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Conserved domains on  [gi|1497512255|gb|AYO60990|]
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elongation factor 1 alpha, partial [Tuberculatus yokoyamai]

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 ...
 1-191 4.30e-124

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: 357.13  E-value: 4.30e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSE 80
Cdd:PTZ00141   85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQ 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  81 NRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSDKMPWFKgwnverkegkadGKCLIEALDAILPPSRPTDK 160
Cdd:PTZ00141  165 ERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GPTLLEALDTLEPPKRPVDK 232

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1497512255 161 ALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:PTZ00141  233 PLRLPLQDVYKIGGIGTVPVGRVETGILKPG 263
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-191 4.30e-124

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 357.13  E-value: 4.30e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSE 80
Cdd:PTZ00141   85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQ 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  81 NRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSDKMPWFKgwnverkegkadGKCLIEALDAILPPSRPTDK 160
Cdd:PTZ00141  165 ERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GPTLLEALDTLEPPKRPVDK 232

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1497512255 161 ALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:PTZ00141  233 PLRLPLQDVYKIGGIGTVPVGRVETGILKPG 263
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-191 1.39e-97

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: 288.76  E-value: 1.39e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVKQLIVGVNKMDSTEppYSE 80
Cdd:COG5256    85 YYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN--YSE 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  81 NRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSDKMPWFKGwnverkegkadgKCLIEALDAILPPSRPTDK 160
Cdd:COG5256   156 KRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDK 223

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1497512255 161 ALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:COG5256   224 PLRIPIQDVYSISGIGTVPVGRVETGVLKVG 254
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-154 1.16e-96

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: 279.38  E-value: 1.16e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSE 80
Cdd:cd01883    77 YRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQ 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1497512255  81 NRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSDKMPWFKGWnverkegkadgkCLIEALDAILPP 154
Cdd:cd01883   157 ERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-191 4.48e-91

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: 272.51  E-value: 4.48e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAFTLGVKQLIVGVNKMDSTEppYSE 80
Cdd:TIGR00483  85 YEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN--YDE 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  81 NRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSDKMPWFKgwnverkegkadGKCLIEALDAILPPSRPTDK 160
Cdd:TIGR00483 159 EEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDALEPPEKPTDK 226

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1497512255 161 ALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:TIGR00483 227 PLRIPIQDVYSITGVGTVPVGRVETGVLKPG 257
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-154 2.52e-40

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: 134.96  E-value: 2.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVKqLIVGVNKMDSTeppySE 80
Cdd:pfam00009  69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DG 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1497512255  81 NRFEEIKKEVSS-YIKKIGYNPAAVAFVPISGWNGDNMLEvsdkmpwfkgwnverkegkadgkcLIEALDAILPP 154
Cdd:pfam00009 137 AELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT------------------------LLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-191 4.30e-124

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 357.13  E-value: 4.30e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSE 80
Cdd:PTZ00141   85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQ 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  81 NRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSDKMPWFKgwnverkegkadGKCLIEALDAILPPSRPTDK 160
Cdd:PTZ00141  165 ERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GPTLLEALDTLEPPKRPVDK 232

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1497512255 161 ALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:PTZ00141  233 PLRLPLQDVYKIGGIGTVPVGRVETGILKPG 263
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-191 1.39e-97

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: 288.76  E-value: 1.39e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVKQLIVGVNKMDSTEppYSE 80
Cdd:COG5256    85 YYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN--YSE 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  81 NRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSDKMPWFKGwnverkegkadgKCLIEALDAILPPSRPTDK 160
Cdd:COG5256   156 KRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDK 223

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1497512255 161 ALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:COG5256   224 PLRIPIQDVYSISGIGTVPVGRVETGVLKVG 254
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-154 1.16e-96

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: 279.38  E-value: 1.16e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSE 80
Cdd:cd01883    77 YRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQ 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1497512255  81 NRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSDKMPWFKGWnverkegkadgkCLIEALDAILPP 154
Cdd:cd01883   157 ERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-191 1.72e-95

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 283.74  E-value: 1.72e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEppYSE 80
Cdd:PRK12317   84 YYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVN--YDE 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  81 NRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSDKMPWFKGwnverkegkadgKCLIEALDAILPPSRPTDK 160
Cdd:PRK12317  157 KRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNG------------PTLLEALDNLKPPEKPTDK 224

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1497512255 161 ALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:PRK12317  225 PLRIPIQDVYSISGVGTVPVGRVETGVLKVG 255
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-191 6.58e-92

