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Conserved domains on  [gi|1368344001|gb|AVP50017|]
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elongation factor 1-alpha, partial [Didymium clavus]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 1-195 2.47e-138

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PTZ00141:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 446  Bit Score: 393.73  E-value: 2.47e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDEKSVNWGQPRYDEIVKETSSFVKKIGYNPEKIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:PTZ00141  137 ALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTL 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  81 LEALDNIVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNV 160
Cdd:PTZ00141  217 LEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNV 296

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1368344001 161 GFNVKNLSVKDIRRGMVAGDSKNDPPRETEFFTAQ 195
Cdd:PTZ00141  297 GFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQ 331
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-195 2.47e-138

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 393.73  E-value: 2.47e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDEKSVNWGQPRYDEIVKETSSFVKKIGYNPEKIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:PTZ00141  137 ALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTL 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  81 LEALDNIVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNV 160
Cdd:PTZ00141  217 LEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNV 296

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1368344001 161 GFNVKNLSVKDIRRGMVAGDSKNDPPRETEFFTAQ 195
Cdd:PTZ00141  297 GFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQ 331
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-195 1.45e-103

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: 304.55  E-value: 1.45e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDekSVNWGQPRYDEIVKETSSFVKKIGYNPEKIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:COG5256   130 AFLARTLGINQLIVAVNKMD--AVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  81 LEALDNIVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNV 160
Cdd:COG5256   208 LEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNI 287

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1368344001 161 GFNVKNLSVKDIRRGMVAGDSKNdPPRETEFFTAQ 195
Cdd:COG5256   288 GFNVRGVEKNDIKRGDVAGHPDN-PPTVAEEFTAQ 321
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-195 1.48e-98

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: 291.77  E-value: 1.48e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDekSVNWGQPRYDEIVKETSSFVKKIGYNPEKIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:TIGR00483 133 AFLARTLGINQLIVAINKMD--SVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTL 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  81 LEALDNIVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNV 160
Cdd:TIGR00483 211 LEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNI 290

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1368344001 161 GFNVKNLSVKDIRRGMVAGDSKNdPPRETEFFTAQ 195
Cdd:TIGR00483 291 GFNVRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQ 324
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 94-184 1.93e-59

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: 180.46  E-value: 1.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  94 SDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIR 173
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                          90
                  ....*....|.
gi 1368344001 174 RGMVAGDSKND 184
Cdd:cd03693    81 RGDVAGDSKND 91
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 112-177 3.46e-16

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


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 69.60  E-value: 3.46e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1368344001 112 GTVPVGRVETGVLKPNMIVTFAPGNNS-----TEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIRRGMV 177
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGkkkivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-195 2.47e-138

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 393.73  E-value: 2.47e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDEKSVNWGQPRYDEIVKETSSFVKKIGYNPEKIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:PTZ00141  137 ALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTL 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  81 LEALDNIVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNV 160
Cdd:PTZ00141  217 LEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNV 296

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1368344001 161 GFNVKNLSVKDIRRGMVAGDSKNDPPRETEFFTAQ 195
Cdd:PTZ00141  297 GFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQ 331
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-195 1.45e-103

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: 304.55  E-value: 1.45e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDekSVNWGQPRYDEIVKETSSFVKKIGYNPEKIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:COG5256   130 AFLARTLGINQLIVAVNKMD--AVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  81 LEALDNIVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNV 160
Cdd:COG5256   208 LEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNI 287

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1368344001 161 GFNVKNLSVKDIRRGMVAGDSKNdPPRETEFFTAQ 195
Cdd:COG5256   288 GFNVRGVEKNDIKRGDVAGHPDN-PPTVAEEFTAQ 321
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-195 1.35e-101

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 300.08  E-value: 1.35e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDEKSVNWGQPRYDEIVKETSSFVKKIGYNPEKIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:PLN00043  137 ALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTL 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  81 LEALDNIVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNV 160
Cdd:PLN00043  217 LEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNV 296

