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Conserved domains on  [gi|1024897047|gb|ANC29382|]
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translation elongation factor-1 alpha, partial [Agaricus sp. SWK014]

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 ...
 1-134 1.92e-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: 217.69  E-value: 1.92e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSTFIKKVGYNPKAV 78
Cdd:PTZ00141  109 ADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKV 188

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1024897047  79 AFVPISGWHGDNMLEESSNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 134
Cdd:PTZ00141  189 PFIPISGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDK 232
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-134 1.92e-70

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 217.69  E-value: 1.92e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSTFIKKVGYNPKAV 78
Cdd:PTZ00141  109 ADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKV 188

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1024897047  79 AFVPISGWHGDNMLEESSNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 134
Cdd:PTZ00141  189 PFIPISGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDK 232
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-129 3.32e-70

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: 209.65  E-value: 3.32e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSTFIKKVGYNPKAV 78
Cdd:cd01883   101 ADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDV 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1024897047  79 AFVPISGWHGDNMLEESSNMPWYKGWtketkagvvkgkTLLDAIDAIEPPV 129
Cdd:cd01883   181 PFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-134 2.31e-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: 165.11  E-value: 2.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPKAVAF 80
Cdd:COG5256   109 ADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPF 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1024897047  81 VPISGWHGDNMLEESSNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 134
Cdd:COG5256   182 IPVSAWKGDNVVKKSDNMPWY------------NGPTLLEALDNLKEPEKPVDK 223
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-105 1.95e-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: 93.59  E-value: 1.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGynPKAVAF 80
Cdd:TIGR02034 104 ADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--FRDVTF 174

                          90       100
                  ....*....|....*....|....*
gi 1024897047  81 VPISGWHGDNMLEESSNMPWYKGWT 105
Cdd:TIGR02034 175 IPLSALKGDNVVSRSESMPWYSGPT 199
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-128 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: 87.58  E-value: 1.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTkwSEDRFNEIIKETS-TFIKKVGYNPKAVA 79
Cdd:pfam00009  93 ADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGEDGEFVP 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1024897047  80 FVPISGWHGDNMleessnmpwykgwtketkagvvkgKTLLDAIDAIEPP 128
Cdd:pfam00009 163 VVPGSALKGEGV------------------------QTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-134 1.92e-70

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 217.69  E-value: 1.92e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSTFIKKVGYNPKAV 78
Cdd:PTZ00141  109 ADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKV 188

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1024897047  79 AFVPISGWHGDNMLEESSNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 134
Cdd:PTZ00141  189 PFIPISGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDK 232
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-129 3.32e-70

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: 209.65  E-value: 3.32e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSTFIKKVGYNPKAV 78
Cdd:cd01883   101 ADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDV 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1024897047  79 AFVPISGWHGDNMLEESSNMPWYKGWtketkagvvkgkTLLDAIDAIEPPV 129
Cdd:cd01883   181 PFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-134 2.25e-51

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 168.34  E-value: 2.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSTFIKKVGYNPKAV 78
Cdd:PLN00043  109 ADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtpKYSKARYDEIVKEVSSYLKKVGYNPDKI 188

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1024897047  79 AFVPISGWHGDNMLEESSNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 134
Cdd:PLN00043  189 PFVPISGFEGDNMIERSTNLDWY------------KGPTLLEALDQINEPKRPSDK 232
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-134 2.31e-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: 165.11  E-value: 2.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPKAVAF 80
Cdd:COG5256   109 ADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPF 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1024897047  81 VPISGWHGDNMLEESSNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 134
Cdd:COG5256   182 IPVSAWKGDNVVKKSDNMPWY------------NGPTLLEALDNLKEPEKPVDK 223
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-134 9.51e-49

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 160.86  E-value: 9.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGgtgefEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPKAVAF 80
Cdd:PRK12317  108 ADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPF 182

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1024897047  81 VPISGWHGDNMLEESSNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 134
Cdd:PRK12317  183 IPVSAFEGDNVVKKSENMPWY------------NGPTLLEALDNLKPPEKPTDK 224
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-134 3.24e-33