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 275.43  E-value: 6.58e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSE 80
Cdd:PLN00043   85 YYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSK 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  81 NRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSDKMPWFKgwnverkegkadGKCLIEALDAILPPSRPTDK 160
Cdd:PLN00043  165 ARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYK------------GPTLLEALDQINEPKRPSDK 232

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1497512255 161 ALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:PLN00043  233 PLRLPLQDVYKIGGIGTVPVGRVETGVIKPG 263
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-191 4.48e-91

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: 272.51  E-value: 4.48e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAFTLGVKQLIVGVNKMDSTEppYSE 80
Cdd:TIGR00483  85 YEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN--YDE 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  81 NRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSDKMPWFKgwnverkegkadGKCLIEALDAILPPSRPTDK 160
Cdd:TIGR00483 159 EEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDALEPPEKPTDK 226

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1497512255 161 ALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:TIGR00483 227 PLRIPIQDVYSITGVGTVPVGRVETGVLKPG 257
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 5-191 3.56e-51

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: 169.88  E-value: 3.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   5 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSENRFE 84
Cdd:COG2895    99 IADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YSEEVFE 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  85 EIKKEVSSYIKKIGYNPaaVAFVPISGWNGDNMLEVSDKMPWFkgwnverkegkaDGKCLIEALDAILPPSRPTDKALRL 164
Cdd:COG2895   170 EIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWY------------DGPTLLEHLETVEVAEDRNDAPFRF 235

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1497512255 165 PLQDVYKiggigtvP-------VGRVETGLLKPG 191
Cdd:COG2895   236 PVQYVNR-------PnldfrgyAGTIASGTVRVG 262
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 5-155 1.14e-42

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: 141.94  E-value: 1.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   5 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSENRFE 84
Cdd:cd04166    82 IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YDEEVFE 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1497512255  85 EIKKEVSSYIKKIGYNPaaVAFVPISGWNGDNMLEVSDKMPWFKgwnverkegkadGKCLIEALDAILPPS 155
Cdd:cd04166   153 EIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETVEIAS 209
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-154 2.52e-40

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: 134.96  E-value: 2.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVKqLIVGVNKMDSTeppySE 80
Cdd:pfam00009  69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DG 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1497512255  81 NRFEEIKKEVSS-YIKKIGYNPAAVAFVPISGWNGDNMLEvsdkmpwfkgwnverkegkadgkcLIEALDAILPP 154
Cdd:pfam00009 137 AELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT------------------------LLDALDEYLPS 187
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 5-186 7.13e-35

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 127.72  E-value: 7.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   5 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSENRFE 84
Cdd:PRK05124  111 IADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVD--YSEEVFE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  85 EIKKEVSSYIKKIGYNPaAVAFVPISGWNGDNMLEVSDKMPWFKgwnverkegkadGKCLIEALDAILPPSRPTDKALRL 164
Cdd:PRK05124  182 RIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWYS------------GPTLLEVLETVDIQRVVDAQPFRF 248

                         170       180
                  ....*....|....*....|....*..
gi 1497512255 165 PLQDVYKI-----GGIGTVPVGRVETG 186
Cdd:PRK05124  249 PVQYVNRPnldfrGYAGTLASGVVKVG 275
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 5-186 1.53e-34

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: 125.56  E-value: 1.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   5 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSENRFE 84
Cdd:TIGR02034  84 VADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFE 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  85 EIKKEVSSYIKKIGynPAAVAFVPISGWNGDNMLEVSDKMPWFKgwnverkegkadGKCLIEALDAILPPSRPTDKALRL 164
Cdd:TIGR02034 155 NIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWYS------------GPTLLEILETVEVERDAQDLPLRF 220

                         170       180
                  ....*....|....*....|....*..
gi 1497512255 165 PLQDVYKI-----GGIGTVPVGRVETG 186
Cdd:TIGR02034 221 PVQYVNRPnldfrGYAGTIASGSVHVG 247
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 5-186 1.46e-32

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 122.73  E-value: 1.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   5 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSENRFE 84
Cdd:PRK05506  108 VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVD--YDQEVFD 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  85 EIKKEVSSYIKKIGYnpAAVAFVPISGWNGDNMLEVSDKMPWFkgwnverkegkaDGKCLIEALDAILPPSRPTDKALRL 164
Cdd:PRK05506  179 EIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWY------------EGPSLLEHLETVEIASDRNLKDFRF 244

