NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1384892693|gb|AWF94279|]
View 

translation elongation factor 1-alpha, partial [Chlorophyllum agaricoides]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-132 5.27e-73

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


The actual alignment was detected with superfamily member cd01883:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 219  Bit Score: 216.97  E-value: 5.27e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIVKETSTFIKKVGY 78
Cdd:cd01883    96 TGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGY 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1384892693  79 NPKAVAFVPISGWHGDNMLEESSNMPWYKGWskenkggvvkgkTLLDAIDAIEL 132
Cdd:cd01883   176 NPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEP 217
 
Name Accession Description Interval E-value
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-132 5.27e-73

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: 216.97  E-value: 5.27e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIVKETSTFIKKVGY 78
Cdd:cd01883    96 TGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGY 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1384892693  79 NPKAVAFVPISGWHGDNMLEESSNMPWYKGWskenkggvvkgkTLLDAIDAIEL 132
Cdd:cd01883   176 NPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEP 217
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-131 5.44e-70

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 216.54  E-value: 5.44e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIVKETSTFIKKVGY 78
Cdd:PTZ00141  104 TGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGY 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1384892693  79 NPKAVAFVPISGWHGDNMLEESSNMPWYkgwskenkggvvKGKTLLDAIDAIE 131
Cdd:PTZ00141  184 NPEKVPFIPISGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLE 224
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-131 5.15e-52

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: 169.34  E-value: 5.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGYNP 80
Cdd:COG5256   104 TGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKV 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1384892693  81 KAVAFVPISGWHGDNMLEESSNMPWYkgwskenkggvvKGKTLLDAIDAIE 131
Cdd:COG5256   177 DKIPFIPVSAWKGDNVVKKSDNMPWY------------NGPTLLEALDNLK 215
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-132 3.12e-26

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: 100.91  E-value: 3.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGynP 80
Cdd:TIGR02034  99 TGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--F 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1384892693  81 KAVAFVPISGWHGDNMLEESSNMPWYkgwskenkggvvKGKTLLDAIDAIEL 132
Cdd:TIGR02034 170 RDVTFIPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEV 209
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-98 1.78e-25

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: 94.90  E-value: 1.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTkwSEDRFNEIVKETS-TFIKKVGYN 79
Cdd:pfam00009  88 RGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGED 157

                          90
                  ....*....|....*....
gi 1384892693  80 PKAVAFVPISGWHGDNMLE 98
Cdd:pfam00009 158 GEFVPVVPGSALKGEGVQT 176
 
Name Accession Description Interval E-value
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-132 5.27e-73

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: 216.97  E-value: 5.27e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIVKETSTFIKKVGY 78
Cdd:cd01883    96 TGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGY 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1384892693  79 NPKAVAFVPISGWHGDNMLEESSNMPWYKGWskenkggvvkgkTLLDAIDAIEL 132
Cdd:cd01883   176 NPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEP 217
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-131 5.44e-70

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 216.54  E-value: 5.44e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIVKETSTFIKKVGY 78
Cdd:PTZ00141  104 TGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGY 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1384892693  79 NPKAVAFVPISGWHGDNMLEESSNMPWYkgwskenkggvvKGKTLLDAIDAIE 131
Cdd:PTZ00141  184 NPEKVPFIPISGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLE 224
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-131 5.15e-52

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: 169.34  E-value: 5.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGYNP 80
Cdd:COG5256   104 TGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKV 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1384892693  81 KAVAFVPISGWHGDNMLEESSNMPWYkgwskenkggvvKGKTLLDAIDAIE 131
Cdd:COG5256   177 DKIPFIPVSAWKGDNVVKKSDNMPWY------------NGPTLLEALDNLK 215
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-130 5.95e-51

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 167.19  E-value: 5.95e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIVKETSTFIKKVGY 78
Cdd:PLN00043  104 TGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtpKYSKARYDEIVKEVSSYLKKVGY 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1384892693  79 NPKAVAFVPISGWHGDNMLEESSNMPWYkgwskenkggvvKGKTLLDAIDAI 130
Cdd:PLN00043  184 NPDKIPFVPISGFEGDNMIERSTNLDWY------------KGPTLLEALDQI 223
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-131 5.47e-50

