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Conserved domains on  [gi|1440910979|gb|AXJ14402|]
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elongation factor 1a, partial [Hortaea werneckii]

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 ...
 1-150 1.52e-95

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 cd01883:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 219  Bit Score: 274.75  E-value: 1.52e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   1 YVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAINKMDTT--KWSEE 78
Cdd:cd01883    78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQE 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1440910979  79 RYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNCPWYKGWeketkakvtgkTLLEAIDNIDPP 150
Cdd:cd01883   158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP-----------TLLEALDSLEPP 218
 
Name Accession Description Interval E-value
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-150 1.52e-95

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: 274.75  E-value: 1.52e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   1 YVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAINKMDTT--KWSEE 78
Cdd:cd01883    78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQE 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1440910979  79 RYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNCPWYKGWeketkakvtgkTLLEAIDNIDPP 150
Cdd:cd01883   158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP-----------TLLEALDSLEPP 218
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-153 8.79e-91

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 270.85  E-value: 8.79e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   1 YVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAINKMD--TTKWSEE 78
Cdd:PTZ00141   86 YFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQE 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1440910979  79 RYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNCPWYKgweketkakvtGKTLLEAIDNIDPPSRP 153
Cdd:PTZ00141  166 RYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK-----------GPTLLEALDTLEPPKRP 229
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-153 5.04e-72

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: 222.12  E-value: 5.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   1 YVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEfeagiskDGQTREHALLAYTLGVKQLIVAINKMDTTKWSEERY 80
Cdd:COG5256    86 YFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRY 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1440910979  81 GEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNCPWYKgweketkakvtGKTLLEAIDNIDPPSRP 153
Cdd:COG5256   159 EEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN-----------GPTLLEALDNLKEPEKP 220
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-153 5.74e-72

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: 222.04  E-value: 5.74e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   1 YVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagisKDGQTREHALLAYTLGVKQLIVAINKMDTTKWSEERY 80
Cdd:TIGR00483  86 EVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEF 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1440910979  81 GEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNCPWYKgweketkakvtGKTLLEAIDNIDPPSRP 153
Cdd:TIGR00483 162 EAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK-----------GKTLLEALDALEPPEKP 223
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-150 2.70e-41

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: 136.12  E-value: 2.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   1 YVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGefeagisKDGQTREHALLAYTLGVKqLIVAINKMDTTkwSEERY 80
Cdd:pfam00009  70 LINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAEL 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1440910979  81 GEIIKETS-AFIKKVGFNPKHVPFVPISGFNGDNMieastncpwykgweketkakvtgKTLLEAIDNIDPP 150
Cdd:pfam00009 140 EEVVEEVSrELLEKYGEDGEFVPVVPGSALKGEGV-----------------------QTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-150 1.52e-95

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: 274.75  E-value: 1.52e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   1 YVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAINKMDTT--KWSEE 78
Cdd:cd01883    78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQE 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1440910979  79 RYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNCPWYKGWeketkakvtgkTLLEAIDNIDPP 150
Cdd:cd01883   158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP-----------TLLEALDSLEPP 218
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-153 8.79e-91

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 270.85  E-value: 8.79e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   1 YVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAINKMD--TTKWSEE 78
Cdd:PTZ00141   86 YFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQE 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1440910979  79 RYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNCPWYKgweketkakvtGKTLLEAIDNIDPPSRP 153
Cdd:PTZ00141  166 RYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK-----------GPTLLEALDTLEPPKRP 229
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-153 5.04e-72

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: 222.12  E-value: 5.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   1 YVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEfeagiskDGQTREHALLAYTLGVKQLIVAINKMDTTKWSEERY 80
Cdd:COG5256    86 YFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRY 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1440910979  81 GEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNCPWYKgweketkakvtGKTLLEAIDNIDPPSRP 153
Cdd:COG5256   159 EEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN-----------GPTLLEALDNLKEPEKP 220
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-153 5.74e-72

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: 222.04  E-value: 5.74e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   1 YVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagisKDGQTREHALLAYTLGVKQLIVAINKMDTTKWSEERY 80
Cdd:TIGR00483  86 EVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEF 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1440910979  81 GEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNCPWYKgweketkakvtGKTLLEAIDNIDPPSRP 153
Cdd:TIGR00483 162 EAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK-----------GKTLLEALDALEPPEKP 223
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-153 1.15e-69