                         170       180
                  ....*....|....*....|....*..
gi 1497512255 165 PLQDVYKI-----GGIGTVPVGRVETG 186
Cdd:PRK05506  245 PVQYVNRPnldfrGFAGTVASGVVRPG 271
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 6-191 4.13e-30

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: 113.71  E-value: 4.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   6 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSENRFE- 84
Cdd:COG0050    80 VDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEm 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  85 EIKKEVSSYikkiGYNPAAVAFVPISGW---NGDNMLEVSDKMpwfkgwnVErkegkadgkcLIEALDAILP-PSRPTDK 160
Cdd:COG0050   153 EVRELLSKY----GFPGDDTPIIRGSALkalEGDPDPEWEKKI-------LE----------LMDAVDSYIPePERDTDK 211

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1497512255 161 ALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:COG0050   212 PFLMPVEDVFSITGRGTVVTGRVERGIIKVG 242
tufA CHL00071
elongation factor Tu
 6-191 1.73e-29

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 112.36  E-value: 1.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   6 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppySENRFEE 85
Cdd:CHL00071   80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQVD---DEELLEL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  86 IKKEVSSYIKKIGYNPAAVAFVPISGWNGdnmLEVSDKMPwfkgwNVERKEGKADGKC--LIEALDAILP-PSRPTDKAL 162
Cdd:CHL00071  150 VELEVRELLSKYDFPGDDIPIVSGSALLA---LEALTENP-----KIKRGENKWVDKIynLMDAVDSYIPtPERDTDKPF 221

                         170       180
                  ....*....|....*....|....*....
gi 1497512255 163 RLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:CHL00071  222 LMAIEDVFSITGRGTVATGRIERGTVKVG 250
PRK12736 PRK12736
elongation factor Tu; Reviewed
 6-191 3.93e-29

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 110.80  E-value: 3.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   6 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppySENRFEE 85
Cdd:PRK12736   80 VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKVDLVD---DEELLEL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  86 IKKEVSSYIKKIGYNPAAVAFVPISGW---NGDnmlevsdkmpwfkgwnvERKEGKADGkcLIEALDAILP-PSRPTDKA 161
Cdd:PRK12736  150 VEMEVRELLSEYDFPGDDIPVIRGSALkalEGD-----------------PKWEDAIME--LMDAVDEYIPtPERDTDKP 210

                         170       180       190
                  ....*....|....*....|....*....|
gi 1497512255 162 LRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:PRK12736  211 FLMPVEDVFTITGRGTVVTGRVERGTVKVG 240
PRK00049 PRK00049
elongation factor Tu; Reviewed
 6-191 5.46e-29

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 110.66  E-value: 5.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   6 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEPPysenrfE- 84
Cdd:PRK00049   80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVDDE------El 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  85 ------EIKKEVSSYikkigynpaavafvpisGWNGDNmlevsdkMPWFKGWNVERKEGKADGKC------LIEALDAIL 152
Cdd:PRK00049  147 lelvemEVRELLSKY-----------------DFPGDD-------TPIIRGSALKALEGDDDEEWekkileLMDAVDSYI 202

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1497512255 153 P-PSRPTDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:PRK00049  203 PtPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVG 242
PLN03127 PLN03127
Elongation factor Tu; Provisional
 6-191 1.39e-28

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 110.30  E-value: 1.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   6 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSENRFEE 85
Cdd:PLN03127  129 VDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEM 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  86 IKKEVSSYIKkigynpaavafvpisgWNGDNmlevsdkMPWFKGWNVERKEGKAD--GKC----LIEALDAILP-PSRPT 158
Cdd:PLN03127  202 ELRELLSFYK----------------FPGDE-------IPIIRGSALSALQGTNDeiGKNailkLMDAVDEYIPePVRVL 258

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1497512255 159 DKALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:PLN03127  259 DKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVG 291
PRK12735 PRK12735
elongation factor Tu; Reviewed
 6-191 4.08e-28

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 108.39  E-value: 4.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   6 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSENRFE- 84
Cdd:PRK12735   80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEm 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  85 EIKKEVSSYikkigynpaavafvpisGWNGDNmlevsdkMPWFKGWNVERKEGKADGKC------LIEALDAILP-PSRP 157
Cdd:PRK12735  153 EVRELLSKY-----------------DFPGDD-------TPIIRGSALKALEGDDDEEWeakileLMDAVDSYIPePERA 208

