42-298 |
4.55e-28 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 117.28 E-value: 4.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYAnakiyklddsSCPRPEcyrscgsstpdefpsdipgtk 121
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAADRLPEEKKRGMTIDLGFA----------YFPLPD--------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 122 gnfrlvRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAK 201
Cdd:TIGR00475 50 ------YRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDADEG-VMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 202 EQYEQILAFVQGTV-AEGAPIIPISAQLKYNIEVVCEYIvKKIPVPL--RDFTSEPRLIVIRSFDVNKPGCevddlkggV 278
Cdd:TIGR00475 123 RTEMFMKQILNSYIfLKNAKIFKTSAKTGQGIGELKKEL-KNLLESLdiKRIQKPLRMAIDRAFKVKGAGT--------V 193
|
250 260
....*....|....*....|
gi 1907207648 279 AGGSILKGVLKVGQEIEVRP 298
Cdd:TIGR00475 194 VTGTAFSGEVKVGDNLRLLP 213
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
42-244 |
8.61e-27 |
|
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: 106.46 E-value: 8.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVV-------KAISGVHTVRFKNEL---------ERNITIKlgyanakiyklddsscprpecyrsc 105
Cdd:pfam00009 4 RNIGIIGHVDHGKTTLTdrllyytGAISKRGEVKGEGEAgldnlpeerERGITIK------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 106 gsSTPDEFPSDIpgtkgnfrlvRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHI 185
Cdd:pfam00009 59 --SAAVSFETKD----------YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-VMPQTREHLRLARQLGVPII 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907207648 186 LILqNKIDLVKES---QAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIP 244
Cdd:pfam00009 126 VFI-NKMDRVDGAeleEVVEEVSRELLEKYGEDGEFVPVVPGSALKGEGVQTLLDALDEYLP 186
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
42-226 |
2.07e-25 |
|
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: 102.83 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKAISGV-HTVRF-KN--ELERNITIKLGYanakiyklddSSCprpecyrscgssTPDEFPSDI 117
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIaSTAAFdKNpqSQERGITLDLGF----------SSF------------EVDKPKHLE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 118 PGTKGNFRLVRhVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILqNKIDLVKE 197
Cdd:cd01889 59 DNENPQIENYQ-ITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-IQTQTAECLVIGELLCKPLIVVL-NKIDLIPE 135
|
170 180 190
....*....|....*....|....*....|...
gi 1907207648 198 SQAKEQYEQILAFVQGTVA----EGAPIIPISA 226
Cdd:cd01889 136 EERKRKIEKMKKRLQKTLEktrlKDSPIIPVSA 168
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
31-296 |
9.78e-23 |
|
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: 99.47 E-value: 9.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 31 LSREIISR-QATINIGTIGHVAHGKSTVVKAISGVHTvrfknelernitiKLGYANAKIYKLDDSScprPEcYRSCG--- 106
Cdd:TIGR00485 1 MAKEKFERtKPHVNVGTIGHVDHGKTTLTAAITTVLA-------------KEGGAAARAYDQIDNA---PE-EKARGiti 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 107 SSTPDEFPSDipgtkgnfrlVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHIL 186
Cdd:TIGR00485 64 NTAHVEYETE----------TRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGVPYIV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 187 ILQNKIDLVKEsqakeqyEQILAFVQGTVAE----------GAPIIPISAqLKyNIEVVCEYIVK----------KIPVP 246
Cdd:TIGR00485 133 VFLNKCDMVDD-------EELLELVEMEVREllsqydfpgdDTPIIRGSA-LK-ALEGDAEWEAKilelmdavdeYIPTP 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907207648 247 LRDfTSEPRLIVIRS-FDVNKpgcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:TIGR00485 204 ERE-IDKPFLLPIEDvFSITG--------RGTVVTGRVERGIIKVGEEVEI 245
|
|
| tufA |
CHL00071 |
elongation factor Tu |
31-296 |
2.15e-22 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 98.88 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 31 LSREIISRQAT-INIGTIGHVAHGKSTVVKAISGVHTVRfknelernitiklgyANAKIYKLDDSSCPRPECYRSCGSST 109
