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Conserved domains on  [gi|1802564774|dbj|BBG82734|]
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translation elongation factor 1-alpha, partial [Sphaerocreas pubescens]

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 ...
 1-158 6.97e-101

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: 296.66  E-value: 6.97e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774   1 RYNEIVKEVSNYLKKIGYNPNTVPFVPISGWHGDNMLEPSTNMPWFKGwtketkagnatgKTLLEAIDAIEPPSRPTDKP 80
Cdd:PTZ00141  166 RYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKP 233

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802564774  81 LRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:PTZ00141  234 LRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRG 311
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-158 6.97e-101

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 296.66  E-value: 6.97e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774   1 RYNEIVKEVSNYLKKIGYNPNTVPFVPISGWHGDNMLEPSTNMPWFKGwtketkagnatgKTLLEAIDAIEPPSRPTDKP 80
Cdd:PTZ00141  166 RYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKP 233

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802564774  81 LRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:PTZ00141  234 LRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRG 311
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-158 8.04e-82

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 247.47  E-value: 8.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774   1 RYNEIVKEVSNYLKKIGYNPNTVPFVPISGWHGDNMLEPSTNMPWFKGwtketkagnatgKTLLEAIDAIEPPSRPTDKP 80
Cdd:TIGR00483 160 EFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKP 227

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802564774  81 LRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:TIGR00483 228 LRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRG 305
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-158 3.81e-78

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: 237.91  E-value: 3.81e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774   1 RYNEIVKEVSNYLKKIGYNPNTVPFVPISGWHGDNMLEPSTNMPWFKGwtketkagnatgKTLLEAIDAIEPPSRPTDKP 80
Cdd:COG5256   157 RYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDKP 224

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802564774  81 LRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:COG5256   225 LRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRG 302
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 77-158 5.43e-54

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: 165.44  E-value: 5.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774  77 TDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIR 156
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80


                  ..
gi 1802564774 157 RG 158
Cdd:cd03693    81 RG 82
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 95-158 9.19e-15

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 64.98  E-value: 9.19e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802564774  95 GTVPVGRVETGIIK*GMVVTFAPVG-----LSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGtgkkkIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVG 69
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-158 6.97e-101

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 296.66  E-value: 6.97e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774   1 RYNEIVKEVSNYLKKIGYNPNTVPFVPISGWHGDNMLEPSTNMPWFKGwtketkagnatgKTLLEAIDAIEPPSRPTDKP 80
Cdd:PTZ00141  166 RYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKP 233

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802564774  81 LRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:PTZ00141  234 LRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRG 311
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-158 8.04e-82

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 247.47  E-value: 8.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774   1 RYNEIVKEVSNYLKKIGYNPNTVPFVPISGWHGDNMLEPSTNMPWFKGwtketkagnatgKTLLEAIDAIEPPSRPTDKP 80
Cdd:TIGR00483 160 EFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKP 227

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802564774  81 LRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:TIGR00483 228 LRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRG 305
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-158 2.67e-79

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 240.98  E-value: 2.67e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774   1 RYNEIVKEVSNYLKKIGYNPNTVPFVPISGWHGDNMLEPSTNMPWFKGwtketkagnatgKTLLEAIDAIEPPSRPTDKP 80
Cdd:PRK12317  158 RYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNG------------PTLLEALDNLKPPEKPTDKP 225

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802564774  81 LRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:PRK12317  226 LRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRG 303
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-158 3.81e-78

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: 237.91  E-value: 3.81e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774   1 RYNEIVKEVSNYLKKIGYNPNTVPFVPISGWHGDNMLEPSTNMPWFKGwtketkagnatgKTLLEAIDAIEPPSRPTDKP 80
Cdd:COG5256   157 RYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDKP 224

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802564774  81 LRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:COG5256   225 LRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRG 302
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-158 1.05e-76

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 234.98  E-value: 1.05e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774   1 RYNEIVKEVSNYLKKIGYNPNTVPFVPISGWHGDNMLEPSTNMPWFKGwtketkagnatgKTLLEAIDAIEPPSRPTDKP 80
Cdd:PLN00043  166 RYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKRPSDKP 233

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802564774  81 LRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:PLN00043  234 LRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRG 311
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 77-158 5.43e-54

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: 165.44  E-value: 5.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774  77 TDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIR 156
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80


                  ..
gi 1802564774 157 RG 158
Cdd:cd03693    81 RG 82
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-145 8.22e-34

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: 122.89  E-value: 8.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774   1 RYNEIVKEVSNYLKKIGYNPNTvpFVPISGWHGDNMLEPSTNMPWFKgwtketkagnatGKTLLEAIDAIEPPSRPTDKP 80
Cdd:COG2895   167 VFEEIVADYRAFAAKLGLEDIT--FIPISALKGDNVVERSENMPWYD------------GPTLLEHLETVEVAEDRNDAP 232

