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Conserved domains on  [gi|808215439|gb|AKD27623|]
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elongation factor-1 alpha, partial [Thermococcus sp. MZ6]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12317 super family cl36107
elongation factor 1-alpha; Reviewed
 1-147 1.92e-94

elongation factor 1-alpha; Reviewed


The actual alignment was detected with superfamily member PRK12317:

Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 279.12  E-value: 1.92e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPASTIfhkpiqGEVKSIEMHHEAMQEALPGDNI 80
Cdd:PRK12317 215 LKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVV------GEVKSIEMHHEELPQAEPGDNI 288

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808215439  81 GFNVRGVGKNDIKRGDVAGHTSNPPTVVrpkDTFKAQIIVLNHPTAITVGYTPVLHAHTLQVAVRFE 147
Cdd:PRK12317 289 GFNVRGVGKKDIKRGDVCGHPDNPPTVA---EEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFE 352
 
Name Accession Description Interval E-value
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-147 1.92e-94

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 279.12  E-value: 1.92e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPASTIfhkpiqGEVKSIEMHHEAMQEALPGDNI 80
Cdd:PRK12317 215 LKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVV------GEVKSIEMHHEELPQAEPGDNI 288

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808215439  81 GFNVRGVGKNDIKRGDVAGHTSNPPTVVrpkDTFKAQIIVLNHPTAITVGYTPVLHAHTLQVAVRFE 147
Cdd:PRK12317 289 GFNVRGVGKKDIKRGDVCGHPDNPPTVA---EEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFE 352
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-147 4.05e-92

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: 272.96  E-value: 4.05e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPAStifhkpIQGEVKSIEMHHEAMQEALPGDNI 80
Cdd:COG5256  214 LKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAG------VVGEVKSIEMHHEELEQAEPGDNI 287

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808215439  81 GFNVRGVGKNDIKRGDVAGHTSNPPTVVrpkDTFKAQIIVLNHPTAITVGYTPVLHAHTLQVAVRFE 147
Cdd:COG5256  288 GFNVRGVEKNDIKRGDVAGHPDNPPTVA---EEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFV 351
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-146 6.71e-73

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 223.97  E-value: 6.71e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439    1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPAStifhkpIQGEVKSIEMHHEAMQEALPGDNI 80
Cdd:TIGR00483 217 LEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAG------VSGEVKSIEMHHEQIEQAEPGDNI 290

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808215439   81 GFNVRGVGKNDIKRGDVAGHTSNPPTVVRpkdTFKAQIIVLNHPTAITVGYTPVLHAHTLQVAVRF 146
Cdd:TIGR00483 291 GFNVRGVSKKDIRRGDVCGHPDNPPKVAK---EFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRF 353
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 8-104 1.52e-53

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: 163.90  E-value: 1.52e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   8 TDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPAStifhkpIQGEVKSIEMHHEAMQEALPGDNIGFNVRGV 87
Cdd:cd03693    1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAG------VTGEVKSVEMHHEPLEEAIPGDNVGFNVKGV 74

                         90
                 ....*....|....*..
gi 808215439  88 GKNDIKRGDVAGHTSNP 104
Cdd:cd03693   75 SVKDIKRGDVAGDSKND 91
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 26-97 9.50e-20

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


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 77.31  E-value: 9.50e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808215439   26 GTVPVGRVETGVLRVGDVVIFEPASTIfHKPIQGEVKSIEMHHEAMQEALPGDNIGFNVRGVGKNDIKRGDV 97
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTG-KKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
 
Name Accession Description Interval E-value
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-147 1.92e-94

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 279.12  E-value: 1.92e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPASTIfhkpiqGEVKSIEMHHEAMQEALPGDNI 80
Cdd:PRK12317 215 LKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVV------GEVKSIEMHHEELPQAEPGDNI 288

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808215439  81 GFNVRGVGKNDIKRGDVAGHTSNPPTVVrpkDTFKAQIIVLNHPTAITVGYTPVLHAHTLQVAVRFE 147
Cdd:PRK12317 289 GFNVRGVGKKDIKRGDVCGHPDNPPTVA---EEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFE 352
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-147 4.05e-92

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: 272.96  E-value: 4.05e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPAStifhkpIQGEVKSIEMHHEAMQEALPGDNI 80
Cdd:COG5256  214 LKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAG------VVGEVKSIEMHHEELEQAEPGDNI 287