Cdd:CHL00071 1 MAREKFERKKPhVNIGTIGHVDHGKTTLTAAITMTLAAK---------------GGAKAKKYDEIDSAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 110 PD-EFPSDipgtkgnfrlVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILIL 188
Cdd:CHL00071 66 AHvEYETE----------NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTKEHILLAKQVGVPNIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 189 QNKIDLVKEsqakeqyEQILAFVQGTVAE----------GAPIIPISAQLK---------------------YN-IEVVC 236
Cdd:CHL00071 135 LNKEDQVDD-------EELLELVELEVREllskydfpgdDIPIVSGSALLAlealtenpkikrgenkwvdkiYNlMDAVD 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907207648 237 EYivkkIPVPLRDfTSEPRLIVIRS-FDVnkPGcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:CHL00071 208 SY----IPTPERD-TDKPFLMAIEDvFSI--TG------RGTVATGRIERGTVKVGDTVEI 255
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
42-296 |
1.50e-20 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 93.09 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKAISGVHTVRFKN-------------ELERNITIKLGYAnakiyklddsscprpecyrscgss 108
Cdd:PRK12736 13 VNIGTIGHVDHGKTTLTAAITKVLAERGLNqakdydsidaapeEKERGITINTAHV------------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 109 tpdEFPSDipgtkgnfrlVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILIL 188
Cdd:PRK12736 69 ---EYETE----------KRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLARQVGVPYLVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 189 QNKIDLVKEsqakeqyEQILAFVQGTVAE----------GAPIIPISA------------QLKYNIEVVCEYivkkIPVP 246
Cdd:PRK12736 135 LNKVDLVDD-------EELLELVEMEVREllseydfpgdDIPVIRGSAlkalegdpkwedAIMELMDAVDEY----IPTP 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907207648 247 LRDfTSEPRLIVIRsfDV-NKPGcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:PRK12736 204 ERD-TDKPFLMPVE--DVfTITG------RGTVVTGRVERGTVKVGDEVEI 245
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
44-291 |
4.76e-20 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 92.81 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 44 IGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYAnakiYklddssCPRPEcyrscGSStpdefpsdipgtkgn 123
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYA----Y------WPQPD-----GRV--------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 124 frlvrhVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQ 203
Cdd:PRK10512 53 ------LGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGV-MAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 204 YEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVK---KIPVPLRDFtsepRLIVIRSFDVNKPGCevddlkggVAG 280
Cdd:PRK10512 126 RRQVKAVLREYGFAEAKLFVTAATEGRGIDALREHLLQlpeREHAAQHRF----RLAIDRAFTVKGAGL--------VVT 193
|
250
....*....|.
gi 1907207648 281 GSILKGVLKVG 291
Cdd:PRK10512 194 GTALSGEVKVG 204
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
42-296 |
1.10e-19 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 90.63 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKAISGVHTVRFKN-------------ELERNITIklgyanakiyklddsscprpecyrscgSS 108
Cdd:PRK00049 13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGAeakaydqidkapeEKARGITI---------------------------NT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 109 TPDEFPSDipgtkgnfrlVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILIL 188
Cdd:PRK00049 66 AHVEYETE----------KRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 189 QNKIDLVKEsqakeqyEQILAFVQGTVAE----------GAPIIPISAQLKYN--------------IEVVCEYIvkkiP 244
Cdd:PRK00049 135 LNKCDMVDD-------EELLELVEMEVREllskydfpgdDTPIIRGSALKALEgdddeewekkilelMDAVDSYI----P 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907207648 245 VPLRDfTSEPRLIVIRsfDV-NKPGcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:PRK00049 204 TPERA-IDKPFLMPIE--DVfSISG------RGTVVTGRVERGIIKVGEEVEI 247
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
42-296 |
2.74e-19 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 89.88 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKAISGVHTvrfknelernitiKLGYANAKIYKLDDSScPRPECYRSCGSSTPDEFPSDipgtk 121
