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Conserved domains on  [gi|702073045|emb|CEA09984|]
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putative eukaryotic translation initiation factor 2 gamma subunit, partial [Plasmodium giganteum]

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
 1-248 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: 504.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   1 SFVDCPGHDILMATMLNGAAVMDAALLLVAGNELCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQKEIRNF 80
Cdd:PTZ00327 120 SFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNF 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  81 VSGTAADSAPIIPISAVLKYNIDVVCEYIVTQICVPKRDFVSLPHMIVIRSFDVNKPGEDVENLQGGVAGGSILHGVLKV 160
Cdd:PTZ00327 200 VKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKRDLTSPPRMIVIRSFDVNKPGEDIENLKGGVAGGSILQGVLKV 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045 161 GDKIEIRPGIISKDEKGEITCRPIVSQIVTMFAENNNLKFGVPGGLIGVGTRIDPILTRADRLVGQVIGHLNKLPDCFAE 240
Cdd:PTZ00327 280 GDEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNELQYAVPGGLIGVGTTIDPTLTRADRLVGQVLGYPGKLPEVYAE 359


                 ....*...
gi 702073045 241 IEISYYLL 248
Cdd:PTZ00327 360 IEIQYYLL 367
 
Name Accession Description Interval E-value
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 1-248 0e+00

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 504.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   1 SFVDCPGHDILMATMLNGAAVMDAALLLVAGNELCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQKEIRNF 80
Cdd:PTZ00327 120 SFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNF 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  81 VSGTAADSAPIIPISAVLKYNIDVVCEYIVTQICVPKRDFVSLPHMIVIRSFDVNKPGEDVENLQGGVAGGSILHGVLKV 160
Cdd:PTZ00327 200 VKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKRDLTSPPRMIVIRSFDVNKPGEDIENLKGGVAGGSILQGVLKV 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045 161 GDKIEIRPGIISKDEKGEITCRPIVSQIVTMFAENNNLKFGVPGGLIGVGTRIDPILTRADRLVGQVIGHLNKLPDCFAE 240
Cdd:PTZ00327 280 GDEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNELQYAVPGGLIGVGTTIDPTLTRADRLVGQVLGYPGKLPEVYAE 359


                 ....*...
gi 702073045 241 IEISYYLL 248
Cdd:PTZ00327 360 IEIQYYLL 367
GCD11 COG5257
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ...
 1-248 1.35e-111

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: 326.41  E-value: 1.35e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   1 SFVDCPGHDILMATMLNGAAVMDAALLLVAGNELCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQKEIRNF 80
Cdd:COG5257   84 SFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSKERALENYEQIKEF 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  81 VSGTAADSAPIIPISAVLKYNIDVVCEYIVTQICVPKRDFVSLPHMIVIRSFDVNKPGEDVENLQGGVAGGSILHGVLKV 160
Cdd:COG5257  164 VKGTVAENAPIIPVSAQHKVNIDALIEAIEEEIPTPERDLSKPPRMLVARSFDVNKPGTPPKDLKGGVIGGSLIQGVLKV 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045 161 GDKIEIRPGiISKDEKGEITCRPIVSQIVTMFAENNNLKFGVPGGLIGVGTRIDPILTRADRLVGQVIGHLNKLPDCFAE 240
Cdd:COG5257  244 GDEIEIRPG-IKVEKGGKTKYEPITTTVVSLRAGGEEVEEAKPGGLVAVGTKLDPSLTKSDSLVGSVAGKPGTLPPVLDS 322


                 ....*...
gi 702073045 241 IEISYYLL 248
Cdd:COG5257  323 LTMEVHLL 330
eif2g_arch TIGR03680
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ...
 1-248 1.22e-105

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: 311.22  E-value: 1.22e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045    1 SFVDCPGHDILMATMLNGAAVMDAALLLVAGNELCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQKEIRNF 80
Cdd:TIGR03680  83 SFVDAPGHETLMATMLSGAALMDGALLVIAANEPCPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSKEKALENYEEIKEF 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   81 VSGTAADSAPIIPISAVLKYNIDVVCEYIVTQICVPKRDFVSLPHMIVIRSFDVNKPGEDVENLQGGVAGGSILHGVLKV 160
Cdd:TIGR03680 163 VKGTVAENAPIIPVSALHNANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNKPGTPPEKLKGGVIGGSLIQGKLKV 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  161 GDKIEIRPGiISKDEKGEITCRPIVSQIVTMFAENNNLKFGVPGGLIGVGTRIDPILTRADRLVGQVIGHLNKLPDCFAE 240
Cdd:TIGR03680 243 GDEIEIRPG-IKVEKGGKTKWEPIYTEITSLRAGGYKVEEARPGGLVGVGTKLDPALTKADALAGQVVGKPGTLPPVWES 321


