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Conserved domains on  [gi|2690027394|ref|WP_334475712|]
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GTP-binding protein, partial [Vibrio sp. 16]

Protein Classification

elongation factor Tu( domain architecture ID 1000100)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK00049 super family cl35051
elongation factor Tu; Reviewed
 1-194 3.25e-145

elongation factor Tu; Reviewed


The actual alignment was detected with superfamily member PRK00049:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 409.19  E-value: 3.25e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQV 80
Cdd:PRK00049   47 YDQIDKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  81 GIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNG--EEQWEAKIVELAEALDSYIPEPE 158
Cdd:PRK00049  127 GVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPE 206

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2690027394 159 RAIDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:PRK00049  207 RAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVG 242
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-194 3.25e-145

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 409.19  E-value: 3.25e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQV 80
Cdd:PRK00049   47 YDQIDKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  81 GIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNG--EEQWEAKIVELAEALDSYIPEPE 158
Cdd:PRK00049  127 GVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPE 206

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2690027394 159 RAIDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:PRK00049  207 RAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVG 242
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-194 1.49e-142

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: 402.22  E-value: 1.49e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQV 80
Cdd:COG0050    47 YDQIDKAPEEKERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  81 GIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNGE--EQWEAKIVELAEALDSYIPEPE 158
Cdd:COG0050   127 GVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPE 206

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2690027394 159 RAIDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:COG0050   207 RDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVG 242
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-194 4.80e-125

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: 357.94  E-value: 4.80e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQV 80
Cdd:TIGR00485  47 YDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  81 GIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNGEEQWEAKIVELAEALDSYIPEPERA 160
Cdd:TIGR00485 127 GVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPERE 206

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2690027394 161 IDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:TIGR00485 207 IDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-157 1.86e-100

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: 288.33  E-value: 1.86e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQV 80
Cdd:cd01884    37 YDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQV 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2690027394  81 GIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNG--EEQWEAKIVELAEALDSYIPEP 157
Cdd:cd01884   117 GVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKALEGddPNKWVDKILELLDALDSYIPTP 195
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 2-155 3.85e-64

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: 195.82  E-value: 3.85e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   2 ASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVG 81
Cdd:pfam00009  42 AGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLG 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2690027394  82 IPyIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNgeeqweakIVELAEALDSYIP 155
Cdd:pfam00009 122 VP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALKGEG--------VQTLLDALDEYLP 186
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-194 3.25e-145

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 409.19  E-value: 3.25e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQV 80
Cdd:PRK00049   47 YDQIDKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  81 GIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNG--EEQWEAKIVELAEALDSYIPEPE 158
Cdd:PRK00049  127 GVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPE 206

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2690027394 159 RAIDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:PRK00049  207 RAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVG 242
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-194 1.09e-142

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 402.68  E-value: 1.09e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQV 80
Cdd:PRK12735   47 YDQIDNAPEEKARGITINTSHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  81 GIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNG--EEQWEAKIVELAEALDSYIPEPE 158
Cdd:PRK12735  127 GVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGddDEEWEAKILELMDAVDSYIPEPE 206

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2690027394 159 RAIDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:PRK12735  207 RAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVG 242
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-194 1.49e-142

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: 402.22  E-value: 1.49e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQV 80
Cdd:COG0050    47 YDQIDKAPEEKERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  81 GIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNGE--EQWEAKIVELAEALDSYIPEPE 158
Cdd:COG0050   127 GVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPE 206

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2690027394 159 RAIDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:COG0050   207 RDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVG 242
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-194 7.63e-136

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 385.45  E-value: 7.63e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQV 80
Cdd:PRK12736   47 YDSIDAAPEEKERGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  81 GIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNGEEQWEAKIVELAEALDSYIPEPERA 160
Cdd:PRK12736  127 GVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEYDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERD 206

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2690027394 161 IDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:PRK12736  207 TDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVG 240
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-194 4.80e-125

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: 357.94  E-value: 4.80e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQV 80
Cdd:TIGR00485  47 YDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  81 GIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNGEEQWEAKIVELAEALDSYIPEPERA 160
Cdd:TIGR00485 127 GVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPERE 206

