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Conserved domains on  [gi|924919400|gb|ALC78216|]
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elongation factor 1 alpha, partial [Meriderma carestiae]

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 ...
 1-155 2.90e-118

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: 340.96  E-value: 2.90e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400   1 CGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQAD 80
Cdd:PTZ00141  31 CGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQAD 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 924919400  81 AAVLVIASPTGEFEAGIAKSGQTREHALLAYTLGVKQMIVAINKMDEKSVNWSQDRYNEIVKETSSFVKKIGYNP 155
Cdd:PTZ00141 111 VAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNP 185
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-155 2.90e-118

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 340.96  E-value: 2.90e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400   1 CGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQAD 80
Cdd:PTZ00141  31 CGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQAD 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 924919400  81 AAVLVIASPTGEFEAGIAKSGQTREHALLAYTLGVKQMIVAINKMDEKSVNWSQDRYNEIVKETSSFVKKIGYNP 155
Cdd:PTZ00141 111 VAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNP 185
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-155 6.52e-114

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: 321.36  E-value: 6.52e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400   1 CGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQAD 80
Cdd:cd01883   23 LGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQAD 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 924919400  81 AAVLVIASPTGEFEAGIAKSGQTREHALLAYTLGVKQMIVAINKMDEKSVNWSQDRYNEIVKETSSFVKKIGYNP 155
Cdd:cd01883  103 VAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNP 177
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 2-155 7.98e-85

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: 254.86  E-value: 7.98e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400   2 GGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADA 81
Cdd:COG5256   32 GAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADA 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 924919400  82 AVLVIASPTGEfeagiakSGQTREHALLAYTLGVKQMIVAINKMDekSVNWSQDRYNEIVKETSSFVKKIGYNP 155
Cdd:COG5256  112 AILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMD--AVNYSEKRYEEVKEEVSKLLKMVGYKV 176
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-155 2.81e-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: 248.62  E-value: 2.81e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400    1 CGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQAD 80
Cdd:TIGR00483  31 CGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQAD 110

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 924919400   81 AAVLVIASPTGEFEagiaKSGQTREHALLAYTLGVKQMIVAINKMDekSVNWSQDRYNEIVKETSSFVKKIGYNP 155
Cdd:TIGR00483 111 AAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMD--SVNYDEEEFEAIKKEVSNLIKKVGYNP 179
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-155 3.56e-51

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: 161.54  E-value: 3.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400    1 CGGIDKRTIEKFEKEAaemgkgsfkyawVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQAD 80
Cdd:pfam00009  27 TGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQAD 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 924919400   81 AAVLVIASPTGefeagiaKSGQTREHALLAYTLGVKqMIVAINKMDEKsvnwSQDRYNEIVKETSS-FVKKIGYNP 155
Cdd:pfam00009  95 GAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DGAELEEVVEEVSReLLEKYGEDG 158
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-155 2.90e-118

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 340.96  E-value: 2.90e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400   1 CGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQAD 80
Cdd:PTZ00141  31 CGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQAD 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 924919400  81 AAVLVIASPTGEFEAGIAKSGQTREHALLAYTLGVKQMIVAINKMDEKSVNWSQDRYNEIVKETSSFVKKIGYNP 155
Cdd:PTZ00141 111 VAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNP 185
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-155 6.52e-114

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: 321.36  E-value: 6.52e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400   1 CGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQAD 80
Cdd:cd01883   23 LGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQAD 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 924919400  81 AAVLVIASPTGEFEAGIAKSGQTREHALLAYTLGVKQMIVAINKMDEKSVNWSQDRYNEIVKETSSFVKKIGYNP 155
Cdd:cd01883  103 VAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNP 177
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 2-155 7.98e-85

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: 254.86  E-value: 7.98e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400   2 GGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADA 81
Cdd:COG5256   32 GAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADA 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 924919400  82 AVLVIASPTGEfeagiakSGQTREHALLAYTLGVKQMIVAINKMDekSVNWSQDRYNEIVKETSSFVKKIGYNP 155
Cdd:COG5256  112 AILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMD--AVNYSEKRYEEVKEEVSKLLKMVGYKV 176
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 2-155 1.43e-84

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 254.08  E-value: 1.43e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400   2 GGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADA 81
Cdd:PRK12317  31 GAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIVDCPGHRDFVKNMITGASQADA 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 924919400  82 AVLVIASPTGEfeaGIAksGQTREHALLAYTLGVKQMIVAINKMDekSVNWSQDRYNEIVKETSSFVKKIGYNP 155
Cdd:PRK12317 111 AVLVVAADDAG---GVM--PQTREHVFLARTLGINQLIVAINKMD--AVNYDEKRYEEVKEEVSKLLKMVGYKP 177
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 2-155 1.49e-83

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 252.32  E-value: 1.49e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400   2 GGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADA 81
Cdd:PLN00043  32 GGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADC 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 924919400  82 AVLVIASPTGEFEAGIAKSGQTREHALLAYTLGVKQMIVAINKMDEKSVNWSQDRYNEIVKETSSFVKKIGYNP 155
Cdd:PLN00043 112 AVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNP 185
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-155 2.81e-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: 248.62  E-value: 2.81e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400    1 CGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQAD 80
Cdd:TIGR00483  31 CGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQAD 110

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 924919400   81 AAVLVIASPTGEFEagiaKSGQTREHALLAYTLGVKQMIVAINKMDekSVNWSQDRYNEIVKETSSFVKKIGYNP 155
Cdd:TIGR00483 111 AAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMD--SVNYDEEEFEAIKKEVSNLIKKVGYNP 179
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-155 3.56e-51