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808215439  81 GFNVRGVGKNDIKRGDVAGHTSNPPTVVrpkDTFKAQIIVLNHPTAITVGYTPVLHAHTLQVAVRFE 147
Cdd:COG5256  288 GFNVRGVEKNDIKRGDVAGHPDNPPTVA---EEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFV 351
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-146 6.71e-73

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 223.97  E-value: 6.71e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439    1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPAStifhkpIQGEVKSIEMHHEAMQEALPGDNI 80
Cdd:TIGR00483 217 LEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAG------VSGEVKSIEMHHEQIEQAEPGDNI 290

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808215439   81 GFNVRGVGKNDIKRGDVAGHTSNPPTVVRpkdTFKAQIIVLNHPTAITVGYTPVLHAHTLQVAVRF 146
Cdd:TIGR00483 291 GFNVRGVSKKDIRRGDVCGHPDNPPKVAK---EFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRF 353
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 3-147 3.90e-63

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 199.59  E-value: 3.90e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   3 EPPK-PTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPAStifhkpIQGEVKSIEMHHEAMQEALPGDNIG 81
Cdd:PTZ00141 224 EPPKrPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSG------VTTEVKSVEMHHEQLAEAVPGDNVG 297

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808215439  82 FNVRGVGKNDIKRGDVAGHTSNPPTvvRPKDTFKAQIIVLNHPTAITVGYTPVLHAHTLQVAVRFE 147
Cdd:PTZ00141 298 FNVKNVSVKDIKRGYVASDSKNDPA--KECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFA 361
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 8-104 1.52e-53

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: 163.90  E-value: 1.52e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   8 TDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPAStifhkpIQGEVKSIEMHHEAMQEALPGDNIGFNVRGV 87
Cdd:cd03693    1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAG------VTGEVKSVEMHHEPLEEAIPGDNVGFNVKGV 74

                         90
                 ....*....|....*..
gi 808215439  88 GKNDIKRGDVAGHTSNP 104
Cdd:cd03693   75 SVKDIKRGDVAGDSKND 91
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-146 3.77e-47

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 157.94  E-value: 3.77e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPAStifhkpIQGEVKSIEMHHEAMQEALPGDNI 80
Cdd:PLN00043 223 INEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTG------LTTEVKSVEMHHESLQEALPGDNV 296

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808215439  81 GFNVRGVGKNDIKRGDVAGHTSNPPTvvRPKDTFKAQIIVLNHPTAITVGYTPVLHAHTLQVAVRF 146
Cdd:PLN00043 297 GFNVKNVAVKDLKRGYVASNSKDDPA--KEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKF 360
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-142 4.35e-27

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: 103.69  E-value: 4.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVV----IFEPASTIfhkpiqgeVKSIEMHHEAMQEALP 76
Cdd:COG0050  202 IPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVeivgIRDTQKTV--------VTGVEMFRKLLDEGEA 273

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808215439  77 GDNIGFNVRGVGKNDIKRGDVAGHtsnpPTVVRPKDTFKAQIIVLN------HpTAITVGYTPVLHAHTLQV 142
Cdd:COG0050  274 GDNVGLLLRGIKREDVERGQVLAK----PGSITPHTKFEAEVYVLSkeeggrH-TPFFNGYRPQFYFRTTDV 340
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-121 6.11e-27

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 103.38  E-value: 6.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVV----IFEPASTIfhkpiqgeVKSIEMHHEAMQEALP 76
Cdd:PRK12735 202 IPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVeivgIKETQKTT--------VTGVEMFRKLLDEGQA 273

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 808215439  77 GDNIGFNVRGVGKNDIKRGDVAGHtsnpPTVVRPKDTFKAQIIVL 121
Cdd:PRK12735 274 GDNVGVLLRGTKREDVERGQVLAK----PGSIKPHTKFEAEVYVL 314
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-121 1.66e-26

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 102.19  E-value: 1.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVV----IFEPASTIfhkpiqgeVKSIEMHHEAMQEALP 76
Cdd:PRK00049 202 IPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVeivgIRDTQKTT--------VTGVEMFRKLLDEGQA 273

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 808215439  77 GDNIGFNVRGVGKNDIKRGDVAGHtsnpPTVVRPKDTFKAQIIVL 121
Cdd:PRK00049 274 GDNVGALLRGIKREDVERGQVLAK----PGSITPHTKFEAEVYVL 314
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-142 7.56e-25

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 97.71  E-value: 7.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVV----IFEPASTIfhkpiqgeVKSIEMHHEAMQEALP 76
Cdd:PRK12736 200 IPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVeivgIKETQKTV--------VTGVEMFRKLLDEGQA 271