Cdd:PLN03127 62 VNVGTIGHVDHGKTTLTAAITKVLA-------------EEGKAKAVAFDEIDKA-PEEKARGITIATAHVEYETA----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 122 gnfrlVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAK 201
Cdd:PLN03127 123 -----KRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDG-PMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 202 EQYE----QILAFVQGTvAEGAPII---PISAQLKYNIEVVCEYIVK-------KIPVPLRDfTSEPRLIVIRS-FDVNK 266
Cdd:PLN03127 197 ELVEmelrELLSFYKFP-GDEIPIIrgsALSALQGTNDEIGKNAILKlmdavdeYIPEPVRV-LDKPFLMPIEDvFSIQG 274
|
250 260 270
....*....|....*....|....*....|
gi 1907207648 267 pgcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:PLN03127 275 --------RGTVATGRVEQGTIKVGEEVEI 296
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
42-296 |
1.10e-18 |
|
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: 87.51 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKAISGVHTVRFKN-------------ELERNITIklgyANAKIyklddsscprpecyrscgss 108
Cdd:COG0050 13 VNIGTIGHVDHGKTTLTAAITKVLAKKGGAkakaydqidkapeEKERGITI----NTSHV-------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 109 tpdEFPSDIpgtkgnfrlvRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILIL 188
Cdd:COG0050 69 ---EYETEK----------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-PMPQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 189 QNKIDLVKEsqakeqyEQILAFVQGTVAE----------GAPIIPISAQLKYNIEVVCEYiVKK-----------IPVPL 247
Cdd:COG0050 135 LNKCDMVDD-------EELLELVEMEVREllskygfpgdDTPIIRGSALKALEGDPDPEW-EKKilelmdavdsyIPEPE 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907207648 248 RDfTSEPRLIVIRsfDV-NKPGcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:COG0050 207 RD-TDKPFLMPVE--DVfSITG------RGTVVTGRVERGIIKVGDEVEI 247
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
42-296 |
2.95e-18 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 86.43 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKAISGVHTVRFKNEL-------------ERNITIklgyANAKIyklddsscprpecyrscgss 108
Cdd:PRK12735 13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAkaydqidnapeekARGITI----NTSHV-------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 109 tpdEFPSDIpgtkgnfrlvRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILIL 188
Cdd:PRK12735 69 ---EYETAN----------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-PMPQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 189 QNKIDLVKEsqakeqyEQILAFVQGTVAE----------GAPIIPISAQLKYNIEVVCEYIVK----------KIPVPLR 248
Cdd:PRK12735 135 LNKCDMVDD-------EELLELVEMEVREllskydfpgdDTPIIRGSALKALEGDDDEEWEAKilelmdavdsYIPEPER 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907207648 249 DfTSEPRLIVIRsfDV-NKPGcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:PRK12735 208 A-IDKPFLMPIE--DVfSISG------RGTVVTGRVERGIVKVGDEVEI 247
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
42-338 |
1.03e-17 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 84.98 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKAI---SGV---HTV----------------------RFKNELERNITIKLGYAnakiykldd 93
Cdd:PRK12317 7 LNLAVIGHVDHGKSTLVGRLlyeTGAideHIIeelreeakekgkesfkfawvmdRLKEERERGVTIDLAHK--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 94 sscprpecyrscgsstpdEFPSDipgtKGNFRLVrhvsfvDCPGHDILMATMLNGAAVMDAALLLIAGNES-CPQPQTSE 172
Cdd:PRK12317 78 ------------------KFETD----KYYFTIV------DCPGHRDFVKNMITGASQADAAVLVVAADDAgGVMPQTRE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 173 HLAAIEIMKLKHILILQNKIDLVKESQA-----KEQYEQILAFVqGTVAEGAPIIPISAQLKYNI------------EVV 235
Cdd:PRK12317 130 HVFLARTLGINQLIVAINKMDAVNYDEKryeevKEEVSKLLKMV-GYKPDDIPFIPVSAFEGDNVvkksenmpwyngPTL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 236 CEYIvKKIPVPLRDfTSEPRLIVIRsfDV-NKPGCevddlkGGVAGGSILKGVLKVGQEIEVRPGivSKDGEGKlmckpi 314
Cdd:PRK12317 209 LEAL-DNLKPPEKP-TDKPLRIPIQ--DVySISGV------GTVPVGRVETGVLKVGDKVVFMPA--GVVGEVK------ 270
|
330 340
....*....|....*....|....
