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Conserved domains on  [gi|2077862637|gb|QYO48056|]
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translation elongation factor 1 alpha, partial [Chlorophyllum brunneum]

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 ...
 1-133 3.88e-70

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: 216.92  E-value: 3.88e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIVKETSTFIKKVGYNPKAVA 78
Cdd:PTZ00141  110 DVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVP 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2077862637  79 FVPISGWHGDNMLEESANMPWYkgwskeikggavKGKTLLDAIDAIEPPVRPSDK 133
Cdd:PTZ00141  190 FIPISGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDK 232
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-133 3.88e-70

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 216.92  E-value: 3.88e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIVKETSTFIKKVGYNPKAVA 78
Cdd:PTZ00141  110 DVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVP 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2077862637  79 FVPISGWHGDNMLEESANMPWYkgwskeikggavKGKTLLDAIDAIEPPVRPSDK 133
Cdd:PTZ00141  190 FIPISGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDK 232
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-128 1.72e-69

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: 208.11  E-value: 1.72e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIVKETSTFIKKVGYNPKAVA 78
Cdd:cd01883   102 DVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVP 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077862637  79 FVPISGWHGDNMLEESANMPWYKGWskeikggavkgkTLLDAIDAIEPPV 128
Cdd:cd01883   182 FIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-133 5.91e-50

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: 163.95  E-value: 5.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGYNPKAVAFV 80
Cdd:COG5256   110 DAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFI 182

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2077862637  81 PISGWHGDNMLEESANMPWYkgwskeikggavKGKTLLDAIDAIEPPVRPSDK 133
Cdd:COG5256   183 PVSAWKGDNVVKKSDNMPWY------------NGPTLLEALDNLKEPEKPVDK 223
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-125 1.28e-23

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: 93.98  E-value: 1.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGynPKAVAFV 80
Cdd:TIGR02034 105 DLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--FRDVTFI 175

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2077862637  81 PISGWHGDNMLEESANMPWYkgwskeikggavKGKTLLDAIDAIE 125
Cdd:TIGR02034 176 PLSALKGDNVVSRSESMPWY------------SGPTLLEILETVE 208
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-127 1.43e-22

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: 87.20  E-value: 1.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTkwSEDRFNEIVKETS-TFIKKVGYNPKAVAF 79
Cdd:pfam00009  94 DGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGEDGEFVPV 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2077862637  80 VPISGWHGDNMleesanmpwykgwskeikggavkgKTLLDAIDAIEPP 127
Cdd:pfam00009 164 VPGSALKGEGV------------------------QTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-133 3.88e-70

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 216.92  E-value: 3.88e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIVKETSTFIKKVGYNPKAVA 78
Cdd:PTZ00141  110 DVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVP 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2077862637  79 FVPISGWHGDNMLEESANMPWYkgwskeikggavKGKTLLDAIDAIEPPVRPSDK 133
Cdd:PTZ00141  190 FIPISGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDK 232
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-128 1.72e-69

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: 208.11  E-value: 1.72e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIVKETSTFIKKVGYNPKAVA 78
Cdd:cd01883   102 DVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVP 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077862637  79 FVPISGWHGDNMLEESANMPWYKGWskeikggavkgkTLLDAIDAIEPPV 128
Cdd:cd01883   182 FIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-133 2.01e-50

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 166.03  E-value: 2.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIVKETSTFIKKVGYNPKAVA 78
Cdd:PLN00043  110 DCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtpKYSKARYDEIVKEVSSYLKKVGYNPDKIP 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2077862637  79 FVPISGWHGDNMLEESANMPWYkgwskeikggavKGKTLLDAIDAIEPPVRPSDK 133
Cdd:PLN00043  190 FVPISGFEGDNMIERSTNLDWY------------KGPTLLEALDQINEPKRPSDK 232
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-133 5.91e-50

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: 163.95  E-value: 5.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGYNPKAVAFV 80
Cdd:COG5256   110 DAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFI 182

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2077862637  81 PISGWHGDNMLEESANMPWYkgwskeikggavKGKTLLDAIDAIEPPVRPSDK 133
Cdd:COG5256   183 PVSAWKGDNVVKKSDNMPWY------------NGPTLLEALDNLKEPEKPVDK 223
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-133 3.53e-48