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1368344001 161 GFNVKNLSVKDIRRGMVAGDSKNDPPRETEFFTAQ 195
Cdd:PLN00043  297 GFNVKNVAVKDLKRGYVASNSKDDPAKEAANFTSQ 331
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-195 8.88e-101

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 297.22  E-value: 8.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDekSVNWGQPRYDEIVKETSSFVKKIGYNPEKIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:PRK12317  131 VFLARTLGINQLIVAINKMD--AVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNGPTL 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  81 LEALDNIVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNV 160
Cdd:PRK12317  209 LEALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNI 288

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1368344001 161 GFNVKNLSVKDIRRGMVAGdSKNDPPRETEFFTAQ 195
Cdd:PRK12317  289 GFNVRGVGKKDIKRGDVCG-HPDNPPTVAEEFTAQ 322
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-195 1.48e-98

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: 291.77  E-value: 1.48e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDekSVNWGQPRYDEIVKETSSFVKKIGYNPEKIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:TIGR00483 133 AFLARTLGINQLIVAINKMD--SVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTL 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  81 LEALDNIVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNV 160
Cdd:TIGR00483 211 LEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNI 290

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1368344001 161 GFNVKNLSVKDIRRGMVAGDSKNdPPRETEFFTAQ 195
Cdd:TIGR00483 291 GFNVRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQ 324
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 94-184 1.93e-59

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: 180.46  E-value: 1.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  94 SDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIR 173
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                          90
                  ....*....|.
gi 1368344001 174 RGMVAGDSKND 184
Cdd:cd03693    81 RGDVAGDSKND 91
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-91 3.54e-54

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: 171.52  E-value: 3.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDEKSVNWGQPRYDEIVKETSSFVKKIGYNPEKIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:cd01883   129 ALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPTL 208

                          90
                  ....*....|.
gi 1368344001  81 LEALDNIVEPK 91
Cdd:cd01883   209 LEALDSLEPPE 219
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-194 1.04e-49

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: 166.03  E-value: 1.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDekSVNWGQPRYDEIVKETSSFVKKIGYnpEKIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:COG2895   140 SYIASLLGIRHVVVAVNKMD--LVDYSEEVFEEIVADYRAFAAKLGL--EDITFIPISALKGDNVVERSENMPWYDGPTL 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  81 LEALDNIVEPKRPSDKPLRVPLQDVYKiggigtvP-------VGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPE 153
Cdd:COG2895   216 LEHLETVEVAEDRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEE 288

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1368344001 154 AVPGDNVGfnvknLSVK---DIRRG-MVAgdSKNDPPRETEFFTA 194
Cdd:COG2895   289 AFAGQSVT-----LTLEdeiDISRGdVIV--AADAPPEVADQFEA 326
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-194 1.39e-31

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 120.03  E-value: 1.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDekSVNWGQPRYDEIVKETSSFVKKIGYnpEKIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:PRK05506  149 SFIASLLGIRHVVLAVNKMD--LVDYDQEVFDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWYEGPSL 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  81 LEALDNI-VEPKRpSDKPLRVPLQDVYKI-----GGIGTvpvgrVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEA 154
Cdd:PRK05506  225 LEHLETVeIASDR-NLKDFRFPVQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEA 298

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1368344001 155 VPGDNVgfnvkNLSVKD---IRRG-MVAgdSKNDPPRETEFFTA 194
Cdd:PRK05506  299 FAGQAV-----TLTLADeidISRGdMLA--RADNRPEVADQFDA 335
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-186 1.77e-30

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 115.78  E-value: 1.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDekSVNWGQPRYDEIVKETSSFVKKIGYNPEkIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:PRK05124  152 SFIATLLGIKHLVVAVNKMD--LVDYSEEVFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWYSGPTL 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  81 LEALDNIVEPKRPSDKPLRVPLQDVYKI-----GGIGTVPVGRVETG----VLKPNM------IVTFaPGNnstevksve 145
Cdd:PRK05124  229 LEVLETVDIQRVVDAQPFRFPVQYVNRPnldfrGYAGTLASGVVKVGdrvkVLPSGKesnvarIVTF-DGD--------- 298

