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Conserved domains on  [gi|1907180503|ref|XP_036008905|]
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elongation factor Tu, mitochondrial isoform X2 [Mus musculus]

Protein Classification

elongation factor Tu( domain architecture ID 1000100)

elongation factor Tu promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis

Gene Ontology:  GO:0005525|GO:0003746|GO:0003924
PubMed:  31708880|17446867|8073502

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TufA super family cl33752
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-303 3.21e-162

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


The actual alignment was detected with superfamily member COG0050:

Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 457.69  E-value: 3.21e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:COG0050    92 MITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPII 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHN 160
Cdd:COG0050   172 RGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIR 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 161 KNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMP 240
Cdd:COG0050   252 DTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRP 331

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907180503 241 VMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 303
Cdd:COG0050   332 QFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKI 394
 
Name Accession Description Interval E-value
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-303 3.21e-162

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: 457.69  E-value: 3.21e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:COG0050    92 MITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPII 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHN 160
Cdd:COG0050   172 RGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIR 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 161 KNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMP 240
Cdd:COG0050   252 DTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRP 331

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907180503 241 VMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 303
Cdd:COG0050   332 QFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKI 394
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-303 5.62e-158

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 446.94  E-value: 5.62e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:PRK00049   92 MITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPII 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHN 160
Cdd:PRK00049  172 RGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIR 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 161 KNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMP 240
Cdd:PRK00049  252 DTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRP 331

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907180503 241 VMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 303
Cdd:PRK00049  332 QFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKI 394
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-303 1.12e-134

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: 387.60  E-value: 1.12e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:TIGR00485  92 MITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPII 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCALEQrDPELGVKsVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHN 160
Cdd:TIGR00485 172 RGSALKALEG-DAEWEAK-ILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLK 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 161 KNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMP 240
Cdd:TIGR00485 250 DTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYRP 329

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907180503 241 VMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 303
Cdd:TIGR00485 330 QFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKI 392
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-114 2.34e-71

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: 219.38  E-value: 2.34e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:cd01884    82 MITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIV 161

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907180503  81 VGSALCALEQRDPELGVKSVQKLLDAVDTYIPVP 114
Cdd:cd01884   162 RGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 209-303 2.90e-36

Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.


Pssm-ID: 397314 [Multi-domain]  Cd Length: 105  Bit Score: 126.23  E-value: 2.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 209 SIQPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRVI-----LPPGK-----ELAMPGEDLKLSLILRQPM 278
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhkLDPGGvsenpEFVMPGDNVIVTVELIKPI 80

                          90       100
                  ....*....|....*....|....*
gi 1907180503 279 ILEKGQRFTLRDGNKTIGTGLVTDV 303
Cdd:pfam03143  81 ALEKGQRFAIREGGRTVAAGVVTEI 105
 
Name Accession Description Interval E-value
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-303 3.21e-162

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: 457.69  E-value: 3.21e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:COG0050    92 MITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPII 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHN 160
Cdd:COG0050   172 RGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIR 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 161 KNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMP 240
Cdd:COG0050   252 DTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRP 331

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907180503 241 VMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 303
Cdd:COG0050   332 QFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKI 394
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-303 5.62e-158

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 446.94  E-value: 5.62e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:PRK00049   92 MITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPII 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHN 160
Cdd:PRK00049  172 RGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIR 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 161 KNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMP 240
Cdd:PRK00049  252 DTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRP 331

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907180503 241 VMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 303
Cdd:PRK00049  332 QFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKI 394
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-303 4.59e-153

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 434.27  E-value: 4.59e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:PRK12735   92 MITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPII 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHN 160
Cdd:PRK12735  172 RGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIVGIK 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 161 KNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMP 240
Cdd:PRK12735  252 ETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFNGYRP 331

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907180503 241 VMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 303
Cdd:PRK12735  332 QFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKI 394
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-303 5.24e-153

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 433.99  E-value: 5.24e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:PRK12736   92 MITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEYDFPGDDIPVI 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCALEQRDPElgVKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHN 160
Cdd:PRK12736  172 RGSALKALEGDPKW--EDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIK 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 161 KNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMP 240
Cdd:PRK12736  250 ETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRHTPFFNNYRP 329