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2690027394 161 IDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:TIGR00485 207 IDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
tufA CHL00071
elongation factor Tu
 1-194 1.43e-116

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 336.93  E-value: 1.43e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQV 80
Cdd:CHL00071   47 YDEIDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  81 GIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALN----------GEEQWEAKIVELAEAL 150
Cdd:CHL00071  127 GVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAV 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2690027394 151 DSYIPEPERAIDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:CHL00071  207 DSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVG 250
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-194 1.10e-114

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 333.33  E-value: 1.10e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQV 80
Cdd:PLN03127   96 FDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQV 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  81 GIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNG--EEQWEAKIVELAEALDSYIPEPE 158
Cdd:PLN03127  176 GVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSALQGtnDEIGKNAILKLMDAVDEYIPEPV 255

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2690027394 159 RAIDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:PLN03127  256 RVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVG 291
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-157 1.86e-100

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: 288.33  E-value: 1.86e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQV 80
Cdd:cd01884    37 YDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQV 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2690027394  81 GIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNG--EEQWEAKIVELAEALDSYIPEP 157
Cdd:cd01884   117 GVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKALEGddPNKWVDKILELLDALDSYIPTP 195
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-194 4.37e-96

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 287.28  E-value: 4.37e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQV 80
Cdd:PLN03126  116 YDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQV 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  81 GIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALN----------GEEQWEAKIVELAEAL 150
Cdd:PLN03126  196 GVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAV 275

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2690027394 151 DSYIPEPERAIDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:PLN03126  276 DSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVG 319
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 2-155 3.85e-64

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: 195.82  E-value: 3.85e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   2 ASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVG 81
Cdd:pfam00009  42 AGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLG 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2690027394  82 IPyIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNgeeqweakIVELAEALDSYIP 155
Cdd:pfam00009 122 VP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALKGEG--------VQTLLDALDEYLP 186
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 5-194 2.08e-57

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: 185.91  E-value: 2.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   5 DNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPY 84
Cdd:COG5256    61 DRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQ 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  85 IIVFMNKCDMVD-DEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNGEEQWEA----KIVELAEALDSyIPEPER 159
Cdd:COG5256   141 LIVAVNKMDAVNySEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNmpwyNGPTLLEALDN-LKEPEK 219

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2690027394 160 AIDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:COG5256   220 PVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVG 254
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-194 2.79e-57

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 185.90  E-value: 2.79e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   1 FASI-DNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATD--GPMPQTREHILLG 77
Cdd:PRK12317   55 FAWVmDRLKEERERGVTIDLAHKKFETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLA 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  78 RQVGIPYIIVFMNKCDMVD-DEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNGEEQWEA----KIVELAEALDS 152
Cdd:PRK12317  135 RTLGINQLIVAINKMDAVNyDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENmpwyNGPTLLEALDN 214

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2690027394 153 yIPEPERAIDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:PRK12317  215 -LKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVG 255
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 4-157 3.83e-43

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: 142.43  E-value: 3.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   4 IDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQvGIP 83
Cdd:cd00881    37 LDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEGVEPQTREHLNIALA-GGL 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2690027394  84 YIIVFMNKCDMvDDEELLELVEMEVRELLSEYDF---PGDDLPVIQGSALGALNGEeqweakivELAEALDSYIPEP 157
Cdd:cd00881   116 PIIVAVNKIDR-VGEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIE--------ELLDAIVEHLPPP 183
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 4-194 1.26e-38

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 137.19  E-value: 1.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   4 IDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMP-------QTREHILL 76
Cdd:PTZ00141   60 LDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  77 GRQVGIPYIIVFMNKCDMVDDEELLELVEMEVREL---LSEYDFPGDDLPVIQGSALGALNGEE-----QWeAKIVELAE 148
Cdd:PTZ00141  140 AFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVsayLKKVGYNPEKVPFIPISGWQGDNMIEksdnmPW-YKGPTLLE 218

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2690027394 149 ALDSYIPePERAIDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:PTZ00141  219 ALDTLEP-PKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPG 263
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 5-93 4.11e-37