                  ....*...
gi 702073045  241 IEISYYLL 248
Cdd:TIGR03680 322 LELEVHLL 329
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 1-118 2.39e-73

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: 221.76  E-value: 2.39e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   1 SFVDCPGHDILMATMLNGAAVMDAALLLVAGNELCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQKEIRNF 80
Cdd:cd01888   80 SFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQALENYEQIKEF 159

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 702073045  81 VSGTAADSAPIIPISAVLKYNIDVVCEYIVTQICVPKR 118
Cdd:cd01888  160 VKGTIAENAPIIPISAQLKYNIDVLCEYIVKKIPTPPR 197
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 2-113 1.00e-14

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: 70.25  E-value: 1.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045    2 FVDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILqNKVELIKEEQSLKQQKEIRN-- 79
Cdd:pfam00009  73 LIDTPGHVDFVKEVIRGLAQADGAILVVDAVE-GVMPQTREHLRLARQLGVPIIVFI-NKMDRVDGAELEEVVEEVSRel 150

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 702073045   80 -FVSGTAADSAPIIPISAVLKYNIDVVCEYIVTQI 113
Cdd:pfam00009 151 lEKYGEDGEFVPVVPGSALKGEGVQTLLDALDEYL 185
 
Name Accession Description Interval E-value
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 1-248 0e+00

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 504.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   1 SFVDCPGHDILMATMLNGAAVMDAALLLVAGNELCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQKEIRNF 80
Cdd:PTZ00327 120 SFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNF 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  81 VSGTAADSAPIIPISAVLKYNIDVVCEYIVTQICVPKRDFVSLPHMIVIRSFDVNKPGEDVENLQGGVAGGSILHGVLKV 160
Cdd:PTZ00327 200 VKGTIADNAPIIPISAQLKYNIDVVLEYICTQIPIPKRDLTSPPRMIVIRSFDVNKPGEDIENLKGGVAGGSILQGVLKV 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045 161 GDKIEIRPGIISKDEKGEITCRPIVSQIVTMFAENNNLKFGVPGGLIGVGTRIDPILTRADRLVGQVIGHLNKLPDCFAE 240
Cdd:PTZ00327 280 GDEIEIRPGIISKDSGGEFTCRPIRTRIVSLFAENNELQYAVPGGLIGVGTTIDPTLTRADRLVGQVLGYPGKLPEVYAE 359


                 ....*...
gi 702073045 241 IEISYYLL 248
Cdd:PTZ00327 360 IEIQYYLL 367
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 1-248 3.06e-113

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 330.66  E-value: 3.06e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   1 SFVDCPGHDILMATMLNGAAVMDAALLLVAGNELCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQKEIRNF 80
Cdd:PRK04000  88 SFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSKERALENYEQIKEF 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  81 VSGTAADSAPIIPISAVLKYNIDVVCEYIVTQICVPKRDFVSLPHMIVIRSFDVNKPGEDVENLQGGVAGGSILHGVLKV 160
Cdd:PRK04000 168 VKGTVAENAPIIPVSALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTPPEKLKGGVIGGSLIQGVLKV 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045 161 GDKIEIRPGIISKdEKGEITCRPIVSQIVTMFAENNNLKFGVPGGLIGVGTRIDPILTRADRLVGQVIGHLNKLPDCFAE 240
Cdd:PRK04000 248 GDEIEIRPGIKVE-EGGKTKWEPITTKIVSLRAGGEKVEEARPGGLVGVGTKLDPSLTKADALAGSVAGKPGTLPPVWES 326


                 ....*...
gi 702073045 241 IEISYYLL 248
Cdd:PRK04000 327 LTIEVHLL 334
GCD11 COG5257
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ...
 1-248 1.35e-111

