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Conserved domains on  [gi|649911186|gb|AIC66040|]
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translation elongation factor 1-alpha, partial [Amanita virosa]

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 ...
 1-147 5.35e-84

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: 253.13  E-value: 5.35e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSTFIKKVG 78
Cdd:PTZ00141 103 ITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVG 182

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 649911186  79 YNPKAVAFVPISGWHGDNMLEESPNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQ 147
Cdd:PTZ00141 183 YNPEKVPFIPISGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDKPLRLPLQ 239
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-147 5.35e-84

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 253.13  E-value: 5.35e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSTFIKKVG 78
Cdd:PTZ00141 103 ITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVG 182

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 649911186  79 YNPKAVAFVPISGWHGDNMLEESPNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQ 147
Cdd:PTZ00141 183 YNPEKVPFIPISGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDKPLRLPLQ 239
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-135 8.44e-77

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: 226.99  E-value: 8.44e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSTFIKKVG 78
Cdd:cd01883   95 ITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVG 174

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 649911186  79 YNPKAVAFVPISGWHGDNMLEESPNMPWYKGWtketkagvvkgkTLLDAIDAIEPPV 135
Cdd:cd01883  175 YNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-147 3.93e-62

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: 196.31  E-value: 3.93e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYN 80
Cdd:COG5256  103 ITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYK 175

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 649911186  81 PKAVAFVPISGWHGDNMLEESPNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQ 147
Cdd:COG5256  176 VDKIPFIPVSAWKGDNVVKKSDNMPWY------------NGPTLLEALDNLKEPEKPVDKPLRIPIQ 230
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 2-147 1.85e-29

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: 110.54  E-value: 1.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186    2 TGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGynP 81
Cdd:TIGR02034  99 TGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--F 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 649911186   82 KAVAFVPISGWHGDNMLEESPNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQ 147
Cdd:TIGR02034 170 RDVTFIPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEVERDAQDLPLRFPVQ 223
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-134 2.12e-26

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: 97.60  E-value: 2.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186    1 ITGTSQADCAILIIAGGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTkwSEDRFNEIIKETS-TFIKKVGY 79
Cdd:pfam00009  87 IRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGE 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 649911186   80 NPKAVAFVPISGWHGDNMleespnmpwykgwtketkagvvkgKTLLDAIDAIEPP 134
Cdd:pfam00009 157 DGEFVPVVPGSALKGEGV------------------------QTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-147 5.35e-84

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 253.13  E-value: 5.35e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSTFIKKVG 78
Cdd:PTZ00141 103 ITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVG 182

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 649911186  79 YNPKAVAFVPISGWHGDNMLEESPNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQ 147
Cdd:PTZ00141 183 YNPEKVPFIPISGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDKPLRLPLQ 239
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-135 8.44e-77

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: 226.99  E-value: 8.44e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSTFIKKVG 78
Cdd:cd01883   95 ITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVG 174

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 649911186  79 YNPKAVAFVPISGWHGDNMLEESPNMPWYKGWtketkagvvkgkTLLDAIDAIEPPV 135
Cdd:cd01883  175 YNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-147 3.93e-62

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: 196.31  E-value: 3.93e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYN 80
Cdd:COG5256  103 ITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYK 175

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 649911186  81 PKAVAFVPISGWHGDNMLEESPNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQ 147
Cdd:COG5256  176 VDKIPFIPVSAWKGDNVVKKSDNMPWY------------NGPTLLEALDNLKEPEKPVDKPLRIPIQ 230
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-147 4.97e-61

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 194.15  E-value: 4.97e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSTFIKKVG 78
Cdd:PLN00043 103 ITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtpKYSKARYDEIVKEVSSYLKKVG 182

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 649911186  79 YNPKAVAFVPISGWHGDNMLEESPNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQ 147
Cdd:PLN00043 183 YNPDKIPFVPISGFEGDNMIERSTNLDWY------------KGPTLLEALDQINEPKRPSDKPLRLPLQ 239
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-147 1.67e-60

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 192.06  E-value: 1.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGgtgefEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYN 80
Cdd:PRK12317 102 ITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYK 176

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 649911186  81 PKAVAFVPISGWHGDNMLEESPNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQ 147
Cdd:PRK12317 177 PDDIPFIPVSAFEGDNVVKKSENMPWY------------NGPTLLEALDNLKPPEKPTDKPLRIPIQ 231
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-147 4.22e-42

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: 144.07  E-value: 4.22e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIaggtgefEA--GISKdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVG 78
Cdd:COG2895  113 VTGASTADLAILLI-------DArkGVLE--QTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLG 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 649911186  79 YNPkaVAFVPISGWHGDNMLEESPNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQ 147
Cdd:COG2895  184 LED--ITFIPISALKGDNVVERSENMPWY------------DGPTLLEHLETVEVAEDRNDAPFRFPVQ 238
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-134 5.46e-36