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907180503 241 VMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 303
Cdd:PRK12736  330 QFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEI 392
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-303 2.57e-144

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 414.22  E-value: 2.57e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:PLN03127  141 MITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPII 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLG-- 158
Cdd:PLN03127  221 RGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGlr 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 159 HNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHF 238
Cdd:PLN03127  301 PGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFFSNY 380

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907180503 239 MPVMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 303
Cdd:PLN03127  381 RPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKV 445
tufA CHL00071
elongation factor Tu
 1-303 3.09e-139

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 399.72  E-value: 3.09e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:CHL00071   92 MITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPGDDIPIV 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCALE--QRDPELG------VKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGD 152
Cdd:CHL00071  172 SGSALLALEalTENPKIKrgenkwVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGD 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 153 ECELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHK 232
Cdd:CHL00071  252 TVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTKEEGGRHT 331

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907180503 233 PFVSHFMPVMFSLTWDMACRVIL-----PPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 303
Cdd:CHL00071  332 PFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGAGVVSKI 407
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-303 1.12e-134

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: 387.60  E-value: 1.12e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:TIGR00485  92 MITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPII 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCALEQrDPELGVKsVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHN 160
Cdd:TIGR00485 172 RGSALKALEG-DAEWEAK-ILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLK 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 161 KNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMP 240
Cdd:TIGR00485 250 DTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYRP 329

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907180503 241 VMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 303
Cdd:TIGR00485 330 QFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKI 392
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-303 2.16e-114

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 338.90  E-value: 2.16e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:PLN03126  161 MITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPII 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCALE--------QRDPELGVKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGD 152
Cdd:PLN03126  241 SGSALLALEalmenpniKRGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGE 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 153 ECELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHK 232
Cdd:PLN03126  321 TVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHS 400

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907180503 233 PFVSHFMPVMFSLTWDMACRVILPPGKE-----LAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDV 303
Cdd:PLN03126  401 PFFAGYRPQFYMRTTDVTGKVTSIMNDKdeeskMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGAGVIQSI 476
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-114 2.34e-71

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: 219.38  E-value: 2.34e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:cd01884    82 MITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIV 161

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907180503  81 VGSALCALEQRDPELGVKSVQKLLDAVDTYIPVP 114
Cdd:cd01884   162 RGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-303 1.55e-58

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: 193.61  E-value: 1.55e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQ-DSEMVELVELEIRELLTEFGYKGEETPV 79
Cdd:COG5256   102 MITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVKEEVSKLLKMVGYKVDKIPF 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  80 IVGSALCA--LEQRDPELGVKSVQKLLDAVDTyIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELL 157
Cdd:COG5256   182 IPVSAWKGdnVVKKSDNMPWYNGPTLLEALDN-LKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFM 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 158 GHNKniRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSiQPH--QKVEAQVYILskeeggrHKPFV 235
Cdd:COG5256   261 PAGV--VGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDN-PPTvaEEFTAQIVVL-------QHPSA 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 236 --SHFMPVMFSLTWDMACRVI-----LPP--GKELA------MPGEDLKLSLILRQPMILEKGQ------RFTLRDGNKT 294
Cdd:COG5256   331 itVGYTPVFHVHTAQVACTFVelvskLDPrtGQVKEenpqflKTGDAAIVKIKPTKPLVIEKFKefpqlgRFAIRDMGQT 410


                  ....*....
gi 1907180503 295 IGTGLVTDV 303
Cdd:COG5256   411 VAAGVVLDV 419
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 1-305 5.04e-57

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: 194.36  E-value: 5.04e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGYkgEETPVI 80
Cdd:COG3276    68 MLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGTFL--EDAPIV 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCaleqrdpelGvKSVQKLLDAVDTYI-PVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGH 159
Cdd:COG3276   145 PVSAVT---------G-EGIDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPS 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 160 NKNIRtvVTGIEMFHKSLERAEAGD----NLgalvRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEeggrhKPFV 235
Cdd:COG3276   215 GKPVR--VRGIQVHGQPVEEAYAGQrvalNL----AGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPSA-----PRPL 283

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907180503 236 SHFMPVMFSL-TWDMACRVILPPGKELAmPGEDLKLSLILRQPMILEKGQRFTLRDGN--KTIGTGLVTDVPA 305
Cdd:COG3276   284 KHWQRVHLHHgTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRVLDPNP 355
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
 211-303 1.71e-56

Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.