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: 326.41  E-value: 1.35e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   1 SFVDCPGHDILMATMLNGAAVMDAALLLVAGNELCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQKEIRNF 80
Cdd:COG5257   84 SFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSKERALENYEQIKEF 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  81 VSGTAADSAPIIPISAVLKYNIDVVCEYIVTQICVPKRDFVSLPHMIVIRSFDVNKPGEDVENLQGGVAGGSILHGVLKV 160
Cdd:COG5257  164 VKGTVAENAPIIPVSAQHKVNIDALIEAIEEEIPTPERDLSKPPRMLVARSFDVNKPGTPPKDLKGGVIGGSLIQGVLKV 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045 161 GDKIEIRPGiISKDEKGEITCRPIVSQIVTMFAENNNLKFGVPGGLIGVGTRIDPILTRADRLVGQVIGHLNKLPDCFAE 240
Cdd:COG5257  244 GDEIEIRPG-IKVEKGGKTKYEPITTTVVSLRAGGEEVEEAKPGGLVAVGTKLDPSLTKSDSLVGSVAGKPGTLPPVLDS 322


                 ....*...
gi 702073045 241 IEISYYLL 248
Cdd:COG5257  323 LTMEVHLL 330
eif2g_arch TIGR03680
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ...
 1-248 1.22e-105

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: 311.22  E-value: 1.22e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045    1 SFVDCPGHDILMATMLNGAAVMDAALLLVAGNELCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQKEIRNF 80
Cdd:TIGR03680  83 SFVDAPGHETLMATMLSGAALMDGALLVIAANEPCPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSKEKALENYEEIKEF 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   81 VSGTAADSAPIIPISAVLKYNIDVVCEYIVTQICVPKRDFVSLPHMIVIRSFDVNKPGEDVENLQGGVAGGSILHGVLKV 160
Cdd:TIGR03680 163 VKGTVAENAPIIPVSALHNANIDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNKPGTPPEKLKGGVIGGSLIQGKLKV 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  161 GDKIEIRPGiISKDEKGEITCRPIVSQIVTMFAENNNLKFGVPGGLIGVGTRIDPILTRADRLVGQVIGHLNKLPDCFAE 240
Cdd:TIGR03680 243 GDEIEIRPG-IKVEKGGKTKWEPIYTEITSLRAGGYKVEEARPGGLVGVGTKLDPALTKADALAGQVVGKPGTLPPVWES 321


                  ....*...
gi 702073045  241 IEISYYLL 248
Cdd:TIGR03680 322 LELEVHLL 329
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 1-118 2.39e-73

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: 221.76  E-value: 2.39e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   1 SFVDCPGHDILMATMLNGAAVMDAALLLVAGNELCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQKEIRNF 80
Cdd:cd01888   80 SFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQALENYEQIKEF 159

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 702073045  81 VSGTAADSAPIIPISAVLKYNIDVVCEYIVTQICVPKR 118
Cdd:cd01888  160 VKGTIAENAPIIPISAQLKYNIDVLCEYIVKKIPTPPR 197
eIF2_gamma_II cd03688
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily ...
 119-230 8.78e-59

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: 181.61  E-value: 8.78e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045 119 DFVSLPHMIVIRSFDVNKPGEDVENLQGGVAGGSILHGVLKVGDKIEIRPGIISKDEkGEITCRPIVSQIVTMFAENNNL 198
Cdd:cd03688    1 DLDKPPRMIVIRSFDVNKPGTEVDDLKGGVIGGSLIQGVLKVGDEIEIRPGIVVKKG-GKTTCRPIFTKIVSLFAEGNDL 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 702073045 199 KFGVPGGLIGVGTRIDPILTRADRLVGQVIGH 230
Cdd:cd03688   80 EEAVPGGLIGVGTKLDPTLTKADRLVGQVVGE 111
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 1-169 1.26e-25

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: 105.00  E-value: 1.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   1 SFVDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQKEIRNF 80
Cdd:COG3276   54 GFVDVPGHEKFIKNMLAGAGGIDLVLLVVAADE-GVMPQTREHLAILDLLGIKRGIVVLTKADLVDEEWLELVEEEIREL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  81 VSGTAADSAPIIPISAVLKYNIDVVCEYIVTQI-CVPKRDFVSLPHMIVIRSFDVnkPGedvenlQGGVAGGSILHGVLK 159
Cdd:COG3276  133 LAGTFLEDAPIVPVSAVTGEGIDELRAALDALAaAVPARDADGPFRLPIDRVFSI--KG------FGTVVTGTLLSGTVR 204

                        170
                 ....*....|
gi 702073045 160 VGDKIEIRPG 169
Cdd:COG3276  205 VGDELELLPS 214
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-109 1.29e-20

