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Conserved domains on  [gi|1767126928|gb|QFQ59979|]
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translation elongation factor 1-alpha, partial [Suillus latteri]

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 ...
 1-109 9.15e-59

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: 186.49  E-value: 9.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126928   1 WSEDRFNEIIKETSTFIKKVGYNPKAVAFVPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRP 80
Cdd:PTZ00141  162 YSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRP 229

                          90       100
                  ....*....|....*....|....*....
gi 1767126928  81 SDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:PTZ00141  230 VDKPLRLPLQDVYKIGGIGTVPVGRVETG 258
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-109 9.15e-59

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 186.49  E-value: 9.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126928   1 WSEDRFNEIIKETSTFIKKVGYNPKAVAFVPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRP 80
Cdd:PTZ00141  162 YSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRP 229

                          90       100
                  ....*....|....*....|....*....
gi 1767126928  81 SDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:PTZ00141  230 VDKPLRLPLQDVYKIGGIGTVPVGRVETG 258
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-109 4.75e-47

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: 155.48  E-value: 4.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126928   1 WSEDRFNEIIKETSTFIKKVGYNPKAVAFVPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRP 80
Cdd:COG5256   153 YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKP 220

                          90       100
                  ....*....|....*....|....*....
gi 1767126928  81 SDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:COG5256   221 VDKPLRIPIQDVYSISGIGTVPVGRVETG 249
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-78 1.93e-32

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: 112.58  E-value: 1.93e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767126928   1 WSEDRFNEIIKETSTFIKKVGYNPKAVAFVPISGWHGDNMLEESPNMPWYKGWtketkggvvkgkTLLDAIDAIEPPV 78
Cdd:cd01883   154 WSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-109 5.36e-15

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: 68.94  E-value: 5.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126928   1 WSEDRFNEIIKETSTFIKKVGynPKAVAFVPISGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPPVRP 80
Cdd:TIGR02034 148 YDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEVERDA 213

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1767126928  81 SDKPLRLPLQDVYKI-----GGIGTVPVGRVETG 109
Cdd:TIGR02034 214 QDLPLRFPVQYVNRPnldfrGYAGTIASGSVHVG 247
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-109 9.15e-59

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 186.49  E-value: 9.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126928   1 WSEDRFNEIIKETSTFIKKVGYNPKAVAFVPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRP 80
Cdd:PTZ00141  162 YSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRP 229

                          90       100
                  ....*....|....*....|....*....
gi 1767126928  81 SDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:PTZ00141  230 VDKPLRLPLQDVYKIGGIGTVPVGRVETG 258
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-109 8.87e-48

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 157.40  E-value: 8.87e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126928   1 WSEDRFNEIIKETSTFIKKVGYNPKAVAFVPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRP 80
Cdd:PRK12317  154 YDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNG------------PTLLEALDNLKPPEKP 221

                          90       100
                  ....*....|....*....|....*....
gi 1767126928  81 SDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:PRK12317  222 TDKPLRIPIQDVYSISGVGTVPVGRVETG 250
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-109 4.75e-47

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: 155.48  E-value: 4.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126928   1 WSEDRFNEIIKETSTFIKKVGYNPKAVAFVPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRP 80
Cdd:COG5256   153 YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKP 220

                          90       100
                  ....*....|....*....|....*....
gi 1767126928  81 SDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:COG5256   221 VDKPLRIPIQDVYSISGIGTVPVGRVETG 249
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-109 9.95e-43

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 144.85  E-value: 9.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126928   1 WSEDRFNEIIKETSTFIKKVGYNPKAVAFVPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRP 80
Cdd:PLN00043  162 YSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKRP 229

                          90       100
                  ....*....|....*....|....*....
gi 1767126928  81 SDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:PLN00043  230 SDKPLRLPLQDVYKIGGIGTVPVGRVETG 258
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-78 1.93e-32

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: 112.58  E-value: 1.93e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767126928   1 WSEDRFNEIIKETSTFIKKVGYNPKAVAFVPISGWHGDNMLEESPNMPWYKGWtketkggvvkgkTLLDAIDAIEPPV 78
Cdd:cd01883   154 WSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-109 9.35e-26

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: 99.01  E-value: 9.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126928   1 WSEDRFNEIIKETSTFIKKVGYNPkaVAFVPISGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPPVRP 80
Cdd:COG2895   163 YSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWY------------DGPTLLEHLETVEVAEDR 228

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1767126928  81 SDKPLRLPLQDVYKIG----GI-GTVPVGRVETG 109
Cdd:COG2895   229 NDAPFRFPVQYVNRPNldfrGYaGTIASGTVRVG 262
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 81-109 4.91e-17