Pssm-ID: 294005 [Multi-domain]  Cd Length: 93  Bit Score: 177.81  E-value: 1.71e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 211 QPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRD 290
Cdd:cd03706     1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80

                          90
                  ....*....|...
gi 1907180503 291 GNKTIGTGLVTDV 303
Cdd:cd03706    81 GGRTIGTGVVTKL 93
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-303 1.70e-53

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 180.51  E-value: 1.70e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAAND--GPMPQTREHLLLAKQIGVEHVVVYVNKADAVQ-DSEMVELVELEIRELLTEFGYKGEET 77
Cdd:PRK12317  101 MITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEEVKEEVSKLLKMVGYKPDDI 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  78 PVIVGSALCA--LEQRDPELGVKSVQKLLDAVDTyIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDEC- 154
Cdd:PRK12317  181 PFIPVSAFEGdnVVKKSENMPWYNGPTLLEALDN-LKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVv 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 155 -ELLGHNKNIRTvvtgIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVmVKPGSIQPHQKVE--AQVYILskeeggrH 231
Cdd:PRK12317  260 fMPAGVVGEVKS----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDV-CGHPDNPPTVAEEftAQIVVL-------Q 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 232 KPFV--SHFMPVMFSLTWDMACRVI-----LPP--GKELA------MPGEDLKLSLILRQPMILEKGQ------RFTLRD 290
Cdd:PRK12317  328 HPSAitVGYTPVFHAHTAQVACTFEelvkkLDPrtGQVAEenpqfiKTGDAAIVKIKPTKPLVIEKVKeipqlgRFAIRD 407

                         330
                  ....*....|...
gi 1907180503 291 GNKTIGTGLVTDV 303
Cdd:PRK12317  408 MGQTIAAGMVIDV 420
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 122-208 3.25e-48

Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 156.14  E-value: 3.25e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 122 FLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRG 201
Cdd:cd03697     1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80


                  ....*..
gi 1907180503 202 LVMVKPG 208
Cdd:cd03697    81 MVLAKPG 87
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-303 1.51e-38

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 141.42  E-value: 1.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMP-------QTREHLLLAKQIGVEHVVVYVNKADAVQ----DSEMVELVElEIRELLTE 69
Cdd:PTZ00141  102 MITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTvnysQERYDEIKK-EVSAYLKK 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  70 FGYKGEETPVIVGSALCA---LEQRDPELGVKSvQKLLDAVDTYIPvPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERG 146
Cdd:PTZ00141  181 VGYNPEKVPFIPISGWQGdnmIEKSDNMPWYKG-PTLLEALDTLEP-PKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETG 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 147 ILKKGDECELLghNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVM--VKPGSIQPHQKVEAQVYILS 224
Cdd:PTZ00141  259 ILKPGMVVTFA--PSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVAsdSKNDPAKECADFTAQVIVLN 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 225 keeggrHKPFVSH-FMPVMFSLTWDMACRV--ILP-----PGKELAMPGEDLK------LSLILRQPMILEKGQ------ 284
Cdd:PTZ00141  337 ------HPGQIKNgYTPVLDCHTAHIACKFaeIESkidrrSGKVLEENPKAIKsgdaaiVKMVPTKPMCVEVFNeypplg 410

                         330
                  ....*....|....*....
gi 1907180503 285 RFTLRDGNKTIGTGLVTDV 303
Cdd:PTZ00141  411 RFAVRDMKQTVAVGVIKSV 429
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 209-303 2.90e-36

Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.


Pssm-ID: 397314 [Multi-domain]  Cd Length: 105  Bit Score: 126.23  E-value: 2.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 209 SIQPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRVI-----LPPGK-----ELAMPGEDLKLSLILRQPM 278
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhkLDPGGvsenpEFVMPGDNVIVTVELIKPI 80

                          90       100
                  ....*....|....*....|....*
gi 1907180503 279 ILEKGQRFTLRDGNKTIGTGLVTDV 303
Cdd:pfam03143  81 ALEKGQRFAIREGGRTVAAGVVTEI 105
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 211-300 8.74e-36

Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.