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1368344001 146 mhhvaLPEAVPGDNVgfnvkNLSVK---DIRRGMVAGDSKNDPP 186
Cdd:PRK05124  299 -----LEEAFAGEAI-----TLVLEdeiDISRGDLLVAADEALQ 332
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-87 6.63e-30

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: 109.20  E-value: 6.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDekSVNWGQPRYDEIVKETSSFVKKIGYNPekIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:cd04166   123 SYIASLLGIRHVVVAVNKMD--LVDYDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYKGPTL 198


                  ....*..
gi 1368344001  81 LEALDNI 87
Cdd:cd04166   199 LEHLETV 205
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-195 9.47e-30

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: 112.85  E-value: 9.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKQMIVAINKMDekSVNWGQPRYDEIVKETSSFVKKIGYNPekIAFVPISGWNGDNMLEKSANLPWYKGPTL 80
Cdd:TIGR02034 125 SYIASLLGIRHVVLAVNKMD--LVDYDEEVFENIKKDYLAFAEQLGFRD--VTFIPLSALKGDNVVSRSESMPWYSGPTL 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  81 LEALDNIVEPKRPSDKPLRVPLQDVYKI-----GGIGTVPVGRVETGvlkpnMIVTFAPGNNSTEVKSVEMHHVALPEAV 155
Cdd:TIGR02034 201 LEILETVEVERDAQDLPLRFPVQYVNRPnldfrGYAGTIASGSVHVG-----DEVVVLPSGRSSRVARIVTFDGDLEQAR 275

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1368344001 156 PGDNVGFNVKNlsVKDIRRG--MVAGDSkndPPRETEFFTAQ 195
Cdd:TIGR02034 276 AGQAVTLTLDD--EIDISRGdlLAAADS---APEVADQFAAT 312
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 2-177 2.68e-23

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: 95.22  E-value: 2.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   2 LLAYTLGVKQMIVAINKMDEKSvnwgQPRYDEIVK-ETSSFVKKIGYNPEKIAFVPISGWNGdnmLEKSANLPWYKGPT- 79
Cdd:COG0050   121 LLARQVGVPYIVVFLNKCDMVD----DEELLELVEmEVRELLSKYGFPGDDTPIIRGSALKA---LEGDPDPEWEKKILe 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  80 LLEALDN-IVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPN---MIVTFAPGNNSTeVKSVEMHHVALPEAV 155
Cdd:COG0050   194 LMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRDTQKTV-VTGVEMFRKLLDEGE 272

                         170       180
                  ....*....|....*....|..
gi 1368344001 156 PGDNVGFNVKNLSVKDIRRGMV 177
Cdd:COG0050   273 AGDNVGLLLRGIKREDVERGQV 294
tufA CHL00071
elongation factor Tu
 2-177 4.72e-23

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 94.64  E-value: 4.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   2 LLAYTLGVKQMIVAINKMDeksvnwgQPRYDEIV----KETSSFVKKIGYNPEKIAFVPISGWNGDNMLEKSANL----- 72
Cdd:CHL00071  121 LLAKQVGVPNIVVFLNKED-------QVDDEELLelveLEVRELLSKYDFPGDDIPIVSGSALLALEALTENPKIkrgen 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  73 PWY-KGPTLLEALDN-IVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPN---MIVTFAPGNNSTeVKSVEMH 147
Cdd:CHL00071  194 KWVdKIYNLMDAVDSyIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGdtvEIVGLRETKTTT-VTGLEMF 272

                         170       180       190
                  ....*....|....*....|....*....|
gi 1368344001 148 HVALPEAVPGDNVGFNVKNLSVKDIRRGMV 177
Cdd:CHL00071  273 QKTLDEGLAGDNVGILLRGIQKEDIERGMV 302
PRK00049 PRK00049
elongation factor Tu; Reviewed
 2-177 6.98e-22