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1497512255 158 TDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:PRK12735  209 IDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVG 242
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 3-119 9.75e-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: 102.76  E-value: 9.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   3 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFtLGVKQLIVGVNKMDSTeppySENR 82
Cdd:cd00881    64 INFIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRV----GEED 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1497512255  83 FEEIKKEVSSYIKKIGY---NPAAVAFVPISGWNGDNMLE 119
Cdd:cd00881   132 FDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 6-191 6.95e-27

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: 104.86  E-value: 6.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   6 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppySENRFEE 85
Cdd:TIGR00485  80 VDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVD---DEELLEL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  86 IKKEVSSYIKKIGYnpaavafvpisgwNGDNmlevsdkMPWFKGWNVERKEGKADGKC----LIEALDAILP-PSRPTDK 160
Cdd:TIGR00485 150 VEMEVRELLSQYDF-------------PGDD-------TPIIRGSALKALEGDAEWEAkileLMDAVDEYIPtPEREIDK 209

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1497512255 161 ALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:TIGR00485 210 PFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
PLN03126 PLN03126
Elongation factor Tu; Provisional
 6-191 9.82e-25

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 100.07  E-value: 9.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   6 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppySENRFEE 85
Cdd:PLN03126  149 VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD---DEELLEL 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  86 IKKEVSSYIKKIGYNPAAvafVPISGWNGDNMLEVSDKMPwfkgwNVERKEGKADGKC--LIEALDAILP-PSRPTDKAL 162
Cdd:PLN03126  219 VELEVRELLSSYEFPGDD---IPIISGSALLALEALMENP-----NIKRGDNKWVDKIyeLMDAVDSYIPiPQRQTDLPF 290

                         170       180
                  ....*....|....*....|....*....
gi 1497512255 163 RLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:PLN03126  291 LLAVEDVFSITGRGTVATGRVERGTVKVG 319
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 6-154 3.05e-22

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: 88.79  E-value: 3.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   6 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppySENRFEE 85
Cdd:cd01884    70 VDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD---DEELLEL 139

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1497512255  86 IKKEVSSYIKKIGYNPAAVAFVPISGWNGdnmLEVSDKMPWFKgwNVERkegkadgkcLIEALDAILPP 154
Cdd:cd01884   140 VEMEVRELLSKYGFDGDDTPIVRGSALKA---LEGDDPNKWVD--KILE---------LLDALDSYIPT 194
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 3-186 1.74e-20

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: 88.05  E-value: 1.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   3 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREH-ALLAFtLGVKQLIVGVNKMDSTEPPysen 81
Cdd:COG3276    53 LGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAA-----DEGVMP--QTREHlAILDL-LGIKRGIVVLTKADLVDEE---- 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  82 RFEEIKKEVSSYIKKIGYNPAAVafVPISGWNGdnmlevsdkmpwfkgwnverkEGKADgkcLIEALDAIL--PPSRPTD 159
Cdd:COG3276   121 WLELVEEEIRELLAGTFLEDAPI--VPVSAVTG---------------------EGIDE---LRAALDALAaaVPARDAD 174

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1497512255 160 KALRLPLQDVYKIGGIGTVpV------GRVETG 186
Cdd:COG3276   175 GPFRLPIDRVFSIKGFGTV-VtgtllsGTVRVG 206
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 158-191 3.13e-19

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: 78.00  E-value: 3.13e-19
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1497512255 158 TDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPG 34
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-191 6.81e-19

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: 83.38  E-value: 6.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppysE 80
Cdd:TIGR00475  50 YRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDADEGVMT-------QTGEHLAVLDLLGIPHTIVVITKADRVN----E 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  81 NRFEEIKKEVSSYIKKIGYNPAAVAFVpISGWNGDNMLEVSDKMpwfkgwnverkegkadgKCLIEALDAilppsRPTDK 160
Cdd:TIGR00475 119 EEIKRTEMFMKQILNSYIFLKNAKIFK-TSAKTGQGIGELKKEL-----------------KNLLESLDI-----KRIQK 175

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1497512255 161 ALRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:TIGR00475 176 PLRMAIDRAFKVKGAGTVVTGTAFSGEVKVG 206
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 5-115 6.53e-18

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: 76.88  E-value: 6.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   5 IIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREHALLAFTLGVKQLIVGVNKMDSTEPPysenRFE 84
Cdd:cd04171    54 FIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLVDED----RLE 122

