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Conserved domains on  [gi|34147630|ref|NP_003312|]
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elongation factor Tu, mitochondrial isoform 1 precursor [Homo sapiens]

Protein Classification

elongation factor Tu( domain architecture ID 18390252)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
50-444 0e+00

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: 657.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:COG0050   2 AKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:COG0050  82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 210 GYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKK 289
Cdd:COG0050 162 GFPGDDTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKV 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 290 GDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 369
Cdd:COG0050 242 GDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147630 370 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:COG0050 322 HTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
 
Name Accession Description Interval E-value
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
50-444 0e+00

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: 657.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:COG0050   2 AKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:COG0050  82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 210 GYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKK 289
Cdd:COG0050 162 GFPGDDTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKV 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 290 GDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 369
Cdd:COG0050 242 GDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147630 370 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:COG0050 322 HTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
PRK00049 PRK00049
elongation factor Tu; Reviewed
50-444 0e+00

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 644.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:PRK00049   2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:PRK00049  82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  210 GYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKK 289
Cdd:PRK00049 162 DFPGDDTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  290 GDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 369
Cdd:PRK00049 242 GEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147630  370 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:PRK00049 322 HTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
50-444 0e+00

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: 562.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630    50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:TIGR00485   2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:TIGR00485  82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   210 GYKGEETPVIVGSALCALEGrDPELGLKsVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKK 289
Cdd:TIGR00485 162 DFPGDDTPIIRGSALKALEG-DAEWEAK-ILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   290 GDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 369
Cdd:TIGR00485 240 GEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGR 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147630   370 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:TIGR00485 320 HTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
59-253 1.19e-142

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: 405.81  E-value: 1.19e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  59 PHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVK 138
Cdd:cd01884   1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 139 NMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPV 218
Cdd:cd01884  81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 34147630 219 IVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVP 253
Cdd:cd01884 161 VRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
58-251 4.33e-81

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: 248.59  E-value: 4.33e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630    58 KPHVNVGTIGHVDHGKTTLTAAI---TKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHA 134
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLlyyTGAISKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   135 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADAVQDSEMVELVELEIRELLTEFGYKGE 214
Cdd:pfam00009  81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVF-INKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 34147630   215 ETPVIVGSALCALegrdpelglkSVQKLLDAVDTYIP 251
Cdd:pfam00009 160 FVPVVPGSALKGE----------GVQTLLDALDEYLP 186
 
Name Accession Description Interval E-value
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
50-444 0e+00

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: 657.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:COG0050   2 AKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:COG0050  82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 210 GYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKK 289
Cdd:COG0050 162 GFPGDDTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKV 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 290 GDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 369
Cdd:COG0050 242 GDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147630 370 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:COG0050 322 HTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
PRK00049 PRK00049
elongation factor Tu; Reviewed
50-444 0e+00

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 644.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:PRK00049   2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:PRK00049  82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  210 GYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKK 289
Cdd:PRK00049 162 DFPGDDTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  290 GDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 369
Cdd:PRK00049 242 GEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147630  370 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:PRK00049 322 HTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
PRK12735 PRK12735
elongation factor Tu; Reviewed
50-444 0e+00

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 629.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:PRK12735   2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:PRK12735  82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  210 GYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKK 289
Cdd:PRK12735 162 DFPGDDTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  290 GDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 369
Cdd:PRK12735 242 GDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGR 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147630  370 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:PRK12735 322 HTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
PRK12736 PRK12736
elongation factor Tu; Reviewed
50-444 0e+00

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 619.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:PRK12736   2 AKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHVD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:PRK12736  82 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  210 GYKGEETPVIVGSALCALEGRDPElgLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKK 289
Cdd:PRK12736 162 DFPGDDIPVIRGSALKALEGDPKW--EDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  290 GDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 369
Cdd:PRK12736 240 GDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGR 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147630  370 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:PRK12736 320 HTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
PLN03127 PLN03127
Elongation factor Tu; Provisional
53-444 0e+00

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 587.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   53 TYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPG 132
Cdd:PLN03127  54 TFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPG 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  133 HADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYK 212
Cdd:PLN03127 134 HADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFP 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  213 GEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDE 292
Cdd:PLN03127 214 GDEIPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEE 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  293 CELLG--HSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGRH 370
Cdd:PLN03127 294 VEIVGlrPGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRH 373
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34147630  371 KPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:PLN03127 374 TPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
tufA CHL00071
elongation factor Tu
50-443 0e+00

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 578.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:CHL00071   2 AREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:CHL00071  82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  210 GYKGEETPVIVGSALCALEG--RDPELGL---KSVQK---LLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGT 281
Cdd:CHL00071 162 DFPGDDIPIVSGSALLALEAltENPKIKRgenKWVDKiynLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGR 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  282 LERGILKKGDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYI 361
Cdd:CHL00071 242 IERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYI 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  362 LSKEEGGRHKPFVSHFMPVMFSLTWDMACRIIL-----PPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGT 436
Cdd:CHL00071 322 LTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGA 401

                 ....*..
gi 34147630  437 GLVTNTL 443
Cdd:CHL00071 402 GVVSKIL 408
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
50-444 0e+00

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: 562.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630    50 AKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTD 129
Cdd:TIGR00485   2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEF 209
Cdd:TIGR00485  82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   210 GYKGEETPVIVGSALCALEGrDPELGLKsVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKK 289
Cdd:TIGR00485 162 DFPGDDTPIIRGSALKALEG-DAEWEAK-ILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   290 GDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGR 369
Cdd:TIGR00485 240 GEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGR 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147630   370 HKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLA 444
Cdd:TIGR00485 320 HTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
PLN03126 PLN03126
Elongation factor Tu; Provisional
44-443 1.63e-170

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 487.59  E-value: 1.63e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   44 RGLAVEAKK-TYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAA 122
Cdd:PLN03126  64 RSFTVRAARgKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETEN 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  123 RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEI 202
Cdd:PLN03126 144 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEV 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  203 RELLTEFGYKGEETPVIVGSALCALEG--RDPELG------LKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGR 274
Cdd:PLN03126 224 RELLSSYEFPGDDIPIISGSALLALEAlmENPNIKrgdnkwVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGR 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  275 GTVVTGTLERGILKKGDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQK 354
Cdd:PLN03126 304 GTVATGRVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTK 383
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  355 VEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRIIL-----PPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRD 429
Cdd:PLN03126 384 FEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSimndkDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIRE 463
                        410
                 ....*....|....
gi 34147630  430 GNRTIGTGLVTNTL 443
Cdd:PLN03126 464 GGKTVGAGVIQSII 477
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
59-253 1.19e-142

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: 405.81  E-value: 1.19e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  59 PHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVK 138
Cdd:cd01884   1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 139 NMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPV 218
Cdd:cd01884  81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 34147630 219 IVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVP 253
Cdd:cd01884 161 VRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
56-441 2.65e-86

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: 270.27  E-value: 2.65e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  56 RDKPHVNVGTIGHVDHGKTTLTAaitKILAEGG---GAKFKKYEE---------------IDNAPEERARGITINAAHVE 117
Cdd:COG5256   3 SEKPHLNLVVIGHVDHGKSTLVG---RLLYETGaidEHIIEKYEEeaekkgkesfkfawvMDRLKEERERGVTIDLAHKK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 118 YSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQ-DSEMVE 196
Cdd:COG5256  80 FETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 197 LVELEIRELLTEFGYKGEETPVIVGSALCA--LEGRDPELGLKSVQKLLDAVDTyIPVPARDLEKPFLLPVEAVYSVPGR 274
Cdd:COG5256 160 EVKEEVSKLLKMVGYKVDKIPFIPVSAWKGdnVVKKSDNMPWYNGPTLLEALDN-LKEPEKPVDKPLRIPIQDVYSISGI 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 275 GTVVTGTLERGILKKGDECELLghSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGsiKPHQK 354
Cdd:COG5256 239 GTVPVGRVETGVLKVGDKVVFM--PAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD--NPPTV 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 355 VE---AQVYILskeeggrHKPFV--SHFMPVMFSLTWDMACRII-----LPP----EKElampgEDLKF-----NLILR- 414
Cdd:COG5256 315 AEeftAQIVVL-------QHPSAitVGYTPVFHVHTAQVACTFVelvskLDPrtgqVKE-----ENPQFlktgdAAIVKi 382
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 34147630 415 ---QPMILEKGQ------RFTLRDGNRTIGTGLVTN 441
Cdd:COG5256 383 kptKPLVIEKFKefpqlgRFAIRDMGQTVAAGVVLD 418
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
56-441 1.97e-82