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 159.32  E-value: 3.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGgtgefEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGYNPKAVAFV 80
Cdd:PRK12317  109 DAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPFI 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2077862637  81 PISGWHGDNMLEESANMPWYkgwskeikggavKGKTLLDAIDAIEPPVRPSDK 133
Cdd:PRK12317  184 PVSAFEGDNVVKKSENMPWY------------NGPTLLEALDNLKPPEKPTDK 224
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 23-133 3.00e-34

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: 122.89  E-value: 3.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637  23 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGYNPkaVAFVPISGWHGDNMLEESANMPWYkg 102
Cdd:COG2895   135 QTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWY-- 210

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2077862637 103 wskeikggavKGKTLLDAIDAIEPPVRPSDK 133
Cdd:COG2895   211 ----------DGPTLLEHLETVEVAEDRNDA 231
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 23-127 1.88e-33

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: 116.13  E-value: 1.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637  23 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGYNPkaVAFVPISGWHGDNMLEESANMPWYkg 102
Cdd:cd04166   118 QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWY-- 193

                          90       100
                  ....*....|....*....|....*
gi 2077862637 103 wskeikggavKGKTLLDAIDAIEPP 127
Cdd:cd04166   194 ----------KGPTLLEHLETVEIA 208
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-125 2.52e-28

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 107.31  E-value: 2.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGYNPKaVAFV 80
Cdd:PRK05124  132 DLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNLD-IRFV 203

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2077862637  81 PISGWHGDNMLEESANMPWYkgwskeikggavKGKTLLDAIDAIE 125
Cdd:PRK05124  204 PLSALEGDNVVSQSESMPWY------------SGPTLLEVLETVD 236
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 23-102 5.88e-27

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 104.24  E-value: 5.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637  23 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGYNpkAVAFVPISGWHGDNMLEESANMPWYKG 102
Cdd:PRK05506  144 QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWYEG 221
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-125 1.28e-23

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: 93.98  E-value: 1.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGynPKAVAFV 80
Cdd:TIGR02034 105 DLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--FRDVTFI 175

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2077862637  81 PISGWHGDNMLEESANMPWYkgwskeikggavKGKTLLDAIDAIE 125
Cdd:TIGR02034 176 PLSALKGDNVVSRSESMPWY------------SGPTLLEILETVE 208
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-127 1.43e-22

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: 87.20  E-value: 1.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTkwSEDRFNEIVKETS-TFIKKVGYNPKAVAF 79
Cdd:pfam00009  94 DGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGEDGEFVPV 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2077862637  80 VPISGWHGDNMleesanmpwykgwskeikggavkgKTLLDAIDAIEPP 127
Cdd:pfam00009 164 VPGSALKGEGV------------------------QTLLDALDEYLPS 187
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-127 4.34e-15

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: 67.71  E-value: 4.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEfeagiskDGQTREHALLAFtLGVRQLIVAVNKMDTTKwsEDRFNEIVKETSTFIKKVGY---NPKAV 77
Cdd:cd00881    87 DGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRVG--EEDFDEVLREIKELLKLIGFtflKGKDV 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077862637  78 AFVPISGWHGDNMLEesanmpwykgwskeikggavkgktLLDAIDAIEPP 127
Cdd:cd00881   157 PIIPISALTGEGIEE------------------------LLDAIVEHLPP 182
tufA CHL00071
elongation factor Tu
 1-133 4.89e-07

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 47.26  E-value: 4.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDttKWSEDRFNEIVK-ETSTFIKKVGYNPKAVAF 79
Cdd:CHL00071  100 DGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKED--QVDDEELLELVElEVRELLSKYDFPGDDIPI 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2077862637  80 VPISGWHGDNMLEESANmpWYKGWSKEIKggavKGKTLLDAIDA-IEPPVRPSDK 133
Cdd:CHL00071  171 VSGSALLALEALTENPK--IKRGENKWVD----KIYNLMDAVDSyIPTPERDTDK 219
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-133 5.61e-07

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: 47.07  E-value: 5.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGgtgefeagisKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIVK-ETSTFIKKVGYNPKA 76
Cdd:COG0050   100 DGAILVVSA----------TDGpmpQTREHILLARQVGVPYIVVFLNKCDMV--DDEELLELVEmEVRELLSKYGFPGDD 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2077862637  77 VAFVPISGWhgdNMLEESANMPWYKgwskeikggavKGKTLLDAIDA-IEPPVRPSDK 133
Cdd:COG0050   168 TPIIRGSAL---KALEGDPDPEWEK-----------KILELMDAVDSyIPEPERDTDK 211
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-127 1.36e-06