Pssm-ID: 294006 [Multi-domain]  Cd Length: 90  Bit Score: 124.16  E-value: 8.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 211 QPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRD 290
Cdd:cd03707     1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80

                          90
                  ....*....|
gi 1907180503 291 GNKTIGTGLV 300
Cdd:cd03707    81 GGRTVGAGVV 90
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-313 1.20e-35

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: 135.39  E-value: 1.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:TIGR00475  67 AIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRV-NEEEIKRTEMFMKQILNSYIFLKNAKIFK 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGsalcALEQRDPELGVKSVQKLLDAVDtyipvpTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHN 160
Cdd:TIGR00475 146 TS----AKTGQGIGELKKELKNLLESLD------IKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPIN 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 161 KNIRtvVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEggrhkpFVSHFMP 240
Cdd:TIGR00475 216 HEVR--VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDPKLRVVVKFIAEVPLLEL------QPYHIAH 287

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907180503 241 VMFSLTwdmaCRVILPPGKeLAMpgedlklsLILRQPMILEKGQRFTLRDGNKTIGTGLVTDVPAMTEEDKNI 313
Cdd:TIGR00475 288 GMSVTT----GKISLLDKG-IAL--------LTLDAPLILAKGDKLVLRDSSGNFLAGARVLEPPVRVKRKAF 347
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-112 1.25e-34

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: 124.56  E-value: 1.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVI 80
Cdd:pfam00009  86 VIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVF-INKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVV 164

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907180503  81 VGSALCALeqrdpelgvkSVQKLLDAVDTYIP 112
Cdd:pfam00009 165 PGSALKGE----------GVQTLLDALDEYLP 186
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 1-225 2.41e-27

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 110.33  E-value: 2.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDG-PMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVElEIRELLTefGYKGEETPV 79
Cdd:PRK04000  102 MLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSKERALENYE-QIKEFVK--GTVAENAPI 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  80 IVGSALcaleqrdpelgvksvQK-----LLDAVDTYIPVPTRDLDKPFLLPVESVYSI--PG------RGTVVTGTLERG 146
Cdd:PRK04000  179 IPVSAL---------------HKvnidaLIEAIEEEIPTPERDLDKPPRMYVARSFDVnkPGtppeklKGGVIGGSLIQG 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 147 ILKKGDECELL------GHNKN----IRTVVTGIEMFHKSLERAEAGDNLG---ALVRGLKREDLRRGLVMVKPGSIQP- 212
Cdd:PRK04000  244 VLKVGDEIEIRpgikveEGGKTkwepITTKIVSLRAGGEKVEEARPGGLVGvgtKLDPSLTKADALAGSVAGKPGTLPPv 323

                         250
                  ....*....|...
gi 1907180503 213 HQKVEAQVYILSK 225
Cdd:PRK04000  324 WESLTIEVHLLER 336
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-303 9.48e-25

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 103.63  E-value: 9.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMP-------QTREHLLLAKQIGVEHVVVYVNKADAVQ---DSEMVELVELEIRELLTEF 70
Cdd:PLN00043  102 MITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTpkySKARYDEIVKEVSSYLKKV 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  71 GYKGEETPVIVGSALCA--LEQRDPELGVKSVQKLLDAVDTyIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGIL 148
Cdd:PLN00043  182 GYNPDKIPFVPISGFEGdnMIERSTNLDWYKGPTLLEALDQ-INEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVI 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 149 KKGDECELLghNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVM--VKPGSIQPHQKVEAQVYILSK- 225
Cdd:PLN00043  261 KPGMVVTFG--PTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAsnSKDDPAKEAANFTSQVIIMNHp 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 226 -EEGGRHKPFV----SHfMPVMFSltwDMACRVILPPGKELAMPGEDLK------LSLILRQPMILEKGQ------RFTL 288
Cdd:PLN00043  339 gQIGNGYAPVLdchtSH-IAVKFA---EILTKIDRRSGKELEKEPKFLKngdagfVKMIPTKPMVVETFSeypplgRFAV 414

                         330
                  ....*....|....*
gi 1907180503 289 RDGNKTIGTGLVTDV 303
Cdd:PLN00043  415 RDMRQTVAVGVIKSV 429
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-220 3.34e-24

Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 101.70  E-value: 3.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITG--TAplDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMV-ELVELEIRELLTEFGYKgEET 77
Cdd:COG2895   112 MVTGasTA--DLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVfEEIVADYRAFAAKLGLE-DIT 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  78 PVIVgSALcaleqrdpeLGVKSVQK-----------LLDAVDTyIPVPTRDLDKPFLLPVESVYSiPG---RGtvVTGTL 143
Cdd:COG2895   189 FIPI-SAL---------KGDNVVERsenmpwydgptLLEHLET-VEVAEDRNDAPFRFPVQYVNR-PNldfRG--YAGTI 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 144 ERGILKKGDECELLGHNKniRTVVTGIEMFHKSLERAEAGDNLGaLVrgLKRE-DLRRGLVMVKPGSiQPH--QKVEAQV 220
Cdd:COG2895   255 ASGTVRVGDEVVVLPSGK--TSTVKSIVTFDGDLEEAFAGQSVT-LT--LEDEiDISRGDVIVAADA-PPEvaDQFEATL 328
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 1-201 7.67e-24

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 101.67  E-value: 7.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVElVELEIRELLTEFGYkgEETPVI 80
Cdd:PRK10512   68 MLAGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGF--AEAKLF 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCaleqrdpELGVKSVQKLLDAvdtyIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHN 160
Cdd:PRK10512  145 VTAATE-------GRGIDALREHLLQ----LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVN 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907180503 161 KNIRtvVTGIEMFHKSLERAEAGDNLGALVRG-LKREDLRRG 201
Cdd:PRK10512  214 KPMR--VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
TypA_BipA TIGR01394
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ...
 9-184 1.52e-20

GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]


Pssm-ID: 273597 [Multi-domain]  Cd Length: 594  Bit Score: 91.98  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   9 DGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNKADavQDSEMVELVELEIRELLTEFGYKGE--ETPVIVGSALC 86
Cdd:TIGR01394  89 DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKID--RPSARPDEVVDEVFDLFAELGADDEqlDFPIVYASGRA 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  87 ALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHNKNIRTV 166
Cdd:TIGR01394 166 GWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMKRDGTIENG 245

                         170       180
                  ....*....|....*....|...
gi 1907180503 167 VTGIEMFHKSLER-----AEAGD 184
Cdd:TIGR01394 246 RISKLLGFEGLERveideAGAGD 268
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-114 1.56e-19

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: 84.27  E-value: 1.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQiGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGY---KGEET 77
Cdd:cd00881    79 TVRGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDV 156

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907180503  78 PVIVGSALCALeqrdpelgvkSVQKLLDAVDTYIPVP 114
Cdd:cd00881   157 PIIPISALTGE----------GIEELLDAIVEHLPPP 183
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 122-203 1.69e-19

Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 81.03  E-value: 1.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 122 FLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHNKNIRtvVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRG 201
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR--VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78


                  ..
gi 1907180503 202 LV 203
Cdd:cd03696    79 FV 80
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 119-208 4.13e-19

Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 80.31  E-value: 4.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 119 DKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLghNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDL 198
Cdd:cd03693     2 DKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFA--PAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDI 79

                          90
                  ....*....|
gi 1907180503 199 RRGLVMVKPG 208
Cdd:cd03693    80 KRGDVAGDSK 89
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-85 8.06e-19

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: 81.88  E-value: 8.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGYkgEETPVI 80
Cdd:cd04171    67 MLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFL--ADAPIF 143


                  ....*
gi 1907180503  81 VGSAL 85
Cdd:cd04171   144 PVSSV 148
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 1-225 7.64e-18

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 83.51  E-value: 7.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDG-PMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVElEIRELLTefGYKGEETPV 79
Cdd:PTZ00327  134 MLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYE-EIRNFVK--GTIADNAPI 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  80 IvgsALCALEQRDpelgvksVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSI--PG------RGTVVTGTLERGILKKG 151
Cdd:PTZ00327  211 I---PISAQLKYN-------IDVVLEYICTQIPIPKRDLTSPPRMIVIRSFDVnkPGedienlKGGVAGGSILQGVLKVG 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 152 DECE----LLGHNKN-------IRTVVTGIEMFHKSLERAEAGDNLGA---LVRGLKREDLRRGLVMVKPGSIQP-HQKV 216
Cdd:PTZ00327  281 DEIEirpgIISKDSGgeftcrpIRTRIVSLFAENNELQYAVPGGLIGVgttIDPTLTRADRLVGQVLGYPGKLPEvYAEI 360


                  ....*....
gi 1907180503 217 EAQVYILSK 225
Cdd:PTZ00327  361 EIQYYLLRR 369
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 211-300 1.11e-17

Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).