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 91.40  E-value: 6.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   2 LLAYTLGVKQMIVAINKMDekSVNwgQPRYDEIVK-ETSSFVKKIGYNPEKIAFVPISGWNGdnmLEKSANLPWYKG-PT 79
Cdd:PRK00049  121 LLARQVGVPYIVVFLNKCD--MVD--DEELLELVEmEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEKKiLE 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  80 LLEALDN-IVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPN---MIVTFAPGNNSTeVKSVEMHHVALPEAV 155
Cdd:PRK00049  194 LMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQ 272

                         170       180
                  ....*....|....*....|..
gi 1368344001 156 PGDNVGFNVKNLSVKDIRRGMV 177
Cdd:PRK00049  273 AGDNVGALLRGIKREDVERGQV 294
PRK12735 PRK12735
elongation factor Tu; Reviewed
 2-177 1.12e-20

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 87.97  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   2 LLAYTLGVKQMIVAINKMDEKSvnwgQPRYDEIVK-ETSSFVKKIGYNPEKIAFVPISGWNGdnmLEKSANLPWYKG-PT 79
Cdd:PRK12735  121 LLARQVGVPYIVVFLNKCDMVD----DEELLELVEmEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEAKiLE 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  80 LLEALDN-IVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPN---MIVTFAPGNNSTeVKSVEMHHVALPEAV 155
Cdd:PRK12735  194 LMDAVDSyIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQ 272

                         170       180
                  ....*....|....*....|..
gi 1368344001 156 PGDNVGFNVKNLSVKDIRRGMV 177
Cdd:PRK12735  273 AGDNVGVLLRGTKREDVERGQV 294
PRK12736 PRK12736
elongation factor Tu; Reviewed
 2-177 4.22e-20

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 86.54  E-value: 4.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   2 LLAYTLGVKQMIVAINKMDEKsvnwGQPRYDEIVK-ETSSFVKKIGYNPEKIAFVPISGW---NGDNMLEKSANlpwykg 77
Cdd:PRK12736  121 LLARQVGVPYLVVFLNKVDLV----DDEELLELVEmEVRELLSEYDFPGDDIPVIRGSALkalEGDPKWEDAIM------ 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  78 pTLLEALDN-IVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPN---MIVTFAPGNNSTeVKSVEMHHVALPE 153
Cdd:PRK12736  191 -ELMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKETQKTV-VTGVEMFRKLLDE 268

                         170       180
                  ....*....|....*....|....
gi 1368344001 154 AVPGDNVGFNVKNLSVKDIRRGMV 177
Cdd:PRK12736  269 GQAGDNVGVLLRGVDRDEVERGQV 292
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 2-177 1.83e-19

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: 84.83  E-value: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   2 LLAYTLGVKQMIVAINKMDEKSVNWGQPRYDEIVKETSSFVKKIGYNPEKIAFVPISGWNGDNMLEKsanlpwyKGPTLL 81
Cdd:TIGR00485 121 LLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEA-------KILELM 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  82 EALD-NIVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPN---MIVTFAPGNNSTeVKSVEMHHVALPEAVPG 157
Cdd:TIGR00485 194 DAVDeYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDEGRAG 272

                         170       180
                  ....*....|....*....|
gi 1368344001 158 DNVGFNVKNLSVKDIRRGMV 177
Cdd:TIGR00485 273 DNVGLLLRGIKREEIERGMV 292
PLN03127 PLN03127
Elongation factor Tu; Provisional
 2-177 2.74e-19

