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Conserved domains on  [gi|563427100|gb|AHB60095|]
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translation elongation factor 1-alpha, partial [Trametes sp. AJ354]

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 ...
 1-129 2.62e-65

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: 204.21  E-value: 2.62e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   1 CAILIIAAGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT-----KDRFNEIIKETSTFIKKVGYNPKAVAF 75
Cdd:PTZ00141 111 VAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKtvnysQERYDEIKKEVSAYLKKVGYNPEKVPF 190

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 563427100  76 VPISGWHGDNMLEESANMTWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 129
Cdd:PTZ00141 191 IPISGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDK 232
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-129 2.62e-65

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 204.21  E-value: 2.62e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   1 CAILIIAAGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT-----KDRFNEIIKETSTFIKKVGYNPKAVAF 75
Cdd:PTZ00141 111 VAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKtvnysQERYDEIKKEVSAYLKKVGYNPEKVPF 190

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 563427100  76 VPISGWHGDNMLEESANMTWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 129
Cdd:PTZ00141 191 IPISGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDK 232
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-124 1.66e-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: 195.02  E-value: 1.66e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   1 CAILIIAAGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT-----KDRFNEIIKETSTFIKKVGYNPKAVAF 75
Cdd:cd01883  103 VAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvnwsQERYDEIKKKVSPFLKKVGYNPKDVPF 182

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 563427100  76 VPISGWHGDNMLEESANMTWYKGWtketkagvvkgkTLLDAIDAIEPPV 124
Cdd:cd01883  183 IPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-129 2.87e-43

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: 146.62  E-value: 2.87e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   1 CAILIIAAGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDTTK---DRFNEIIKETSTFIKKVGYNPKAVAFVP 77
Cdd:COG5256  111 AAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNyseKRYEEVKEEVSKLLKMVGYKVDKIPFIP 183

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 563427100  78 ISGWHGDNMLEESANMTWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 129
Cdd:COG5256  184 VSAWKGDNVVKKSDNMPWY------------NGPTLLEALDNLKEPEKPVDK 223
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-123 7.82e-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: 85.27  E-value: 7.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100    1 CAILIIAAGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTKD-RFNEIIKETS-TFIKKVGYNPKAVAFVPI 78
Cdd:pfam00009  95 GAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRVDGaELEEVVEEVSrELLEKYGEDGEFVPVVPG 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 563427100   79 SGWHGDNMleesanmtwykgwtketkagvvkgKTLLDAIDAIEPP 123
Cdd:pfam00009 167 SALKGEGV------------------------QTLLDALDEYLPS 187
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 2-100 6.85e-19

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: 80.88  E-value: 6.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100    2 AILIIAAGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTT---KDRFNEIIKETSTFIKKVGynPKAVAFVPI 78
Cdd:TIGR02034 107 AVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVdydEEVFENIKKDYLAFAEQLG--FRDVTFIPL 177

                          90       100
                  ....*....|....*....|..
gi 563427100   79 SGWHGDNMLEESANMTWYKGWT 100
Cdd:TIGR02034 178 SALKGDNVVSRSESMPWYSGPT 199
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-129 2.62e-65

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 204.21  E-value: 2.62e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   1 CAILIIAAGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT-----KDRFNEIIKETSTFIKKVGYNPKAVAF 75
Cdd:PTZ00141 111 VAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKtvnysQERYDEIKKEVSAYLKKVGYNPEKVPF 190

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 563427100  76 VPISGWHGDNMLEESANMTWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 129
Cdd:PTZ00141 191 IPISGWQGDNMIEKSDNMPWY------------KGPTLLEALDTLEPPKRPVDK 232
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-124 1.66e-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: 195.02  E-value: 1.66e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   1 CAILIIAAGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT-----KDRFNEIIKETSTFIKKVGYNPKAVAF 75
Cdd:cd01883  103 VAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvnwsQERYDEIKKKVSPFLKKVGYNPKDVPF 182

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 563427100  76 VPISGWHGDNMLEESANMTWYKGWtketkagvvkgkTLLDAIDAIEPPV 124
Cdd:cd01883  183 IPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-129 2.55e-48

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 160.26  E-value: 2.55e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   1 CAILIIAAGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT-----KDRFNEIIKETSTFIKKVGYNPKAVAF 75
Cdd:PLN00043 111 CAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtpkysKARYDEIVKEVSSYLKKVGYNPDKIPF 190

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 563427100  76 VPISGWHGDNMLEESANMTWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 129
Cdd:PLN00043 191 VPISGFEGDNMIERSTNLDWY------------KGPTLLEALDQINEPKRPSDK 232
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-129 2.87e-43

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: 146.62  E-value: 2.87e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   1 CAILIIAAGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDTTK---DRFNEIIKETSTFIKKVGYNPKAVAFVP 77
Cdd:COG5256  111 AAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNyseKRYEEVKEEVSKLLKMVGYKVDKIPFIP 183

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 563427100  78 ISGWHGDNMLEESANMTWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 129
Cdd:COG5256  184 VSAWKGDNVVKKSDNMPWY------------NGPTLLEALDNLKEPEKPVDK 223
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 2-129 3.15e-42