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802564774  81 LRLPLQDVYKiggigtvP-------VGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGF 145
Cdd:COG2895   233 FRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTL 297
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-73 7.05e-32

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: 113.35  E-value: 7.05e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1802564774   1 RYNEIVKEVSNYLKKIGYNPNTVPFVPISGWHGDNMLEPSTNMPWFKGWtketkagnatgkTLLEAIDAIEPP 73
Cdd:cd01883   158 RYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
tufA CHL00071
elongation factor Tu
 4-158 3.89e-21

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 88.09  E-value: 3.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774   4 EIVK-EVSNYLKKIGYNPNTVPFVPISGWHG-DNMLEPSTNMPWFKGWTKETKagnatgkTLLEAIDA-IEPPSRPTDKP 80
Cdd:CHL00071  148 ELVElEVRELLSKYDFPGDDIPIVSGSALLAlEALTENPKIKRGENKWVDKIY-------NLMDAVDSyIPTPERDTDKP 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774  81 LRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFapVGL----STEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIR 156
Cdd:CHL00071  221 FLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEI--VGLretkTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIE 298


                  ..
gi 1802564774 157 RG 158
Cdd:CHL00071  299 RG 300
PRK00049 PRK00049
elongation factor Tu; Reviewed
 63-158 4.97e-21

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 87.55  E-value: 4.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774  63 LLEAIDA-IEPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFapVGL----STEVKSVEMHHEQLTEG 137
Cdd:PRK00049  194 LMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEI--VGIrdtqKTTVTGVEMFRKLLDEG 271

                          90       100
                  ....*....|....*....|.
gi 1802564774 138 VPGDNVGFNVKNVSVKEIRRG 158
Cdd:PRK00049  272 QAGDNVGALLRGIKREDVERG 292
PRK12735 PRK12735
elongation factor Tu; Reviewed
 63-158 1.10e-20

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 86.82  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774  63 LLEAIDA-IEPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFapVGLS----TEVKSVEMHHEQLTEG 137
Cdd:PRK12735  194 LMDAVDSyIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEI--VGIKetqkTTVTGVEMFRKLLDEG 271

                          90       100
                  ....*....|....*....|.
gi 1802564774 138 VPGDNVGFNVKNVSVKEIRRG 158
Cdd:PRK12735  272 QAGDNVGVLLRGTKREDVERG 292
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 63-158 1.29e-19

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: 83.66  E-value: 1.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774  63 LLEAIDA-IEPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFapVGL----STEVKSVEMHHEQLTEG 137
Cdd:COG0050   194 LMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEI--VGIrdtqKTVVTGVEMFRKLLDEG 271

                          90       100
                  ....*....|....*....|.
gi 1802564774 138 VPGDNVGFNVKNVSVKEIRRG 158
Cdd:COG0050   272 EAGDNVGLLLRGIKREDVERG 292
PLN03127 PLN03127
Elongation factor Tu; Provisional
 63-158 5.61e-19

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 82.18  E-value: 5.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774  63 LLEAIDAIEP-PSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK*G---MVVTFAPVG-LSTEVKSVEMHHEQLTEG 137
Cdd:PLN03127  243 LMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPGGpLKTTVTGVEMFKKILDQG 322

                          90       100
                  ....*....|....*....|.
gi 1802564774 138 VPGDNVGFNVKNVSVKEIRRG 158
Cdd:PLN03127  323 QAGDNVGLLLRGLKREDVQRG 343
PRK12736 PRK12736
elongation factor Tu; Reviewed
 63-158 6.44e-19

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 81.91  E-value: 6.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774  63 LLEAIDA-IEPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFapVGLSTEVKS----VEMHHEQLTEG 137
Cdd:PRK12736  192 LMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEI--VGIKETQKTvvtgVEMFRKLLDEG 269

                          90       100
                  ....*....|....*....|.
gi 1802564774 138 VPGDNVGFNVKNVSVKEIRRG 158
Cdd:PRK12736  270 QAGDNVGVLLRGVDRDEVERG 290
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 81-158 1.19e-18

Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 75.38  E-value: 1.19e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802564774  81 LRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNvsVKEIRRG 158
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTG 76
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 63-158 3.68e-18

translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. 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. [Protein synthesis, Translation factors]


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 79.82  E-value: 3.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774  63 LLEAIDA-IEPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFapVGL----STEVKSVEMHHEQLTEG 137
Cdd:TIGR00485 192 LMDAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEI--VGLkdtrKTTVTGVEMFRKELDEG 269

                          90       100
                  ....*....|....*....|.
gi 1802564774 138 VPGDNVGFNVKNVSVKEIRRG 158
Cdd:TIGR00485 270 RAGDNVGLLLRGIKREEIERG 290
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-143 1.40e-17