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 164.33  E-value: 5.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGgtgefEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGYNP 80
Cdd:PRK12317  103 TGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKP 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1384892693  81 KAVAFVPISGWHGDNMLEESSNMPWYkgwskenkggvvKGKTLLDAIDAIE 131
Cdd:PRK12317  178 DDIPFIPVSAFEGDNVVKKSENMPWY------------NGPTLLEALDNLK 216
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-131 4.78e-36

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: 127.51  E-value: 4.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIaggtgefEA--GISKdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGY 78
Cdd:COG2895   114 TGASTADLAILLI-------DArkGVLE--QTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLGL 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1384892693  79 NPkaVAFVPISGWHGDNMLEESSNMPWYkgwskenkggvvKGKTLLDAIDAIE 131
Cdd:COG2895   185 ED--ITFIPISALKGDNVVERSENMPWY------------DGPTLLEHLETVE 223
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-131 2.47e-35

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: 120.75  E-value: 2.47e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGYNP 80
Cdd:cd04166    97 TGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYLAFAASLGIED 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1384892693  81 kaVAFVPISGWHGDNMLEESSNMPWYkgwskenkggvvKGKTLLDAIDAIE 131
Cdd:cd04166   170 --ITFIPISALEGDNVVSRSENMPWY------------KGPTLLEHLETVE 206
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-131 1.61e-30

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 113.47  E-value: 1.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGYNP 80
Cdd:PRK05124  126 TGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNL 198

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1384892693  81 KaVAFVPISGWHGDNMLEESSNMPWYkgwskenkggvvKGKTLLDAIDAIE 131
Cdd:PRK05124  199 D-IRFVPLSALEGDNVVSQSESMPWY------------SGPTLLEVLETVD 236
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-108 2.90e-29

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 110.79  E-value: 2.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGYNp 80
Cdd:PRK05506  123 TGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH- 194

                          90       100
                  ....*....|....*....|....*...
gi 1384892693  81 kAVAFVPISGWHGDNMLEESSNMPWYKG 108
Cdd:PRK05506  195 -DVTFIPISALKGDNVVTRSARMPWYEG 221
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-132 3.12e-26

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: 100.91  E-value: 3.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIVKETSTFIKKVGynP 80
Cdd:TIGR02034  99 TGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--F 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1384892693  81 KAVAFVPISGWHGDNMLEESSNMPWYkgwskenkggvvKGKTLLDAIDAIEL 132
Cdd:TIGR02034 170 RDVTFIPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEV 209
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-98 1.78e-25

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: 94.90  E-value: 1.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTkwSEDRFNEIVKETS-TFIKKVGYN 79
Cdd:pfam00009  88 RGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGED 157

                          90
                  ....*....|....*....
gi 1384892693  80 PKAVAFVPISGWHGDNMLE 98
Cdd:pfam00009 158 GEFVPVVPGSALKGEGVQT 176
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-98 6.40e-17

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: 72.71  E-value: 6.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEfeagiskDGQTREHALLAFtLGVRQLIVAVNKMDTTKwsEDRFNEIVKETSTFIKKVGY-- 78
Cdd:cd00881    81 RGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRVG--EEDFDEVLREIKELLKLIGFtf 150

                          90       100
                  ....*....|....*....|.
gi 1384892693  79 -NPKAVAFVPISGWHGDNMLE 98
Cdd:cd00881   151 lKGKDVPIIPISALTGEGIEE 171
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-53 2.75e-09

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: 52.59  E-value: 2.75e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMD 53
Cdd:cd01884    84 TGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKAD 129
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-53 1.21e-08

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: 51.69  E-value: 1.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1384892693   1 TGTSQADCAILIIAGgtgefeagisKDG---QTREHALLAFTLGVRQLIVAVNKMD 53
Cdd:COG0050    94 TGAAQMDGAILVVSA----------TDGpmpQTREHILLARQVGVPYIVVFLNKCD 139
tufA CHL00071
elongation factor Tu
 1-128 4.98e-08