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1497512255  85 EIKKEVSSYIKKIGYNPAAVafVPISGWNGD 115
Cdd:cd04171   123 LVEEEILELLAGTFLADAPI--FPVSSVTGE 151
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 6-107 9.05e-10

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 56.98  E-value: 9.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   6 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFeagisknGQTREH-ALLAFTlGVKQLIVGVNKMDSTEPPysenRFE 84
Cdd:PRK10512   56 IDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHlAILQLT-GNPMLTVALTKADRVDEA----RIA 123

                          90       100
                  ....*....|....*....|...
gi 1497512255  85 EIKKEVSSYIKKIGYnPAAVAFV 107
Cdd:PRK10512  124 EVRRQVKAVLREYGF-AEAKLFV 145
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 3-117 8.71e-09

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: 52.47  E-value: 8.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   3 VTIIDAPGHRDFiKNMIT-GTSQADCAVLIVAAGTGeFEAgiskngQTRE---HALLAFTlgvkQLIVGVNKMDstEPPY 78
Cdd:cd01887    51 ITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVAINKID--KPYG 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1497512255  79 SENRFEEIKKEVSSY---IKKIGYNpaaVAFVPISGWNGDNM 117
Cdd:cd01887   117 TEADPERVKNELSELglvGEEWGGD---VSIVPISAKTGEGI 155
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 3-119 1.44e-08

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: 52.27  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   3 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefeagiskN-----GQTREHaLLAF-TLGVKQLIVGVNKMDSTEP 76
Cdd:cd01888    79 VSFVDCPGHEILMATMLSGAAVMDGALLLIAA-----------NepcpqPQTSEH-LAALeIMGLKHIIILQNKIDLVKE 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1497512255  77 PYSENRFEEIKKevssYIKKIGYNPAAVafVPIS---GWNGDNMLE 119
Cdd:cd01888   147 EQALENYEQIKE----FVKGTIAENAPI--IPISaqlKYNIDVLCE 186
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 3-117 3.41e-08

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 52.16  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   3 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAgiskngQTREHaLLAFT-LGVKQLIVGVNKMDSTEPPYSEN 81
Cdd:PRK04000   87 VSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEH-LMALDiIGIKNIVIVQNKIDLVSKERALE 159

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1497512255  82 RFEEIKKEVSSYIkkigynpAAVA-FVPISGWNGDNM 117
Cdd:PRK04000  160 NYEQIKEFVKGTV-------AENApIIPVSALHKVNI 189
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 3-98 5.75e-08

GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.


Pssm-ID: 206728 [Multi-domain]  Cd Length: 224  Bit Score: 50.75  E-value: 5.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   3 VTIIDAPGHRDFIKNMITGTS--QADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVKQLIVgVNKMDSTeppySE 80
Cdd:cd04165    86 VTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGANAGI-------IGMTKEHLGLALALKVPVFVV-VTKIDMT----PA 153

                          90
                  ....*....|....*...
gi 1497512255  81 NRFEEIKKEVSSYIKKIG 98
Cdd:cd04165   154 NVLQETLKDLKRLLKSPG 171
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 2-119 2.14e-06

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 46.92  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   2 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefeagiskN-----GQTREHALLAFTLGVKQLIVGVNKMDSTEP 76
Cdd:PTZ00327  118 HVSFVDCPGHDILMATMLNGAAVMDAALLLIAA-----------NescpqPQTSEHLAAVEIMKLKHIIILQNKIDLVKE 186

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1497512255  77 PYSENRFEEIKKEVSSYIKKigynpaAVAFVPIS---GWNGDNMLE 119
Cdd:PTZ00327  187 AQAQDQYEEIRNFVKGTIAD------NAPIIPISaqlKYNIDVVLE 226
PRK10218 PRK10218
translational GTPase TypA;
1-190 5.39e-05

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 42.77  E-value: 5.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVgVNKMD--STEPPY 78
Cdd:PRK10218   68 YRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIVV-INKVDrpGARPDW 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255  79 SENRFEEIKKEVSSYIKKIGYnPA--AVAFVPISGWNGDNMLEvsDKMPWFKGwnverkegkadgkclieALDAILPPSR 156
Cdd:PRK10218  140 VVDQVFDLFVNLDATDEQLDF-PIvyASALNGIAGLDHEDMAE--DMTPLYQA-----------------IVDHVPAPDV 199

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1497512255 157 PTDKALRLPLQDVYKIGGIGTVPVGRVETGLLKP 190
Cdd:PRK10218  200 DLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKP 233
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 3-94 5.72e-05