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808215439  77 GDNIGFNVRGVGKNDIKRGDVAGHtsnpPTVVRPKDTFKAQIIVLN------HpTAITVGYTPVLHAHTLQV 142
Cdd:PRK12736 272 GDNVGVLLRGVDRDEVERGQVLAK----PGSIKPHTKFKAEVYILTkeeggrH-TPFFNNYRPQFYFRTTDV 338
tufA CHL00071
elongation factor Tu
 1-142 1.03e-23

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 94.64  E-value: 1.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVV----IFEPASTIfhkpiqgeVKSIEMHHEAMQEALP 76
Cdd:CHL00071 210 IPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVeivgLRETKTTT--------VTGLEMFQKTLDEGLA 281

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808215439  77 GDNIGFNVRGVGKNDIKRGDVaghTSNPPTvVRPKDTFKAQIIVLN------HpTAITVGYTPVLHAHTLQV 142
Cdd:CHL00071 282 GDNVGILLRGIQKEDIERGMV---LAKPGT-ITPHTKFEAQVYILTkeeggrH-TPFFPGYRPQFYVRTTDV 348
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-142 5.14e-23

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: 92.92  E-value: 5.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439    1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVifepaSTIFHKPIQ-GEVKSIEMHHEAMQEALPGDN 79
Cdd:TIGR00485 200 IPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEV-----EIVGLKDTRkTTVTGVEMFRKELDEGRAGDN 274

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808215439   80 IGFNVRGVGKNDIKRGDVAGHtsnpPTVVRPKDTFKAQIIVLNHP-----TAITVGYTPVLHAHTLQV 142
Cdd:TIGR00485 275 VGLLLRGIKREEIERGMVLAK----PGSIKPHTKFEAEVYVLSKEeggrhTPFFSGYRPQFYFRTTDV 338
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-143 1.83e-22

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 91.81  E-value: 1.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVifEPASTIFHKPIQGEVKSIEMHHEAMQEALPGDNI 80
Cdd:PLN03127 251 IPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEV--EIVGLRPGGPLKTTVTGVEMFKKILDQGQAGDNV 328

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808215439  81 GFNVRGVGKNDIKRGDVAGHtsnpPTVVRPKDTFKAQIIVLNHP-----TAITVGYTPVLHAHTLQVA 143
Cdd:PLN03127 329 GLLLRGLKREDVQRGQVICK----PGSIKTYKKFEAEIYVLTKDeggrhTPFFSNYRPQFYLRTADVT 392
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-142 1.05e-21

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 89.67  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVV----IFEPASTIfhkpiqgeVKSIEMHHEAMQEALP 76
Cdd:PLN03126 279 IPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVdivgLRETRSTT--------VTGVEMFQKILDEALA 350

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808215439  77 GDNIGFNVRGVGKNDIKRGDVAGHtsnpPTVVRPKDTFKAQIIVLNHP-----TAITVGYTPVLHAHTLQV 142
Cdd:PLN03126 351 GDNVGLLLRGIQKADIQRGMVLAK----PGSITPHTKFEAIVYVLKKEeggrhSPFFAGYRPQFYMRTTDV 417
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 14-100 6.51e-21

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: 80.64  E-value: 6.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439  14 IPIQDVYSIKGVGTVPVGRVETGVLRVGDVVifepasTI--FHKPIQGEVKSIEMHHEAMQEALPGDNIGFNVRGVGKND 91
Cdd:cd03697    3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEV------EIvgFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKED 76


                 ....*....
gi 808215439  92 IKRGDVAGH 100
Cdd:cd03697   77 VERGMVLAK 85
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 26-97 9.50e-20

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


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 77.31  E-value: 9.50e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808215439   26 GTVPVGRVETGVLRVGDVVIFEPASTIfHKPIQGEVKSIEMHHEAMQEALPGDNIGFNVRGVGKNDIKRGDV 97
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTG-KKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 4-145 1.11e-18

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: 81.11  E-value: 1.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   4 PPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPAstifhkPIQGEVKSIEMHHEAMQEALPGDNIGFN 83
Cdd:COG3276  169 PARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPS------GKPVRVRGIQVHGQPVEEAYAGQRVALN 242

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808215439  84 VRGVGKNDIKRGDVAGHtsnpPTVVRPKDTFKAQIIVLNH-PTAITVGyTPV-LHAHTLQVAVR 145
Cdd:COG3276  243 LAGVEKEEIERGDVLAA----PGALRPTDRIDVRLRLLPSaPRPLKHW-QRVhLHHGTAEVLAR 301
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 12-97 1.43e-18