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: 127.99  E-value: 4.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   5 DNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDG-------PMPQTREHILLG 77
Cdd:cd01883    53 DKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLA 132

                          90
                  ....*....|....*.
gi 2690027394  78 RQVGIPYIIVFMNKCD 93
Cdd:cd01883   133 RTLGVKQLIVAVNKMD 148
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 8-194 2.23e-34

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: 127.72  E-value: 2.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   8 PEERERGITIATSHVEYDTPS-RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYII 86
Cdd:COG3276    29 KEEKKRGITIDLGFAYLPLPDgRRLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  87 VFMNKCDMvDDEELLELVEMEVRELLSEYDFPgdDLPVIQGSAL-GAlnGeeqweakIVELAEALDSYIPE-PERAIDQP 164
Cdd:COG3276   109 VVLTKADL-VDEEWLELVEEEIRELLAGTFLE--DAPIVPVSAVtGE--G-------IDELRAALDALAAAvPARDADGP 176

                         170       180       190
                  ....*....|....*....|....*....|
gi 2690027394 165 FLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:COG3276   177 FRLPIDRVFSIKGFGTVVTGTLLSGTVRVG 206
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 3-194 4.18e-33

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: 123.83  E-value: 4.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   3 SIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGI 82
Cdd:TIGR00475  24 AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGI 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  83 PYIIVFMNKCDmVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGalNGEEQWEAKIVELAEALDSyipepeRAID 162
Cdd:TIGR00475 104 PHTIVVITKAD-RVNEEEIKRTEMFMKQILNSYIFLKNAKIFKTSAKTG--QGIGELKKELKNLLESLDI------KRIQ 174

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2690027394 163 QPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:TIGR00475 175 KPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVG 206
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 4-194 3.23e-28

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 109.41  E-value: 3.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   4 IDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMP-------QTREHILL 76
Cdd:PLN00043   60 LDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  77 GRQVGIPYIIVFMNKCDMVDDEELLELVEMEVREL---LSEYDFPGDDLPVIQGSALGALNGEE-----QWeAKIVELAE 148
Cdd:PLN00043  140 AFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVssyLKKVGYNPDKIPFVPISGFEGDNMIErstnlDW-YKGPTLLE 218

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2690027394 149 ALDSyIPEPERAIDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:PLN00043  219 ALDQ-INEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPG 263
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 5-160 3.50e-27

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: 101.14  E-value: 3.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   5 DNAPEERERGITIATSHVEYDTPS-RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIP 83
Cdd:cd04171    25 DRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDVPGHEKFVKNMLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIK 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2690027394  84 YIIVFMNKCDMvDDEELLELVEMEVRELLSEYDFPgdDLPVIQGSalgALNGEEqweakIVELAEALDSyIPEPERA 160
Cdd:cd04171   105 KGLVVLTKADL-VDEDRLELVEEEILELLAGTFLA--DAPIFPVS---SVTGEG-----IEELKNYLDE-LAEPQSK 169
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 5-194 1.84e-23

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 96.66  E-value: 1.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   5 DNAPEERERGITIATSHVEYDTPS-RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIP 83
Cdd:PRK10512   26 DRLPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNP 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  84 YIIVFMNKCDMVDDEELLELVEMEVrELLSEYDFPGDDLPVIqgsalGALNGEeqweaKIVELAEALdSYIPEPERAIDQ 163
Cdd:PRK10512  106 MLTVALTKADRVDEARIAEVRRQVK-AVLREYGFAEAKLFVT-----AATEGR-----GIDALREHL-LQLPEREHAAQH 173

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2690027394 164 PFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:PRK10512  174 RFRLAIDRAFTVKGAGLVVTGTALSGEVKVG 204
eif2g_arch TIGR03680
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ...
 29-194 3.14e-23

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: 95.12  E-value: 3.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  29 RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLGRQVGIPYIIVFMNKCDMvDDEELLELVEME 107
Cdd:TIGR03680  80 RRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDL-VSKEKALENYEE 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394 108 VRELLSEYdfPGDDLPVIQGSALGALNgeeqweakIVELAEALDSYIPEPERAIDQPFLMPIEDVFSIQGRGT------- 180
Cdd:TIGR03680 159 IKEFVKGT--VAENAPIIPVSALHNAN--------IDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNKPGTppeklkg 228