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: 85.35  E-value: 1.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   1 SFVDCPGHDILMATMLNGAAVMDAALLLVAGNELCpQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQKEIRNF 80
Cdd:cd04171   53 GFIDVPGHEKFVKNMLAGAGGIDAVLLVVAADEGI-MPQTREHLEILELLGIKKGLVVLTKADLVDEDRLELVEEEILEL 131

                         90       100
                 ....*....|....*....|....*....
gi 702073045  81 VSGTAADSAPIIPISAVLKYNIDVVCEYI 109
Cdd:cd04171  132 LAGTFLADAPIFPVSSVTGEGIEELKNYL 160
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 3-166 5.67e-18

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: 82.13  E-value: 5.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045    3 VDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQ-QKEIRNFV 81
Cdd:TIGR00485  80 VDCPGHADYVKNMITGAAQMDGAILVVSATD-GPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELvEMEVRELL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   82 S--GTAADSAPIIPISAVLKYN------------IDVVCEYIVTqicvPKRDfVSLPHMIVIrsfdvnkpgEDVENLQ-- 145
Cdd:TIGR00485 159 SqyDFPGDDTPIIRGSALKALEgdaeweakilelMDAVDEYIPT----PERE-IDKPFLLPI---------EDVFSITgr 224

                         170       180
                  ....*....|....*....|.
gi 702073045  146 GGVAGGSILHGVLKVGDKIEI 166
Cdd:TIGR00485 225 GTVVTGRVERGIIKVGEEVEI 245
PRK12736 PRK12736
elongation factor Tu; Reviewed
 3-228 1.45e-17

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 80.76  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   3 VDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQ-QKEIRNFV 81
Cdd:PRK12736  80 VDCPGHADYVKNMITGAAQMDGAILVVAATD-GPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELvEMEVRELL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  82 S--GTAADSAPIIPISAVLKYN------------IDVVCEYIVTqicvPKRDfVSLPHMIvirsfdvnkPGEDVENL--Q 145
Cdd:PRK12736 159 SeyDFPGDDIPVIRGSALKALEgdpkwedaimelMDAVDEYIPT----PERD-TDKPFLM---------PVEDVFTItgR 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045 146 GGVAGGSILHGVLKVGDKIEIrpgiiskdekgeITCRPIVSQIVT---MFaeNNNLKFGVPGGLIGVGTR-IDpiltRAD 221
Cdd:PRK12736 225 GTVVTGRVERGTVKVGDEVEI------------VGIKETQKTVVTgveMF--RKLLDEGQAGDNVGVLLRgVD----RDE 286


                 ....*..
gi 702073045 222 RLVGQVI 228
Cdd:PRK12736 287 VERGQVL 293
tufA CHL00071
elongation factor Tu
 3-166 8.26e-17

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 78.85  E-value: 8.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   3 VDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLK-QQKEIRNFV 81
Cdd:CHL00071  80 VDCPGHADYVKNMITGAAQMDGAILVVSAAD-GPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLElVELEVRELL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  82 S--GTAADSAPIIPISAVLK---------------------YN-IDVVCEYIVTqicvPKRdfvslphmivirsfDVNKP 137
Cdd:CHL00071 159 SkyDFPGDDIPIVSGSALLAlealtenpkikrgenkwvdkiYNlMDAVDSYIPT----PER--------------DTDKP 220

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 702073045 138 G----EDVENL--QGGVAGGSILHGVLKVGDKIEI 166
Cdd:CHL00071 221 FlmaiEDVFSItgRGTVATGRIERGTVKVGDTVEI 255
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-113 1.50e-16

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: 75.02  E-value: 1.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   1 SFVDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKrILILQNKVELIKEEQSLKQQKEIRNF 80
Cdd:cd00881   65 NFIDTPGHEDFSKETVRGLAQADGALLVVDANE-GVEPQTREHLNIALAGGLP-IIVAVNKIDRVGEEDFDEVLREIKEL 142

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 702073045  81 VSGTAADS-----APIIPISAVLKYNIDVVCEYIVTQI 113
Cdd:cd00881  143 LKLIGFTFlkgkdVPIIPISALTGEGIEELLDAIVEHL 180
PLN03127 PLN03127
Elongation factor Tu; Provisional
 3-228 2.90e-16

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 77.56  E-value: 2.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   3 VDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQ-QKEIRNFV 81
Cdd:PLN03127 129 VDCPGHADYVKNMITGAAQMDGGILVVSAPD-GPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELvEMELRELL 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  82 S--GTAADSAPIIPISAV--LKYNIDVVCEYIVTQICVPKRDFVSLPHMIVIRSFDVnkPGEDVENLQ--GGVAGGSILH 155
Cdd:PLN03127 208 SfyKFPGDEIPIIRGSALsaLQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLM--PIEDVFSIQgrGTVATGRVEQ 285

