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Conserved domains on  [gi|569012472|ref|XP_006531673|]
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eukaryotic translation initiation factor 2 subunit 3, Y-linked isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00327 super family cl36550
eukaryotic translation initiation factor 2 gamma subunit; Provisional
1-287 0e+00

eukaryotic translation initiation factor 2 gamma subunit; Provisional


The actual alignment was detected with superfamily member PTZ00327:

Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 536.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472   1 MKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPLRDFTSEPRLIVI 80
Cdd:PTZ00327 169 MKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKRDLTSPPRMIVI 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472  81 RSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDGEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGV 160
Cdd:PTZ00327 249 RSFDVNKPGEDIENLKGGVAGGSILQGVLKVGDEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNELQYAVPGGLIGV 328
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472 161 GTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLSTGGRVSA 240
Cdd:PTZ00327 329 GTTIDPTLTRADRLVGQVLGYPGKLPEVYAEIEIQYYLLRRLLGVKSQDGKKATKVAKLKKGESLMINIGSTTTGGRVVG 408
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 569012472 241 VKAD-LGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIK 287
Cdd:PTZ00327 409 IKDDgIAKLELTTPVCTSVGEKIALSRRVDKHWRLIGWGTIRKGVPVK 456
 
Name Accession Description Interval E-value
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
1-287 0e+00

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 536.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472   1 MKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPLRDFTSEPRLIVI 80
Cdd:PTZ00327 169 MKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKRDLTSPPRMIVI 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472  81 RSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDGEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGV 160
Cdd:PTZ00327 249 RSFDVNKPGEDIENLKGGVAGGSILQGVLKVGDEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNELQYAVPGGLIGV 328
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472 161 GTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLSTGGRVSA 240
Cdd:PTZ00327 329 GTTIDPTLTRADRLVGQVLGYPGKLPEVYAEIEIQYYLLRRLLGVKSQDGKKATKVAKLKKGESLMINIGSTTTGGRVVG 408
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 569012472 241 VKAD-LGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIK 287
Cdd:PTZ00327 409 IKDDgIAKLELTTPVCTSVGEKIALSRRVDKHWRLIGWGTIRKGVPVK 456
eif2g_arch TIGR03680
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ...
1-281 2.51e-109

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: 322.77  E-value: 2.51e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472    1 MKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPLRDFTSEPRLIVI 80
Cdd:TIGR03680 132 IGIKNIVIVQNKIDLVSKEKALENYEEIKEFVKGTVAENAPIIPVSALHNANIDALLEAIEKFIPTPERDLDKPPLMYVA 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472   81 RSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDGeGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGV 160
Cdd:TIGR03680 212 RSFDVNKPGTPPEKLKGGVIGGSLIQGKLKVGDEIEIRPGIKVEKG-GKTKWEPIYTEITSLRAGGYKVEEARPGGLVGV 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472  161 GTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVrtegdKKAAKVQKLSKNEVLMVNIGSLSTGGRVSA 240
Cdd:TIGR03680 291 GTKLDPALTKADALAGQVVGKPGTLPPVWESLELEVHLLERVVGT-----EEELKVEPIKTGEVLMLNVGTATTVGVVTS 365
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 569012472  241 VKADLGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIR 281
Cdd:TIGR03680 366 ARKDEIEVKLKRPVCAEEGDRVAISRRVGGRWRLIGYGIIK 406
eIF2_gamma_II cd03688
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily ...
70-183 4.43e-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: 207.03  E-value: 4.43e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472  70 DFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDGeGKLMCKPIFSKIVSLFAEHNDL 149
Cdd:cd03688    1 DLDKPPRMIVIRSFDVNKPGTEVDDLKGGVIGGSLIQGVLKVGDEIEIRPGIVVKKG-GKTTCRPIFTKIVSLFAEGNDL 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 569012472 150 QYAAPGGLIGVGTKIDPTLCRADRMVGQVLGAVG 183
Cdd:cd03688   80 EEAVPGGLIGVGTKLDPTLTKADRLVGQVVGEPG 113
eIF2_C pfam09173
Initiation factor eIF2 gamma, C terminal; Members of this family, which are found in the ...
190-280 1.23e-42

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: 141.10  E-value: 1.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472  190 TELEISYFLLRRLLGVRTEgdkkaAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALSRRVE 269
Cdd:pfam09173   1 TELEIEYHLLERVVGVKEE-----KKVEPIKKGEVLMLNVGTATTGGVVTSVKKDEAEVELKKPVCAEKGERVAISRRIG 75
                          90
                  ....*....|.
gi 569012472  270 KHWRLIGWGQI 280
Cdd:pfam09173  76 GRWRLIGWGII 86
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
3-120 1.98e-10

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: 61.08  E-value: 1.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472   3 LKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKI-PVPLRDFTSEPRLIVIR 81
Cdd:COG3276  104 IKRGIVVLTKADLVDEEWLELVEEEIRELLAGTFLEDAPIVPVSAVTGEGIDELRAALDALAaAVPARDADGPFRLPIDR 183
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 569012472  82 SFDVnkpgcevddlKG-G-VAGGSILKGVLKVGQEIEVRPG 120
Cdd:COG3276  184 VFSI----------KGfGtVVTGTLLSGTVRVGDELELLPS 214
 