                         170
                  ....*....|....*
gi 2690027394 181 -VVTGRIERGILTVG 194
Cdd:TIGR03680 229 gVIGGSLIQGKLKVG 243
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 9-94 1.63e-22

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: 89.94  E-value: 1.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   9 EERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVF 88
Cdd:cd04166    58 AEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVA 137


                  ....*.
gi 2690027394  89 MNKCDM 94
Cdd:cd04166   138 VNKMDL 143
GCD11 COG5257
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ...
 34-194 4.10e-22

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: 92.21  E-value: 4.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  34 VDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLGRQVGIPYIIVFMNKCDMvddeellelveMEVRELL 112
Cdd:COG5257    86 VDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL-----------VSKERAL 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394 113 SEY----DFP----GDDLPVIQGSALGALNgeeqweakIVELAEALDSYIPEPERAIDQPFLMPIEDVFSIQGRGT---- 180
Cdd:COG5257   155 ENYeqikEFVkgtvAENAPIIPVSAQHKVN--------IDALIEAIEEEIPTPERDLSKPPRMLVARSFDVNKPGTppkd 226

                         170
                  ....*....|....*...
gi 2690027394 181 ----VVTGRIERGILTVG 194
Cdd:COG5257   227 lkggVIGGSLIQGVLKVG 244
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 10-194 1.08e-21

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: 90.92  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  10 ERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFM 89
Cdd:COG2895    76 EREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAV 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  90 NKCD---------------MvddeellelvemevRELLSEYDFPgdDLPVIQGSalgALNGEeqweaKIVE--------- 145
Cdd:COG2895   156 NKMDlvdyseevfeeivadY--------------RAFAAKLGLE--DITFIPIS---ALKGD-----NVVErsenmpwyd 211

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2690027394 146 ---LAEALDSyIPEPERAIDQPFLMPIEDV--FSIQGRGtvVTGRIERGILTVG 194
Cdd:COG2895   212 gptLLEHLET-VEVAEDRNDAPFRFPVQYVnrPNLDFRG--YAGTIASGTVRVG 262
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 34-194 5.98e-21

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 88.76  E-value: 5.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  34 VDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLGRQVGIPYIIVFMNKCDMvddeellelveMEVRELL 112
Cdd:PRK04000   90 VDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL-----------VSKERAL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394 113 SEY----DFP----GDDLPVIQGSALGALNgeeqweakIVELAEALDSYIPEPERAIDQPFLMPIEDVFSIQGRGT---- 180
Cdd:PRK04000  159 ENYeqikEFVkgtvAENAPIIPVSALHKVN--------IDALIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTppek 230

                         170
                  ....*....|....*...
gi 2690027394 181 ----VVTGRIERGILTVG 194
Cdd:PRK04000  231 lkggVIGGSLIQGVLKVG 248
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 2-93 2.61e-19

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 81.26  E-value: 2.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   2 ASIDNAPEERERGITI--ATSHVEYDTPSRHYAH------------VDCPGHADYVKNMITGAAQMDGGILVVAATDGPM 67
Cdd:cd01889    27 AAFDKNPQSQERGITLdlGFSSFEVDKPKHLEDNenpqienyqitlVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQ 106

                          90       100
                  ....*....|....*....|....*.
gi 2690027394  68 PQTREHILLGRQVGIPYIIVfMNKCD 93
Cdd:cd01889   107 TQTAECLVIGELLCKPLIVV-LNKID 131
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 9-159 3.58e-17

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: 75.77  E-value: 3.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   9 EERERGITI-------------------ATSHVEYDTPS--------RHYAHVDCPGHADYVKNMITGAAQMDGGILVVA 61
Cdd:cd01888    30 EELKRNITIklgyanakiykcpncgcprPYDTPECECPGcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  62 ATDG-PMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEellelvemevrELLSEYDF--------PGDDLPVIQGSAlga 132
Cdd:cd01888   110 ANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE-----------QALENYEQikefvkgtIAENAPIIPISA--- 175