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 216.88  E-value: 1.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   1 YVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAINKMDTT--KWSEE 78
Cdd:PLN00043   86 YCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtpKYSKA 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1440910979  79 RYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNCPWYKgweketkakvtGKTLLEAIDNIDPPSRP 153
Cdd:PLN00043  166 RYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYK-----------GPTLLEALDQINEPKRP 229
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-153 1.92e-69

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 215.56  E-value: 1.92e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   1 YVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefEAGISKDGQTREHALLAYTLGVKQLIVAINKMDTTKWSEERY 80
Cdd:PRK12317   85 YFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVNYDEKRY 159

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1440910979  81 GEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNCPWYKgweketkakvtGKTLLEAIDNIDPPSRP 153
Cdd:PRK12317  160 EEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYN-----------GPTLLEALDNLKPPEKP 221
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 4-153 4.49e-47

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: 157.56  E-value: 4.49e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   4 VIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdgQTREHALLAYTLGVKQLIVAINKMDTTKWSEERYGEI 83
Cdd:COG2895    99 IADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVFEEI 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979  84 IKETSAFIKKVGFNPKHvpFVPISGFNGDNMIEASTNCPWYKgweketkakvtGKTLLEAIDNIDPPSRP 153
Cdd:COG2895   172 VADYRAFAAKLGLEDIT--FIPISALKGDNVVERSENMPWYD-----------GPTLLEHLETVEVAEDR 228
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 4-151 7.34e-47

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: 151.18  E-value: 7.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   4 VIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdgQTREHALLAYTLGVKQLIVAINKMDTTKWSEERYGEI 83
Cdd:cd04166    82 IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEI 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1440910979  84 IKETSAFIKKVGFNPKHvpFVPISGFNGDNMIEASTNCPWYKgweketkakvtGKTLLEAIDNIDPPS 151
Cdd:cd04166   155 KADYLAFAASLGIEDIT--FIPISALEGDNVVSRSENMPWYK-----------GPTLLEHLETVEIAS 209
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-150 2.70e-41

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: 136.12  E-value: 2.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   1 YVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGefeagisKDGQTREHALLAYTLGVKqLIVAINKMDTTkwSEERY 80
Cdd:pfam00009  70 LINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAEL 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1440910979  81 GEIIKETS-AFIKKVGFNPKHVPFVPISGFNGDNMieastncpwykgweketkakvtgKTLLEAIDNIDPP 150
Cdd:pfam00009 140 EEVVEEVSrELLEKYGEDGEFVPVVPGSALKGEGV-----------------------QTLLDALDEYLPS 187
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 6-148 9.65e-37

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 131.19  E-value: 9.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   6 DAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdgQTREHALLAYTLGVKQLIVAINKMDTTKWSEERYGEIIK 85
Cdd:PRK05124  113 DTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIRE 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1440910979  86 ETSAFIKKVGFNPkHVPFVPISGFNGDNMIEASTNCPWYKgweketkakvtGKTLLEAIDNID 148
Cdd:PRK05124  186 DYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWYS-----------GPTLLEVLETVD 236
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 4-126 7.74e-35

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 127.35  E-value: 7.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   4 VIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdgQTREHALLAYTLGVKQLIVAINKMDTTKWSEERYGEI 83
Cdd:PRK05506  108 VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEI 180

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1440910979  84 IKETSAFIKKVGFNpkHVPFVPISGFNGDNMIEASTNCPWYKG 126
Cdd:PRK05506  181 VADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWYEG 221
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 4-147 3.30e-33

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: 120.56  E-value: 3.30e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   4 VIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdgQTREHALLAYTLGVKQLIVAINKMDTTKWSEERYGEI 83
Cdd:TIGR02034  84 VADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENI 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1440910979  84 IKETSAFIKKVGFNPKHvpFVPISGFNGDNMIEASTNCPWYkgweketkakvTGKTLLEAIDNI 147
Cdd:TIGR02034 157 KKDYLAFAEQLGFRDVT--FIPLSALKGDNVVSRSESMPWY-----------SGPTLLEILETV 207
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 2-151 1.45e-28