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 84.49  E-value: 2.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   2 LLAYTLGVKQMIVAINKMDEKSvnwgQPRYDEIV----KETSSFVKKIGYNPEKIAFVPISGWNGDN-MLEKSANLpwyk 76
Cdd:PLN03127  170 LLARQVGVPSLVVFLNKVDVVD----DEELLELVemelRELLSFYKFPGDEIPIIRGSALSALQGTNdEIGKNAIL---- 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  77 gpTLLEALDN-IVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPN---MIVTFAPGNN-STEVKSVEMHHVAL 151
Cdd:PLN03127  242 --KLMDAVDEyIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPGGPlKTTVTGVEMFKKIL 319

                         170       180
                  ....*....|....*....|....*.
gi 1368344001 152 PEAVPGDNVGFNVKNLSVKDIRRGMV 177
Cdd:PLN03127  320 DQGQAGDNVGLLLRGLKREDVQRGQV 345
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 98-177 6.03e-19

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: 76.92  E-value: 6.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  98 LRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNVGFNVKNlsVKDIRRGMV 177
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 101-177 1.29e-18

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: 76.40  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001 101 PLQDVYKIGGIGTVPVGRVETGVLKPNM---IVTFAPGNNSTeVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIRRGMV 177
Cdd:cd03697     4 PIEDVFSIPGRGTVVTGRIERGVIKVGDeveIVGFKETLKTT-VTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
GTPBP1 COG5258
GTPase [General function prediction only];
13-191 2.08e-17

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 79.21  E-value: 2.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  13 IVAINKMDEKSVNwgqpRYDEIVKETSSFVKKIGYNPekiafVPISGWNG-DNMLEKSAN--LPWYK-------GPTLLE 82
Cdd:COG5258   264 IVAITKIDKVDDE----RVEEVEREIENLLRIVGRTP-----LEVESRHDvDAAIEEINGrvVPILKtsavtgeGLDLLD 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  83 ALDNIVEPKR-PSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNS----TEVKSVEMHHVALPEAVPG 157
Cdd:COG5258   335 ELFERLPKRAtDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGsfreVEVKSIEMHYHRVDKAEAG 414

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1368344001 158 DNVGFNVKNLSVKDIRRGMVAGDSKNDPPRETEF 191
Cdd:COG5258   415 RIVGIALKGVEEEELERGMVLLPRDADPKAVREF 448
PLN03126 PLN03126
Elongation factor Tu; Provisional
 2-177 9.91e-17

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 77.35  E-value: 9.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   2 LLAYTLGVKQMIVAINKMDeksvnwgQPRYDEIVK----ETSSFVKKIGYNPEKIAFVPISGWNGDNMLEKSANLP---- 73
Cdd:PLN03126  190 LLAKQVGVPNMVVFLNKQD-------QVDDEELLElvelEVRELLSSYEFPGDDIPIISGSALLALEALMENPNIKrgdn 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  74 -WY-KGPTLLEALDNIVE-PKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFA--PGNNSTEVKSVEMHH 148
Cdd:PLN03126  263 kWVdKIYELMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVglRETRSTTVTGVEMFQ 342

                         170       180
                  ....*....|....*....|....*....
gi 1368344001 149 VALPEAVPGDNVGFNVKNLSVKDIRRGMV 177
Cdd:PLN03126  343 KILDEALAGDNVGLLLRGIQKADIQRGMV 371
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 98-177 3.29e-16

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: 69.86  E-value: 3.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  98 LRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIRRGMV 177
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 112-177 3.46e-16

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


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 69.60  E-value: 3.46e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1368344001 112 GTVPVGRVETGVLKPNMIVTFAPGNNS-----TEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIRRGMV 177
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGkkkivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-90 4.77e-15

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: 69.86  E-value: 4.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   1 ALLAYTLGVKqMIVAINKMDEKSvnwgQPRYDEIVKETSS-FVKKIGYNPEKIAFVPISGWNGDNMleksanlpwykgPT 79
Cdd:pfam00009 114 LRLARQLGVP-IIVFINKMDRVD----GAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGV------------QT 176