                         170       180
                  ....*....|....*....|....*..
gi 2690027394 133 lngeeQWEAKIVELAEALDSYIPEPER 159
Cdd:cd01888   176 -----QLKYNIDVLCEYIVKKIPTPPR 197
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 29-194 4.80e-17

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 78.12  E-value: 4.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  29 RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEME 107
Cdd:PTZ00327  117 RHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEI 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394 108 VRELLSEYdfpGDDLPVIQGSAlgalngeeQWEAKIVELAEALDSYIPEPERAIDQPFLM----------PIEDVFSIqg 177
Cdd:PTZ00327  197 RNFVKGTI---ADNAPIIPISA--------QLKYNIDVVLEYICTQIPIPKRDLTSPPRMivirsfdvnkPGEDIENL-- 263

                         170
                  ....*....|....*..
gi 2690027394 178 RGTVVTGRIERGILTVG 194
Cdd:PTZ00327  264 KGGVAGGSILQGVLKVG 280
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 4-94 8.76e-17

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: 77.03  E-value: 8.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   4 IDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIP 83
Cdd:TIGR02034  55 VDGLQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIR 134

                          90
                  ....*....|.
gi 2690027394  84 YIIVFMNKCDM 94
Cdd:TIGR02034 135 HVVLAVNKMDL 145
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 10-94 3.48e-16

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 75.74  E-value: 3.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  10 ERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFM 89
Cdd:PRK05506   85 EREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAV 164


                  ....*
gi 2690027394  90 NKCDM 94
Cdd:PRK05506  165 NKMDL 169
TypA_BipA TIGR01394
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ...
 10-194 7.98e-16

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: 74.65  E-value: 7.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  10 ERERGITIATSHVEYDTPSRHYAHVDCPGHADY------VKNMItgaaqmDGGILVVAATDGPMPQTREHILLGRQVGIP 83
Cdd:TIGR01394  45 ERERGITILAKNTAIRYNGTKINIVDTPGHADFggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLK 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  84 yIIVFMNKCDMVDDEELLELVEMEvrELLSEYDFPGD--DLPVIQGSALG--ALNGEEQWEAKIVELAEALDSYIPEPER 159
Cdd:TIGR01394 119 -PIVVINKIDRPSARPDEVVDEVF--DLFAELGADDEqlDFPIVYASGRAgwASLDLDDPSDNMAPLFDAIVRHVPAPKG 195

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2690027394 160 AIDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:TIGR01394 196 DLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKG 230
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 10-194 5.22e-15

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 72.36  E-value: 5.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  10 ERERGITIA---TShVEY-DTpsrhyaH---VDCPGHADY------VKNMItgaaqmDGGILVVAATDGPMPQTRehILL 76
Cdd:COG1217    50 ERERGITILaknTA-VRYkGV------KiniVDTPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  77 GR--QVGIPyIIVFMNKCDmvddeellelvemevR------ELLSE-YD-FpgDDL---------PVIQGSALG--ALNG 135
Cdd:COG1217   115 KKalELGLK-PIVVINKID---------------RpdarpdEVVDEvFDlF--IELgatdeqldfPVVYASARNgwASLD 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2690027394 136 EEQWEAKIVELAEALDSYIPEPERAIDQPFLMpieDVFSIQ-----GRgtVVTGRIERGILTVG 194
Cdd:COG1217   177 LDDPGEDLTPLFDTILEHVPAPEVDPDGPLQM---LVTNLDysdyvGR--IAIGRIFRGTIKKG 235
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 165-194 1.13e-14

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: 66.00  E-value: 1.13e-14
                          10        20        30
                  ....*....|....*....|....*....|
gi 2690027394 165 FLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:cd03697     1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVG 30
PRK10218 PRK10218
translational GTPase TypA;
4-189 3.91e-14

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 69.74  E-value: 3.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   4 IDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIP 83
Cdd:PRK10218   43 MDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  84 YIIVfMNKCDMVDDEELLELVEMEvrELLSEYDFPGD--DLPVIQGSALGALNG--EEQWEAKIVELAEALDSYIPEPER 159
Cdd:PRK10218  123 PIVV-INKVDRPGARPDWVVDQVF--DLFVNLDATDEqlDFPIVYASALNGIAGldHEDMAEDMTPLYQAIVDHVPAPDV 199