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: 123.06  E-value: 5.46e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYN 80
Cdd:cd04166   96 VTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYLAFAASLGIE 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 649911186  81 PkaVAFVPISGWHGDNMLEESPNMPWYkgwtketkagvvKGKTLLDAIDAIEPP 134
Cdd:cd04166  169 D--ITFIPISALEGDNVVSRSENMPWY------------KGPTLLEHLETVEIA 208
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-147 2.63e-32

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 118.86  E-value: 2.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYN 80
Cdd:PRK05124 125 ATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGN 197

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 649911186  81 PKaVAFVPISGWHGDNMLEESPNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQ 147
Cdd:PRK05124 198 LD-IRFVPLSALEGDNVVSQSESMPWY------------SGPTLLEVLETVDIQRVVDAQPFRFPVQ 251
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-147 3.75e-31

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 116.57  E-value: 3.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYN 80
Cdd:PRK05506 122 VTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH 194

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 649911186  81 pkAVAFVPISGWHGDNMLEESPNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQ 147
Cdd:PRK05506 195 --DVTFIPISALKGDNVVTRSARMPWY------------EGPSLLEHLETVEIASDRNLKDFRFPVQ 247
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 2-147 1.85e-29

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: 110.54  E-value: 1.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186    2 TGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGynP 81
Cdd:TIGR02034  99 TGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--F 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 649911186   82 KAVAFVPISGWHGDNMLEESPNMPWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQ 147
Cdd:TIGR02034 170 RDVTFIPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEVERDAQDLPLRFPVQ 223
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-134 2.12e-26

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: 97.60  E-value: 2.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186    1 ITGTSQADCAILIIAGGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTkwSEDRFNEIIKETS-TFIKKVGY 79
Cdd:pfam00009  87 IRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGE 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 649911186   80 NPKAVAFVPISGWHGDNMleespnmpwykgwtketkagvvkgKTLLDAIDAIEPP 134
Cdd:pfam00009 157 DGEFVPVVPGSALKGEGV------------------------QTLLDALDEYLPS 187
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-134 1.59e-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: 74.64  E-value: 1.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEfeagiskDGQTREHALLAFtLGVRQLIVAVNKMDTTKwsEDRFNEIIKETSTFIKKVGY- 79
Cdd:cd00881   80 VRGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRVG--EEDFDEVLREIKELLKLIGFt 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 649911186  80 --NPKAVAFVPISGWHGDNMLEespnmpwykgwtketkagvvkgktLLDAIDAIEPP 134
Cdd:cd00881  150 flKGKDVPIIPISALTGEGIEE------------------------LLDAIVEHLPP 182
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-145 1.31e-12

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: 63.63  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGgtgefeagisKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwsEDrfNEIIK----ETSTF 73
Cdd:COG0050   93 ITGAAQMDGAILVVSA----------TDGpmpQTREHILLARQVGVPYIVVFLNKCDMV---DD--EELLElvemEVREL 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 649911186  74 IKKVGYNPKAVAFVPISGWhgdNMLEESPNMPWYKgwtketkagvvKGKTLLDAIDA-IEPPVRPSDKPLRLP 145
Cdd:COG0050  158 LSKYGFPGDDTPIIRGSAL---KALEGDPDPEWEK-----------KILELMDAVDSyIPEPERDTDKPFLMP 216
tufA CHL00071
elongation factor Tu
 1-147 2.83e-12

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 62.67  E-value: 2.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDttKWSEDRFNEIIK-ETSTFIKKVGY 79
Cdd:CHL00071  93 ITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKED--QVDDEELLELVElEVRELLSKYDF 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 649911186  80 NPKAVAFVPISGWHGDNMLEESPNmpwykgWTKETKAGVVKGKTLLDAIDA-IEPPVRPSDKPLRLPLQ 147
Cdd:CHL00071 164 PGDDIPIVSGSALLALEALTENPK------IKRGENKWVDKIYNLMDAVDSyIPTPERDTDKPFLMAIE 226
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-147 2.68e-11

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 59.96  E-value: 2.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIK-ETSTFIKK 76
Cdd:PRK12736  93 ITGAAQMDGAILVVA----------ATDGpmpQTREHILLARQVGVPYLVVFLNKVDLV--DDEELLELVEmEVRELLSE 160

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 649911186  77 VGYNPKAVAFVPISGWHGdnmLEESPnmPWYKgwtketkagvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQ 147
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKA---LEGDP--KWED-----------AIMELMDAVDEyIPTPERDTDKPFLMPVE 216
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-54 4.22e-10