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


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 69.52  E-value: 4.91e-17
                          10        20
                  ....*....|....*....|....*....
gi 1767126928  81 SDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETG 29
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-77 1.25e-16

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: 71.45  E-value: 1.25e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767126928   1 WSEDRFNEIIKETSTFIKKVGYNPkaVAFVPISGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPP 77
Cdd:cd04166   146 YDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWY------------KGPTLLEHLETVEIA 208
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-109 7.98e-16

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 71.50  E-value: 7.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126928   1 WSEDRFNEIIKETSTFIKKVGYNpkAVAFVPISGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPPVRP 80
Cdd:PRK05506  172 YDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWY------------EGPSLLEHLETVEIASDR 237

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1767126928  81 SDKPLRLPLQDVYKI-----GGIGTVPVGRVETG 109
Cdd:PRK05506  238 NLKDFRFPVQYVNRPnldfrGFAGTVASGVVRPG 271
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-109 5.36e-15

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: 68.94  E-value: 5.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126928   1 WSEDRFNEIIKETSTFIKKVGynPKAVAFVPISGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPPVRP 80
Cdd:TIGR02034 148 YDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEVERDA 213

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1767126928  81 SDKPLRLPLQDVYKI-----GGIGTVPVGRVETG 109
Cdd:TIGR02034 214 QDLPLRFPVQYVNRPnldfrGYAGTIASGSVHVG 247
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 2-109 1.04e-14

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 68.02  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126928   2 SEDRFNEIIKETSTFIKKVGYNPKaVAFVPISGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPPVRPS 81
Cdd:PRK05124  176 SEEVFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWY------------SGPTLLEVLETVDIQRVVD 242

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1767126928  82 DKPLRLPLQDVYKI-----GGIGTVPVGRVETG 109
Cdd:PRK05124  243 AQPFRFPVQYVNRPnldfrGYAGTLASGVVKVG 275
PRK00049 PRK00049
elongation factor Tu; Reviewed
 41-109 5.08e-10

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 54.81  E-value: 5.08e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126928  41 LEESPNMPWYKgwtketkggvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:PRK00049  179 LEGDDDEEWEK-----------KILELMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERG 237
PRK12736 PRK12736
elongation factor Tu; Reviewed
 67-109 1.03e-09

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 53.79  E-value: 1.03e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1767126928  67 LLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:PRK12736  192 LMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERG 235
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 67-109 1.45e-09

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: 53.62  E-value: 1.45e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1767126928  67 LLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:COG0050   194 LMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERG 237
PRK12735 PRK12735
elongation factor Tu; Reviewed
 67-109 1.55e-09

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 53.30  E-value: 1.55e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1767126928  67 LLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:PRK12735  194 LMDAVDSyIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERG 237
tufA CHL00071
elongation factor Tu
 11-109 3.87e-09

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 52.27  E-value: 3.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126928  11 KETSTFIKKVGYNPKAVAFVPISGWHGDNMLEESPNmpwykgWTKETKGGVVKGKTLLDAIDA-IEPPVRPSDKPLRLPL 89
Cdd:CHL00071  152 LEVRELLSKYDFPGDDIPIVSGSALLALEALTENPK------IKRGENKWVDKIYNLMDAVDSyIPTPERDTDKPFLMAI 225

                          90       100
                  ....*....|....*....|
gi 1767126928  90 QDVYKIGGIGTVPVGRVETG 109
Cdd:CHL00071  226 EDVFSITGRGTVATGRIERG 245
PLN03127 PLN03127
Elongation factor Tu; Provisional
 67-109 6.19e-09

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 51.75  E-value: 6.19e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1767126928  67 LLDAIDAIEP-PVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:PLN03127  243 LMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQG 286
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 67-109 8.02e-08

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: 48.62  E-value: 8.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1767126928  67 LLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:TIGR00485 192 LMDAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERG 235
PLN03126 PLN03126
Elongation factor Tu; Provisional
 67-109 4.98e-06

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 43.45  E-value: 4.98e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1767126928  67 LLDAIDAIEP-PVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:PLN03126  271 LMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERG 314
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 84-109 3.12e-03

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: 34.03  E-value: 3.12e-03
                          10        20
                  ....*....|....*....|....*.
gi 1767126928  84 PLRLPLQDVYKIGGIGTVPVGRVETG 109
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAG 26
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 67-109 7.74e-03

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: 34.50  E-value: 7.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1767126928  67 LLDAIDAI--EPPVRPSDKPLRLPLQDVYKIGGIGTVpV------GRVETG 109
Cdd:COG3276   157 LRAALDALaaAVPARDADGPFRLPIDRVFSIKGFGTV-VtgtllsGTVRVG 206
 
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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