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 260.24  E-value: 1.97e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   56 RDKPHVNVGTIGHVDHGKTTLtaaITKILAEGGGA---KFKKYEE---------------IDNAPEERARGITINAAHVE 117
Cdd:PRK12317   2 KEKPHLNLAVIGHVDHGKSTL---VGRLLYETGAIdehIIEELREeakekgkesfkfawvMDRLKEERERGVTIDLAHKK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  118 YSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAAND--GPMPQTREHLLLARQIGVEHVVVYVNKADAVQ-DSEM 194
Cdd:PRK12317  79 FETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  195 VELVELEIRELLTEFGYKGEETPVIVGSalcALEG-----RDPELGLKSVQKLLDAVDTyIPVPARDLEKPFLLPVEAVY 269
Cdd:PRK12317 159 YEEVKEEVSKLLKMVGYKPDDIPFIPVS---AFEGdnvvkKSENMPWYNGPTLLEALDN-LKPPEKPTDKPLRIPIQDVY 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  270 SVPGRGTVVTGTLERGILKKGDEC--ELLGHSKNIRTvvtgIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPG 347
Cdd:PRK12317 235 SISGVGTVPVGRVETGVLKVGDKVvfMPAGVVGEVKS----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPD 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  348 siKPHQKVE---AQVYILskeeggrHKPFV--SHFMPVMFSLTWDMACRII-----LPP----EKE----LAMPGEDLKF 409
Cdd:PRK12317 311 --NPPTVAEeftAQIVVL-------QHPSAitVGYTPVFHAHTAQVACTFEelvkkLDPrtgqVAEenpqFIKTGDAAIV 381
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 34147630  410 NLILRQPMILEKGQ------RFTLRDGNRTIGTGLVTN 441
Cdd:PRK12317 382 KIKPTKPLVIEKVKeipqlgRFAIRDMGQTIAAGMVID 419
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
58-251 4.33e-81

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: 248.59  E-value: 4.33e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630    58 KPHVNVGTIGHVDHGKTTLTAAI---TKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHA 134
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLlyyTGAISKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   135 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADAVQDSEMVELVELEIRELLTEFGYKGE 214
Cdd:pfam00009  81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVF-INKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 34147630   215 ETPVIVGSALCALegrdpelglkSVQKLLDAVDTYIP 251
Cdd:pfam00009 160 FVPVVPGSALKGE----------GVQTLLDALDEYLP 186
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
61-444 4.35e-76

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: 249.83  E-value: 4.35e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  61 VNVGTIGHVDHGKTTLTAAITKIlaegggakfkkyeEIDNAPEERARGITINAAhveystaarhYAHT-----------D 129
Cdd:COG3276   1 MIIGTAGHIDHGKTTLVKALTGI-------------DTDRLKEEKKRGITIDLG----------FAYLplpdgrrlgfvD 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEF 209
Cdd:COG3276  58 VPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGT 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 210 GYkgEETPVIVGSalcALEGrdpelglKSVQKLLDAVDTYI-PVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILK 288
Cdd:COG3276 137 FL--EDAPIVPVS---AVTG-------EGIDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVR 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 289 KGDECELLGhsKNIRTVVTGIEMFHKSLERAEAGD----NLgalvRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSK 364
Cdd:COG3276 205 VGDELELLP--SGKPVRVRGIQVHGQPVEEAYAGQrvalNL----AGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPS 278
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 365 EeggrhKPFVSHFMPVMFSL-TWDMACRIILPPEKELAmPGEDLKFNLILRQPMILEKGQRFTLRDGN--RTIGTGLVTN 441
Cdd:COG3276 279 A-----PRPLKHWQRVHLHHgTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRVLD 352

                ...
gi 34147630 442 TLA 444
Cdd:COG3276 353 PNP 355
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
56-439 1.89e-60

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 203.83  E-value: 1.89e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   56 RDKPHVNVGTIGHVDHGKTTLTAAIT---------------KILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYST 120
Cdd:PTZ00141   3 KEKTHINLVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFET 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  121 AARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMP-------QTREHLLLARQIGVEHVVVYVNKADAVQ--- 190
Cdd:PTZ00141  83 PKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTvny 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  191 -DSEMVELVElEIRELLTEFGYKGEETPVIVGSALCA--LEGRDPELGLKSVQKLLDAVDTYIPvPARDLEKPFLLPVEA 267
Cdd:PTZ00141 163 sQERYDEIKK-EVSAYLKKVGYNPEKVPFIPISGWQGdnMIEKSDNMPWYKGPTLLEALDTLEP-PKRPVDKPLRLPLQD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  268 VYSVPGRGTVVTGTLERGILKKGDECELLghSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVM--VK 345
Cdd:PTZ00141 241 VYKIGGIGTVPVGRVETGILKPGMVVTFA--PSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVAsdSK 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  346 PGSIKPHQKVEAQVYILSkeeggrHKPFVSH-FMPVMFSLTWDMACRI-------------ILPPEKELAMPGEDLKFNL 411
Cdd:PTZ00141 319 NDPAKECADFTAQVIVLN------HPGQIKNgYTPVLDCHTAHIACKFaeieskidrrsgkVLEENPKAIKSGDAAIVKM 392
                        410       420       430
                 ....*....|....*....|....*....|....
gi 34147630  412 ILRQPMILEKGQ------RFTLRDGNRTIGTGLV 439
Cdd:PTZ00141 393 VPTKPMCVEVFNeypplgRFAVRDMKQTVAVGVI 426
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
350-442 1.01e-55

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: 179.73  E-value: 1.01e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 350 KPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRD 429
Cdd:cd03706   1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80
                        90
                ....*....|...
gi 34147630 430 GNRTIGTGLVTNT 442
Cdd:cd03706  81 GGRTIGTGVVTKL 93
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
61-437 1.76e-55

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: 193.94  E-value: 1.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630    61 VNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNM 140
Cdd:TIGR00475   1 MIIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   141 ITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGYKGEETPVIV 220
Cdd:TIGR00475  68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRV-NEEEIKRTEMFMKQILNSYIFLKNAKIFKT 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   221 GsalcALEGRDPELGLKSVQKLLDAVDTyipvpaRDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSK 300
Cdd:TIGR00475 147 S----AKTGQGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINH 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   301 NIRtvVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEggrhkpFVSHFMPV 380
Cdd:TIGR00475 217 EVR--VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDPKLRVVVKFIAEVPLLEL------QPYHIAHG 288
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 34147630   381 MFSLTwdmacRIILPPEKELAMpgedlkfnLILRQPMILEKGQRFTLRDGNRTIGTG 437
Cdd:TIGR00475 289 MSVTT-----GKISLLDKGIAL--------LTLDAPLILAKGDKLVLRDSSGNFLAG 332
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
62-253 1.98e-52

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: 174.41  E-value: 1.98e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  62 NVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMI 141
Cdd:cd00881   1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 142 TGTAPLDGCILVVAANDGPMPQTREHLLLARQiGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGY---KGEETPV 218
Cdd:cd00881  81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
                       170       180       190
                ....*....|....*....|....*....|....*
gi 34147630 219 IVGSALcalegrdpeLGLKsVQKLLDAVDTYIPVP 253
Cdd:cd00881 159 IPISAL---------TGEG-IEELLDAIVEHLPPP 183
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
261-347 1.84e-46

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: 155.37  E-value: 1.84e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 261 FLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRG 340
Cdd:cd03697   1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80

                ....*..
gi 34147630 341 LVMVKPG 347
Cdd:cd03697  81 MVLAKPG 87
eif2g_arch TIGR03680
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ...
59-351 4.30e-45

translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.