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 702073045 156 GVLKVGDKIEIRPGIISKDEKGEITCrpivsqiVTMFAEnnNLKFGVPGGLIGVGTRidpILTRADRLVGQVI 228
Cdd:PLN03127 286 GTIKVGEEVEIVGLRPGGPLKTTVTG-------VEMFKK--ILDQGQAGDNVGLLLR---GLKREDVQRGQVI 346
PLN03126 PLN03126
Elongation factor Tu; Provisional
 3-166 1.97e-15

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 75.04  E-value: 1.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   3 VDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQ-QKEIRNFV 81
Cdd:PLN03126 149 VDCPGHADYVKNMITGAAQMDGAILVVSGAD-GPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELvELEVRELL 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  82 SGTA--ADSAPIIPISAVLK---------------------YNI-DVVCEYIVtqicVPKRDfVSLPHMIVIrsfdvnkp 137
Cdd:PLN03126 228 SSYEfpGDDIPIISGSALLAlealmenpnikrgdnkwvdkiYELmDAVDSYIP----IPQRQ-TDLPFLLAV-------- 294

                        170       180       190
                 ....*....|....*....|....*....|.
gi 702073045 138 gEDVENL--QGGVAGGSILHGVLKVGDKIEI 166
Cdd:PLN03126 295 -EDVFSItgRGTVATGRVERGTVKVGETVDI 324
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 2-168 7.18e-15

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: 73.37  E-value: 7.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045    2 FVDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQKEIRNFV 81
Cdd:TIGR00475  54 FIDVPGHEKFISNAIAGGGGIDAALLVVDADE-GVMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIKRTEMFMKQIL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   82 SGTA-ADSAPIIPISAVLKYNIDVVCEYIVTqicVPKRDFVSLPH----MIVIRSFDVNKPGEdvenlqggVAGGSILHG 156
Cdd:TIGR00475 133 NSYIfLKNAKIFKTSAKTGQGIGELKKELKN---LLESLDIKRIQkplrMAIDRAFKVKGAGT--------VVTGTAFSG 201

                         170
                  ....*....|..
gi 702073045  157 VLKVGDKIEIRP 168
Cdd:TIGR00475 202 EVKVGDNLRLLP 213
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 2-113 1.00e-14

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: 70.25  E-value: 1.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045    2 FVDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILqNKVELIKEEQSLKQQKEIRN-- 79
Cdd:pfam00009  73 LIDTPGHVDFVKEVIRGLAQADGAILVVDAVE-GVMPQTREHLRLARQLGVPIIVFI-NKMDRVDGAELEEVVEEVSRel 150

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 702073045   80 -FVSGTAADSAPIIPISAVLKYNIDVVCEYIVTQI 113
Cdd:pfam00009 151 lEKYGEDGEFVPVVPGSALKGEGVQTLLDALDEYL 185
PRK00049 PRK00049
elongation factor Tu; Reviewed
 3-166 1.01e-14

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 72.53  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   3 VDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQ-QKEIRNFV 81
Cdd:PRK00049  80 VDCPGHADYVKNMITGAAQMDGAILVVSAAD-GPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELvEMEVRELL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  82 S--GTAADSAPIIPISAVLKYN--------------IDVVCEYIVTqicvPKRDfVSLPHMIvirsfdvnkPGEDVENLQ 145
Cdd:PRK00049 159 SkyDFPGDDTPIIRGSALKALEgdddeewekkilelMDAVDSYIPT----PERA-IDKPFLM---------PIEDVFSIS 224

                        170       180
                 ....*....|....*....|...
gi 702073045 146 G--GVAGGSILHGVLKVGDKIEI 166
Cdd:PRK00049 225 GrgTVVTGRVERGIIKVGEEVEI 247
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 3-168 3.93e-14

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 71.11  E-value: 3.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   3 VDCPGHDILMATMLNGAAVMDAALLLVAGNE-LCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQslKQQKEIRNFV 81
Cdd:PRK12317  89 VDCPGHRDFVKNMITGASQADAAVLVVAADDaGGVMPQTREHVFLARTLGINQLIVAINKMDAVNYDE--KRYEEVKEEV 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  82 S------GTAADSAPIIPISA-----VLK-------YNIDVVCEYIvTQICVPKRDfVSLPHMIvirsfdvnkPGEDVEN 143
Cdd:PRK12317 167 SkllkmvGYKPDDIPFIPVSAfegdnVVKksenmpwYNGPTLLEAL-DNLKPPEKP-TDKPLRI---------PIQDVYS 235