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: 42.22  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   3 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRehaLLAFTLgvKQL----IVGVNKMDsTEPPY 78
Cdd:cd04168    66 VNIIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTR---ILFRLL--RKLniptIIFVNKID-RAGAD 132

                          90
                  ....*....|....*.
gi 1497512255  79 SENRFEEIKKEVSSYI 94
Cdd:cd04168   133 LEKVYQEIKEKLSPDI 148
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 164-191 4.13e-04

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: 37.88  E-value: 4.13e-04
                          10        20
                  ....*....|....*....|....*...
gi 1497512255 164 LPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:cd03697     3 MPIEDVFSIPGRGTVVTGRIERGVIKVG 30
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 1-127 4.73e-04

Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.


Pssm-ID: 206730 [Multi-domain]  Cd Length: 213  Bit Score: 39.56  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTgefeaGISKNGQT--REhallAFTLGVKQLIVgVNKMDS--TE- 75
Cdd:cd04167    71 YLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTSVTERliRH----AIQEGLPMVLV-INKIDRliLEl 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1497512255  76 --PPYSENR-FEEIKKEVSSYIKKIGyNPAAVAFVPISGwngdNMLEVSDKMPWF 127
Cdd:cd04167   141 klPPTDAYYkLRHTIDEINNYIASFS-TTEGFLVSPELG----NVLFASSKFGFC 190
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 162-191 1.76e-03

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: 35.70  E-value: 1.76e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1497512255 162 LRLPLQDVYKIGGIGTVPVGRVETGLLKPG 191
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVG 30
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 1-72 2.38e-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: 37.19  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAGTGEFEagiskngQTR---EHALLAftlGVKqLIVGVNKM 71
Cdd:cd01891    65 TKINIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP-------QTRfvlKKALEA---GLK-PIVVINKI 127


                  .
gi 1497512255  72 D 72
Cdd:cd01891   128 D 128
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 1-120 2.57e-03

LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.


Pssm-ID: 206677 [Multi-domain]  Cd Length: 179  Bit Score: 37.13  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   1 YYVTIIDAPGHRDFikNMITGTSQADC--AVLIVAAGTGeFEAgiskngQTREHALLAFTLGVKQLIVgVNKMD--STEP 76
Cdd:cd01890    67 YLLNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------QTLANFYLALENNLEIIPV-INKIDlpAADP 136

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1497512255  77 pysenrfEEIKKEVSSYikkIGYNPAAVafVPISGWNGDNMLEV 120
Cdd:cd01890   137 -------DRVKQEIEDV---LGLDASEA--ILVSAKTGLGVEDL 168
infB CHL00189
translation initiation factor 2; Provisional
 3-119 2.74e-03

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 37.89  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   3 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREhALLAFTLGVKQLIVGVNKMDSTeppysENR 82
Cdd:CHL00189  297 IVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIE-AINYIQAANVPIIVAINKIDKA-----NAN 363

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1497512255  83 FEEIKKEVSSY---IKKIGynpAAVAFVPIS---GWNGDNMLE 119
Cdd:CHL00189  364 TERIKQQLAKYnliPEKWG---GDTPMIPISasqGTNIDKLLE 403
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
3-72 5.08e-03

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 37.03  E-value: 5.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1497512255   3 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRehALLAFT--LGVKQLIVgVNKMD 72
Cdd:PRK12740   62 INLIDTPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TVWRQAekYGVPRIIF-VNKMD 123
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 5-72 5.18e-03

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 36.92  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   5 IIDAPGHRDF------IKNMitgtsqADCAVLIVAAgtgeFEagisknG---QTR---EHALlafTLGVKqLIVGVNKMD 72
Cdd:COG1217    73 IVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlKKAL---ELGLK-PIVVINKID 132
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 3-124 6.56e-03

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 35.90  E-value: 6.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1497512255   3 VTIIDAPGHRDFIKNMITGT-----SQADCAVLIVAAGTGEFEAGIskngqTREHALLAFTLGVKQLIVGvNKMDSTEPP 77
Cdd:cd00882    49 LVLVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRESEEDA-----KLLILRRLRKEGIPIILVG-NKIDLLEER 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1497512255  78 ysenrfEEIKKEVSSYIKKIGYNPaavaFVPISGWNGDNMLEVSDKM 124
Cdd:cd00882   123 ------EVEELLRLEELAKILGVP----VFEVSAKTGEGVDELFEKL 159
 
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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