Pssm-ID: 274720 [Multi-domain]  Cd Length: 406  Bit Score: 161.76  E-value: 4.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630    59 PHVNVGTIGHVDHGKTTLTAAITKILaegggakfkkyeeIDNAPEERARGITINAAHVE--------------YSTAA-- 122
Cdd:TIGR03680   3 PEVNIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPvc 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   123 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQD 191
Cdd:TIGR03680  70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   192 SEMVELVElEIRELLTefGYKGEETPVIVGSALCALegrdpelglkSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSV 271
Cdd:TIGR03680 150 EKALENYE-EIKEFVK--GTVAENAPIIPVSALHNA----------NIDALLEAIEKFIPTPERDLDKPPLMYVARSFDV 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   272 --PG------RGTVVTGTLERGILKKGDECELL--------GHSK--NIRTVVTGIEMFHKSLERAEAGDNLG---ALVR 330
Cdd:TIGR03680 217 nkPGtppeklKGGVIGGSLIQGKLKVGDEIEIRpgikvekgGKTKwePIYTEITSLRAGGYKVEEARPGGLVGvgtKLDP 296
                         330       340
                  ....*....|....*....|.
gi 34147630   331 GLKREDLRRGLVMVKPGSIKP 351
Cdd:TIGR03680 297 ALTKADALAGQVVGKPGTLPP 317
GTPBP1 COG5258
GTPase [General function prediction only];
56-443 4.04e-44

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 162.03  E-value: 4.04e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  56 RDKPHVNVGTIGHVDHGKTTLTAA-ITKILAEGGGAKFKKyeeIDNAPEERARGIT---------------IN------- 112
Cdd:COG5258 118 KDPEHIVVGVAGHVDHGKSTLVGTlVTGKLDDGNGGTRSF---LDVQPHEVERGLSadlsyavygfdddgpVRmknplrk 194
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 113 ---AAHVEysTAARHYAHTDCPGHADYVKNMITGTA--PLDGCILVVAANDGPMPQTREHL--LLARQIGvehVVVYVNK 185
Cdd:COG5258 195 tdrARVVE--ESDKLVSFVDTVGHEPWLRTTIRGLVgqKLDYGLLVVAADDGPTHTTREHLgiLLAMDLP---VIVAITK 269
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 186 ADAVqDSEMVELVELEIRELLTEFGykgeETPVIVGS------ALCALEGR-DPELGLKSVQK----LLDAVDTYIPVPA 254
Cdd:COG5258 270 IDKV-DDERVEEVEREIENLLRIVG----RTPLEVESrhdvdaAIEEINGRvVPILKTSAVTGegldLLDELFERLPKRA 344
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 255 RDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECeLLGHSKN---IRTVVTGIEMFHKSLERAEAGDNLGALVRG 331
Cdd:COG5258 345 TDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDEL-LIGPTKDgsfREVEVKSIEMHYHRVDKAEAGRIVGIALKG 423
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 332 LKREDLRRGLVMVKPGSI-KPHQKVEAQVYILSK----EEGgrhkpfvshFMPVMFSLTWDMACRIIlPPEKELAMPGED 406
Cdd:COG5258 424 VEEEELERGMVLLPRDADpKAVREFEAEVMVLNHpttiKEG---------YEPVVHLETISEAVRFE-PIDKGYLLPGDS 493
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 34147630 407 ----LKFnliLRQPMILEKGQRFTLRDGnRTIGTGLVTNTL 443
Cdd:COG5258 494 grvrLRF---KYRPYYVEEGQRFVFREG-RSKGVGTVTDIL 530
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
62-224 1.10e-41

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: 147.25  E-value: 1.10e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  62 NVGTIGHVDHGKTTLTAaitKILAEGGG------AKFKKYEE------------IDNAPEERARGITINAAHVEYSTAAR 123
Cdd:cd01883   1 NLVVIGHVDAGKSTLTG---HLLYKLGGvdkrtiEKYEKEAKemgkesfkyawvLDKLKEERERGVTIDVGLAKFETEKY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 124 HYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-------PMPQTREHLLLARQIGVEHVVVYVNKADAVQ---DSE 193
Cdd:cd01883  78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTvnwSQE 157
                       170       180       190
                ....*....|....*....|....*....|.
gi 34147630 194 MVELVELEIRELLTEFGYKGEETPVIVGSAL 224
Cdd:cd01883 158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGF 188
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
59-364 3.47e-40

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 148.85  E-value: 3.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   59 PHVNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITI-------------NAAHVEYSTAA--- 122
Cdd:PRK04000   8 PEVNIGMVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIrlgyadatirkcpDCEEPEAYTTEpkc 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  123 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQD 191
Cdd:PRK04000  75 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  192 SEMVELVElEIRELLTefGYKGEETPVIVGSALcalegrdpelglksvQK-----LLDAVDTYIPVPARDLEKPFLLPVE 266
Cdd:PRK04000 155 ERALENYE-QIKEFVK--GTVAENAPIIPVSAL---------------HKvnidaLIEAIEEEIPTPERDLDKPPRMYVA 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  267 AVYSV--PG------RGTVVTGTLERGILKKGDECELL----------GHSKNIRTVVTGIEMFHKSLERAEAGDNLG-- 326
Cdd:PRK04000 217 RSFDVnkPGtppeklKGGVIGGSLIQGVLKVGDEIEIRpgikveeggkTKWEPITTKIVSLRAGGEKVEEARPGGLVGvg 296
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 34147630  327 -ALVRGLKREDLRRGLVMVKPGSIKP-HQKVEAQVYILSK 364
Cdd:PRK04000 297 tKLDPSLTKADALAGSVAGKPGTLPPvWESLTIEVHLLER 336
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
56-439 6.15e-40

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 149.08  E-value: 6.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   56 RDKPHVNVGTIGHVDHGKTTLTAAIT---------------KILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYST 120
Cdd:PLN00043   3 KEKVHINIVVIGHVDSGKSTTTGHLIyklggidkrvierfeKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFET 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  121 AARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMP-------QTREHLLLARQIGVEHVVVYVNKADAVQ--- 190
Cdd:PLN00043  83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTpky 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  191 DSEMVELVELEIRELLTEFGYKGEETPVIvgsALCALEG-----RDPELGLKSVQKLLDAVDTyIPVPARDLEKPFLLPV 265
Cdd:PLN00043 163 SKARYDEIVKEVSSYLKKVGYNPDKIPFV---PISGFEGdnmieRSTNLDWYKGPTLLEALDQ-INEPKRPSDKPLRLPL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  266 EAVYSVPGRGTVVTGTLERGILKKGDECELLghSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVM-- 343
Cdd:PLN00043 239 QDVYKIGGIGTVPVGRVETGVIKPGMVVTFG--PTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAsn 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  344 VKPGSIKPHQKVEAQVYILSK--EEGGRHKPFV----SHfMPVMFSltwDMACRIILPPEKELAMPGEDLK------FNL 411
Cdd:PLN00043 317 SKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLdchtSH-IAVKFA---EILTKIDRRSGKELEKEPKFLKngdagfVKM 392
                        410       420       430
                 ....*....|....*....|....*....|....
gi 34147630  412 ILRQPMILEKGQ------RFTLRDGNRTIGTGLV 439
Cdd:PLN00043 393 IPTKPMVVETFSeypplgRFAVRDMRQTVAVGVI 426
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
63-224 6.68e-40

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: 141.20  E-value: 6.68e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  63 VGTIGHVDHGKTTLTAAITKIlaegggakfkkyeEIDNAPEERARGITINA--AHVEYSTAaRHYAHTDCPGHADYVKNM 140
Cdd:cd04171   2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLgfAYLDLPDG-KRLGFIDVPGHEKFVKNM 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 141 ITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVqDSEMVELVELEIRELLTEFGYkgEETPVIV 220
Cdd:cd04171  68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFL--ADAPIFP 144