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: 45.27  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRfnEIVK-ETSTFIKKVGYNPKAVAF 79
Cdd:cd01884    90 DGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVDDEELL--ELVEmEVRELLSKYGFDGDDTPI 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2077862637  80 VPISGWhgdNMLEESANMPWYKgwskeikggavKGKTLLDAIDA-IEPP 127
Cdd:cd01884   161 VRGSAL---KALEGDDPNKWVD-----------KILELLDALDSyIPTP 195
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-133 2.91e-06

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 44.94  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIVK-ETSTFIKKVGYNPKA 76
Cdd:PRK12736  100 DGAILVVA----------ATDGpmpQTREHILLARQVGVPYLVVFLNKVDLV--DDEELLELVEmEVRELLSEYDFPGDD 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2077862637  77 VAFVPISGWHGdnmLEESanmpwyKGWSKEIKGgavkgktLLDAIDA-IEPPVRPSDK 133
Cdd:PRK12736  168 IPVIRGSALKA---LEGD------PKWEDAIME-------LMDAVDEyIPTPERDTDK 209
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-133 1.29e-04

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 40.17  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGtgefeagiskDG---QTREHALLAFTLGVRQLIVAVNKMDTTKWSEdrFNEIVK-ETSTFIKKVGYNPKA 76
Cdd:PRK00049  100 DGAILVVSAA----------DGpmpQTREHILLARQVGVPYIVVFLNKCDMVDDEE--LLELVEmEVRELLSKYDFPGDD 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2077862637  77 VAFVPISGWHGdnmLEESANMPWYKgwskeikggavKGKTLLDAIDA-IEPPVRPSDK 133
Cdd:PRK00049  168 TPIIRGSALKA---LEGDDDEEWEK-----------KILELMDAVDSyIPTPERAIDK 211
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 1-47 2.50e-04

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: 39.51  E-value: 2.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077862637   1 DCAILIIAggtgefeagiSKDG---QTREH-ALLAFtLGVRQLIVAVNKMD 47
Cdd:COG3276    76 DLVLLVVA----------ADEGvmpQTREHlAILDL-LGIKRGIVVLTKAD 115
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-80 2.75e-04

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: 39.47  E-value: 2.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIVKETSTFIKKVGYNPKAV 77
Cdd:TIGR00475  75 DAALLVVD----------ADEGvmtQTGEHLAVLDLLGIPHTIVVITKADRV--NEEEIKRTEMFMKQILNSYIFLKNAK 142


                  ...
gi 2077862637  78 AFV 80
Cdd:TIGR00475 143 IFK 145
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 23-90 3.90e-04

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 38.68  E-value: 3.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077862637  23 QTREHaLLAFT-LGVRQLIVAVNKMDTTkwSEDR----FNEIVKetstFIKkvGYNPKAVAFVPISGWHGDNM 90
Cdd:PRK04000  126 QTKEH-LMALDiIGIKNIVIVQNKIDLV--SKERalenYEQIKE----FVK--GTVAENAPIIPVSALHKVNI 189
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-133 6.21e-04

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 38.27  E-value: 6.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077862637   1 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEdrFNEIV----KETSTFIKKVGYNpka 76
Cdd:PLN03127  149 DGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEE--LLELVemelRELLSFYKFPGDE--- 216

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2077862637  77 vafVPIsgwhgdnmLEESAnMPWYKGWSKEIKGGAVkgKTLLDAIDAIEP-PVRPSDK 133
Cdd:PLN03127  217 ---IPI--------IRGSA-LSALQGTNDEIGKNAI--LKLMDAVDEYIPePVRVLDK 260
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-72 6.67e-04

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: 37.58  E-value: 6.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077862637   1 DCAILIIAGgtgefEAGISKdgQTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIVKETSTFIKKVGY 72
Cdd:cd04171    75 DAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLV--DEDRLELVEEEILELLAGTFL 137
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-47 1.13e-03

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 37.67  E-value: 1.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2077862637   1 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMD 47
Cdd:PLN03126  169 DGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQD 208
 
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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