                        170       180
                 ....*....|....*....|....*..
gi 702073045 144 LQ--GGVAGGSILHGVLKVGDKIEIRP 168
Cdd:PRK12317 236 ISgvGTVPVGRVETGVLKVGDKVVFMP 262
PRK12735 PRK12735
elongation factor Tu; Reviewed
 3-166 3.93e-14

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 71.02  E-value: 3.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   3 VDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQ-QKEIRNFV 81
Cdd:PRK12735  80 VDCPGHADYVKNMITGAAQMDGAILVVSAAD-GPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELvEMEVRELL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  82 S--GTAADSAPIIPISAVLKYN--------------IDVVCEYIVTqicvPKRDfVSLPHMIvirsfdvnkPGEDVENLQ 145
Cdd:PRK12735 159 SkyDFPGDDTPIIRGSALKALEgdddeeweakilelMDAVDSYIPE----PERA-IDKPFLM---------PIEDVFSIS 224

                        170       180
                 ....*....|....*....|...
gi 702073045 146 --GGVAGGSILHGVLKVGDKIEI 166
Cdd:PRK12735 225 grGTVVTGRVERGIVKVGDEVEI 247
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 2-96 1.15e-13

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: 67.39  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   2 FVDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILqNKVELIKEEQS----LKQQKEI 77
Cdd:cd01889   72 LVDCPGHASLIRTIIGGAQIIDLMLLVVDAKK-GIQTQTAECLVIGELLCKPLIVVL-NKIDLIPEEERkrkiEKMKKRL 149

                         90
                 ....*....|....*....
gi 702073045  78 RNFVSGTAADSAPIIPISA 96
Cdd:cd01889  150 QKTLEKTRLKDSPIIPVSA 168
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 3-166 2.18e-13

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: 68.64  E-value: 2.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   3 VDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQ-QKEIRNFV 81
Cdd:COG0050   80 VDCPGHADYVKNMITGAAQMDGAILVVSATD-GPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELvEMEVRELL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  82 S--GTAADSAPIIPISAVLKYNIDVVCEY---IV-------TQICVPKRDfVSLPHMIvirsfdvnkPGEDVENLQG-G- 147
Cdd:COG0050  159 SkyGFPGDDTPIIRGSALKALEGDPDPEWekkILelmdavdSYIPEPERD-TDKPFLM---------PVEDVFSITGrGt 228

                        170
                 ....*....|....*....
gi 702073045 148 VAGGSILHGVLKVGDKIEI 166
Cdd:COG0050  229 VVTGRVERGIIKVGDEVEI 247
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 3-235 1.42e-12

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: 66.50  E-value: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   3 VDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQslKQQKEIRNFVS 82
Cdd:COG5256   90 IDAPGHRDFVKNMITGASQADAAILVVSAKD-GVMGQTREHAFLARTLGINQLIVAVNKMDAVNYSE--KRYEEVKEEVS 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  83 ------GTAADSAPIIPISAVLKYNIDVVCEYI-----------VTQICVPKRDfVSLPHMIvirsfdvnkPGEDVENLQ 145
Cdd:COG5256  167 kllkmvGYKVDKIPFIPVSAWKGDNVVKKSDNMpwyngptlleaLDNLKEPEKP-VDKPLRI---------PIQDVYSIS 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045 146 --GGVAGGSILHGVLKVGDKIEIRPGIISkdekGEitcrpiVSQIVTMFAEnnnLKFGVPGGLIGVGTRidpILTRADRL 223
Cdd:COG5256  237 giGTVPVGRVETGVLKVGDKVVFMPAGVV----GE------VKSIEMHHEE---LEQAEPGDNIGFNVR---GVEKNDIK 300

                        250
                 ....*....|..
gi 702073045 224 VGQVIGHLNKLP 235
Cdd:COG5256  301 RGDVAGHPDNPP 312
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 3-103 8.45e-12

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: 62.22  E-value: 8.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   3 VDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQ-QKEIRNFV 81
Cdd:cd01884   70 VDCPGHADYIKNMITGAAQMDGAILVVSATD-GPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELvEMEVRELL 148