                ....
gi 34147630 221 GSAL 224
Cdd:cd04171 145 VSSV 148
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
65-359 3.72e-39

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: 146.39  E-value: 3.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  65 TIGHVDHGKTTLT---------------AAITKILAEGGgakfkkYEEIDNAP------EERARGITINAAHVEYSTAAR 123
Cdd:COG2895  22 TCGSVDDGKSTLIgrllydtksifedqlAALERDSKKRG------TQEIDLALltdglqAEREQGITIDVAYRYFSTPKR 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 124 HYAHTDCPGHADYVKNMITG--TAplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMV-ELVEL 200
Cdd:COG2895  96 KFIIADTPGHEQYTRNMVTGasTA--DLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVfEEIVA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 201 EIRELLTEFGYKgEETPVIVgSalcALEG-----RDPEL----GlksvQKLLDAVDTyIPVPARDLEKPFLLPVEAVYSv 271
Cdd:COG2895 174 DYRAFAAKLGLE-DITFIPI-S---ALKGdnvveRSENMpwydG----PTLLEHLET-VEVAEDRNDAPFRFPVQYVNR- 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 272 PG---RGtvVTGTLERGILKKGDECELLGHskNIRTVVTGIEMFHKSLERAEAGDNLGaLVrgLKRE-DLRRGLVMVKPG 347
Cdd:COG2895 243 PNldfRG--YAGTIASGTVRVGDEVVVLPS--GKTSTVKSIVTFDGDLEEAFAGQSVT-LT--LEDEiDISRGDVIVAAD 315
                       330
                ....*....|...
gi 34147630 348 S-IKPHQKVEAQV 359
Cdd:COG2895 316 ApPEVADQFEATL 328
GCD11 COG5257
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ...
59-296 1.23e-38

Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444075 [Multi-domain]  Cd Length: 408  Bit Score: 144.59  E-value: 1.23e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  59 PHVNVGTIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVE--------------YSTAA-- 122
Cdd:COG5257   4 PEVNIGVVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYADatfykcpnceppeaYTTEPkc 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 123 ----------RHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQD 191
Cdd:COG5257  71 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 192 SEMVELVElEIRELLTefGYKGEETPVIVGSALcalegrdpelglksvQK-----LLDAVDTYIPVPARDLEKPFLLPVE 266
Cdd:COG5257 151 ERALENYE-QIKEFVK--GTVAENAPIIPVSAQ---------------HKvnidaLIEAIEEEIPTPERDLSKPPRMLVA 212
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 34147630 267 AVYSV--PG------RGTVVTGTLERGILKKGDECELL 296
Cdd:COG5257 213 RSFDVnkPGtppkdlKGGVIGGSLIQGVLKVGDEIEIR 250
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
65-340 3.33e-38

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 146.73  E-value: 3.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   65 TIGHVDHGKTTLTAAITKILAegggakfkkyeeiDNAPEERARGITINAAHVEYSTA-ARHYAHTDCPGHADYVKNMITG 143
Cdd:PRK10512   5 TAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWPQPdGRVLGFIDVPGHEKFLSNMLAG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  144 TAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVElVELEIRELLTEFGYkgEETPVIVGSA 223
Cdd:PRK10512  72 VGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGF--AEAKLFVTAA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  224 LCalegrdpELGLKSVQKLLDAvdtyIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSKNIR 303
Cdd:PRK10512 149 TE-------GRGIDALREHLLQ----LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMR 217
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 34147630  304 tvVTGIEMFHKSLERAEAGDNLGALVRG-LKREDLRRG 340
Cdd:PRK10512 218 --VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
348-441 2.76e-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: 129.31  E-value: 2.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   348 SIKPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRII-----LPPEK-----ELAMPGEDLKFNLILRQPM 417
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhkLDPGGvsenpEFVMPGDNVIVTVELIKPI 80
                          90       100
                  ....*....|....*....|....
gi 34147630   418 ILEKGQRFTLRDGNRTIGTGLVTN 441
Cdd:pfam03143  81 ALEKGQRFAIREGGRTVAAGVVTE 104
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
350-439 5.28e-35

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: 125.32  E-value: 5.28e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 350 KPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRD 429
Cdd:cd03707   1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80
                        90
                ....*....|
gi 34147630 430 GNRTIGTGLV 439
Cdd:cd03707  81 GGRTVGAGVV 90
TypA_BipA TIGR01394
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ...
62-323 1.08e-33

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: 133.58  E-value: 1.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630    62 NVGTIGHVDHGKTTLtaaITKILAEGGgaKFKKYEEI-----DNAPEERARGITINAAHVeystaARHYAHT-----DCP 131
Cdd:TIGR01394   3 NIAIIAHVDHGKTTL---VDALLKQSG--TFRANEAVaervmDSNDLERERGITILAKNT-----AIRYNGTkinivDTP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   132 GHADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADavQDSEMVELVELEIREL 205
Cdd:TIGR01394  73 GHADFggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKID--RPSARPDEVVDEVFDL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   206 LTEFGYKGE--ETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLE 283
Cdd:TIGR01394 144 FAELGADDEqlDFPIVYASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVH 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 34147630   284 RGILKKGDECELLGHSKNIRTVVTGIEMFHKSLER-----AEAGD 323
Cdd:TIGR01394 224 RGTVKKGQQVALMKRDGTIENGRISKLLGFEGLERveideAGAGD 268
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
61-364 2.90e-31

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 125.12  E-value: 2.90e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   61 VNVGTIGHVDHGKTTLTAAITKILAegggAKFKkyeeidnapEERARGITI-----NA------------AHVEYS---- 119
Cdd:PTZ00327  35 INIGTIGHVAHGKSTVVKALSGVKT----VRFK---------REKVRNITIklgyaNAkiykcpkcprptCYQSYGsskp 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  120 ------------TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKA 186
Cdd:PTZ00327 102 dnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKI 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  187 DAVQDSEMVELVElEIRELLTefGYKGEETPVIVGSALcalegrdpelgLK-SVQKLLDAVDTYIPVPARDLEKPFLLPV 265
Cdd:PTZ00327 182 DLVKEAQAQDQYE-EIRNFVK--GTIADNAPIIPISAQ-----------LKyNIDVVLEYICTQIPIPKRDLTSPPRMIV 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  266 EAVYSV--PG------RGTVVTGTLERGILKKGDECELLG--HSKN---------IRTVVTGIEMFHKSLERAEAGDNLG 326
Cdd:PTZ00327 248 IRSFDVnkPGedienlKGGVAGGSILQGVLKVGDEIEIRPgiISKDsggeftcrpIRTRIVSLFAENNELQYAVPGGLIG 327
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 34147630  327 A---LVRGLKREDLRRGLVMVKPGSIKP-HQKVEAQVYILSK 364
Cdd:PTZ00327 328 VgttIDPTLTRADRLVGQVLGYPGKLPEvYAEIEIQYYLLRR 369
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
61-255 6.14e-30

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: 115.06  E-value: 6.14e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  61 VNVGTIGHVDHGKTTLTAAITKILAEgggaKFKkyEEIDnapeeraRGITI-----NA--------------AHVEYS-- 119
Cdd:cd01888   1 INIGTIGHVAHGKTTLVKALSGVWTV----RHK--EELK-------RNITIklgyaNAkiykcpncgcprpyDTPECEcp 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 120 ------TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDG-PMPQTREHLLLARQIGVEHVVVYVNKADAVQDS 192
Cdd:cd01888  68 gcggetKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34147630 193 EMVELVElEIRELLTefGYKGEETPVIVGSALcalegrdpelgLK-SVQKLLDAVDTYIPVPAR 255
Cdd:cd01888 148 QALENYE-QIKEFVK--GTIAENAPIIPISAQ-----------LKyNIDVLCEYIVKKIPTPPR 197
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
65-224 4.89e-29