                         170       180       190
                  ....*....|....*....|....*....|
gi 2690027394 160 AIDQPFLMPIEDVFSIQGRGTVVTGRIERG 189
Cdd:PRK10218  200 DLDGPFQMQISQLDYNSYVGVIGIGRIKRG 229
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 10-94 7.89e-14

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 68.79  E-value: 7.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  10 ERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFM 89
Cdd:PRK05124   88 EREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAV 167


                  ....*
gi 2690027394  90 NKCDM 94
Cdd:PRK05124  168 NKMDL 172
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 5-93 8.87e-14

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: 66.46  E-value: 8.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   5 DNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADY------VKNMItgaaqmDGGILVVAATDGPMPQTRehILLGR 78
Cdd:cd01891    41 DSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFggeverVLSMV------DGVLLLVDASEGPMPQTR--FVLKK 112

                          90
                  ....*....|....*..
gi 2690027394  79 --QVGIPyIIVFMNKCD 93
Cdd:cd01891   113 alEAGLK-PIVVINKID 128
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 13-150 1.54e-13

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: 65.19  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  13 RGIT--IATSHVEYDTPSRHYAHVDCPGHADYvKNMITGAAQM-DGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFM 89
Cdd:cd01887    31 GGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARGASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAI 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2690027394  90 NKCDmvdDEELLELVEMEVRELLSEYDFPGDDL----PVIQGSALGALNGEEQWEAkIVELAEAL 150
Cdd:cd01887   109 NKID---KPYGTEADPERVKNELSELGLVGEEWggdvSIVPISAKTGEGIDDLLEA-ILLLAEVL 169
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 10-93 1.38e-12

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: 63.79  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  10 ERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTRehIL--LGRQVGIPYIIv 87
Cdd:cd04168    45 ERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISAVEGVQAQTR--ILfrLLRKLNIPTII- 121


                  ....*.
gi 2690027394  88 FMNKCD 93
Cdd:cd04168   122 FVNKID 127
IF-2 TIGR00487
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ...
 14-194 2.09e-12

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: 64.79  E-value: 2.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  14 GIT--IATSHVEYDTpSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNK 91
Cdd:TIGR00487 119 GITqhIGAYHVENED-GKMITFLDTPGHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINK 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  92 CDMVDDEELLELVEMEVRELLSEyDFPGDDLpVIQGSALGALNGEEQWEAkIVELAEALDsYIPEPERAIDQPFLmpieD 171
Cdd:TIGR00487 197 IDKPEANPDRVKQELSEYGLVPE-DWGGDTI-FVPVSALTGDGIDELLDM-ILLQSEVEE-LKANPNGQASGVVI----E 268

                         170       180
                  ....*....|....*....|...
gi 2690027394 172 VFSIQGRGTVVTGRIERGILTVG 194
Cdd:TIGR00487 269 AQLDKGRGPVATVLVQSGTLRVG 291
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
5-93 3.84e-11

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 60.91  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   5 DNAPEERERGITIATS--HVEYDtpSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGI 82
Cdd:PRK12740   36 DFMPEERERGISITSAatTCEWK--GHKINLIDTPGHVDFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGV 113

                          90
                  ....*....|.
gi 2690027394  83 PyIIVFMNKCD 93
Cdd:PRK12740  114 P-RIIFVNKMD 123
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 5-93 3.09e-10

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: 58.52  E-value: 3.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   5 DNAPEERERGITIATS--HVEYDTpsrhyaH----VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTrehILLGR 78
Cdd:COG0480    50 DWMPEEQERGITITSAatTCEWKG------HkiniIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQT---ETVWR 120

                          90
                  ....*....|....*...
gi 2690027394  79 QV---GIPyIIVFMNKCD 93
Cdd:COG0480   121 QAdkyGVP-RIVFVNKMD 137
PRK13351 PRK13351
elongation factor G-like protein;
5-93 1.74e-09