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 78.43  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774   1 RYNEIVKEVSNYLKKIGYNpnTVPFVPISGWHGDNMLEPSTNMPWFkgwtketkagnaTGKTLLEAIDAIEPPSRPTDKP 80
Cdd:PRK05506  176 VFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWY------------EGPSLLEHLETVEIASDRNLKD 241

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802564774  81 LRLPLQDVYKI-----GGIGTvpvgrVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNV 143
Cdd:PRK05506  242 FRFPVQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAV 304
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 83-158 3.97e-17

Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 71.40  E-value: 3.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774  83 LPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFapVGLSTEVKSV----EMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:cd03697     3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEI--VGFKETLKTTvtgiEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 81-158 5.19e-17

Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. 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' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 71.02  E-value: 5.19e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802564774  81 LRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
PLN03126 PLN03126
Elongation factor Tu; Provisional
 63-158 2.61e-16

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 74.65  E-value: 2.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774  63 LLEAIDAIEP-PSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFapVGL----STEVKSVEMHHEQLTEG 137
Cdd:PLN03126  271 LMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDI--VGLretrSTTVTGVEMFQKILDEA 348

                          90       100
                  ....*....|....*....|.
gi 1802564774 138 VPGDNVGFNVKNVSVKEIRRG 158
Cdd:PLN03126  349 LAGDNVGLLLRGIQKADIQRG 369
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-143 2.82e-16

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: 74.33  E-value: 2.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774   1 RYNEIVKEVSNYLKKIGynPNTVPFVPISGWHGDNMLEPSTNMPWFkgwtketkagnaTGKTLLEAIDAIEPPSRPTDKP 80
Cdd:TIGR02034 152 VFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEVERDAQDLP 217

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802564774  81 LRLPLQDVYKI-----GGIGTVPVGRVETgiik*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNV 143
Cdd:TIGR02034 218 LRFPVQYVNRPnldfrGYAGTIASGSVHV-----GDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAV 280
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-143 3.17e-15

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 71.48  E-value: 3.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774   1 RYNEIVKEVSNYLKKIGYNPNtVPFVPISGWHGDNMLEPSTNMPWFKgwtketkagnatGKTLLEAIDAIEPPSRPTDKP 80
Cdd:PRK05124  179 VFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWYS------------GPTLLEVLETVDIQRVVDAQP 245

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802564774  81 LRLPLQDVYKI-----GGIGTvpvgrVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNV 143
Cdd:PRK05124  246 FRFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAI 308
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 63-158 3.64e-15

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: 71.48  E-value: 3.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774  63 LLEAIDAI--EPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPG 140
Cdd:COG3276   157 LRAALDALaaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAG 236

                          90
                  ....*....|....*...
gi 1802564774 141 DNVGFNVKNVSVKEIRRG 158
Cdd:COG3276   237 QRVALNLAGVEKEEIERG 254
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 95-158 9.19e-15

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 64.98  E-value: 9.19e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802564774  95 GTVPVGRVETGIIK*GMVVTFAPVG-----LSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGtgkkkIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVG 69
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-74 1.17e-13

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: 65.28  E-value: 1.17e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802564774   1 RYNEIVKEVSNYLKKIGYNPntVPFVPISGWHGDNMLEPSTNMPWFKgwtketkagnatGKTLLEAIDAIEPPS 74
Cdd:cd04166   150 VFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETVEIAS 209
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 80-158 3.66e-13

Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.


Pssm-ID: 293912 [Multi-domain]  Cd Length: 84  Bit Score: 60.99  E-value: 3.66e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802564774  80 PLRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVG 79
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 80-158 3.84e-10

Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 293906 [Multi-domain]  Cd Length: 82  Bit Score: 53.26  E-value: 3.84e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802564774  80 PLRLPLQDVYKigGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPG 77
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 80-158 1.54e-09

Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation 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: 293899 [Multi-domain]  Cd Length: 84  Bit Score: 51.73  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802564774  80 PLRLPLQDVYKiGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMH-HEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 87-158 4.76e-09

Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 50.68  E-value: 4.76e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802564774  87 DVYKIGGIGTVPVGRVETGIIK*GMVVTFAP--VG--LSTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRG 158
Cdd:cd03694     7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPdaDGkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKG 82
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 81-145 1.20e-08

Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 49.10  E-value: 1.20e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1802564774  81 LRLPLQDVYKIGGIGTVPVGRVETGIIK*GMVVTFAPVGLSTEVKSVEMHHEQLTEGVPGDNVGF 145
Cdd:cd03695     1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-73 3.44e-07

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: 47.52  E-value: 3.44e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802564774   1 RYNEIVKEVSN-YLKKIGYNPNTVPFVPISGWHGDNMlepstnmpwfkgwtketkagnatgKTLLEAIDAIEPP 73
Cdd:pfam00009 138 ELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGV------------------------QTLLDALDEYLPS 187
 
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.
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