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 49.96  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDttKWSEDRFNEIVK-ETSTFIKKVGYN 79
Cdd:CHL00071   94 TGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKED--QVDDEELLELVElEVRELLSKYDFP 164

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1384892693  80 PKAVAFVPISGWHGDNMLEESSNmpwykgWSKENKGGVVKGKTLLDAID 128
Cdd:CHL00071  165 GDDIPIVSGSALLALEALTENPK------IKRGENKWVDKIYNLMDAVD 207
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-53 5.15e-07

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 46.86  E-value: 5.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1384892693   1 TGTSQADCAILIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMD 53
Cdd:PRK12736   94 TGAAQMDGAILVVA----------ATDGpmpQTREHILLARQVGVPYLVVFLNKVD 139
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-53 7.52e-07

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 46.72  E-value: 7.52e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1384892693   1 TGTSQADCAILIIAGGtgefeagiskDG---QTREHALLAFTLGVRQLIVAVNKMD 53
Cdd:PRK00049   94 TGAAQMDGAILVVSAA----------DGpmpQTREHILLARQVGVPYIVVFLNKCD 139
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-53 3.75e-06

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 44.61  E-value: 3.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMD 53
Cdd:PLN03126  163 TGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQD 208
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-59 7.68e-06

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 43.66  E-value: 7.68e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1384892693   1 TGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSE 59
Cdd:PLN03127  143 TGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEE 194
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 2-86 1.02e-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: 40.63  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   2 GTSQADCAILIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIVKETSTFIKKVGY 78
Cdd:TIGR00475  70 GGGGIDAALLVVD----------ADEGvmtQTGEHLAVLDLLGIPHTIVVITKADRV--NEEEIKRTEMFMKQILNSYIF 137


                  ....*...
gi 1384892693  79 NPKAVAFV 86
Cdd:TIGR00475 138 LKNAKIFK 145
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 2-78 1.85e-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: 39.13  E-value: 1.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1384892693   2 GTSQADCAILIIAGgtgefEAGISKdgQTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIVKETSTFIKKVGY 78
Cdd:cd04171    70 GAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLV--DEDRLELVEEEILELLAGTFL 137
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 7-53 2.43e-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: 2.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1384892693   7 DCAILIIAggtgefeagiSKDG---QTREH-ALLAFtLGVRQLIVAVNKMD 53
Cdd:COG3276    76 DLVLLVVA----------ADEGvmpQTREHlAILDL-LGIKRGIVVLTKAD 115
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 29-96 2.49e-04

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 39.45  E-value: 2.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1384892693  29 QTREHaLLAFT-LGVRQLIVAVNKMDTTkwSEDR----FNEIVKetstFIKkvGYNPKAVAFVPISGWHGDNM 96
Cdd:PRK04000  126 QTKEH-LMALDiIGIKNIVIVQNKIDLV--SKERalenYEQIKE----FVK--GTVAENAPIIPVSALHKVNI 189
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 2-96 2.45e-03

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: 35.91  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   2 GTSQADCAILIIAGGTGeFEAgiskdgQTRE---HALLAFTlgvrQLIVAVNKMDTTKWSE---DRFNEIVKETSTFIKK 75
Cdd:cd01887    69 GASVTDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVAINKIDKPYGTEadpERVKNELSELGLVGEE 137

                          90       100
                  ....*....|....*....|.
gi 1384892693  76 VGynpKAVAFVPISGWHGDNM 96
Cdd:cd01887   138 WG---GDVSIVPISAKTGEGI 155
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 1-89 7.83e-03

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 34.98  E-value: 7.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384892693   1 TGTSQADCAILIIAGGTGefeagiSKDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSE--DRFNEIVKetstFIKkvGY 78
Cdd:PTZ00327  136 NGAAVMDAALLLIAANES------CPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQaqDQYEEIRN----FVK--GT 203

                          90
                  ....*....|.
gi 1384892693  79 NPKAVAFVPIS 89
Cdd:PTZ00327  204 IADNAPIIPIS 214
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH