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Conserved domains on  [gi|1767126922|gb|QFQ59976|]
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translation elongation factor 1-alpha, partial [Suillus latteri]

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 ...
 1-145 3.84e-81

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: 245.81  E-value: 3.84e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922   1 LIIAGGTGEF*AGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSTFIKKVGYNPKAVAFVPI 78
Cdd:PTZ00141  114 LVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPI 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767126922  79 SGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIG 145
Cdd:PTZ00141  194 SGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIG 248
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-145 3.84e-81

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 245.81  E-value: 3.84e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922   1 LIIAGGTGEF*AGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSTFIKKVGYNPKAVAFVPI 78
Cdd:PTZ00141  114 LVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPI 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767126922  79 SGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIG 145
Cdd:PTZ00141  194 SGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIG 248
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-124 1.16e-64

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: 196.17  E-value: 1.16e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922   1 LIIAGGTGEF*AGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSTFIKKVGYNPKAVAFVPI 78
Cdd:cd01883   106 LVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPI 185

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1767126922  79 SGWHGDNMLEESPNMPWYKGWtketkggvvkgkTLLDAIDAIEPPV 124
Cdd:cd01883   186 SGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 18-145 1.19e-59

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: 189.76  E-value: 1.19e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  18 GQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPKAVAFVPISGWHGDNMLEESPNMPWYk 97
Cdd:COG5256   124 GQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWY- 202

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1767126922  98 gwtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIG 145
Cdd:COG5256   203 -----------NGPTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIG 239
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 19-138 1.33e-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: 102.45  E-value: 1.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  19 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGynPKAVAFVPISGWHGDNMLEESPNMPWYkg 98
Cdd:TIGR02034 120 QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY-- 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1767126922  99 wtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDV 138
Cdd:TIGR02034 196 ----------SGPTLLEILETVEVERDAQDLPLRFPVQYV 225
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 18-123 9.91e-19

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: 77.95  E-value: 9.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  18 GQTREHALLAFTLGVRqLIVAVNKMDTTkwSEDRFNEIIKETS-TFIKKVGYNPKAVAFVPISGWHGDNMleespnmpwy 96
Cdd:pfam00009 108 PQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGEDGEFVPVVPGSALKGEGV---------- 174

                          90       100
                  ....*....|....*....|....*..
gi 1767126922  97 kgwtketkggvvkgKTLLDAIDAIEPP 123
Cdd:pfam00009 175 --------------QTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-145 3.84e-81

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 245.81  E-value: 3.84e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922   1 LIIAGGTGEF*AGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSTFIKKVGYNPKAVAFVPI 78
Cdd:PTZ00141  114 LVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPI 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767126922  79 SGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIG 145
Cdd:PTZ00141  194 SGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIG 248
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-124 1.16e-64

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: 196.17  E-value: 1.16e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922   1 LIIAGGTGEF*AGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSTFIKKVGYNPKAVAFVPI 78
Cdd:cd01883   106 LVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPI 185

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1767126922  79 SGWHGDNMLEESPNMPWYKGWtketkggvvkgkTLLDAIDAIEPPV 124
Cdd:cd01883   186 SGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 18-145 1.19e-59

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: 189.76  E-value: 1.19e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  18 GQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPKAVAFVPISGWHGDNMLEESPNMPWYk 97
Cdd:COG5256   124 GQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWY- 202

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1767126922  98 gwtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIG 145
Cdd:COG5256   203 -----------NGPTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIG 239
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 18-145 4.74e-59

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 188.21  E-value: 4.74e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  18 GQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPKAVAFVPISGWHGDNMLEESPNMPWYk 97
Cdd:PRK12317  125 PQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWY- 203

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1767126922  98 gwtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIG 145
Cdd:PRK12317  204 -----------NGPTLLEALDNLKPPEKPTDKPLRIPIQDVYSISGVG 240
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-145 1.02e-58

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 187.99  E-value: 1.02e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922   1 LIIAGGTGEF*AGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSTFIKKVGYNPKAVAFVPI 78
Cdd:PLN00043  114 LIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtpKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPI 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767126922  79 SGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIG 145
Cdd:PLN00043  194 SGFEGDNMIERSTNLDWY------------KGPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIG 248
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 19-140 3.77e-41

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: 141.76  E-value: 3.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  19 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPkaVAFVPISGWHGDNMLEESPNMPWYkg 98
Cdd:COG2895   135 QTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWY-- 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1767126922  99 wtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYK 140
Cdd:COG2895   211 ----------DGPTLLEHLETVEVAEDRNDAPFRFPVQYVNR 242
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 19-123 1.97e-32