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: 103.53  E-value: 1.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   2 VTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEfeagiskDGQTREHALLAyTLGVKQLIVAINKMDTTKwsEERYG 81
Cdd:cd00881    64 INFIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIA-LAGGLPIIVAVNKIDRVG--EEDFD 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1440910979  82 EIIKETSAFIKKVGF---NPKHVPFVPISGFNGDNMieastncpwykgweketkakvtgKTLLEAIDNIDPPS 151
Cdd:cd00881   134 EVLREIKELLKLIGFtflKGKDVPIIPISALTGEGI-----------------------EELLDAIVEHLPPP 183
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 5-150 1.71e-24

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: 93.42  E-value: 1.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   5 IDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdgQTREHALLAYTLGVKQLIVAINKMDTTKwSEERYGEII 84
Cdd:cd01884    70 VDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD-DEELLELVE 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1440910979  85 KETSAFIKKVGFNPKHVPFVPISGFNGdnmIEASTNCPWYKGWEKetkakvtgktLLEAIDNIDPP 150
Cdd:cd01884   142 MEVRELLSKYGFDGDDTPIVRGSALKA---LEGDDPNKWVDKILE----------LLDALDSYIPT 194
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 5-153 5.95e-22

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: 90.21  E-value: 5.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   5 IDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeagisKDG---QTREHALLAYTLGVKQLIVAINKMDTTkwSEERYG 81
Cdd:COG0050    80 VDCPGHADYVKNMITGAAQMDGAILVVSA----------TDGpmpQTREHILLARQVGVPYIVVFLNKCDMV--DDEELL 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1440910979  82 EIIK-ETSAFIKKVGFNPKHVPFVPISGFNGdnmIEASTNCPWYKG-WEketkakvtgktLLEAIDN-IDPPSRP 153
Cdd:COG0050   148 ELVEmEVRELLSKYGFPGDDTPIIRGSALKA---LEGDPDPEWEKKiLE-----------LMDAVDSyIPEPERD 208
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 2-111 2.39e-19

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: 83.42  E-value: 2.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   2 VTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeagisKDG---QTREH-ALLAyTLGVKQLIVAINKMDTTkwSE 77
Cdd:COG3276    53 LGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAA----------DEGvmpQTREHlAILD-LLGIKRGIVVLTKADLV--DE 119

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1440910979  78 ERYGEIIKETSAFIKKVGFnpKHVPFVPISGFNG 111
Cdd:COG3276   120 EWLELVEEEIRELLAGTFL--EDAPIVPVSAVTG 151
PRK12736 PRK12736
elongation factor Tu; Reviewed
 5-153 4.18e-19

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 82.30  E-value: 4.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   5 IDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeagisKDG---QTREHALLAYTLGVKQLIVAINKMDTTkwSEERYG 81
Cdd:PRK12736   80 VDCPGHADYVKNMITGAAQMDGAILVVAA----------TDGpmpQTREHILLARQVGVPYLVVFLNKVDLV--DDEELL 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1440910979  82 EIIK-ETSAFIKKVGFNPKHVPFVPISGF---NGDNmieastncPWYKGWEKetkakvtgktLLEAIDN-IDPPSRP 153
Cdd:PRK12736  148 ELVEmEVRELLSEYDFPGDDIPVIRGSALkalEGDP--------KWEDAIME----------LMDAVDEyIPTPERD 206
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 5-112 5.90e-19

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


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 78.42  E-value: 5.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   5 IDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefEAGISKdgQTREHALLAYTLGVKQLIVAINKMDTTkwSEERYGEII 84
Cdd:cd04171    55 IDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLV--DEDRLELVE 125

                          90       100
                  ....*....|....*....|....*...
gi 1440910979  85 KETSAFIKKVGFNPkhVPFVPISGFNGD 112
Cdd:cd04171   126 EEILELLAGTFLAD--APIFPVSSVTGE 151
PRK00049 PRK00049
elongation factor Tu; Reviewed
 5-153 1.60e-18

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 80.62  E-value: 1.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   5 IDAPGHRDFIKNMITGTSQADCAVLIIAAGtgefeagiskDG---QTREHALLAYTLGVKQLIVAINKMDTTKwsEERYG 81
Cdd:PRK00049   80 VDCPGHADYVKNMITGAAQMDGAILVVSAA----------DGpmpQTREHILLARQVGVPYIVVFLNKCDMVD--DEELL 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1440910979  82 EIIK-ETSAFIKKVGFNPKHVPFVPISGFNGdnmIEASTNCPWYKGWEKetkakvtgktLLEAIDN-IDPPSRP 153
Cdd:PRK00049  148 ELVEmEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEKKILE----------LMDAVDSyIPTPERA 208
tufA CHL00071
elongation factor Tu
 5-152 1.83e-18

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 80.39  E-value: 1.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   5 IDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdgQTREHALLAYTLGVKQLIVAINKMDttKWSEERYGEII 84
Cdd:CHL00071   80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKED--QVDDEELLELV 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979  85 K-ETSAFIKKVGFNPKHVPFVPISGFNGdnmIEASTNCPWYKGWEKETKAKVtgKTLLEAIDN-IDPPSR 152
Cdd:CHL00071  151 ElEVRELLSKYDFPGDDIPIVSGSALLA---LEALTENPKIKRGENKWVDKI--YNLMDAVDSyIPTPER 215
PRK12735 PRK12735
elongation factor Tu; Reviewed
 5-71 1.81e-16

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 74.87  E-value: 1.81e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   5 IDAPGHRDFIKNMITGTSQADCAVLIIAAGtgefeagiskDG---QTREHALLAYTLGVKQLIVAINKMD 71
Cdd:PRK12735   80 VDCPGHADYVKNMITGAAQMDGAILVVSAA----------DGpmpQTREHILLARQVGVPYIVVFLNKCD 139
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 2-116 3.82e-16

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: 74.14  E-value: 3.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   2 VTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeagisKDG---QTREHALLAYTLGVKQLIVAINKMDTTkwSEE 78
Cdd:TIGR00475  52 LGFIDVPGHEKFISNAIAGGGGIDAALLVVDA----------DEGvmtQTGEHLAVLDLLGIPHTIVVITKADRV--NEE 119

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1440910979  79 RYGEIIKETSAFIKKVGFNpKHVPFVPISGFNGDNMIE 116
Cdd:TIGR00475 120 EIKRTEMFMKQILNSYIFL-KNAKIFKTSAKTGQGIGE 156
PLN03126 PLN03126
Elongation factor Tu; Provisional
 5-152 1.05e-15

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 72.73  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   5 IDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdgQTREHALLAYTLGVKQLIVAINKMDTTkwSEERYGEII 84
Cdd:PLN03126  149 VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQV--DDEELLELV 219

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979  85 K-ETSAFIKKVGFNPKHVPFVPISGFNGdnmIEASTNCPWYKGWEKETKAKVTgkTLLEAIDNIDP-PSR 152
Cdd:PLN03126  220 ElEVRELLSSYEFPGDDIPIISGSALLA---LEALMENPNIKRGDNKWVDKIY--ELMDAVDSYIPiPQR 284
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 5-117 1.32e-15

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: 72.50  E-value: 1.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   5 IDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdgQTREHALLAYTLGVKQLIVAINKMDTTkwSEERYGEII 84
Cdd:TIGR00485  80 VDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV--DDEELLELV 150

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1440910979  85 K-ETSAFIKKVGFNPKHVPFV---PISGFNGDNMIEA 117
Cdd:TIGR00485 151 EmEVRELLSQYDFPGDDTPIIrgsALKALEGDAEWEA 187
PLN03127 PLN03127
Elongation factor Tu; Provisional
 5-77 1.84e-15

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 72.16  E-value: 1.84e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1440910979   5 IDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdgQTREHALLAYTLGVKQLIVAINKMDTTKWSE 77
Cdd:PLN03127  129 VDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEE 194
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 2-117 2.65e-12

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 61.51  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   2 VTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGefeagiSKDGQTREHALLAYTLGVKQLIVAINKMDTTKWSE--ER 79
Cdd:cd01888    79 VSFVDCPGHEILMATMLSGAAVMDGALLLIAANEP------CPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQalEN 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1440910979  80 YGEI---IKETSAFikkvgfnpkHVPFVPIS---GFNGDNMIEA 117
Cdd:cd01888   153 YEQIkefVKGTIAE---------NAPIIPISaqlKYNIDVLCEY 187
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 2-117 1.35e-11

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 61.02  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   2 VTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEAgiskdgQTREHALLAYTLGVKQLIVAINKMDTTkwSEERYG 81
Cdd:PRK04000   87 VSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEHLMALDIIGIKNIVIVQNKIDLV--SKERAL 158