Pssm-ID: 275447 [Multi-domain]  Cd Length: 102  Bit Score: 77.05  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 211 QPHQKVEAQVYILSKEeggrhKPFVSHFMPVMFSLTWDMACRVILPPGKE-----------LAMPGEDLKLSLILRQPMI 279
Cdd:cd01513     1 QAVWKFDAKVIVLEHP-----KPIRPGYKPVMDVGTAHVPGRIAKLLSKEdgktkekkppdSLQPGENGTVEVELQKPVV 75

                          90       100
                  ....*....|....*....|....*..
gi 1907180503 280 LEKG------QRFTLRDGNKTIGTGLV 300
Cdd:cd01513    76 LERGkefptlGRFALRDGGRTVGAGLI 102
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 122-203 6.22e-17

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: 74.22  E-value: 6.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 122 FLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGhnKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKreDLRRG 201
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP--KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76


                  ..
gi 1907180503 202 LV 203
Cdd:cd01342    77 DT 78
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 9-184 1.01e-16

Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 80.45  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   9 DGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNK-------ADAVQDsEMVEL-VELEIRELLTEFgykgeetPVI 80
Cdd:COG1217    94 DGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVV-INKidrpdarPDEVVD-EVFDLfIELGATDEQLDF-------PVV 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSAL---CALEQRDPElgvKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESV-YSiPGRGTVVTGTLERGILKKGDECEL 156
Cdd:COG1217   165 YASARngwASLDLDDPG---EDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLdYS-DYVGRIAIGRIFRGTIKKGQQVAL 240

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1907180503 157 LGHNKNIRTV-VTGIEMFHKsLER-----AEAGD 184
Cdd:COG1217   241 IKRDGKVEKGkITKLFGFEG-LERveveeAEAGD 273
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-85 2.65e-16

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: 76.38  E-value: 2.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDG-------PMPQTREHLLLAKQIGVEHVVVYVNKADAVQ---DSEMVELVELEIRELLTEF 70
Cdd:cd01883    94 MITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTvnwSQERYDEIKKKVSPFLKKV 173

                          90
                  ....*....|....*
gi 1907180503  71 GYKGEETPVIVGSAL 85
Cdd:cd01883   174 GYNPKDVPFIPISGF 188
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 136-205 2.10e-15

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: 69.99  E-value: 2.10e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907180503 136 GTVVTGTLERGILKKGDECELLGHN---KNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMV 205
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGtgkKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 122-205 4.15e-15

Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 69.56  E-value: 4.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 122 FLLPVESVYSIPGRGTVVTGTLERGILKKGDECeLLGHNKN---IRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDL 198
Cdd:cd03694     1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLGPDADgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79


                  ....*..
gi 1907180503 199 RRGLVMV 205
Cdd:cd03694    80 RKGMVLV 86
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 1-116 3.32e-14

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: 69.99  E-value: 3.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDG-PMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVElEIRELLTefGYKGEETPV 79
Cdd:cd01888    94 MLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQALENYE-QIKEFVK--GTIAENAPI 170

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907180503  80 IVGSALcaleqrdpeLGVkSVQKLLDAVDTYIPVPTR 116
Cdd:cd01888   171 IPISAQ---------LKY-NIDVLCEYIVKKIPTPPR 197
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-220 6.50e-14

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 71.87  E-value: 6.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEmvELVElEIRELLTEFGYKGEETPVI 80
Cdd:PRK05124  124 MATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDYSE--EVFE-RIREDYLTFAEQLPGNLDI 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  81 VGSALCALEqrdpelGVKSVQK-----------LLDAVDTyIPVPTRDLDKPFLLPVESVySIPG---RGtvVTGTLERG 146
Cdd:PRK05124  201 RFVPLSALE------GDNVVSQsesmpwysgptLLEVLET-VDIQRVVDAQPFRFPVQYV-NRPNldfRG--YAGTLASG 270