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 56.11  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   5 DNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPy 84
Cdd:PRK13351   49 DWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIP- 127


                  ....*....
gi 2690027394  85 IIVFMNKCD 93
Cdd:PRK13351  128 RLIFINKMD 136
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 5-93 2.37e-09

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: 54.54  E-value: 2.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   5 DNAPEERERGITIATSHV----EYDTPSRHYAH-----VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTreHIL 75
Cdd:cd01885    39 DTREDEQERGITIKSSAIslyfEYEEEKMDGNDylinlIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT--ETV 116

                          90       100
                  ....*....|....*....|
gi 2690027394  76 LgRQVGIPYI--IVFMNKCD 93
Cdd:cd01885   117 L-RQALEERVkpVLVINKID 135
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 5-93 3.09e-09

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: 54.91  E-value: 3.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   5 DNAPEERERGITIATS--HVEYDTpSRHYAhVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGI 82
Cdd:cd04170    40 DYDPEEKKRKMSIETSvaPLEWNG-HKINL-IDTPGYADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKL 117

                          90
                  ....*....|.
gi 2690027394  83 PyIIVFMNKCD 93
Cdd:cd04170   118 P-RIIFINKMD 127
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 161-194 8.76e-09

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: 50.65  E-value: 8.76e-09
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2690027394 161 IDQPFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPG 34
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 14-93 1.50e-08

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: 53.48  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  14 GIT--IATSHVEydTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFMNK 91
Cdd:COG0532    36 GITqhIGAYQVE--TNGGKITFLDTPGHEAFTAMRARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINK 112


                  ..
gi 2690027394  92 CD 93
Cdd:COG0532   113 ID 114
infB CHL00189
translation initiation factor 2; Provisional
 14-151 2.60e-08

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 52.91  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  14 GIT--IATSHVEYDTPS--RHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPyIIVFM 89
Cdd:CHL00189  276 GITqkIGAYEVEFEYKDenQKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAI 354

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2690027394  90 NKCDMVDDEELLELVEMEVRELLSEyDFpGDDLPVIQGSALGALNGEEQWEAkIVELAEALD 151
Cdd:CHL00189  355 NKIDKANANTERIKQQLAKYNLIPE-KW-GGDTPMIPISASQGTNIDKLLET-ILLLAEIED 413
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
 4-93 2.55e-07

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: 49.90  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   4 IDNAPEERERGITIATSHV----EYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTrEHILlgRQ 79
Cdd:TIGR00490  57 LDFDEQEQERGITINAANVsmvhEYEGNEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVL--RQ 133

                          90
                  ....*....|....*.
gi 2690027394  80 VGIPYI--IVFMNKCD 93
Cdd:TIGR00490 134 ALKENVkpVLFINKVD 149
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 5-93 4.04e-07

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 49.48  E-value: 4.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   5 DNAPEERERGITIATSHV----EYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTrEHILlgRQV 80
Cdd:PRK07560   59 DFDEEEQARGITIKAANVsmvhEYEGKEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQA 135

                          90
                  ....*....|....*
gi 2690027394  81 GIPYI--IVFMNKCD 93
Cdd:PRK07560  136 LRERVkpVLFINKVD 150
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 2-93 1.39e-06

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: 47.10  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   2 ASIDNAPEERERGITIATSHVEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTrehILLGRQV- 80
Cdd:cd01886    37 ATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQT---ETVWRQAd 113

                          90
                  ....*....|....*
gi 2690027394  81 --GIPYIIvFMNKCD 93
Cdd:cd01886   114 ryGVPRIA-FVNKMD 127
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 165-194 3.35e-06

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: 43.28  E-value: 3.35e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 2690027394 165 FLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVG 30
PTZ00416 PTZ00416
elongation factor 2; Provisional
 5-93 2.06e-05

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 44.27  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   5 DNAPEERERGITIATS----HVEYDTPSRHYAH------VDCPGHADYvKNMITGAAQM-DGGILVVAATDGPMPQTrEH 73
Cdd:PTZ00416   58 DTRADEQERGITIKSTgislYYEHDLEDGDDKQpflinlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ET 135