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1440910979  82 EIIKETSAFIKkvGFNPKHVPFVPIS---GFNGDNMIEA 117
Cdd:PRK04000  159 ENYEQIKEFVK--GTVAENAPIIPVSalhKVNIDALIEA 195
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 2-114 7.31e-11

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 57.10  E-value: 7.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   2 VTVIDAPGHRDFiKNMIT-GTSQADCAVLIIAAGTGeFEAgiskdgQTRE---HALLAYTlgvkQLIVAINKMDTTKWSE 77
Cdd:cd01887    51 ITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVAINKIDKPYGTE 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1440910979  78 ---ERYGEIIKETSAFIKKVGfnpKHVPFVPISGFNGDNM 114
Cdd:cd01887   119 adpERVKNELSELGLVGEEWG---GDVSIVPISAKTGEGI 155
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 5-96 1.44e-09

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 55.44  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   5 IDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeagisKDG---QTREH-ALLAYTlGVKQLIVAINKMDTTkwSEERY 80
Cdd:PRK10512   56 IDVPGHEKFLSNMLAGVGGIDHALLVVAC----------DDGvmaQTREHlAILQLT-GNPMLTVALTKADRV--DEARI 122

                          90
                  ....*....|....*.
gi 1440910979  81 GEIIKETSAFIKKVGF 96
Cdd:PRK10512  123 AEVRRQVKAVLREYGF 138
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 1-116 2.74e-08

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 51.54  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   1 YVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGefeagiSKDGQTREHALLAYTLGVKQLIVAINKMDTTKWSE--E 78
Cdd:PTZ00327  118 HVSFVDCPGHDILMATMLNGAAVMDAALLLIAANES------CPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQaqD 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1440910979  79 RYGEIIKetsaFIKkvGFNPKHVPFVPIS---GFNGDNMIE 116
Cdd:PTZ00327  192 QYEEIRN----FVK--GTIADNAPIIPISaqlKYNIDVVLE 226
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 2-83 8.39e-06

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


Pssm-ID: 206731 [Multi-domain]  Cd Length: 237  Bit Score: 43.76  E-value: 8.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   2 VTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeagisKDG---QTRE--HALLAYTLGVkqlIVAINKMDTTKWS 76
Cdd:cd04168    66 VNIIDTPGHMDFIAEVERSLSVLDGAILVISA----------VEGvqaQTRIlfRLLRKLNIPT---IIFVNKIDRAGAD 132


                  ....*...
gi 1440910979  77 EER-YGEI 83
Cdd:cd04168   133 LEKvYQEI 140
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 2-71 2.29e-05

Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 43.08  E-value: 2.29e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1440910979   2 VTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeagisKDG---QTRE---HALLAytlGVKqLIVAINKMD 71
Cdd:COG0532    53 ITFLDTPGHEAFTAMRARGAQVTDIVILVVAA----------DDGvmpQTIEainHAKAA---GVP-IIVAINKID 114
infB CHL00189
translation initiation factor 2; Provisional
 2-114 5.16e-05

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 42.13  E-value: 5.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910979   2 VTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeagisKDG---QTREhALLAYTLGVKQLIVAINKMDTTKWSEE 78
Cdd:CHL00189  297 IVFLDTPGHEAFSSMRSRGANVTDIAILIIAA----------DDGvkpQTIE-AINYIQAANVPIIVAINKIDKANANTE 365

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1440910979  79 RYGEIIKETSAFIKKVGfnpKHVPFVPISGFNGDNM 114
Cdd:CHL00189  366 RIKQQLAKYNLIPEKWG---GDTPMIPISASQGTNI 398
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
2-71 2.85e-04

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 39.72  E-value: 2.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1440910979   2 VTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGefeagisKDGQTRehALLAYT--LGVKQLIVaINKMD 71
Cdd:PRK12740   62 INLIDTPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TVWRQAekYGVPRIIF-VNKMD 123
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 2-71 5.87e-03

Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.


Pssm-ID: 206678 [Multi-domain]  Cd Length: 194  Bit Score: 35.65  E-value: 5.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1440910979   2 VTVIDAPGHRDF------IKNMitgtsqADCAVLIIAAGTGEFEagiskdgQTR---EHALLAytlGVKqLIVAINKMD 71
Cdd:cd01891    67 INIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP-------QTRfvlKKALEA---GLK-PIVVINKID 128
 
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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