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907180503 147 ILKKGDECELL--GHNKNIRTVVTgiemFHKSLERAEAGDnlgALVRGLKRE-DLRRGLVMVKPGS-IQPHQKVEAQV 220
Cdd:PRK05124  271 VVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGE---AITLVLEDEiDISRGDLLVAADEaLQAVQHASADV 341
PRK10218 PRK10218
translational GTPase TypA;
8-184 4.35e-11

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 63.57  E-value: 4.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   8 LDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNKADavQDSEMVELVELEIRELLTEFGYKGEET--PVIVGSAL 85
Cdd:PRK10218   92 VDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVD--RPGARPDWVVDQVFDLFVNLDATDEQLdfPIVYASAL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  86 CALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHNKNIRT 165
Cdd:PRK10218  169 NGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRN 248

                         170       180
                  ....*....|....*....|....
gi 1907180503 166 VVTGIEMFHKSLER-----AEAGD 184
Cdd:PRK10218  249 AKVGKVLGHLGLERietdlAEAGD 272
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 9-114 3.05e-10

Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.


Pssm-ID: 206678 [Multi-domain]  Cd Length: 194  Bit Score: 58.76  E-value: 3.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   9 DGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNKADavQDSEMVELVELEIRELLTEFGYKGE--ETPVIVGSALC 86
Cdd:cd01891    90 DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKID--RPDARPEEVVDEVFDLFLELNATDEqlDFPIVYASAKN 166

                          90       100
                  ....*....|....*....|....*...
gi 1907180503  87 ALEQRDPELGVKSVQKLLDAVDTYIPVP 114
Cdd:cd01891   167 GWASLNLDDPSEDLDPLFETIIEHVPAP 194
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-85 3.21e-10

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


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 58.74  E-value: 3.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMV-ELVELEIRELLTEFGYkgEETPV 79
Cdd:cd04166    95 MVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVfEEIKADYLAFAASLGI--EDITF 172


                  ....*.
gi 1907180503  80 IVGSAL 85
Cdd:cd04166   173 IPISAL 178
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-220 2.41e-09

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 58.02  E-value: 2.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   1 MITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMV-ELVELEIRELLTEFGYkGEETPV 79
Cdd:PRK05506  121 MVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVfDEIVADYRAFAAKLGL-HDVTFI 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  80 IVgSALCA--LEQRDPELGVKSVQKLLDAVDTyIPVPTRDLDKPFLLPVESVYSiPG---RGtvVTGTLERGILKKGDEC 154
Cdd:PRK05506  200 PI-SALKGdnVVTRSARMPWYEGPSLLEHLET-VEIASDRNLKDFRFPVQYVNR-PNldfRG--FAGTVASGVVRPGDEV 274

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907180503 155 ELLGHNKniRTVVTGIEMFHKSLERAEAGDnlgALVRGLKRE-DLRRGLVMVKPGSiQPH--QKVEAQV 220
Cdd:PRK05506  275 VVLPSGK--TSRVKRIVTPDGDLDEAFAGQ---AVTLTLADEiDISRGDMLARADN-RPEvaDQFDATV 337
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 9-85 2.58e-09

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: 55.56  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   9 DGCILVVAANDGPMPQTREHLLLAKQIGVEhVVVYVNKADAVQDSEmvELVElEIRELLTEFGYKGEE----TPVIVGSA 84
Cdd:cd01887    74 DIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTE--ADPE-RVKNELSELGLVGEEwggdVSIVPISA 149


                  .
gi 1907180503  85 L 85
Cdd:cd01887   150 K 150
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 12-152 5.14e-07

Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 50.78  E-value: 5.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  12 ILVVAANDGPMPQTREHLLLAKQIGVEhVVVYVNKADAVQ-DSEMV--ELVELEIreLLTEFGykGeETPVIVGSALcal 88
Cdd:COG0532    79 ILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGaNPDRVkqELAEHGL--VPEEWG--G-DTIFVPVSAK--- 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503  89 eQRdpeLGvksVQKLLDAV-----------DtyipvPTRD---------LDKpfllpvesvysipGRGTVVTGTLERGIL 148
Cdd:COG0532   150 -TG---EG---IDELLEMIllqaevlelkaN-----PDRPargtvieakLDK-------------GRGPVATVLVQNGTL 204