                         90       100
                 ....*....|....*....|....
gi 702073045  82 S--GTAADSAPIIPISAVLKYNID 103
Cdd:cd01884  149 SkyGFDGDDTPIVRGSALKALEGD 172
infB CHL00189
translation initiation factor 2; Provisional
 2-166 8.87e-09

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 55.61  E-value: 8.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   2 FVDCPGHDILMATMLNGAAVMDAALLLVAGNELCpQPQTSEHLAAVEIMRLKrILILQNKVE-----LIKEEQSLKQQke 76
Cdd:CHL00189 299 FLDTPGHEAFSSMRSRGANVTDIAILIIAADDGV-KPQTIEAINYIQAANVP-IIVAINKIDkananTERIKQQLAKY-- 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  77 irNFVSGTAADSAPIIPISAVLKYNIDVVCEYI--VTQICVPKRDFVSLPHMIVIRSFdvnkpgedVENLQGGVAGGSIL 154
Cdd:CHL00189 375 --NLIPEKWGGDTPMIPISASQGTNIDKLLETIllLAEIEDLKADPTQLAQGIILEAH--------LDKTKGPVATILVQ 444

                        170
                 ....*....|..
gi 702073045 155 HGVLKVGDKIEI 166
Cdd:CHL00189 445 NGTLHIGDIIVI 456
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 146-229 2.15e-08

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 49.96  E-value: 2.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045  146 GGVAGGSILHGVLKVGDKIEIRPGIISKDekgeitcrPIVSQIVTMFAENNNLKFGVPGGLIGVGTRIDPILtraDRLVG 225
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKK--------KIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLE---DIRVG 69


                  ....
gi 702073045  226 QVIG 229
Cdd:pfam03144  70 DTLT 73
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 3-102 6.75e-08

CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 51.42  E-value: 6.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   3 VDCPGHDILMATMLNGAAVMDAALLLVAGNELCpQPQTSEHLAAVEIMRLKRILILQNKVELI--KEEQSLKQQKEIRNF 80
Cdd:cd04166   83 ADTPGHEQYTRNMVTGASTADLAILLVDARKGV-LEQTRRHSYIASLLGIRHVVVAVNKMDLVdyDEEVFEEIKADYLAF 161

                         90       100
                 ....*....|....*....|..
gi 702073045  81 VSGTAADSAPIIPISAVLKYNI 102
Cdd:cd04166  162 AASLGIEDITFIPISALEGDNV 183
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 3-96 2.03e-06

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: 47.10  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   3 VDCPGHDILMATMLNGAAVMDAALLLV--------AGNELcpQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQ 74
Cdd:cd01883   82 IDAPGHRDFVKNMITGASQADVAVLVVsarkgefeAGFEK--GGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERY 159

                         90       100
                 ....*....|....*....|....*...
gi 702073045  75 KEIRNFVS------GTAADSAPIIPISA 96
Cdd:cd01883  160 DEIKKKVSpflkkvGYNPKDVPFIPISG 187
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 2-52 3.78e-06

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 47.35  E-value: 3.78e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 702073045   2 FVDCPGHDILMATMLNGAAVMDAALLLVAgnelCPQ---PQTSEHLAaveIMRL 52
Cdd:PRK10512  55 FIDVPGHEKFLSNMLAGVGGIDHALLVVA----CDDgvmAQTREHLA---ILQL 101
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
2-110 6.95e-05

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 43.05  E-value: 6.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   2 FVDCPG--------HDILMATMLNGAAVMDAALLLVAGNElcpqPQTSEHLAAVEIMR---LKRILILqNKVELIKEEQS 70
Cdd:COG1159   55 FVDTPGihkpkrklGRRMNKAAWSALEDVDVILFVVDATE----KIGEGDEFILELLKklkTPVILVI-NKIDLVKKEEL 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 702073045  71 LKQQKEIRNFvsgtaADSAPIIPISAVLKYNIDVVCEYIV 110
Cdd:COG1159  130 LPLLAEYSEL-----LDFAEIVPISALKGDNVDELLDEIA 164
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 143-214 5.34e-04

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: 37.63  E-value: 5.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 702073045 143 NLQGGVAGGSILHGVLKVGDKIEIRPGIISKdekgeitcrpIVSQIVTMFAEnnnLKFGVPGGLIGVGTRID 214
Cdd:cd01342   12 PGRGRVAGGRVESGTLKVGDEIRILPKGITG----------RVTSIERFHEE---VDEAKAGDIVGIGILGV 70
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 2-112 6.18e-04