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: 113.05  E-value: 4.89e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  65 TIGHVDHGKTTLTAAI---TKILAEGGGAKFKKY-------EEIDNA------PEERARGITINAAHVEYSTAARHYAHT 128
Cdd:cd04166   4 TCGSVDDGKSTLIGRLlydSKSIFEDQLAALERSkssgtqgEKLDLAllvdglQAEREQGITIDVAYRYFSTPKRKFIIA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 129 DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMV-ELVELEIRELLT 207
Cdd:cd04166  84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVfEEIKADYLAFAA 163
                       170
                ....*....|....*..
gi 34147630 208 EFGYkgEETPVIVGSAL 224
Cdd:cd04166 164 SLGI--EDITFIPISAL 178
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
65-351 5.73e-29

sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 213679 [Multi-domain]  Cd Length: 406  Bit Score: 117.47  E-value: 5.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630    65 TIGHVDHGKTTLTAAI---TKILAEGGGAKFKK--------YEEIDNA------PEERARGITINAAHVEYSTAARHYAH 127
Cdd:TIGR02034   5 TCGSVDDGKSTLIGRLlhdTKQIYEDQLAALERdskkhgtqGGEIDLAllvdglQAEREQGITIDVAYRYFSTDKRKFIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   128 TDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMV-ELVELEIRELL 206
Cdd:TIGR02034  85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVfENIKKDYLAFA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   207 TEFGYKgeetpVIVGSALCALEGRDPELGLKSV-----QKLLDAVDTyIPVPARDLEKPFLLPVEAVySVPG---RGtvV 278
Cdd:TIGR02034 165 EQLGFR-----DVTFIPLSALKGDNVVSRSESMpwysgPTLLEILET-VEVERDAQDLPLRFPVQYV-NRPNldfRG--Y 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34147630   279 TGTLERGILKKGDECELLGHSKNIRtvVTGIEMFHKSLERAEAGDnlgALVRGLKRE-DLRRGLVMVKPGSIKP 351
Cdd:TIGR02034 236 AGTIASGSVHVGDEVVVLPSGRSSR--VARIVTFDGDLEQARAGQ---AVTLTLDDEiDISRGDLLAAADSAPE 304
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
62-323 2.67e-28

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 117.81  E-value: 2.67e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  62 NVGTIGHVDHGKTTLtaaITKILAEGGgaKFKKYEEI-----DNAPEERARGITINAAHveysTAARHYAHT----DCPG 132
Cdd:COG1217   8 NIAIIAHVDHGKTTL---VDALLKQSG--TFRENQEVaervmDSNDLERERGITILAKN----TAVRYKGVKinivDTPG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 133 HADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNK-------ADAVQDsEMVEL-V 198
Cdd:COG1217  79 HADFggeverVLSMV------DGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVV-INKidrpdarPDEVVD-EVFDLfI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 199 ELEIRELLTEFgykgeetPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAV-YSvPGRGTV 277
Cdd:COG1217 151 ELGATDEQLDF-------PVVYASARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLdYS-DYVGRI 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 34147630 278 VTGTLERGILKKGDECELLGHSKNIRTV-VTGIEMFHKsLER-----AEAGD 323
Cdd:COG1217 223 AIGRIFRGTIKKGQQVALIKRDGKVEKGkITKLFGFEG-LERveveeAEAGD 273
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
62-253 2.80e-26

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: 104.98  E-value: 2.80e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  62 NVGTIGHVDHGKTTLtaaITKILAEGGGakFKKYEEI-----DNAPEERARGITINAAHveystAARHYAHT-----DCP 131
Cdd:cd01891   4 NIAIIAHVDHGKTTL---VDALLKQSGT--FRENEEVgervmDSNDLERERGITILAKN-----TAITYKDTkiniiDTP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 132 GHADY------VKNMItgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADavQDSEMVELVELEIREL 205
Cdd:cd01891  74 GHADFggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKID--RPDARPEEVVDEVFDL 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 34147630 206 LTEFGYKGE--ETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVP 253
Cdd:cd01891 145 FLELNATDEqlDFPIVYASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP 194
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
65-450 6.30e-26

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 109.62  E-value: 6.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   65 TIGHVDHGKTTL-------TAAI------------TKILAEGggakfkkyEEIDNA------PEERARGITINAAHVEYS 119
Cdd:PRK05124  32 TCGSVDDGKSTLigrllhdTKQIyedqlaslhndsKRHGTQG--------EKLDLAllvdglQAEREQGITIDVAYRYFS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  120 TAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEmvELVE 199
Cdd:PRK05124 104 TEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDYSE--EVFE 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  200 lEIRELLTEFGYKGEETPVIVGSALCALEG-----RDPELGLKSVQKLLDAVDTyIPVPARDLEKPFLLPVEAVySVPG- 273
Cdd:PRK05124 182 -RIREDYLTFAEQLPGNLDIRFVPLSALEGdnvvsQSESMPWYSGPTLLEVLET-VDIQRVVDAQPFRFPVQYV-NRPNl 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  274 --RGtvVTGTLERGILKKGDECELL--GHSKNIRTVVTgiemFHKSLERAEAGDnlgALVRGLKRE-DLRRGLVMVKPGS 348
Cdd:PRK05124 259 dfRG--YAGTLASGVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGE---AITLVLEDEiDISRGDLLVAADE 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  349 -IKPHQKVEAQV-------------Y---ILSKEEGGRHKPfVSHFMPVMfSLTWDMAcriilppeKELAMPG---EDLK 408
Cdd:PRK05124 330 aLQAVQHASADVvwmaeqplqpgqsYdikIAGKKTRARVDA-IRYQVDIN-TLTQREA--------ENLPLNGiglVELT 399
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 34147630  409 FNlilrQPMILEKGQR------FTL--RDGNRTIGTGLVTNTLAMTEEEK 450
Cdd:PRK05124 400 FD----EPLVLDPYQQnrvtggFIFidRLTNVTVGAGMVREPLAQATAAP 445
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
61-224 1.15e-23

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: 97.82  E-value: 1.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  61 VNVGTIGHVDHGKTTLTAAITKILAEgggAKFkkyeeiDNAPEERARGITIN----------AAHVEYSTAARH--YAHT 128
Cdd:cd01889   1 VNVGLLGHVDSGKTSLAKALSEIAST---AAF------DKNPQSQERGITLDlgfssfevdkPKHLEDNENPQIenYQIT 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 129 --DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADAVQDSEMVELVElEIRELL 206
Cdd:cd01889  72 lvDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEERKRKIE-KMKKRL 149
                       170       180
                ....*....|....*....|
gi 34147630 207 --TEFGYKGEETPVIVGSAL 224
Cdd:cd01889 150 qkTLEKTRLKDSPIIPVSAK 169
PRK10218 PRK10218
translational GTPase TypA;
62-323 6.82e-23

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 101.71  E-value: 6.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   62 NVGTIGHVDHGKTTLtaaITKILAEGG--GAKFKKYEEI-DNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVK 138
Cdd:PRK10218   7 NIAIIAHVDHGKTTL---VDKLLQQSGtfDSRAETQERVmDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  139 NMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADavQDSEMVELVELEIRELLTEFGYKGEET-- 216
Cdd:PRK10218  84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVD--RPGARPDWVVDQVFDLFVNLDATDEQLdf 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  217 PVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELL 296
Cdd:PRK10218 161 PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
                        250       260       270
                 ....*....|....*....|....*....|..
gi 34147630  297 GHSKNIRTVVTGIEMFHKSLER-----AEAGD 323
Cdd:PRK10218 241 DSEGKTRNAKVGKVLGHLGLERietdlAEAGD 272
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
46-347 1.50e-22