                  ....
gi 1907180503 149 KKGD 152
Cdd:COG0532   205 KVGD 208
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 121-204 2.74e-06

Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 293906 [Multi-domain]  Cd Length: 82  Bit Score: 44.78  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 121 PFLLPVESVYSipGRGTVVTGTLERGILKKGDECeLLGHNKNiRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRR 200
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKL-VLMPNKT-KVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISP 76


                  ....
gi 1907180503 201 GLVM 204
Cdd:cd04089    77 GFVL 80
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 121-204 2.98e-06

Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation 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: 293899 [Multi-domain]  Cd Length: 84  Bit Score: 44.80  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 121 PFLLPVESVYSIPgRGTVVTGTLERGILKKGDECELLGHNKNIrtVVTGIEM-FHKSLERAEAGDNLGALVRGLKREDLR 199
Cdd:cd03698     1 PFRLSIDDKYKSP-RGTTVTGKLEAGSIQKNQVLYDMPSQQDA--EVKNIIRnSDEETDWAIAGDTVTLRLRGIEVEDIQ 77


                  ....*
gi 1907180503 200 RGLVM 204
Cdd:cd03698    78 PGDIL 82
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 122-206 3.54e-05

Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 41.40  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 122 FLLPVESVYSiPG---RGtvVTGTLERGILKKGDECELLGHNKniRTVVTGIEMFHKSLERAEAGDnlgALVRGLKRE-D 197
Cdd:cd03695     1 FRFPVQYVNR-PNldfRG--YAGTIASGSIRVGDEVTVLPSGK--TSRVKSIVTFDGELDSAGAGE---AVTLTLEDEiD 72


                  ....*....
gi 1907180503 198 LRRGLVMVK 206
Cdd:cd03695    73 VSRGDLIVR 81
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 126-192 5.32e-05

Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.


Pssm-ID: 293910 [Multi-domain]  Cd Length: 80  Bit Score: 41.13  E-value: 5.32e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907180503 126 VESVYSIPGRgTVVTGTLERGILKKGDECELlghnKNIRTVVTGIEMFHKSLERAEAGDNLGALVRG 192
Cdd:cd16265     5 VEKVFKILGR-QVLTGEVESGVIYVGYKVKG----DKGVALIRAIEREHRKVDFAVAGDEVALILEG 66
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 2-85 1.91e-04

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: 41.58  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503   2 ITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVyVNKADAVQDSEMVELVElEIRELL--TEFGYKGEETPV 79
Cdd:cd01889    86 IGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEERKRKIE-KMKKRLqkTLEKTRLKDSPI 163


                  ....*.
gi 1907180503  80 IVGSAL 85
Cdd:cd01889   164 IPVSAK 169
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 121-204 4.16e-04

Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.


Pssm-ID: 293912 [Multi-domain]  Cd Length: 84  Bit Score: 38.65  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907180503 121 PFLLPVESVYSIPGRGTVVTGTLERGILKKGDecELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRR 200
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGD--KVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78


                  ....
gi 1907180503 201 GLVM 204
Cdd:cd16267    79 GSIL 82
selB_III cd15491
Domain III of selenocysteine-specific translation elongation factor; This family represents ...
 235-300 4.85e-04

Domain III of selenocysteine-specific translation elongation factor; This family represents domain III of bacterial selenocysteine (Sec)-specific elongation factor (EFSec), homologous to domain III of EF-Tu. SelB is a specialized translation elongation factor responsible for the co-translational incorporation of selenocysteine into proteins by recoding of a UGA stop codon in the presence of a downstream mRNA hairpin loop, called Sec insertion sequence (SECIS) element.


Pssm-ID: 294012 [Multi-domain]  Cd Length: 87  Bit Score: 38.58  E-value: 4.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907180503 235 VSHFMPVMFSL-TWDMACRVILPPGKELAmPGEDLKLSLILRQPMILEKGQRFTLRDGN--KTIGTGLV 300
Cdd:cd15491    20 LKHRTRVRLHLgTSEVLGRVVLLDRDELA-PGEEALAQLRLEEPVVAKRGDRFILRSYSpmRTIGGGRV 87
 
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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