Name Accession Description Interval E-value
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
1-287 0e+00

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 536.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472   1 MKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPLRDFTSEPRLIVI 80
Cdd:PTZ00327 169 MKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKRDLTSPPRMIVI 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472  81 RSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDGEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGV 160
Cdd:PTZ00327 249 RSFDVNKPGEDIENLKGGVAGGSILQGVLKVGDEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNELQYAVPGGLIGV 328
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472 161 GTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLSTGGRVSA 240
Cdd:PTZ00327 329 GTTIDPTLTRADRLVGQVLGYPGKLPEVYAEIEIQYYLLRRLLGVKSQDGKKATKVAKLKKGESLMINIGSTTTGGRVVG 408
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 569012472 241 VKAD-LGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIK 287
Cdd:PTZ00327 409 IKDDgIAKLELTTPVCTSVGEKIALSRRVDKHWRLIGWGTIRKGVPVK 456
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
1-281 1.30e-117

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 343.76  E-value: 1.30e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472   1 MKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPLRDFTSEPRLIVI 80
Cdd:PRK04000 137 IGIKNIVIVQNKIDLVSKERALENYEQIKEFVKGTVAENAPIIPVSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVA 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472  81 RSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDGeGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGV 160
Cdd:PRK04000 217 RSFDVNKPGTPPEKLKGGVIGGSLIQGVLKVGDEIEIRPGIKVEEG-GKTKWEPITTKIVSLRAGGEKVEEARPGGLVGV 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472 161 GTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEgdkkaAKVQKLSKNEVLMVNIGSLSTGGRVSA 240
Cdd:PRK04000 296 GTKLDPSLTKADALAGSVAGKPGTLPPVWESLTIEVHLLERVVGTKEE-----LKVEPIKTGEPLMLNVGTATTVGVVTS 370
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 569012472 241 VKADLGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIR 281
Cdd:PRK04000 371 ARKDEAEVKLKRPVCAEEGDRVAISRRVGGRWRLIGYGIIK 411
eif2g_arch TIGR03680
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ...
1-281 2.51e-109

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: 322.77  E-value: 2.51e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472    1 MKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPLRDFTSEPRLIVI 80
Cdd:TIGR03680 132 IGIKNIVIVQNKIDLVSKEKALENYEEIKEFVKGTVAENAPIIPVSALHNANIDALLEAIEKFIPTPERDLDKPPLMYVA 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472   81 RSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDGeGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGV 160
Cdd:TIGR03680 212 RSFDVNKPGTPPEKLKGGVIGGSLIQGKLKVGDEIEIRPGIKVEKG-GKTKWEPIYTEITSLRAGGYKVEEARPGGLVGV 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472  161 GTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVrtegdKKAAKVQKLSKNEVLMVNIGSLSTGGRVSA 240
Cdd:TIGR03680 291 GTKLDPALTKADALAGQVVGKPGTLPPVWESLELEVHLLERVVGT-----EEELKVEPIKTGEVLMLNVGTATTVGVVTS 365
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 569012472  241 VKADLGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIR 281
Cdd:TIGR03680 366 ARKDEIEVKLKRPVCAEEGDRVAISRRVGGRWRLIGYGIIK 406
eIF2_gamma_II cd03688
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily ...
70-183 4.43e-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: 207.03  E-value: 4.43e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472  70 DFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDGeGKLMCKPIFSKIVSLFAEHNDL 149
Cdd:cd03688    1 DLDKPPRMIVIRSFDVNKPGTEVDDLKGGVIGGSLIQGVLKVGDEIEIRPGIVVKKG-GKTTCRPIFTKIVSLFAEGNDL 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 569012472 150 QYAAPGGLIGVGTKIDPTLCRADRMVGQVLGAVG 183
Cdd:cd03688   80 EEAVPGGLIGVGTKLDPTLTKADRLVGQVVGEPG 113
eIF2_gamma_III cd15490
Domain III of eukaryotic initiation factor eIF2 gamma; This family represents the C-terminal ...
186-280 3.05e-48

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: 155.75  E-value: 3.05e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472 186 PEIFTELEISYFLLRRLLGVRTEgdkkaAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALS 265
Cdd:cd15490    1 PPVYTELEIEYHLLERVVGVKEE-----IKVEKIKKGEVLMLNIGSATTGGVVTSVKKDEAEVELKRPVCAEIGERVAIS 75
                         90
                 ....*....|....*
gi 569012472 266 RRVEKHWRLIGWGQI 280
Cdd:cd15490   76 RRIDGRWRLIGWGII 90
eIF2_C pfam09173
Initiation factor eIF2 gamma, C terminal; Members of this family, which are found in the ...
190-280 1.23e-42