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 100.39  E-value: 1.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   46 LAVEAKKTYVRdkphvnVGTIGHVDHGKTTLT---------------AAITKILAEGGgakfKKYEEIDNA------PEE 104
Cdd:PRK05506  16 LAQHERKSLLR------FITCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVG----TQGDEIDLAllvdglAAE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  105 RARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVN 184
Cdd:PRK05506  86 REQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVN 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  185 KADAVQDSEMV-ELVELEIRELLTEFGYkgeetPVIVGSALCALEG-----RDPELGLKSVQKLLDAVDTyIPVPARDLE 258
Cdd:PRK05506 166 KMDLVDYDQEVfDEIVADYRAFAAKLGL-----HDVTFIPISALKGdnvvtRSARMPWYEGPSLLEHLET-VEIASDRNL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  259 KPFLLPVEAVySVPG---RGtvVTGTLERGILKKGDECELLGHSKniRTVVTGIEMFHKSLERAEAGDnlgALVRGLKRE 335
Cdd:PRK05506 240 KDFRFPVQYV-NRPNldfRG--FAGTVASGVVRPGDEVVVLPSGK--TSRVKRIVTPDGDLDEAFAGQ---AVTLTLADE 311
                        330
                 ....*....|...
gi 34147630  336 -DLRRGLVMVKPG 347
Cdd:PRK05506 312 iDISRGDMLARAD 324
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
67-224 4.48e-19

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: 84.06  E-value: 4.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  67 GHVDHGKTTLTAAITKIlaegggakfkkyeeidNAPEERARGIT--INAAHVEYSTAARHYAHTDCPGHADYvKNMIT-G 143
Cdd:cd01887   7 GHVDHGKTTLLDKIRKT----------------NVAAGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRArG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 144 TAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQDSEmvELVElEIRELLTEFGYKGEE----TPVI 219
Cdd:cd01887  70 ASVTDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTE--ADPE-RVKNELSELGLVGEEwggdVSIV 145

                ....*
gi 34147630 220 VGSAL 224
Cdd:cd01887 146 PISAK 150
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
350-439 1.73e-18

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: 80.51  E-value: 1.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 350 KPHQKVEAQVYILSKEeggrhKPFVSHFMPVMFSLTWDMACRIILPPEKE-----------LAMPGEDLKFNLILRQPMI 418
Cdd:cd01513   1 QAVWKFDAKVIVLEHP-----KPIRPGYKPVMDVGTAHVPGRIAKLLSKEdgktkekkppdSLQPGENGTVEVELQKPVV 75
                        90       100
                ....*....|....*....|....*..
gi 34147630 419 LEKG------QRFTLRDGNRTIGTGLV 439
Cdd:cd01513  76 LERGkefptlGRFALRDGGRTVGAGLI 102
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
261-342 6.26e-18

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: 78.34  E-value: 6.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 261 FLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGhsKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRG 340
Cdd:cd03696   1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPP--LGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78

                ..
gi 34147630 341 LV 342
Cdd:cd03696  79 FV 80
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
258-347 1.66e-17

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: 77.23  E-value: 1.66e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 258 EKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLghSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDL 337
Cdd:cd03693   2 DKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFA--PAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDI 79
                        90
                ....*....|
gi 34147630 338 RRGLVMVKPG 347
Cdd:cd03693  80 KRGDVAGDSK 89
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
62-333 9.52e-17

translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]


Pssm-ID: 129581 [Multi-domain]  Cd Length: 720  Bit Score: 83.02  E-value: 9.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630    62 NVGTIGHVDHGKTTLT-------AAITKILAegGGAKFKKYEEidnapEERARGITINAAHV----EYSTAARHYAHTDC 130
Cdd:TIGR00490  21 NIGIVAHIDHGKTTLSdnllagaGMISEELA--GQQLYLDFDE-----QEQERGITINAANVsmvhEYEGNEYLINLIDT 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   131 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLllaRQIGVEHV--VVYVNKADAVQDSEMVELVELEIR----- 203
Cdd:TIGR00490  94 PGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVL---RQALKENVkpVLFINKVDRLINELKLTPQELQERfikii 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   204 -------------ELLTEFGYKGEETPVIVGSAL-----------------------CAlEGRDPELGLKS--VQKLLDA 245
Cdd:TIGR00490 171 tevnklikamapeEFRDKWKVRVEDGSVAFGSAYynwaisvpsmkktgigfkdiykyCK-EDKQKELAKKSplHQVVLDM 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   246 VDTYIPVPAR-------------------------DLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSK 300
Cdd:TIGR00490 250 VIRHLPSPIEaqkyripviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKA 329
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 34147630   301 NIRTVVTGIEMFHKSLERAE--AGdNLGALVrGLK 333
Cdd:TIGR00490 330 KARIQQVGVYMGPERVEVDEipAG-NIVAVI-GLK 362
PRK07560 PRK07560
elongation factor EF-2; Reviewed
62-356 1.37e-16

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 82.22  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   62 NVGTIGHVDHGKTTLT-----AA--ITKILAegGGAKFKKYEEidnapEERARGITINAAHV----EYSTAARHYAHTDC 130
Cdd:PRK07560  22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA--GEQLALDFDE-----EEQARGITIKAANVsmvhEYEGKEYLINLIDT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  131 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTrEHLLlaRQIGVEHV--VVYVNKAD------AVQDSEMVE-LVEL- 200
Cdd:PRK07560  95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQALRERVkpVLFINKVDrlikelKLTPQEMQQrLLKIi 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  201 -EIRELLTEFG---YKG------EETPVIVGSAL-----------------------CaLEGRDPELGLKS--VQKLLDA 245
Cdd:PRK07560 172 kDVNKLIKGMApeeFKEkwkvdvEDGTVAFGSALynwaisvpmmqktgikfkdiidyY-EKGKQKELAEKAplHEVVLDM 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  246 VDTYIPVPAR------------DLEK-------------PFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSK 300
Cdd:PRK07560 251 VVKHLPNPIEaqkyripkiwkgDLNSevgkamlncdpngPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKK 330
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34147630  301 NIRTVVTGIEM--FHKSLERAEAGdNLGALVrGLKreDLRRGLVMVKPGSIKPHQKVE 356
Cdd:PRK07560 331 KNRVQQVGIYMgpEREEVEEIPAG-NIAAVT-GLK--DARAGETVVSVEDMTPFESLK 384
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
261-342 1.57e-16

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: 1.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 261 FLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGhsKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKreDLRRG 340
Cdd:cd01342   1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP--KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76

                ..
gi 34147630 341 LV 342
Cdd:cd01342  77 DT 78
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
62-187 8.58e-16

Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.


Pssm-ID: 206672 [Multi-domain]  Cd Length: 218  Bit Score: 76.12  E-value: 8.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  62 NVGTIGHVDHGKTTLT---AAITKILAE--GGGAKFkkyeeIDNAPEERARGITINAAHV----EYSTAARHYAH----- 127
Cdd:cd01885   2 NICIIAHVDHGKTTLSdslLASAGIISEklAGKARY-----LDTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinl 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34147630 128 TDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLllaRQIGVEHV--VVYVNKAD 187
Cdd:cd01885  77 IDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVL---RQALEERVkpVLVINKID 135
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
62-208 9.71e-16

Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.