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 143.91  E-value: 3.15e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   2 AILIIAAgtgefEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT---KDRFNEIIKETSTFIKKVGYNPKAVAFVPI 78
Cdd:PRK12317 111 AVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVnydEKRYEEVKEEVSKLLKMVGYKPDDIPFIPV 185

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 563427100  79 SGWHGDNMLEESANMTWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 129
Cdd:PRK12317 186 SAFEGDNVVKKSENMPWY------------NGPTLLEALDNLKPPEKPTDK 224
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 2-123 6.57e-28

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: 101.49  E-value: 6.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   2 AILIIAAGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTT---KDRFNEIIKETSTFIKKVGYNPkaVAFVPI 78
Cdd:cd04166  105 AILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVdydEEVFEEIKADYLAFAASLGIED--ITFIPI 175

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 563427100  79 SGWHGDNMLEESANMTWYkgwtketkagvvKGKTLLDAIDAIEPP 123
Cdd:cd04166  176 SALEGDNVVSRSENMPWY------------KGPTLLEHLETVEIA 208
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 2-129 1.91e-27

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: 104.40  E-value: 1.91e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   2 AILIIAAGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTT---KDRFNEIIKETSTFIKKVGYNPkaVAFVPI 78
Cdd:COG2895  122 AILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVdysEEVFEEIVADYRAFAAKLGLED--ITFIPI 192

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 563427100  79 SGWHGDNMLEESANMTWYkgwtketkagvvKGKTLLDAIDAIEPPVRPSDK 129
Cdd:COG2895  193 SALKGDNVVERSENMPWY------------DGPTLLEHLETVEVAEDRNDA 231
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 2-121 6.71e-24

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 94.98  E-value: 6.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   2 AILIIAAGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTT---KDRFNEIIKETSTFIKKVGYNPKaVAFVPI 78
Cdd:PRK05124 134 AILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVdysEEVFERIREDYLTFAEQLPGNLD-IRFVPL 205

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 563427100  79 SGWHGDNMLEESANMTWYkgwtketkagvvKGKTLLDAIDAIE 121
Cdd:PRK05124 206 SALEGDNVVSQSESMPWY------------SGPTLLEVLETVD 236
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-123 7.82e-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: 85.27  E-value: 7.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100    1 CAILIIAAGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTKD-RFNEIIKETS-TFIKKVGYNPKAVAFVPI 78
Cdd:pfam00009  95 GAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRVDGaELEEVVEEVSrELLEKYGEDGEFVPVVPG 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 563427100   79 SGWHGDNMleesanmtwykgwtketkagvvkgKTLLDAIDAIEPP 123
Cdd:pfam00009 167 SALKGEGV------------------------QTLLDALDEYLPS 187
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 22-98 4.05e-21

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 87.29  E-value: 4.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100  22 QTREHALLAFTLGVRQLIVAVNKMDT---TKDRFNEIIKETSTFIKKVGYNpkAVAFVPISGWHGDNMLEESANMTWYKG 98
Cdd:PRK05506 144 QTRRHSFIASLLGIRHVVLAVNKMDLvdyDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWYEG 221
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 2-100 6.85e-19

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: 80.88  E-value: 6.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100    2 AILIIAAGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTT---KDRFNEIIKETSTFIKKVGynPKAVAFVPI 78
Cdd:TIGR02034 107 AVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVdydEEVFENIKKDYLAFAEQLG--FRDVTFIPL 177

                          90       100
                  ....*....|....*....|..
gi 563427100   79 SGWHGDNMLEESANMTWYKGWT 100
Cdd:TIGR02034 178 SALKGDNVVSRSESMPWYSGPT 199
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-123 5.97e-14

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: 64.62  E-value: 5.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   1 CAILIIAAGTGEfeagiskDGQTREHALLAFtLGVRQLIVAVNKMDTT-KDRFNEIIKETSTFIKKVGY---NPKAVAFV 76
Cdd:cd00881   88 GALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRVgEEDFDEVLREIKELLKLIGFtflKGKDVPII 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 563427100  77 PISGWHGDNMLEesanmtwykgwtketkagvvkgktLLDAIDAIEPP 123
Cdd:cd00881  160 PISALTGEGIEE------------------------LLDAIVEHLPP 182
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 2-129 1.25e-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: 48.61  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   2 AILIIAAgtgefeagisKDG---QTREHALLAFTLGVRQLIVAVNKMDTTKDrfNEIIK----ETSTFIKKVGYNPKAVA 74
Cdd:COG0050  102 AILVVSA----------TDGpmpQTREHILLARQVGVPYIVVFLNKCDMVDD--EELLElvemEVRELLSKYGFPGDDTP 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 563427100  75 FVPISGWhgdNMLEESANMTWYKgwtketkagvvKGKTLLDAIDA-IEPPVRPSDK 129
Cdd:COG0050  170 IIRGSAL---KALEGDPDPEWEK-----------KILELMDAVDSyIPEPERDTDK 211
tufA CHL00071
elongation factor Tu
 2-129 7.98e-07