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: 120.19  E-value: 3.24e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIaggtgefEA--GISKdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPkaV 78
Cdd:COG2895   119 ADLAILLI-------DArkGVLE--QTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLGLED--I 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1024897047  79 AFVPISGWHGDNMLEESSNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 134
Cdd:COG2895   188 TFIPISALKGDNVVERSENMPWY------------DGPTLLEHLETVEVAEDRNDA 231
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-128 7.97e-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: 114.59  E-value: 7.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPkaVAF 80
Cdd:cd04166   102 ADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYLAFAASLGIED--ITF 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1024897047  81 VPISGWHGDNMLEESSNMPWYkgwtketkagvvKGKTLLDAIDAIEPP 128
Cdd:cd04166   173 IPISALEGDNVVSRSENMPWY------------KGPTLLEHLETVEIA 208
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-126 1.08e-27

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 105.77  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPKaVAF 80
Cdd:PRK05124  131 CDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNLD-IRF 202

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1024897047  81 VPISGWHGDNMLEESSNMPWYkgwtketkagvvKGKTLLDAIDAIE 126
Cdd:PRK05124  203 VPLSALEGDNVVSQSESMPWY------------SGPTLLEVLETVD 236
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-103 6.63e-26

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 101.16  E-value: 6.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNpkAVAF 80
Cdd:PRK05506  128 ADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH--DVTF 198

                          90       100
                  ....*....|....*....|...
gi 1024897047  81 VPISGWHGDNMLEESSNMPWYKG 103
Cdd:PRK05506  199 IPISALKGDNVVTRSARMPWYEG 221
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-105 1.95e-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: 93.59  E-value: 1.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGynPKAVAF 80
Cdd:TIGR02034 104 ADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--FRDVTF 174

                          90       100
                  ....*....|....*....|....*
gi 1024897047  81 VPISGWHGDNMLEESSNMPWYKGWT 105
Cdd:TIGR02034 175 IPLSALKGDNVVSRSESMPWYSGPT 199
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-128 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: 87.58  E-value: 1.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTkwSEDRFNEIIKETS-TFIKKVGYNPKAVA 79
Cdd:pfam00009  93 ADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGEDGEFVP 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1024897047  80 FVPISGWHGDNMleessnmpwykgwtketkagvvkgKTLLDAIDAIEPP 128
Cdd:pfam00009 163 VVPGSALKGEGV------------------------QTLLDALDEYLPS 187
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-128 2.50e-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: 68.48  E-value: 2.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGEfeagiskDGQTREHALLAFtLGVRQLIVAVNKMDTTKwsEDRFNEIIKETSTFIKKVGY---NPKA 77
Cdd:cd00881    86 ADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRVG--EEDFDEVLREIKELLKLIGFtflKGKD 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1024897047  78 VAFVPISGWHGDNMLEessnmpwykgwtketkagvvkgktLLDAIDAIEPP 128
Cdd:cd00881   156 VPIIPISALTGEGIEE------------------------LLDAIVEHLPP 182
tufA CHL00071
elongation factor Tu
 2-134 5.70e-07

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 46.87  E-value: 5.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   2 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDttKWSEDRFNEIIK-ETSTFIKKVGYNPKAVAF 80
Cdd:CHL00071  100 DGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKED--QVDDEELLELVElEVRELLSKYDFPGDDIPI 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1024897047  81 VPISGWHGDNMLEESSNmpwykgWTKETKAGVVKGKTLLDAIDA-IEPPVRPSDK 134
Cdd:CHL00071  171 VSGSALLALEALTENPK------IKRGENKWVDKIYNLMDAVDSyIPTPERDTDK 219
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 2-134 5.82e-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: 5.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   2 DCAILIIAGgtgefeagisKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwsEDrfNEIIK----ETSTFIKKVGYN 74
Cdd:COG0050   100 DGAILVVSA----------TDGpmpQTREHILLARQVGVPYIVVFLNKCDMV---DD--EELLElvemEVRELLSKYGFP 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024897047  75 PKAVAFVPISGWhgdNMLEESSNMPWYKgwtketkagvvKGKTLLDAIDA-IEPPVRPSDK 134
Cdd:COG0050   165 GDDTPIIRGSAL---KALEGDPDPEWEK-----------KILELMDAVDSyIPEPERDTDK 211
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 2-128 2.22e-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: 44.88  E-value: 2.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   2 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKwSEDRFNEIIKETSTFIKKVGYNPKAVAFV 81
Cdd:cd01884    90 DGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD-DEELLELVEMEVRELLSKYGFDGDDTPIV 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1024897047  82 PISGWhgdNMLEESSNMPWYKgwtketkagvvKGKTLLDAIDA-IEPP 128
Cdd:cd01884   162 RGSAL---KALEGDDPNKWVD-----------KILELLDALDSyIPTP 195
PRK12736 PRK12736
elongation factor Tu; Reviewed
 2-134 2.70e-05