Pssm-ID: 206731 [Multi-domain]  Cd Length: 237  Bit Score: 76.51  E-value: 9.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  62 NVGTIGHVDHGKTTLT-------AAITKIlaeggGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHA 134
Cdd:cd04168   1 NIGILAHVDAGKTTLTesllytsGAIREL-----GSVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHM 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147630 135 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAV-QDSEMvelVELEIRELLTE 208
Cdd:cd04168  76 DFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIP-TIIFVNKIDRAgADLEK---VYQEIKEKLSP 146
IF-2 TIGR00487
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ...
58-291 1.25e-15

translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]


Pssm-ID: 273102 [Multi-domain]  Cd Length: 587  Bit Score: 79.04  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630    58 KPHVnVGTIGHVDHGKTTLTAAITKIlaegggakfkkyeeidNAPEERARGIT--INAAHVEYSTAaRHYAHTDCPGHAD 135
Cdd:TIGR00487  86 RPPV-VTIMGHVDHGKTSLLDSIRKT----------------KVAQGEAGGITqhIGAYHVENEDG-KMITFLDTPGHEA 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   136 YVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADavQDSEMVELVELEirelLTEFGYKGE- 214
Cdd:TIGR00487 148 FTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKID--KPEANPDRVKQE----LSEYGLVPEd 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   215 ---ETPVIVGSALCAlegrdpelglKSVQKLLDA------VDTYIPVPARDLEKpfllPVEAVYSVPGRGTVVTGTLERG 285
Cdd:TIGR00487 221 wggDTIFVPVSALTG----------DGIDELLDMillqseVEELKANPNGQASG----VVIEAQLDKGRGPVATVLVQSG 286

                  ....*.
gi 34147630   286 ILKKGD 291
Cdd:TIGR00487 287 TLRVGD 292
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
275-344 1.51e-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: 71.14  E-value: 1.51e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34147630   275 GTVVTGTLERGILKKGDECELLGHS---KNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMV 344
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGtgkKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
66-330 2.92e-15

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 78.24  E-value: 2.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   66 IGHVDHGKTTLTAAitkILAEGGgaKFKKYEEI-------DNAPEERARGITIN--AAHVEYstaaRHYAHT--DCPGHA 134
Cdd:PRK12740   1 VGHSGAGKTTLTEA---ILFYTG--AIHRIGEVedgtttmDFMPEERERGISITsaATTCEW----KGHKINliDTPGHV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  135 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKAD-----------AVQD------------ 191
Cdd:PRK12740  72 DFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIF-VNKMDragadffrvlaQLQEklgapvvplqlp 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  192 ---------------------------------SEMVELVElEIRELLTE-------------FGykGEE---------- 215
Cdd:PRK12740 151 igegddftgvvdllsmkayrydeggpseeieipAELLDRAE-EAREELLEalaefddelmekyLE--GEElseeeikagl 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  216 ---------TPVIVGSAlcalegrdpeLGLKSVQKLLDAVDTYIPVPAR-----------------DLEKPFLLPVEAVY 269
Cdd:PRK12740 228 rkatlageiVPVFCGSA----------LKNKGVQRLLDAVVDYLPSPLEvppvdgedgeegaelapDPDGPLVALVFKTM 297
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147630  270 SVPGRGTVVTGTLERGILKKGDECELLGHSKNIRtvVTGIEMFH----KSLERAEAGDnLGALVR 330
Cdd:PRK12740 298 DDPFVGKLSLVRVYSGTLKKGDTLYNSGTGKKER--VGRLYRMHgkqrEEVDEAVAGD-IVAVAK 359
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
261-344 5.90e-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: 69.94  E-value: 5.90e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 261 FLLPVEAVYSVPGRGTVVTGTLERGILKKGDECeLLGHSKN---IRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDL 337
Cdd:cd03694   1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLGPDADgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79

                ....*..
gi 34147630 338 RRGLVMV 344
Cdd:cd03694  80 RKGMVLV 86
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
62-187 2.80e-14

Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 75.08  E-value: 2.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  62 NVGTIGHVDHGKTTLTAAitkILAEGGgaKFKKYEEI-------DNAPEERARGITIN--AAHVEYstaaRHYAHT--DC 130
Cdd:COG0480  11 NIGIVAHIDAGKTTLTER---ILFYTG--AIHRIGEVhdgntvmDWMPEEQERGITITsaATTCEW----KGHKINiiDT 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 34147630 131 PGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHvVVYVNKAD 187
Cdd:COG0480  82 PGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPR-IVFVNKMD 137
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
65-291 8.44e-14

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: 73.12  E-value: 8.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  65 TI-GHVDHGKTTLTAAI--TKIlAEGggakfkkyeeidnapeErARGIT--INAAHVEYSTaaRHYAHTDCPGHADYVKn 139
Cdd:COG0532   8 TVmGHVDHGKTSLLDAIrkTNV-AAG----------------E-AGGITqhIGAYQVETNG--GKITFLDTPGHEAFTA- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 140 M------ITgtaplDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQ-DSEMV--ELVELEIreLLTEFG 210
Cdd:COG0532  67 MrargaqVT-----DIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGaNPDRVkqELAEHGL--VPEEWG 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 211 ykGeETPVIVGSalcALEGrdpeLGLksvQKLLDAVdtyipvpardlekpfLLPVE-----AVYSVPGRGTVVTGTLE-- 283
Cdd:COG0532 139 --G-DTIFVPVS---AKTG----EGI---DELLEMI---------------LLQAEvlelkANPDRPARGTVIEAKLDkg 190
                       250
                ....*....|....*...
gi 34147630 284 ----------RGILKKGD 291
Cdd:COG0532 191 rgpvatvlvqNGTLKVGD 208
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
62-253 9.97e-13

LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.


Pssm-ID: 206677 [Multi-domain]  Cd Length: 179  Bit Score: 66.40  E-value: 9.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  62 NVGTIGHVDHGKTTLTAAI---TKILAEGGgakfKKYEEIDNAPEERARGITINAahveySTAARHYAHT---------- 128
Cdd:cd01890   2 NFSIIAHIDHGKSTLADRLlelTGTVSERE----MKEQVLDSMDLERERGITIKA-----QAVRLFYKAKdgeeyllnli 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 129 DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADAVqdSEMVELVELEIRELLte 208
Cdd:cd01890  73 DTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPV-INKIDLP--AADPDRVKQEIEDVL-- 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 34147630 209 fGYKGEEtpVIVGSAlcalegrdpELGLkSVQKLLDAVDTYIPVP 253
Cdd:cd01890 148 -GLDASE--AILVSA---------KTGL-GVEDLLEAIVERIPPP 179
PRK13351 PRK13351
elongation factor G-like protein;
62-187 1.90e-12

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 69.21  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   62 NVGTIGHVDHGKTTLTAAitkILAEGGgaKFKKYEEIDNA-------PEERARGITINAAhveysTAARHYAHT-----D 129
Cdd:PRK13351  10 NIGILAHIDAGKTTLTER---ILFYTG--KIHKMGEVEDGttvtdwmPQEQERGITIESA-----ATSCDWDNHrinliD 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34147630  130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHvVVYVNKAD 187
Cdd:PRK13351  80 TPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPR-LIFINKMD 136
infB CHL00189
translation initiation factor 2; Provisional
53-246 9.91e-12

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 67.16  E-value: 9.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   53 TYVRDKPHVNVgtIGHVDHGKTTLTAAITKilaegggakfkkyeeiDNAPEERARGIT--INAAHVE--YSTAARHYAHT 128
Cdd:CHL00189 239 NSINRPPIVTI--LGHVDHGKTTLLDKIRK----------------TQIAQKEAGGITqkIGAYEVEfeYKDENQKIVFL 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  129 DCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQDSemVELV--ELEIRELL 206
Cdd:CHL00189 301 DTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANAN--TERIkqQLAKYNLI 377
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 34147630  207 TEfgYKGEETPVIvgsALCALEGRDpelglksVQKLLDAV 246
Cdd:CHL00189 378 PE--KWGGDTPMI---PISASQGTN-------IDKLLETI 405
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
62-188 1.94e-11

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 64.15  E-value: 1.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  62 NVGTIGHVDHGKTTLTAAitkILAEGG-----GAKFKKYEEIDNAPEERARGITINA--AHVEYSTaARHYAhTDCPGHA 134
Cdd:cd04170   1 NIALVGHSGSGKTTLAEA---LLYATGaidrlGRVEDGNTVSDYDPEEKKRKMSIETsvAPLEWNG-HKINL-IDTPGYA 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 34147630 135 DYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVyVNKADA 188
Cdd:cd04170  76 DFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIF-INKMDR 128
PTZ00416 PTZ00416
elongation factor 2; Provisional
57-187 3.19e-11

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 65.45  E-value: 3.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   57 DKPHV--NVGTIGHVDHGKTTLT-AAITK--ILAEG--GGAKFkkyeeIDNAPEERARGITINaahveySTA-ARHYAHT 128
Cdd:PTZ00416  14 DNPDQirNMSVIAHVDHGKSTLTdSLVCKagIISSKnaGDARF-----TDTRADEQERGITIK------STGiSLYYEHD 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34147630  129 ---------------DCPGHADYVKNMitgTAPL---DGCILVVAANDGPMPQTrEHLLlaRQIGVEHV--VVYVNKAD 187
Cdd:PTZ00416  83 ledgddkqpflinliDSPGHVDFSSEV---TAALrvtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVD 155
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
62-187 7.70e-11

Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.