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: 141.10  E-value: 1.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472  190 TELEISYFLLRRLLGVRTEgdkkaAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALSRRVE 269
Cdd:pfam09173   1 TELEIEYHLLERVVGVKEE-----KKVEPIKKGEVLMLNVGTATTGGVVTSVKKDEAEVELKKPVCAEKGERVAISRRIG 75
                          90
                  ....*....|.
gi 569012472  270 KHWRLIGWGQI 280
Cdd:pfam09173  76 GRWRLIGWGII 86
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
1-69 4.11e-39

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: 135.86  E-value: 4.11e-39
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569012472   1 MKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPLR 69
Cdd:cd01888  129 MGLKHIIILQNKIDLVKEEQALENYEQIKEFVKGTIAENAPIIPISAQLKYNIDVLCEYIVKKIPTPPR 197
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
3-120 1.98e-10

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: 61.08  E-value: 1.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472   3 LKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKI-PVPLRDFTSEPRLIVIR 81
Cdd:COG3276  104 IKRGIVVLTKADLVDEEWLELVEEEIRELLAGTFLEDAPIVPVSAVTGEGIDELRAALDALAaAVPARDADGPFRLPIDR 183
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 569012472  82 SFDVnkpgcevddlKG-G-VAGGSILKGVLKVGQEIEVRPG 120
Cdd:COG3276  184 VFSI----------KGfGtVVTGTLLSGTVRVGDELELLPS 214
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
97-180 9.16e-09

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: 9.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472   97 GGVAGGSILKGVLKVGQEIEVRPGIVSKdgegklmcKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLcraDRMVG 176
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGK--------KKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLE---DIRVG 69

                  ....
gi 569012472  177 QVLG 180
Cdd:pfam03144  70 DTLT 73
era PRK00089
GTPase Era; Reviewed
2-65 1.76e-06

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 48.51  E-value: 1.76e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569012472   2 KLKHILILqNKIDLVKEsqaKEQYEQILAFVQGTVaEGAPIIPISAQLKYNIEVVCEYIVKKIP 65
Cdd:PRK00089 113 KTPVILVL-NKIDLVKD---KEELLPLLEELSELM-DFAEIVPISALKGDNVDELLDVIAKYLP 171
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
75-172 8.02e-06

Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 43.02  E-value: 8.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472  75 PRLIVIRSFDVNKpgcevddlKGGVAGGSILKGVLKVGQEIEVRPgivskdgegklmcKPIFSKIVSLFAEHNDLQYAAP 154
Cdd:cd01342    1 LVMQVFKVFYIPG--------RGRVAGGRVESGTLKVGDEIRILP-------------KGITGRVTSIERFHEEVDEAKA 59
                         90
                 ....*....|....*...
gi 569012472 155 GGLIGVGTKIDPTLCRAD 172
Cdd:cd01342   60 GDIVGIGILGVKDILTGD 77
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
4-67 1.44e-05

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: 44.59  E-value: 1.44e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569012472   4 KHILILQNKIDLVKESQAKEQYEQILAFVQGTVA-----EGAPIIPISAQLKYNIEVVCEYIVKKIPVP 67
Cdd:cd00881  115 LPIIVAVNKIDRVGEEDFDEVLREIKELLKLIGFtflkgKDVPIIPISALTGEGIEELLDAIVEHLPPP 183
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
2-66 1.76e-05

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 45.36  E-value: 1.76e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569012472   2 KLKHILILqNKIDLVKesqaKEQYEQILAFVQGTvAEGAPIIPISAQLKYNIEVVCEYIVKKIPV 66
Cdd:COG1159  111 KTPVILVI-NKIDLVK----KEELLPLLAEYSEL-LDFAEIVPISALKGDNVDELLDEIAKLLPE 169
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
1-60 2.32e-05

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: 43.75  E-value: 2.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012472   1 MKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYI 60
Cdd:cd04171  101 LGIKKGLVVLTKADLVDEDRLELVEEEILELLAGTFLADAPIFPVSSVTGEGIEELKNYL 160
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
1-65 4.39e-05

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: 43.28  E-value: 4.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569012472    1 MKLKHILILqNKIDLVKES---QAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIP 65
Cdd:pfam00009 120 LGVPIIVFI-NKMDRVDGAeleEVVEEVSRELLEKYGEDGEFVPVVPGSALKGEGVQTLLDALDEYLP 186
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
1-63 4.36e-04

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: 40.14  E-value: 4.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569012472   1 MKLKHILILqNKIDLVK-ESQAKEQYEQILAFVQGtvaegAPIIPISAQLKYNIEVVCEYIVKK 63
Cdd:cd04163  110 SKTPVILVL-NKIDLVKdKEDLLPLLEKLKELHPF-----AEIFPISALKGENVDELLEYIVEY 167
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
6-64 1.95e-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: 38.17  E-value: 1.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 569012472   6 ILILqNKIDLVKESQAKEQYEQILAFVQGTvaegaPIIPISAQLKYNIEVVCEYIVKKI 64
Cdd:cd01898  118 IVVL-NKIDLLDAEERFEKLKELLKELKGK-----KVFPISALTGEGLDELLKKLAKLL 170
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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