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


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 74.87  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439  12 LRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPAStifhkpIQGEVKSIEMHHEAMQEALPGDNIGFNVRGVGKND 91
Cdd:cd03696    1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLG------KEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKE 74


                 ....*.
gi 808215439  92 IKRGDV 97
Cdd:cd03696   75 LERGFV 80
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 12-97 3.25e-18

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: 73.84  E-value: 3.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439  12 LRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVifepasTIFHKPIQGEVKSIEMHHEAMQEALPGDNIGFNVRGVgkND 91
Cdd:cd01342    1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEI------RILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGV--KD 72


                 ....*.
gi 808215439  92 IKRGDV 97
Cdd:cd01342   73 ILTGDT 78
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 109-147 5.24e-15

Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to ribosomes. EF-1 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 model represents the alpha subunit, which is the counterpart of bacterial EF-Tu for archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha).


Pssm-ID: 294004 [Multi-domain]  Cd Length: 104  Bit Score: 66.06  E-value: 5.24e-15
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 808215439 109 RPKDTFKAQIIVLNHPTAITVGYTPVLHAHTLQVAVRFE 147
Cdd:cd03705    1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFA 39
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 11-97 5.09e-14

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: 62.92  E-value: 5.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439  11 PLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPAStifhkpIQGEVKSIEMHHEAMQEALPGDNIGFNVRGVGKN 90
Cdd:cd16267    1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSN------ETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPN 74


                 ....*..
gi 808215439  91 DIKRGDV 97
Cdd:cd16267   75 HLRVGSI 81
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-122 1.22e-13

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: 66.65  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVY----SIKGVgtvpVGRVETGVLRVGDVVIFEPA---STifhkpiqgeVKSIEMHHEAMQE 73
Cdd:COG2895  222 VEVAEDRNDAPFRFPVQYVNrpnlDFRGY----AGTIASGTVRVGDEVVVLPSgktST---------VKSIVTFDGDLEE 288

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 808215439  74 ALPGDNIGF----NVrgvgknDIKRGDVAGHTSNPPTVVrpkDTFKAQIIVLN 122
Cdd:COG2895  289 AFAGQSVTLtledEI------DISRGDVIVAADAPPEVA---DQFEATLVWMD 332
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 6-118 1.37e-12

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: 63.74  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439    6 KPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEPAStifhKPIQgeVKSIEMHHEAMQEALPGDNIGFNVR 85
Cdd:TIGR00475 171 KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPIN----HEVR--VKAIQAQNQDVEIAYAGQRIALNLM 244

                          90       100       110
                  ....*....|....*....|....*....|...
gi 808215439   86 GVGKNDIKRGDVAghTSNPPTVVRPKDTFKAQI 118
Cdd:TIGR00475 245 DVEPESLKRGLLI--LTPEDPKLRVVVKFIAEV 275
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 11-97 1.58e-12

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


Pssm-ID: 293906 [Multi-domain]  Cd Length: 82  Bit Score: 59.04  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439  11 PLRIPIQDVYsiKGVGTVPVGRVETGVLRVGDVVIFEPASTIFhkpiqgEVKSIEMHHEAMQEALPGDNIGFNVRGVGKN 90
Cdd:cd04089    1 PLRMPILDKY--KDMGTVVMGKVESGTIRKGQKLVLMPNKTKV------EVTGIYIDEEEVDSAKPGENVKLKLKGVEEE 72


                 ....*..
gi 808215439  91 DIKRGDV 97
Cdd:cd04089   73 DISPGFV 79
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 16-97 3.80e-12

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: 58.39  E-value: 3.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439  16 IQDVYSIKGVGTVPVGRVETGVLRVGDVVIFEP-ASTIFHkPIQgeVKSIEMHHEAMQEALPGDNIGFNVRGVGKNDIKR 94
Cdd:cd03694    5 IDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPdADGKFR-PVT--VKSIHRNRQPVDRARAGQSASFALKKIKRESLRK 81


                 ...
gi 808215439  95 GDV 97
Cdd:cd03694   82 GMV 84
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 108-147 1.57e-08

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


Pssm-ID: 397314 [Multi-domain]  Cd Length: 105  Bit Score: 49.19  E-value: 1.57e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 808215439  108 VRPKDTFKAQIIVLNH-----PTAITVGYTPVLHAHTLQVAVRFE 147
Cdd:pfam03143   2 IKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFV 46
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 16-97 5.33e-08