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 46.49  E-value: 7.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   2 AILIIAAGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKDrfNEII----KETSTFIKKVGYNPKAVAFVP 77
Cdd:CHL00071 102 AILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQVDD--EELLelveLEVRELLSKYDFPGDDIPIVS 172

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 563427100  78 ISGWHGDNMLEESANmtwykgWTKETKAGVVKGKTLLDAIDA-IEPPVRPSDK 129
Cdd:CHL00071 173 GSALLALEALTENPK------IKRGENKWVDKIYNLMDAVDSyIPTPERDTDK 219
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 2-123 1.33e-06

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 45.27  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   2 AILIIAAGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKDrfNEIIK----ETSTFIKKVGYNPKAVAFVP 77
Cdd:cd01884   92 AILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVDD--EELLElvemEVRELLSKYGFDGDDTPIVR 162

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 563427100  78 ISGWhgdNMLEEsanmtwykgwtKETKAGVVKGKTLLDAIDA-IEPP 123
Cdd:cd01884  163 GSAL---KALEG-----------DDPNKWVDKILELLDALDSyIPTP 195
PRK12736 PRK12736
elongation factor Tu; Reviewed
 2-129 3.24e-06

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 44.55  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   2 AILIIAAgtgefeagisKDG---QTREHALLAFTLGVRQLIVAVNKMDTTKDrfNEIIK----ETSTFIKKVGYNPKAVA 74
Cdd:PRK12736 102 AILVVAA----------TDGpmpQTREHILLARQVGVPYLVVFLNKVDLVDD--EELLElvemEVRELLSEYDFPGDDIP 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 563427100  75 FVPISGWHGdnmLEESanmtwyKGWTKETKAgvvkgktLLDAIDA-IEPPVRPSDK 129
Cdd:PRK12736 170 VIRGSALKA---LEGD------PKWEDAIME-------LMDAVDEyIPTPERDTDK 209
PRK00049 PRK00049
elongation factor Tu; Reviewed
 2-129 2.81e-05

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 42.10  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   2 AILIIAAGtgefeagiskDG---QTREHALLAFTLGVRQLIVAVNKMDTTKDRfnEIIK----ETSTFIKKVGYNPKAVA 74
Cdd:PRK00049 102 AILVVSAA----------DGpmpQTREHILLARQVGVPYIVVFLNKCDMVDDE--ELLElvemEVRELLSKYDFPGDDTP 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 563427100  75 FVPISGWHGdnmLEESANMTWYKgwtketkagvvKGKTLLDAIDA-IEPPVRPSDK 129
Cdd:PRK00049 170 IIRGSALKA---LEGDDDEEWEK-----------KILELMDAVDSyIPTPERAIDK 211
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 2-86 5.58e-05

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 40.99  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   2 AILIIAAGTGEFEAgiskdgQTREHaLLAFT-LGVRQLIVAVNKMDT-TKDRFNEIIKETSTFIKkvGYNPKAVAFVPIS 79
Cdd:PRK04000 112 AILVIAANEPCPQP------QTKEH-LMALDiIGIKNIVIVQNKIDLvSKERALENYEQIKEFVK--GTVAENAPIIPVS 182


                 ....*..
gi 563427100  80 GWHGDNM 86
Cdd:PRK04000 183 ALHKVNI 189
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 2-66 9.06e-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: 40.63  E-value: 9.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 563427100    2 AILIIAAgtgefeagisKDG---QTREHALLAFTLGVRQLIVAVNKMDTTKDrfnEIIKETSTFIKKV 66
Cdd:TIGR00475  77 ALLVVDA----------DEGvmtQTGEHLAVLDLLGIPHTIVVITKADRVNE---EEIKRTEMFMKQI 131
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 2-46 1.06e-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: 40.28  E-value: 1.06e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 563427100   2 AILIIAAgtgefeagisKDG---QTREH-ALLAFtLGVRQLIVAVNKMD 46
Cdd:COG3276   78 VLLVVAA----------DEGvmpQTREHlAILDL-LGIKRGIVVLTKAD 115
PLN03127 PLN03127
Elongation factor Tu; Provisional
 2-129 2.22e-04

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 39.42  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563427100   2 AILIIAAGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKDRfnEI-------IKETSTFIKKVGYNpkava 74
Cdd:PLN03127 151 GILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDE--ELlelvemeLRELLSFYKFPGDE----- 216

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 563427100  75 fVPIsgwhgdnmLEESAnMTWYKGWTKET-KAGVVKgktLLDAIDAIEP-PVRPSDK 129
Cdd:PLN03127 217 -IPI--------IRGSA-LSALQGTNDEIgKNAILK---LMDAVDEYIPePVRVLDK 260
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-68 3.59e-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: 3.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 563427100   1 CAILIIAAgtgefEAGISKdgQTREHALLAFTLGVRQLIVAVNKMDTT-KDRFNEIIKETSTFIKKVGY 68
Cdd:cd04171   76 AVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLVdEDRLELVEEEILELLAGTFL 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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