Pssm-ID: 206673 [Multi-domain]  Cd Length: 270  Bit Score: 62.51  E-value: 7.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  62 NVGTIGHVDHGKTTLTAAI------TKILAE--GGGAKfkkyeeIDNAPEERARGITINAAhveySTAARHYAHT----D 129
Cdd:cd01886   1 NIGIIAHIDAGKTTTTERIlyytgrIHKIGEvhGGGAT------MDWMEQERERGITIQSA----ATTCFWKDHRiniiD 70
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 34147630 130 CPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKAD 187
Cdd:cd01886  71 TPGHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVP-RIAFVNKMD 127
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
62-187 1.77e-10

Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.


Pssm-ID: 206730 [Multi-domain]  Cd Length: 213  Bit Score: 60.36  E-value: 1.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  62 NVGTIGHVDHGKTTLT-----AAITKILAEGGGAKFKKYeeIDNAPEERARGITINAAHVEYSTA-ARHYAHT----DCP 131
Cdd:cd04167   2 NVCIAGHLHHGKTSLLdmlieQTHKRTPSVKLGWKPLRY--TDTRKDEQERGISIKSNPISLVLEdSKGKSYLiniiDTP 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 34147630 132 GHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVeHVVVYVNKAD 187
Cdd:cd04167  80 GHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGL-PMVLVINKID 134
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
57-187 6.83e-08

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 55.12  E-value: 6.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630   57 DKPH--VNVGTIGHVDHGKTTLT---AAITKILAE--GGGAKFkkyeeIDNAPEERARGITINAAHV----EYSTAA-RH 124
Cdd:PLN00116  14 DKKHniRNMSVIAHVDHGKSTLTdslVAAAGIIAQevAGDVRM-----TDTRADEAERGITIKSTGIslyyEMTDESlKD 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34147630  125 YAHT-----------DCPGHADYVKNMitgTAPL---DGCILVVAANDGPMPQTrEHLLlaRQIGVEHV--VVYVNKAD 187
Cdd:PLN00116  89 FKGErdgneylinliDSPGHVDFSSEV---TAALritDGALVVVDCIEGVCVQT-ETVL--RQALGERIrpVLTVNKMD 161
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
260-343 1.68e-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: 45.55  E-value: 1.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 260 PFLLPVEAVYSvpGRGTVVTGTLERGILKKGDECELLghSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRR 339
Cdd:cd04089   1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLM--PNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISP 76

                ....
gi 34147630 340 GLVM 343
Cdd:cd04089  77 GFVL 80
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
260-343 1.80e-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: 45.96  E-value: 1.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 260 PFLLPVEAVYSVPgRGTVVTGTLERGILKKGDecELLGHSKNIRTVVTGIEM-FHKSLERAEAGDNLGALVRGLKREDLR 338
Cdd:cd03698   1 PFRLSIDDKYKSP-RGTTVTGKLEAGSIQKNQ--VLYDMPSQQDAEVKNIIRnSDEETDWAIAGDTVTLRLRGIEVEDIQ 77

                ....*
gi 34147630 339 RGLVM 343
Cdd:cd03698  78 PGDIL 82
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
66-187 5.16e-06

Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.


Pssm-ID: 206732 [Multi-domain]  Cd Length: 268  Bit Score: 47.98  E-value: 5.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  66 IGHVDHGKTTLTaaiTKILAEGG---------GAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADY 136
Cdd:cd04169   8 ISHPDAGKTTLT---EKLLLFGGaiqeagavkARKSRKHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDF 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 34147630 137 VKNMI-TGTApLDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKAD 187
Cdd:cd04169  85 SEDTYrTLTA-VDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLD 134
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
62-200 9.21e-06

GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.


Pssm-ID: 206728 [Multi-domain]  Cd Length: 224  Bit Score: 46.51  E-value: 9.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  62 NVGTIGHVDHGKTTLTAAITK-ILAEG-GGAK---FKKYEEIdnapeERARGITINAAHVEYSTAAR----HYAHT---- 128
Cdd:cd04165   1 RVAVVGNVDAGKSTLLGVLTQgELDNGrGKARlnlFRHKHEV-----ESGRTSSVSNDILGFDSDGEvvnyPDNHLgeld 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 129 --------------DCPGHADYVKNMI---TGTAPlDGCILVVAANDGPMPQTREHLLLARQIGVEhVVVYVNKADAVQD 191
Cdd:cd04165  76 veiceksskvvtfiDLAGHERYLKTTVfgmTGYAP-DYAMLVVGANAGIIGMTKEHLGLALALKVP-VFVVVTKIDMTPA 153

                ....*....
gi 34147630 192 SEMVELVEL 200
Cdd:cd04165 154 NVLQETLKD 162
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
66-224 2.06e-05

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 44.75  E-value: 2.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630  66 IGHVDHGKTTLTAAITkilaegggakfkkYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTA 145
Cdd:cd00882   3 VGRGGVGKSSLLNALL-------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 146 PL-----DGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYV-NKADAVQDSEMVELVELEIRElltefgyKGEETPVI 219
Cdd:cd00882  70 RLllrgaDLILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVgNKIDLLEEREVEELLRLEELA-------KILGVPVF 142

                ....*
gi 34147630 220 VGSAL 224
Cdd:cd00882 143 EVSAK 147
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
61-187 3.18e-05

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 44.28  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630    61 VNVGTIGHVDHGKTTLTAAITK----ILAEGGGAkfkkyEEIDNAPEERARGITINAAHVeystaarhyahtDCPGHADY 136
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGnkgsITEYYPGT-----TRNYVTTVIEEDGKTYKFNLL------------DTAGQEDY 64
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 34147630   137 ---VKNMITGTAP----LDGCILVVAANDGPMPQTREhLLLARQIGVEhVVVYVNKAD 187
Cdd:TIGR00231  65 daiRRLYYPQVERslrvFDIVILVLDVEEILEKQTKE-IIHHADSGVP-IILVGNKID 120
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
261-345 7.57e-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: 41.01  E-value: 7.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 261 FLLPVEAVYSvPG---RGtvVTGTLERGILKKGDECELLghSKNIRTVVTGIEMFHKSLERAEAGDnlgALVRGLKRE-D 336
Cdd:cd03695   1 FRFPVQYVNR-PNldfRG--YAGTIASGSIRVGDEVTVL--PSGKTSRVKSIVTFDGELDSAGAGE---AVTLTLEDEiD 72

                ....*....
gi 34147630 337 LRRGLVMVK 345
Cdd:cd03695  73 VSRGDLIVR 81
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
260-343 7.80e-05

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: 40.96  E-value: 7.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147630 260 PFLLPVEAVYSVPGRGTVVTGTLERGILKKGDecELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRR 339
Cdd:cd16267   1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGD--KVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78

                ....
gi 34147630 340 GLVM 343
Cdd:cd16267  79 GSIL 82
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
265-331 1.41e-04

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: 40.36  E-value: 1.41e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34147630 265 VEAVYSVPGRgTVVTGTLERGILKKGDECELlghsKNIRTVVTGIEMFHKSLERAEAGDNLGALVRG 331
Cdd:cd16265   5 VEKVFKILGR-QVLTGEVESGVIYVGYKVKG----DKGVALIRAIEREHRKVDFAVAGDEVALILEG 66
selB_III cd15491
Domain III of selenocysteine-specific translation elongation factor; This family represents ...
374-439 1.46e-03

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: 37.42  E-value: 1.46e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34147630 374 VSHFMPVMFSL-TWDMACRIILPPEKELAmPGEDLKFNLILRQPMILEKGQRFTLRDGN--RTIGTGLV 439
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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