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


Pssm-ID: 293910 [Multi-domain]  Cd Length: 80  Bit Score: 47.29  E-value: 5.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439  16 IQDVYSIKGvGTVPVGRVETGVLRVGDVVIFEPAStifhkpiqGEVKSIEMHHEAMQEALPGDNIGFNVRGVGKndIKRG 95
Cdd:cd16265    5 VEKVFKILG-RQVLTGEVESGVIYVGYKVKGDKGV--------ALIRAIEREHRKVDFAVAGDEVALILEGKIK--VKEG 73


                 ..
gi 808215439  96 DV 97
Cdd:cd16265   74 DV 75
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 1-96 2.73e-07

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 48.51  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   1 IPEPPKPTDKPLRIPIQDVYSIKGVGTVPVGRVETGVLRVGDVVIFepasTIFHKPIQgeVKSIEMHHEAMQEALPGDNI 80
Cdd:PRK10512 164 LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWL----TGVNKPMR--VRGLHAQNQPTEQAQAGQRI 237

                         90
                 ....*....|....*..
gi 808215439  81 GFNVRG-VGKNDIKRGD 96
Cdd:PRK10512 238 ALNIAGdAEKEQINRGD 254
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 12-97 4.81e-07

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


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 44.86  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439  12 LRIPIQDVY----SIKGVgtvpVGRVETGVLRVGDVVIFEPASTIFHkpiqgeVKSIEMHHEAMQEALPGDNIGFNV-RG 86
Cdd:cd03695    1 FRFPVQYVNrpnlDFRGY----AGTIASGSIRVGDEVTVLPSGKTSR------VKSIVTFDGELDSAGAGEAVTLTLeDE 70

                         90
                 ....*....|.
gi 808215439  87 VgknDIKRGDV 97
Cdd:cd03695   71 I---DVSRGDL 78
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 114-147 4.89e-07

Domain III of the GP-1 family of GTPases; This family 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 the 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: 294007 [Multi-domain]  Cd Length: 87  Bit Score: 44.82  E-value: 4.89e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 808215439 114 FKAQIIVLNHPTAITVGYTPVLHAHTLQVAVRFE 147
Cdd:cd03708    6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARII 39
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 11-98 5.02e-07

Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 293899 [Multi-domain]  Cd Length: 84  Bit Score: 44.80  E-value: 5.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439  11 PLRIPIQDVYSIKGvGTVPVGRVETGVLRVGDVVIFEPASTifhkpiQGEVKSIEMH-HEAMQEALPGDNIGFNVRGVGK 89
Cdd:cd03698    1 PFRLSIDDKYKSPR-GTTVTGKLEAGSIQKNQVLYDMPSQQ------DAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEV 73


                 ....*....
gi 808215439  90 NDIKRGDVA 98
Cdd:cd03698   74 EDIQPGDIL 82
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 109-146 1.20e-05

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


Pssm-ID: 275447 [Multi-domain]  Cd Length: 102  Bit Score: 41.61  E-value: 1.20e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 808215439 109 RPKDTFKAQIIVLNHPTAITVGYTPVLHAHTLQVAVRF 146
Cdd:cd01513    1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRI 38
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 114-146 9.94e-04

C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.


Pssm-ID: 294008 [Multi-domain]  Cd Length: 109  Bit Score: 36.37  E-value: 9.94e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 808215439 114 FKAQIIVLNHPTAITVGYTPVLHAHTLQVAVRF 146
Cdd:cd04093    8 FEARIVTFDLQVPILKGTPVVLHRHSLSEPATI 40
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 9-119 1.64e-03

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 37.60  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215439   9 DKPLRIPIQDV---------YSikgvgtvpvGRVETGVLRVGDVVIFEPASTifhkpiQGEVKSIEMHHEAMQEALPG-- 77
Cdd:PRK05506 239 LKDFRFPVQYVnrpnldfrgFA---------GTVASGVVRPGDEVVVLPSGK------TSRVKRIVTPDGDLDEAFAGqa 303

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 808215439  78 ------DNIgfnvrgvgknDIKRGDVAGHTSNPPTVvrpKDTFKAQII 119
Cdd:PRK05506 304 vtltlaDEI----------DISRGDMLARADNRPEV---ADQFDATVV 338
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 112-147 3.78e-03

C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions: N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 294003 [Multi-domain]  Cd Length: 108  Bit Score: 34.84  E-value: 3.78e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 808215439 112 DTFKAQIIVLNHPTAI-TVGYTPVLHAHTLQVAVRFE 147
Cdd:cd03704    4 TEFEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTIT 40
 
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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