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: 113.82  E-value: 1.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  19 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPkaVAFVPISGWHGDNMLEESPNMPWYkg 98
Cdd:cd04166   118 QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWY-- 193

                          90       100
                  ....*....|....*....|....*
gi 1767126922  99 wtketkggvvKGKTLLDAIDAIEPP 123
Cdd:cd04166   194 ----------KGPTLLEHLETVEIA 208
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 19-138 4.32e-29

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 110.00  E-value: 4.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  19 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPKaVAFVPISGWHGDNMLEESPNMPWYkg 98
Cdd:PRK05124  147 QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWY-- 223

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1767126922  99 wtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDV 138
Cdd:PRK05124  224 ----------SGPTLLEVLETVDIQRVVDAQPFRFPVQYV 253
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 19-138 1.35e-28

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 109.25  E-value: 1.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  19 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNpkAVAFVPISGWHGDNMLEESPNMPWYkg 98
Cdd:PRK05506  144 QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWY-- 219

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1767126922  99 wtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDV 138
Cdd:PRK05506  220 ----------EGPSLLEHLETVEIASDRNLKDFRFPVQYV 249
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 19-138 1.33e-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: 102.45  E-value: 1.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  19 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGynPKAVAFVPISGWHGDNMLEESPNMPWYkg 98
Cdd:TIGR02034 120 QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY-- 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1767126922  99 wtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDV 138
Cdd:TIGR02034 196 ----------SGPTLLEILETVEVERDAQDLPLRFPVQYV 225
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 18-123 9.91e-19

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: 77.95  E-value: 9.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  18 GQTREHALLAFTLGVRqLIVAVNKMDTTkwSEDRFNEIIKETS-TFIKKVGYNPKAVAFVPISGWHGDNMleespnmpwy 96
Cdd:pfam00009 108 PQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGEDGEFVPVVPGSALKGEGV---------- 174

                          90       100
                  ....*....|....*....|....*..
gi 1767126922  97 kgwtketkggvvkgKTLLDAIDAIEPP 123
Cdd:pfam00009 175 --------------QTLLDALDEYLPS 187
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 18-123 1.10e-11

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: 59.23  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  18 GQTREHALLAFtLGVRQLIVAVNKMDTTKwsEDRFNEIIKETSTFIKKVGY---NPKAVAFVPISGWHGDNMLEespnmp 94
Cdd:cd00881   101 PQTREHLNIAL-AGGLPIIVAVNKIDRVG--EEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE------ 171

                          90       100
                  ....*....|....*....|....*....
gi 1767126922  95 wykgwtketkggvvkgktLLDAIDAIEPP 123
Cdd:cd00881   172 ------------------LLDAIVEHLPP 182
tufA CHL00071
elongation factor Tu
 17-145 1.89e-11

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 60.36  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  17 DG---QTREHALLAFTLGVRQLIVAVNKMDttKWSEDRFNEIIK-ETSTFIKKVGYNPKAVAFVPISGWHGDNMLEESPN 92
Cdd:CHL00071  110 DGpmpQTKEHILLAKQVGVPNIVVFLNKED--QVDDEELLELVElEVRELLSKYDFPGDDIPIVSGSALLALEALTENPK 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1767126922  93 mpwykgWTKETKGGVVKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIG 145
Cdd:CHL00071  188 ------IKRGENKWVDKIYNLMDAVDSyIPTPERDTDKPFLMAIEDVFSITGRG 235
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 17-145 4.27e-11

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: 59.01  E-value: 4.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  17 DG---QTREHALLAFTLGVRQLIVAVNKMDTTkwsEDrfNEIIK----ETSTFIKKVGYNPKAVAFVPISGWhgdNMLEE 89
Cdd:COG0050   110 DGpmpQTREHILLARQVGVPYIVVFLNKCDMV---DD--EELLElvemEVRELLSKYGFPGDDTPIIRGSAL---KALEG 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1767126922  90 SPNMPWYKgwtketkggvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIG 145
Cdd:COG0050   182 DPDPEWEK-----------KILELMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRG 227
PRK12736 PRK12736
elongation factor Tu; Reviewed
 17-145 1.57e-10

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 57.65  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  17 DG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIK-ETSTFIKKVGYNPKAVAFVPISGWHGdnmLEESPn 92
Cdd:PRK12736  110 DGpmpQTREHILLARQVGVPYLVVFLNKVDLV--DDEELLELVEmEVRELLSEYDFPGDDIPVIRGSALKA---LEGDP- 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1767126922  93 mPWYKgwtketkggvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIG 145
Cdd:PRK12736  184 -KWED-----------AIMELMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRG 225
PRK00049 PRK00049
elongation factor Tu; Reviewed
 17-145 1.16e-08