gi 1907207648 315 fskivSLFAEHNDLQYAAPGGLIG 338
Cdd:PRK12317 271 -----SIEMHHEELPQAEPGDNIG 289
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
42-195 |
1.18e-17 |
|
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: 81.09 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKAISGVHTvrfknelernitiKLGYANAKIYKLDDSScprPEcYRSCG---SSTPDEFPSDip 118
Cdd:cd01884 3 VNVGTIGHVDHGKTTLTAAITKVLA-------------KKGGAKAKKYDEIDKA---PE-EKARGitiNTAHVEYETA-- 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907207648 119 gtkgnfrlVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILQNKIDLV 195
Cdd:cd01884 64 --------NRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDG-PMPQTREHLLLARQVGVPYIVVFLNKADMV 131
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
42-296 |
1.78e-17 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 84.67 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKAISGVhtvrfknelerniTIKLGYANAKIYKLDDSScprPEcYRSCG---SSTPDEFPSDip 118
Cdd:PLN03126 82 VNIGTIGHVDHGKTTLTAALTMA-------------LASMGGSAPKKYDEIDAA---PE-ERARGitiNTATVEYETE-- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 119 gtkgnfrlVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILQNKIDLVKEs 198
Cdd:PLN03126 143 --------NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADG-PMPQTKEHILLAKQVGVPNMVVFLNKQDQVDD- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 199 qakeqyEQILAFVQGTVAE----------GAPIIPISAQLKYN------------------IEVVCEYIVKKIPVPLRDf 250
Cdd:PLN03126 213 ------EELLELVELEVREllssyefpgdDIPIISGSALLALEalmenpnikrgdnkwvdkIYELMDAVDSYIPIPQRQ- 285
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907207648 251 TSEPRLIVIRS-FDVNKpgcevddlKGGVAGGSILKGVLKVGQEIEV 296
Cdd:PLN03126 286 TDLPFLLAVEDvFSITG--------RGTVATGRVERGTVKVGETVDI 324
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
42-338 |
2.89e-17 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 83.44 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKAI---SGV---HTV----------------------RFKNELERNITIKLGYAnakiykldd 93
Cdd:COG5256 8 LNLVVIGHVDHGKSTLVGRLlyeTGAideHIIekyeeeaekkgkesfkfawvmdRLKEERERGVTIDLAHK--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 94 sscprpecyrscgsstpdEFPSDipgtKGNFRLVrhvsfvDCPGHDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEH 173
Cdd:COG5256 79 ------------------KFETD----KYYFTII------DAPGHRDFVKNMITGASQADAAILVVSAKDG-VMGQTREH 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 174 LAAIEIMKLKHILILQNKIDLVKESQA-----KEQYEQILAFVqGTVAEGAPIIPISAQLKYNI---------------- 232
Cdd:COG5256 130 AFLARTLGINQLIVAVNKMDAVNYSEKryeevKEEVSKLLKMV-GYKVDKIPFIPVSAWKGDNVvkksdnmpwyngptll 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 233 EVVCEYIVKKIPV--PLRdftseprlIVIRsfDV-NKPGCevddlkGGVAGGSILKGVLKVGQEIEVRPgiVSKDGEGKl 309
Cdd:COG5256 209 EALDNLKEPEKPVdkPLR--------IPIQ--DVySISGI------GTVPVGRVETGVLKVGDKVVFMP--AGVVGEVK- 269
|
330 340
....*....|....*....|....*....
gi 1907207648 310 mckpifskivSLFAEHNDLQYAAPGGLIG 338
Cdd:COG5256 270 ----------SIEMHHEELEQAEPGDNIG 288
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
133-232 |
3.85e-10 |
|
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: 59.51 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 133 VDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQakEQYEQI----L 208
Cdd:cd04166 83 ADTPGHEQYTRNMVTGASTADLAILLVDARKGV-LEQTRRHSYIASLLGIRHVVVAVNKMDLVDYDE--EVFEEIkadyL 159
|
90 100
....*....|....*....|....
gi 1907207648 209 AFVQGTVAEGAPIIPISAQLKYNI 232
Cdd:cd04166 160 AFAASLGIEDITFIPISALEGDNV 183
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
26-313 |
7.22e-10 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 61.39 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 26 TKLTPLSREIISRQATIN---IGTI-GHVAHGKSTVVKAIsgvHTVRFKNELERNITIKLGyANAKIYKLDDSScprpec 101
Cdd:CHL00189 225 EKTSNLDNTSAFTENSINrppIVTIlGHVDHGKTTLLDKI---RKTQIAQKEAGGITQKIG-AYEVEFEYKDEN------ 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 102 yrscgsstpdefpsdipgtkgnfrlvRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAAIEIMK 181
Cdd:CHL00189 295 --------------------------QKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGV-KPQTIEAINYIQAAN 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 182 LKhILILQNKIDlvKESQAKEQYEQILAfVQGTVAEG----APIIPISAQLKYNIEVVCEYIV--------KKIPvplrd 249
Cdd:CHL00189 348 VP-IIVAINKID--KANANTERIKQQLA-KYNLIPEKwggdTPMIPISASQGTNIDKLLETILllaeiedlKADP----- 418
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907207648 250 fTSEPRLIVIRSFdvnkpgceVDDLKGGVAGGSILKGVLKVGQEI-------EVRpGIVSKDGEGKLMCKP 313
Cdd:CHL00189 419 -TQLAQGIILEAH--------LDKTKGPVATILVQNGTLHIGDIIvigtsyaKIR-GMINSLGNKINLATP 479
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
276-359 |
7.95e-10 |
|
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: 54.96 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 276 GGVAGGSILKGVLKVGQEIEVRPGIVSKdgegklmcKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPtlcRADRMVG 355
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGK--------KKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVG---LEDIRVG 69
|
....