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: 55.28  E-value: 4.22e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 649911186   1 ITGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMD 54
Cdd:cd01884   83 ITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKAD 129
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-145 2.92e-09

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 54.04  E-value: 2.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGtgefeagiskDG---QTREHALLAFTLGVRQLIVAVNKMDTtkwSEDRfnEIIK----ETSTF 73
Cdd:PRK00049  93 ITGAAQMDGAILVVSAA----------DGpmpQTREHILLARQVGVPYIVVFLNKCDM---VDDE--ELLElvemEVREL 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 649911186  74 IKKVGYNPKAVAFVPISGWHGdnmLEESPNMPWYKgwtketkagvvKGKTLLDAIDA-IEPPVRPSDKPLRLP 145
Cdd:PRK00049 158 LSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEK-----------KILELMDAVDSyIPTPERAIDKPFLMP 216
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-147 1.09e-08

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 52.52  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSE--DRFNEIIKETSTFIKKVG 78
Cdd:PLN03127 142 ITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEEllELVEMELRELLSFYKFPG 214

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186  79 YNPKAVAFVPISGWHGDNmleespnmpwykgwTKETKAGVVKgktLLDAIDAIEP-PVRPSDKPLRLPLQ 147
Cdd:PLN03127 215 DEIPIIRGSALSALQGTN--------------DEIGKNAILK---LMDAVDEYIPePVRVLDKPFLMPIE 267
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-147 3.54e-08

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 51.15  E-value: 3.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   1 ITGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKwSEDRFNEIIKETSTFIKKVGYN 80
Cdd:PLN03126 162 ITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD-DEELLELVELEVRELLSSYEFP 233

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 649911186  81 PKAVAFVPISGWHGDNMLEESPNMpwykgwTKETKAGVVKGKTLLDAIDAIEP-PVRPSDKPLRLPLQ 147
Cdd:PLN03126 234 GDDIPIISGSALLALEALMENPNI------KRGDNKWVDKIYELMDAVDSYIPiPQRQTDLPFLLAVE 295
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 8-145 9.25e-07

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: 46.83  E-value: 9.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   8 DCAILIIAggtgefeagiSKDG---QTREH-ALLAFtLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKkvGYNPKA 83
Cdd:COG3276   76 DLVLLVVA----------ADEGvmpQTREHlAILDL-LGIKRGIVVLTKADLV--DEEWLELVEEEIRELLA--GTFLED 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 649911186  84 VAFVPISGwhgdnmleespnmpwykgwtkETKAGVvkgKTLLDAIDAI--EPPVRPSDKPLRLP 145
Cdd:COG3276  141 APIVPVSA---------------------VTGEGI---DELRAALDALaaAVPARDADGPFRLP 180
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-87 6.00e-05

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: 41.78  E-value: 6.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186    1 ITGTSQADCAILIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKKV 77
Cdd:TIGR00475  68 IAGGGGIDAALLVVD----------ADEGvmtQTGEHLAVLDLLGIPHTIVVITKADRV--NEEEIKRTEMFMKQILNSY 135

                          90
                  ....*....|
gi 649911186   78 GYNPKAVAFV 87
Cdd:TIGR00475 136 IFLKNAKIFK 145
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-79 6.52e-05

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: 40.67  E-value: 6.52e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 649911186   1 ITGTSQADCAILIIAGgtgefEAGISKdgQTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKKVGY 79
Cdd:cd04171   68 LAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLV--DEDRLELVEEEILELLAGTFL 137
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 30-144 7.16e-04

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 38.29  E-value: 7.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186  30 QTREHaLLAFT-LGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKkvGYNPKAVAFVPISGWHGDNMleespnmpwyk 108
Cdd:PRK04000 126 QTKEH-LMALDiIGIKNIVIVQNKIDLV--SKERALENYEQIKEFVK--GTVAENAPIIPVSALHKVNI----------- 189

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 649911186 109 gwtketkagvvkgKTLLDAIDA-IEPPVRPSDKPLRL 144
Cdd:PRK04000 190 -------------DALIEAIEEeIPTPERDLDKPPRM 213
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 3-97 1.41e-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: 37.07  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649911186   3 GTSQADCAILIIAGGTGeFEAgiskdgQTRE---HALLAFTlgvrQLIVAVNKMDTTKWSE---DRFNEIIKETSTFIKK 76
Cdd:cd01887   69 GASVTDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVAINKIDKPYGTEadpERVKNELSELGLVGEE 137

                         90       100
                 ....*....|....*....|.
gi 649911186  77 VGynpKAVAFVPISGWHGDNM 97
Cdd:cd01887  138 WG---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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