                          90       100
                  ....*....|....*....|..
gi 2690027394  74 ILlgRQVGIPYI--IVFMNKCD 93
Cdd:PTZ00416  136 VL--RQALQERIrpVLFINKVD 155
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 34-137 5.85e-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: 41.67  E-value: 5.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  34 VDCPGHADYVKNMITGAAQM-----DGGILVVAATDGPMPQ--TREHILLGRQVGIPYIIVFmNKCDMVDDEELLELVEM 106
Cdd:cd00882    52 VDTPGLDEFGGLGREELARLllrgaDLILLVVDSTDRESEEdaKLLILRRLRKEGIPIILVG-NKIDLLEEREVEELLRL 130

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2690027394 107 EVRELLSeydfpgdDLPVIQGSALGALNGEE 137
Cdd:cd00882   131 EELAKIL-------GVPVFEVSAKTGEGVDE 154
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 164-194 9.17e-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: 39.42  E-value: 9.17e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2690027394 164 PFLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVG 31
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 165-194 1.16e-04

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


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 39.17  E-value: 1.16e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2690027394 165 FLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVG 30
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 10-94 2.68e-04

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: 39.82  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  10 ERERGITI----ATSHVEYDTPSRHYAH-VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPy 84
Cdd:cd01890    43 ERERGITIkaqaVRLFYKAKDGEEYLLNlIDTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLE- 121

                          90
                  ....*....|
gi 2690027394  85 IIVFMNKCDM 94
Cdd:cd01890   122 IIPVINKIDL 131
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 165-194 2.82e-04

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: 38.35  E-value: 2.82e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2690027394 165 FLMPIEDVFSIQGRGTVVTGRIERGILTVG 194
Cdd:cd03694     1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREG 30
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 7-93 3.09e-04

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: 39.66  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   7 APEERERGIT--IATSHVEYDTPSRHYAHVDCPGHADYVK------NMITGAAQM-DGGILVVAATDGPMPQTREHILLg 77
Cdd:TIGR00231  27 SITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDAirrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHH- 105

                          90
                  ....*....|....*.
gi 2690027394  78 RQVGIPyIIVFMNKCD 93
Cdd:TIGR00231 106 ADSGVP-IILVGNKID 120
prfC PRK00741
peptide chain release factor 3; Provisional
 10-93 9.56e-04

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 39.35  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  10 ERERGITIATSHVEYDtpsrhYAH-----VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPy 84
Cdd:PRK00741   60 EKQRGISVTSSVMQFP-----YRDclinlLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTP- 133


                  ....*....
gi 2690027394  85 IIVFMNKCD 93
Cdd:PRK00741  134 IFTFINKLD 142
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 50-137 1.58e-03

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 37.61  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  50 AAQMDGGILVVAATDGPMPQTREHILLgRQVGIPYIIVFmNKCDMVDDEELLELVEMEVRELLSeydfpgdDLPVIQGSA 129
Cdd:cd00880    74 ADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVL-NKIDLVPESEEEELLRERKLELLP-------DLPVIAVSA 144


                  ....*...
gi 2690027394 130 LGALNGEE 137
Cdd:cd00880   145 LPGEGIDE 152
PRK04004 PRK04004
translation initiation factor IF-2; Validated
 34-93 3.38e-03

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 37.47  E-value: 3.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  34 VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVfMNKCD 93
Cdd:PRK04004   76 IDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANKID 134
PRK14845 PRK14845
translation initiation factor IF-2; Provisional
 34-93 8.41e-03

translation initiation factor IF-2; Provisional


Pssm-ID: 237833 [Multi-domain]  Cd Length: 1049  Bit Score: 36.40  E-value: 8.41e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394   34 VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYiIVFMNKCD 93
Cdd:PRK14845   531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTPF-VVAANKID 589
aIF-2 TIGR00491
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ...
 34-93 9.25e-03

translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]


Pssm-ID: 273104 [Multi-domain]  Cd Length: 591  Bit Score: 36.33  E-value: 9.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2690027394  34 VDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYiIVFMNKCD 93
Cdd:TIGR00491  74 IDTPGHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPF-VVAANKID 132
 
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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