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 42.24  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   2 DCAILIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIK-ETSTFIKKVGYNPKA 77
Cdd:PRK12736  100 DGAILVVA----------ATDGpmpQTREHILLARQVGVPYLVVFLNKVDLV--DDEELLELVEmEVRELLSEYDFPGDD 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1024897047  78 VAFVPISGWHGdnmLEESSnmPWYKgwtketkagvvKGKTLLDAIDA-IEPPVRPSDK 134
Cdd:PRK12736  168 IPVIRGSALKA---LEGDP--KWED-----------AIMELMDAVDEyIPTPERDTDK 209
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-81 1.86e-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: 39.86  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKKVGYNPKA 77
Cdd:TIGR00475  74 IDAALLVVD----------ADEGvmtQTGEHLAVLDLLGIPHTIVVITKADRV--NEEEIKRTEMFMKQILNSYIFLKNA 141


                  ....
gi 1024897047  78 VAFV 81
Cdd:TIGR00475 142 KIFK 145
PRK00049 PRK00049
elongation factor Tu; Reviewed
 2-48 1.99e-04

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 39.79  E-value: 1.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024897047   2 DCAILIIAGGtgefeagiskDG---QTREHALLAFTLGVRQLIVAVNKMD 48
Cdd:PRK00049  100 DGAILVVSAA----------DGpmpQTREHILLARQVGVPYIVVFLNKCD 139
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 2-84 2.07e-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: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   2 DCAILIIAggtgefeagiSKDG---QTREH-ALLAFtLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKkvGYNPKA 77
Cdd:COG3276    76 DLVLLVVA----------ADEGvmpQTREHlAILDL-LGIKRGIVVLTKADLV--DEEWLELVEEEIRELLA--GTFLED 140


                  ....*..
gi 1024897047  78 VAFVPIS 84
Cdd:COG3276   141 APIVPVS 147
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 2-73 3.72e-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: 38.36  E-value: 3.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024897047   2 DCAILIIAGgtgefEAGISKdgQTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKKVGY 73
Cdd:cd04171    75 DAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLV--DEDRLELVEEEILELLAGTFL 137
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 24-91 6.69e-04

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 38.29  E-value: 6.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024897047  24 QTREHaLLAFT-LGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKkvGYNPKAVAFVPISGWHGDNM 91
Cdd:PRK04000  126 QTKEH-LMALDiIGIKNIVIVQNKIDLV--SKERALENYEQIKEFVK--GTVAENAPIIPVSALHKVNI 189
PLN03127 PLN03127
Elongation factor Tu; Provisional
 2-134 7.20e-04

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 38.27  E-value: 7.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   2 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSE--DRFNEIIKETSTFIKKVGYNpkava 79
Cdd:PLN03127  149 DGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEEllELVEMELRELLSFYKFPGDE----- 216

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1024897047  80 fVPISgwhgdnmleESSNMPWYKGWTKET-KAGVVKgktLLDAIDAIEP-PVRPSDK 134
Cdd:PLN03127  217 -IPII---------RGSALSALQGTNDEIgKNAILK---LMDAVDEYIPePVRVLDK 260
PLN03126 PLN03126
Elongation factor Tu; Provisional
 2-48 1.24e-03

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 37.29  E-value: 1.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1024897047   2 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMD 48
Cdd:PLN03126  169 DGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQD 208
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 1-91 3.32e-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: 35.53  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024897047   1 ADCAILIIAGGTGeFEAgiskdgQTRE---HALLAFTlgvrQLIVAVNKMDTTKWSE---DRFNEIIKETSTFIKKVGyn 74
Cdd:cd01887    73 TDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVAINKIDKPYGTEadpERVKNELSELGLVGEEWG-- 139

                          90
                  ....*....|....*..
gi 1024897047  75 pKAVAFVPISGWHGDNM 91
Cdd:cd01887   140 -GDVSIVPISAKTGEGI 155
 
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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