gi 1907207648 356 QVLG 359
Cdd:pfam03144 70 DTLT 73
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
42-306 |
8.61e-10 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 60.72 E-value: 8.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKA-ISG----------VHTVRFKNELERNITIKLGYAnakIYKLDDSS---CPRPEcyrscgs 107
Cdd:COG5258 123 IVVGVAGHVDHGKSTLVGTlVTGklddgnggtrSFLDVQPHEVERGLSADLSYA---VYGFDDDGpvrMKNPL------- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 108 STPDEfpsdipgtkgnFRLV----RHVSFVDCPGHDILMATMLNG--AAVMDAALLLIAGNEScPQPQTSEHLAAIEIMK 181
Cdd:COG5258 193 RKTDR-----------ARVVeesdKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDG-PTHTTREHLGILLAMD 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 182 LKhILILQNKIDLVKESQAKE---QYEQILAFVQGTV--------AEGA---------PIIPISAQLKYNIEVVCEYIvK 241
Cdd:COG5258 261 LP-VIVAITKIDKVDDERVEEverEIENLLRIVGRTPlevesrhdVDAAieeingrvvPILKTSAVTGEGLDLLDELF-E 338
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907207648 242 KIPVPLRDFTSEPRLIVIRSFDVnkPGCevddlkGGVAGGSILKGVLKVGQEIEVRPgivSKDGE 306
Cdd:COG5258 339 RLPKRATDEDEPFLMYIDRIYNV--TGV------GTVVSGTVKSGKVEAGDELLIGP---TKDGS 392
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
43-226 |
2.28e-09 |
|
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: 57.50 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 43 NIGTIGHVAHGKSTVVKAI---SGV---HTV----------------------RFKNELERNITIKLGYAnakiykldds 94
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLlykLGGvdkRTIekyekeakemgkesfkyawvldKLKEERERGVTIDVGLA---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 95 scprpecyrscgsstpdEFPSDipgtkgnfrlVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESC------PQP 168
Cdd:cd01883 71 -----------------KFETE----------KYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEfeagfeKGG 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907207648 169 QTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQI----LAFVQ--GTVAEGAPIIPISA 226
Cdd:cd01883 124 QTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIkkkvSPFLKkvGYNPKDVPFIPISG 187
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
131-306 |
3.81e-08 |
|
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: 55.48 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 131 SFV--DCPGH-----DilMATmlnGAAVMDAALLLI-AGNEScpQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKe 202
Cdd:COG2895 96 KFIiaDTPGHeqytrN--MVT---GASTADLAILLIdARKGV--LEQTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEV- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 203 qYEQI----LAFVQGTVAEGAPIIPISAqLK-------------YNIEVVCEYIvKKIPVPlRDFTSEP-RLIVIrsfDV 264
Cdd:COG2895 168 -FEEIvadyRAFAAKLGLEDITFIPISA-LKgdnvversenmpwYDGPTLLEHL-ETVEVA-EDRNDAPfRFPVQ---YV 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907207648 265 NKPGcevDDLKgGVAgGSILKGVLKVGQEIEVRP--------GIVSKDGE 306
Cdd:COG2895 241 NRPN---LDFR-GYA-GTIASGTVRVGDEVVVLPsgktstvkSIVTFDGD 285
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
132-253 |
7.99e-08 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 53.51 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 132 FVDCPG--------HDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILqNKIDLVKEsqaKEQ 203
Cdd:PRK00089 57 FVDTPGihkpkralNRAMNKAAWSSLKDVDLVLFVVDADEK-IGPGDEFILEKLKKVKTPVILVL-NKIDLVKD---KEE 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907207648 204 YEQILAFVQGTVaEGAPIIPISAQLKYNIEVVCEYIVKKIPV-------------PLRDFTSE 253
Cdd:PRK00089 132 LLPLLEELSELM-DFAEIVPISALKGDNVDELLDVIAKYLPEgppyypedqitdrPERFLAAE 193
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
134-334 |
1.33e-07 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 53.76 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 134 DCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQakEQYEQI----LA 209
Cdd:PRK05124 113 DTPGHEQYTRNMATGASTCDLAILLIDARKGV-LDQTRRHSFIATLLGIKHLVVAVNKMDLVDYSE--EVFERIredyLT 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 210 FVQ--GTVAEgAPIIPISAqLK-------------YNIEVVCEyIVKKIPVPlRDFTSEP-RLIVIRsfdVNKPGCEVDD 273
Cdd:PRK05124 190 FAEqlPGNLD-IRFVPLSA-LEgdnvvsqsesmpwYSGPTLLE-VLETVDIQ-RVVDAQPfRFPVQY---VNRPNLDFRG 262
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907207648 274 LKGGVAGGSIlkgvlKVGQEIEVRP-GIVSKdgegklmckpiFSKIVSLfaeHNDLQYAAPG 334
Cdd:PRK05124 263 YAGTLASGVV-----KVGDRVKVLPsGKESN-----------VARIVTF---DGDLEEAFAG 305
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
120-260 |
1.52e-07 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 52.68 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 120 TKGNFRLVrhvsFVDCPG--------HDILMATMLNGAAVMDAALLLIAGNEScPQPQTSEHLAAIEIMKLKHILILqNK 191
Cdd:COG1159 47 TREDAQIV----FVDTPGihkpkrklGRRMNKAAWSALEDVDVILFVVDATEK-IGEGDEFILELLKKLKTPVILVI-NK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 192 IDLVKesqaKEQYEQILAFVQGTvAEGAPIIPISAQLKYNIEVVCEYIVKKIPV-------------PLRDFTSEprliV 258
Cdd:COG1159 121 IDLVK----KEELLPLLAEYSEL-LDFAEIVPISALKGDNVDELLDEIAKLLPEgppyypedqitdrPERFLAAE----I 191
|
..
gi 1907207648 259 IR 260
Cdd:COG1159 192 IR 193
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
43-246 |
5.39e-07 |
|
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: 49.45 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 43 NIGTIGHVAHGKSTVVKAI---SGVHTVRFKN---------ELERNITIKLgyANAKI-YKLDDsscprpecyrscgsst 109
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSEREMKeqvldsmdlERERGITIKA--QAVRLfYKAKD---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 110 pdefpsdipgtKGNFRLvrhvSFVDCPGH-DI-------LMATmlngaavmDAALLLIAGNESCpQPQTSEHL-AAIEiM 180
Cdd:cd01890 64 -----------GEEYLL----NLIDTPGHvDFsyevsrsLAAC--------EGALLVVDATQGV-EAQTLANFyLALE-N 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907207648 181 KLKHILILqNKIDLVKES--QAKEQYEQILafvqGTVAEGApiIPISAQLKYNIEVVCEYIVKKIPVP 246
Cdd:cd01890 119 NLEIIPVI-NKIDLPAADpdRVKQEIEDVL----GLDASEA--ILVSAKTGLGVEDLLEAIVERIPPP 179
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
254-351 |
8.51e-07 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 46.49 E-value: 8.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 254 PRLIVIRSFDVNKpgcevddlKGGVAGGSILKGVLKVGQEIEVRPgivskdgegklmcKPIFSKIVSLFAEHNDLQYAAP 333
Cdd:cd01342 1 LVMQVFKVFYIPG--------RGRVAGGRVESGTLKVGDEIRILP-------------KGITGRVTSIERFHEEVDEAKA 59
|
90
....*....|....*...
gi 1907207648 334 GGLIGVGTKIDPTLCRAD 351
Cdd:cd01342 60 GDIVGIGILGVKDILTGD 77
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
132-241 |
7.06e-06 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 45.91 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 132 FVDCPGHD--------ILMATMLNGAavmDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQ 203
Cdd:cd00882 51 LVDTPGLDefgglgreELARLLLRGA---DLILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEEL 127
|
90 100 110
....*....|....*....|....*....|....*...
gi 1907207648 204 YEQILAFVQgtvaEGAPIIPISAQLKYNIEVVCEYIVK 241
Cdd:cd00882 128 LRLEELAKI----LGVPVFEVSAKTGEGVDELFEKLIE 161
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
134-306 |
8.73e-06 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 48.00 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 134 DCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKeqYEQI----LA 209
Cdd:PRK05506 110 DTPGHEQYTRNMVTGASTADLAIILVDARKGV-LTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEV--FDEIvadyRA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 210 FVQGTVAEGAPIIPISAQLKYNIEVVCE----Y-------IVKKIPVPLRDFTSEPRLIVIRsfdVNKPGCEVDDLKGGV 278
Cdd:PRK05506 187 FAAKLGLHDVTFIPISALKGDNVVTRSArmpwYegpslleHLETVEIASDRNLKDFRFPVQY---VNRPNLDFRGFAGTV 263
|
170 180 190
....*....|....*....|....*....|..
gi 1907207648 279 AGGSILKG----VLKVGQEIEVRpGIVSKDGE 306
Cdd:PRK05506 264 ASGVVRPGdevvVLPSGKTSRVK-RIVTPDGD 294
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
129-342 |
1.05e-05 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 47.82 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 129 HVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNES------CPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKE 202
Cdd:PTZ00141 86 YFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGefeagiSKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 203 QYEQILAFVQ------GTVAEGAPIIPISAQLKYN-IEVVCEYIVKKIP---------VPLRDFTSEPRLIVIRsfDVNK 266
Cdd:PTZ00141 166 RYDEIKKEVSaylkkvGYNPEKVPFIPISGWQGDNmIEKSDNMPWYKGPtllealdtlEPPKRPVDKPLRLPLQ--DVYK 243
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907207648 267 PGCevddlKGGVAGGSILKGVLKVGQEIEVRPGIVSKDgegklmCKpifskivSLFAEHNDLQYAAPGGLIGVGTK 342
Cdd:PTZ00141 244 IGG-----IGTVPVGRVETGILKPGMVVTFAPSGVTTE------VK-------SVEMHHEQLAEAVPGDNVGFNVK 301
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
120-242 |
1.28e-05 |
|
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: 45.53 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 120 TKGNFRLVrhvsFVDCPG----HDILMaTMLNGAAVM-----DAALLLIAGNESCPqPQTSEHLAAIEIMKLKHILILqN 190
Cdd:cd04163 47 TDDDAQII----FVDTPGihkpKKKLG-ERMVKAAWSalkdvDLVLFVVDASEWIG-EGDEFILELLKKSKTPVILVL-N 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907207648 191 KIDLVK-ESQAKEQYEQILAFVQGtvaegAPIIPISAQLKYNIEVVCEYIVKK 242
Cdd:cd04163 120 KIDLVKdKEDLLPLLEKLKELHPF-----AEIFPISALKGENVDELLEYIVEY 167
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
149-245 |
5.39e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 41.73 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 149 AAVMDAALLLIAGNEscpqPQTSEH-----LAAIEIMKLKHILILqNKIDLVKEsqaKEQYEQILAFVQGTvaeGAPIIP 223
Cdd:PRK00098 78 AANVDQAVLVFAAKE----PDFSTDlldrfLVLAEANGIKPIIVL-NKIDLLDD---LEEARELLALYRAI---GYDVLE 146
|
90 100
....*....|....*....|..
gi 1907207648 224 ISAQLKYNIEVVCEYIVKKIPV 245
Cdd:PRK00098 147 LSAKEGEGLDELKPLLAGKVTV 168
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
42-233 |
6.22e-04 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 40.73 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKSTVVKAISGvhtvRFKNELERNITIKlgyanAKIYKlddsscprpecyrscgsstpdefpSDIPGTK 121
Cdd:COG1100 4 KKIVVVGTGGVGKTSLVNRLVG----DIFSLEKYLSTNG-----VTIDK------------------------KELKLDG 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 122 GNFRLVrhvsFVDCPGHDI------LMATMLNGAavmDAALLLIAGNESCPQPQTSEHLAAIEIMKLKH-ILILQNKIDL 194
Cdd:COG1100 51 LDVDLV----IWDTPGQDEfretrqFYARQLTGA---SLYLFVVDGTREETLQSLYELLESLRRLGKKSpIILVLNKIDL 123
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907207648 195 VKESQAKEQYEQILAFVQgtvAEGAPIIPISAQLKYNIE 233
Cdd:COG1100 124 YDEEEIEDEERLKEALSE---DNIVEVVATSAKTGEGVE 159
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
33-193 |
8.10e-04 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 41.96 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 33 REIISRQATI-NIGTIGHVAHGKST-----VVKA--ISGVHT--VRF----KNELERNITIKlgyanakiyklddsscpr 98
Cdd:PTZ00416 10 REIMDNPDQIrNMSVIAHVDHGKSTltdslVCKAgiISSKNAgdARFtdtrADEQERGITIK------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 99 pecyrSCGSSTPDEFPSDIPGTKGNFRlvrhVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNES-CPQPQTSEHLAAI 177
Cdd:PTZ00416 72 -----STGISLYYEHDLEDGDDKQPFL----INLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGvCVQTETVLRQALQ 142
|
170
....*....|....*.
gi 1907207648 178 EimKLKHILILqNKID 193
Cdd:PTZ00416 143 E--RIRPVLFI-NKVD 155
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
129-224 |
8.18e-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: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 129 HVSFVDCPGHDILMATMLNGAAVMDAALLLIAGnESCPQPQTSEHLAAIEIMKLKHILILqNKIDlvkesQAKEQYEQIL 208
Cdd:cd04170 65 KINLIDTPGYADFVGETLSALRAVDAALIVVEA-QSGVEVGTEKVWEFLDDAKLPRIIFI-NKMD-----RARADFDKTL 137
|
90
....*....|....*.
gi 1907207648 209 AFVQGTVaeGAPIIPI 224
Cdd:cd04170 138 AALREAF--GRPVVPI 151
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
42-226 |
1.59e-03 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 40.84 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 42 INIGTIGHVAHGKST----VVKAISGVHT---VRFKNELERNITIKLGYAnakiYKLDDSSCPRPEcyrscgsstpdEFP 114
Cdd:PLN00043 8 INIVVIGHVDSGKSTttghLIYKLGGIDKrviERFEKEAAEMNKRSFKYA----WVLDKLKAERER-----------GIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 115 SDIPGTKgnFRLVRH-VSFVDCPGHDILMATMLNGAAVMDAALLLI----AGNES--CPQPQTSEHLAAIEIMKLKHILI 187
Cdd:PLN00043 73 IDIALWK--FETTKYyCTVIDAPGHRDFIKNMITGTSQADCAVLIIdsttGGFEAgiSKDGQTREHALLAFTLGVKQMIC 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907207648 188 LQNKIDLVKESQAKEQYEQILAFVQ------GTVAEGAPIIPISA 226
Cdd:PLN00043 151 CCNKMDATTPKYSKARYDEIVKEVSsylkkvGYNPDKIPFVPISG 195
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
153-243 |
1.65e-03 |
|
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440253 [Multi-domain] Cd Length: 448 Bit Score: 40.81 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 153 DAALLLIAGNEscpqPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQyeqilafvqgtVAEGAPIIPISAQLKYNI 232
Cdd:COG0486 294 DLVLLLLDASE----PLTEEDEEILEKLKDKPVIVVLNKIDLPSEADGELK-----------SLPGEPVIAISAKTGEGI 358
|
90
....*....|.
gi 1907207648 233 EVVCEYIVKKI 243
Cdd:COG0486 359 DELKEAILELV 369
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
178-243 |
2.04e-03 |
|
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: 38.94 E-value: 2.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907207648 178 EIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTvaegaPIIPISAQLKYNIEVVCEYIVKKI 243
Cdd:cd01898 110 PGLAEKPRIVVLNKIDLLDAEERFEKLKELLKELKGK-----KVFPISALTGEGLDELLKKLAKLL 170
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
132-196 |
3.72e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 39.87 E-value: 3.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907207648 132 FVDCPGHDILMATMLNGAAVMDAALLLIAGNESCpQPQTSEhlaAIEIMKL--KHILILQNKIDLVK 196
Cdd:PRK14845 530 FIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGF-KPQTIE---AINILRQykTPFVVAANKIDLIP 592
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
115-226 |
4.67e-03 |
|
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: 37.61 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907207648 115 SDIPGT-----KGNFRL--VRHVSFVDCPG-------HDILMATMLNGAAVMDAALLLIAGNESCPQPQtsEHLAAIEIM 180
Cdd:cd00880 26 SPIPGTtrdpvRKEWELlpLGPVVLIDTPGldeegglGRERVEEARQVADRADLVLLVVDSDLTPVEEE--AKLGLLRER 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907207648 181 KLKHILILqNKIDLVKESQAKEQYEQ-ILAFVQgtvaeGAPIIPISA 226
Cdd:cd00880 104 GKPVLLVL-NKIDLVPESEEEELLRErKLELLP-----DLPVIAVSA 144
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
174-243 |
8.91e-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: 37.38 E-value: 8.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907207648 174 LAAIEIMKLKHILILqNKIDLVKESQAKEQ---YEQIlafvqgtvaeGAPIIPISAQLKYNIEVVCEYIVKKI 243
Cdd:cd01854 26 LVAAEASGIEPVIVL-NKADLVDDEELEELleiYEKL----------GYPVLAVSAKTGEGLDELRELLKGKT 87
|
|
| |