                          90
                  ....*....|.
gi 1368344001  80 LLEALDNIVEP 90
Cdd:pfam00009 177 LLDALDEYLPS 187
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 104-177 1.09e-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: 61.08  E-value: 1.09e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1368344001 104 DVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNN----STEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIRRGMV 177
Cdd:cd03694     7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADgkfrPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 97-172 2.99e-12

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: 59.83  E-value: 2.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  97 PLRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNV-----GFNVKNLSVKD 171
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVtltltGIDPNHLRVGS 80


                  .
gi 1368344001 172 I 172
Cdd:cd16267    81 I 81
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 97-177 1.10e-11

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: 58.27  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  97 PLRVPLQDVYKigGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIRRGM 176
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78


                  .
gi 1368344001 177 V 177
Cdd:cd04089    79 V 79
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 97-180 2.07e-09

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: 52.12  E-value: 2.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  97 PLRVPLQDVYKiGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMH-HVALPEAVPGDNVGFNVKNLSVKDIRRG 175
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79


                  ....*
gi 1368344001 176 MVAGD 180
Cdd:cd03698    80 DILSS 84
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 7-90 1.14e-07

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: 49.60  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   7 LGVKQMIVAINKMDEKsvnwGQPRYDEIVKETSSFVKKIGY---NPEKIAFVPISGWNGDNMLEksanlpwykgptLLEA 83
Cdd:cd00881   112 AGGLPIIVAVNKIDRV----GEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE------------LLDA 175


                  ....*..
gi 1368344001  84 LDNIVEP 90
Cdd:cd00881   176 IVEHLPP 182
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 98-162 1.59e-06

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: 44.48  E-value: 1.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1368344001  98 LRVPLQDVYKIGGIGTVPVGRVETGVLKPNMIVTFAPGNNSTEVKSVEMHHVALPEAVPGDNVGF 162
Cdd:cd03695     1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 103-161 1.50e-03

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: 36.12  E-value: 1.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1368344001 103 QDVYKIGGiGTVPVGRVETGVLKPNMIVTfaPGNNSTEVKSVEMHHVALPEAVPGDNVG 161
Cdd:cd16265     6 EKVFKILG-RQVLTGEVESGVIYVGYKVK--GDKGVALIRAIEREHRKVDFAVAGDEVA 61
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 7-191 2.16e-03

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 37.91  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   7 LGVKQMIVAINKMD----EKSVNwgqpRYDEIVKetssFVKkiGYNPEKIAFVPISGWNGDNMleksanlpwykgPTLLE 82
Cdd:PRK04000  137 IGIKNIVIVQNKIDlvskERALE----NYEQIKE----FVK--GTVAENAPIIPVSALHKVNI------------DALIE 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001  83 ALDN-IVEPKRPSDKPlrvPLQ------DVYK--------IGGI--GTVPVGRVETG---VLKPNMIVTFAPGNN----S 138
Cdd:PRK04000  195 AIEEeIPTPERDLDKP---PRMyvarsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeiEIRPGIKVEEGGKTKwepiT 271

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1368344001 139 TEVKSVEMHHVALPEAVPGDNVGFNVK---NLSVKDIRRGMVAGDSKNDPPRETEF 191
Cdd:PRK04000  272 TKIVSLRAGGEKVEEARPGGLVGVGTKldpSLTKADALAGSVAGKPGTLPPVWESL 327
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 2-90 2.66e-03

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: 37.18  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344001   2 LLAYTLGVKQMIVAINKMDEKsvnwGQPRYDEIVK-ETSSFVKKIGYNPEKIAFVPISGWNGdnmLEKSANLPWYKG-PT 79
Cdd:cd01884   111 LLARQVGVPYIVVFLNKADMV----DDEELLELVEmEVRELLSKYGFDGDDTPIVRGSALKA---LEGDDPNKWVDKiLE 183

                          90
                  ....*....|.
gi 1368344001  80 LLEALDNIVEP 90
Cdd:cd01884   184 LLDALDSYIPT 194
 
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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