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 39.38  E-value: 6.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   2 FVDCPGHDILMATMLNGAAVMDAALLLVAGNElCPQPQTSEhlaAVEIMRLKR--ILILQNKVELI----KEEQSLKQQK 75
Cdd:cd01887   53 FIDTPGHEAFTNMRARGASVTDIAILVVAADD-GVMPQTIE---AINHAKAANvpIIVAINKIDKPygteADPERVKNEL 128

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 702073045  76 EIRNFVSGTAADSAPIIPISAVLKYNIDVVCEYIVTQ 112
Cdd:cd01887  129 SELGLVGEEWGGDVSIVPISAKTGEGIDDLLEAILLL 165
PRK14845 PRK14845
translation initiation factor IF-2; Provisional
 2-80 7.39e-04

translation initiation factor IF-2; Provisional


Pssm-ID: 237833 [Multi-domain]  Cd Length: 1049  Bit Score: 40.64  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045    2 FVDCPGHDILMATMLNGAAVMDAALLLVAGNELCpQPQTSEhlaAVEIMRLKR--ILILQNKVELIKEEQSLKQQKEIRN 79
Cdd:PRK14845  530 FIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGF-KPQTIE---AINILRQYKtpFVVAANKIDLIPGWNISEDEPFLLN 605


                  .
gi 702073045   80 F 80
Cdd:PRK14845  606 F 606
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 2-112 9.18e-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: 38.98  E-value: 9.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   2 FVDCPG----HDILMaTMLNGAAVM-----DAALLLVAGNElcpqPQTSEH---LAAVEIMRLKRILILqNKVELIKEEQ 69
Cdd:cd04163   55 FVDTPGihkpKKKLG-ERMVKAAWSalkdvDLVLFVVDASE----WIGEGDefiLELLKKSKTPVILVL-NKIDLVKDKE 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 702073045  70 SLKQQKEIRNFVSgtaaDSAPIIPISAVLKYNIDVVCEYIVTQ 112
Cdd:cd04163  129 DLLPLLEKLKELH----PFAEIFPISALKGENVDELLEYIVEY 167
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 3-95 1.08e-03

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 39.73  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   3 VDCPGHDILMATMLNGAAVMDAALLLVAGNE------LCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQKE 76
Cdd:PTZ00141  90 IDAPGHRDFIKNMITGTSQADVAILVVASTAgefeagISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDE 169

                         90       100
                 ....*....|....*....|....*
gi 702073045  77 IRNFVS------GTAADSAPIIPIS 95
Cdd:PTZ00141 170 IKKEVSaylkkvGYNPEKVPFIPIS 194
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 53-113 2.61e-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: 37.40  E-value: 2.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 702073045  53 KRILILqNKVELIKEEQSLKQQKEIRNFVSGTaadsaPIIPISAVLKYNIDVVCEYIVTQI 113
Cdd:cd01898  116 PRIVVL-NKIDLLDAEERFEKLKELLKELKGK-----KVFPISALTGEGLDELLKKLAKLL 170
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-96 4.74e-03

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 37.76  E-value: 4.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   1 SFVDCPGHDILMATMLNGAAVMDAALLLV----AGNE--LCPQPQTSEHLAAVEIMRLKRILILQNKVELIKEEQSLKQQ 74
Cdd:PLN00043  88 TVIDAPGHRDFIKNMITGTSQADCAVLIIdsttGGFEagISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARY 167

                         90       100
                 ....*....|....*....|....*...
gi 702073045  75 KEIRNFVS------GTAADSAPIIPISA 96
Cdd:PLN00043 168 DEIVKEVSsylkkvGYNPDKIPFVPISG 195
era PRK00089
GTPase Era; Reviewed
 2-110 6.23e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 36.95  E-value: 6.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702073045   2 FVDCPG--------HDILMATMLNGAAVMDAALLLV-AGNELCPQPQT-SEHLAAVEImrlKRILILqNKVELIKE-EQS 70
Cdd:PRK00089  57 FVDTPGihkpkralNRAMNKAAWSSLKDVDLVLFVVdADEKIGPGDEFiLEKLKKVKT---PVILVL-NKIDLVKDkEEL 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 702073045  71 LKQQKEIRNFVsgtaaDSAPIIPISAVLKYNIDVVCEYIV 110
Cdd:PRK00089 133 LPLLEELSELM-----DFAEIVPISALKGDNVDELLDVIA 167
 
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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