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 52.11  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  17 DG---QTREHALLAFTLGVRQLIVAVNKMDTtkwSEDRfnEIIK----ETSTFIKKVGYNPKAVAFVPISGWHGdnmLEE 89
Cdd:PRK00049  110 DGpmpQTREHILLARQVGVPYIVVFLNKCDM---VDDE--ELLElvemEVRELLSKYDFPGDDTPIIRGSALKA---LEG 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1767126922  90 SPNMPWYKgwtketkggvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIG 145
Cdd:PRK00049  182 DDDEEWEK-----------KILELMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRG 227
PLN03127 PLN03127
Elongation factor Tu; Provisional
 19-145 2.38e-08

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 51.36  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  19 QTREHALLAFTLGVRQLIVAVNKMDTTKWSE--DRFNEIIKETSTFIKKVGYNPKAVAFVPISGWHGDNmleespnmpwy 96
Cdd:PLN03127  164 QTKEHILLARQVGVPSLVVFLNKVDVVDDEEllELVEMELRELLSFYKFPGDEIPIIRGSALSALQGTN----------- 232

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1767126922  97 kgwTKETKGGVVKgktLLDAIDAIEP-PVRPSDKPLRLPLQDVYKIGGIG 145
Cdd:PLN03127  233 ---DEIGKNAILK---LMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRG 276
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 127-145 1.20e-07

Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 46.41  E-value: 1.20e-07
                          10
                  ....*....|....*....
gi 1767126922 127 SDKPLRLPLQDVYKIGGIG 145
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIG 19
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-145 1.08e-06

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 46.53  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922   1 LIIAGGTGEF*agiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKwSEDRFNEIIKETSTFIKKVGYNPKAVAFVPISG 80
Cdd:PLN03126  173 LVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD-DEELLELVELEVRELLSSYEFPGDDIPIISGSA 244

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767126922  81 WHGDNMLEESPNMPwyKGWTKetkgGVVKGKTLLDAIDAIEP-PVRPSDKPLRLPLQDVYKIGGIG 145
Cdd:PLN03126  245 LLALEALMENPNIK--RGDNK----WVDKIYELMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRG 304
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 19-145 5.16e-06

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: 44.86  E-value: 5.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  19 QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKKVGYNPKAVAFVpISGWHGDNMLEESPNMpwykg 98
Cdd:TIGR00475  90 QTGEHLAVLDLLGIPHTIVVITKADRV--NEEEIKRTEMFMKQILNSYIFLKNAKIFK-TSAKTGQGIGELKKEL----- 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1767126922  99 wtketkggvvkgKTLLDAIDAieppvRPSDKPLRLPLQDVYKIGGIG 145
Cdd:TIGR00475 162 ------------KNLLESLDI-----KRIQKPLRMAIDRAFKVKGAG 191
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 19-145 7.51e-06

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: 44.13  E-value: 7.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  19 QTREH-ALLAFtLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKkvGYNPKAVAFVPISGWHGDNmLEEspnmpwyk 97
Cdd:COG3276    91 QTREHlAILDL-LGIKRGIVVLTKADLV--DEEWLELVEEEIRELLA--GTFLEDAPIVPVSAVTGEG-IDE-------- 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1767126922  98 gwtketkggvvkgktLLDAIDAI--EPPVRPSDKPLRLPLQDVYKIGGIG 145
Cdd:COG3276   157 ---------------LRAALDALaaAVPARDADGPFRLPIDRVFSIKGFG 191
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 17-43 1.19e-04

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: 40.26  E-value: 1.19e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1767126922  17 DG---QTREHALLAFTLGVRQLIVAVNKMD 43
Cdd:cd01884   100 DGpmpQTREHLLLARQVGVPYIVVFLNKAD 129
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 19-133 1.03e-03

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 37.91  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767126922  19 QTREHaLLAFT-LGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKkvGYNPKAVAFVPISGWHGDNMleespnmpwyk 97
Cdd:PRK04000  126 QTKEH-LMALDiIGIKNIVIVQNKIDLV--SKERALENYEQIKEFVK--GTVAENAPIIPVSALHKVNI----------- 189

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1767126922  98 gwtketkggvvkgKTLLDAIDA-IEPPVRPSDKPLRL 133
Cdd:PRK04000  190 -------------DALIEAIEEeIPTPERDLDKPPRM 213
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 19-68 2.19e-03

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: 36.43  E-value: 2.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1767126922  19 QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKKVGY 68
Cdd:cd04171    90 QTREHLEILELLGIKKGLVVLTKADLV--DEDRLELVEEEILELLAGTFL 137
 
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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