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: 161.54  E-value: 3.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400    1 CGGIDKRTIEKFEKEAaemgkgsfkyawVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQAD 80
Cdd:pfam00009  27 TGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQAD 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 924919400   81 AAVLVIASPTGefeagiaKSGQTREHALLAYTLGVKqMIVAINKMDEKsvnwSQDRYNEIVKETSS-FVKKIGYNP 155
Cdd:pfam00009  95 GAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DGAELEEVVEEVSReLLEKYGEDG 158
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 9-155 1.17e-43

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: 148.70  E-value: 1.17e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400   9 IEKFEKEAAEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKY-YItIIDAPGHRDFIKNMITGTSQADAAVLVIA 87
Cdd:COG2895   49 LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPKRkFI-IADTPGHEQYTRNMVTGASTADLAILLID 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 924919400  88 sptgefeagiAKSG---QTREHALLAYTLGVKQMIVAINKMDekSVNWSQDRYNEIVKETSSFVKKIGYNP 155
Cdd:COG2895  128 ----------ARKGvleQTRRHSYIASLLGIRHVVVAVNKMD--LVDYSEEVFEEIVADYRAFAAKLGLED 186
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 8-155 7.92e-43

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: 140.78  E-value: 7.92e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400   8 TIEKFEKEAAEMGKgsFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIA 87
Cdd:cd04166   33 ALERSKSSGTQGEK--LDLALLVDGLQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLVD 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 924919400  88 SPTGEFEagiaksgQTREHALLAYTLGVKQMIVAINKMDekSVNWSQDRYNEIVKETSSFVKKIGYNP 155
Cdd:cd04166  111 ARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMD--LVDYDEEVFEEIKADYLAFAASLGIED 169
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 28-154 5.97e-36

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: 122.40  E-value: 5.97e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  28 WVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGEfeagiakSGQTREHA 107
Cdd:cd00881   35 TFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHL 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 924919400 108 LLAyTLGVKQMIVAINKMDEKsvnwSQDRYNEIVKETSSFVKKIGYN 154
Cdd:cd00881  108 NIA-LAGGLPIIVAVNKIDRV----GEEDFDEVLREIKELLKLIGFT 149
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 26-155 3.70e-34

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 124.26  E-value: 3.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  26 YAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGEFEagiaksgQTRE 105
Cdd:PRK05124  78 LALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRR 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 924919400 106 HALLAYTLGVKQMIVAINKMDekSVNWSQDRYNEIVKETSSFVKKIGYNP 155
Cdd:PRK05124 151 HSFIATLLGIKHLVVAVNKMD--LVDYSEEVFERIREDYLTFAEQLPGNL 198
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 22-152 1.56e-32

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 120.80  E-value: 1.56e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  22 GSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGEFEagiaksg 101
Cdd:PRK05506  71 DEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT------- 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 924919400 102 QTREHALLAYTLGVKQMIVAINKMDekSVNWSQDRYNEIVKETSSFVKKIG 152
Cdd:PRK05506 144 QTRRHSFIASLLGIRHVVLAVNKMD--LVDYDQEVFDEIVADYRAFAAKLG 192
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 22-152 2.61e-30

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: 112.85  E-value: 2.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400   22 GSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGEFEagiaksg 101
Cdd:TIGR02034  47 GEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE------- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 924919400  102 QTREHALLAYTLGVKQMIVAINKMDekSVNWSQDRYNEIVKETSSFVKKIG 152
Cdd:TIGR02034 120 QTRRHSYIASLLGIRHVVLAVNKMD--LVDYDEEVFENIKKDYLAFAEQLG 168
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 17-126 8.59e-30

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: 106.90  E-value: 8.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  17 AEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGEFEag 96
Cdd:cd01884   27 AKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-- 104

                         90       100       110
                 ....*....|....*....|....*....|
gi 924919400  97 iaksgQTREHALLAYTLGVKQMIVAINKMD 126
Cdd:cd01884  105 -----QTREHLLLARQVGVPYIVVFLNKAD 129
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 17-126 1.79e-29

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: 110.63  E-value: 1.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  17 AEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGEFEag 96
Cdd:COG0050   37 AKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-- 114

                         90       100       110
                 ....*....|....*....|....*....|
gi 924919400  97 iaksgQTREHALLAYTLGVKQMIVAINKMD 126
Cdd:COG0050  115 -----QTREHILLARQVGVPYIVVFLNKCD 139
PRK12736 PRK12736
elongation factor Tu; Reviewed
 14-126 9.15e-28

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 105.80  E-value: 9.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  14 KEAAEMGKGSFK-YAWVlDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGE 92
Cdd:PRK12736  34 KVLAERGLNQAKdYDSI-DAAPEEKERGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGP 112

                         90       100       110
                 ....*....|....*....|....*....|....
gi 924919400  93 FEagiaksgQTREHALLAYTLGVKQMIVAINKMD 126
Cdd:PRK12736 113 MP-------QTREHILLARQVGVPYLVVFLNKVD 139
PRK00049 PRK00049
elongation factor Tu; Reviewed
 17-126 7.05e-27

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 103.73  E-value: 7.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  17 AEMGKGSFK-YAWVlDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGEFEa 95
Cdd:PRK00049  37 AKKGGAEAKaYDQI-DKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP- 114

                         90       100       110
                 ....*....|....*....|....*....|.
gi 924919400  96 giaksgQTREHALLAYTLGVKQMIVAINKMD 126
Cdd:PRK00049 115 ------QTREHILLARQVGVPYIVVFLNKCD 139
PRK12735 PRK12735
elongation factor Tu; Reviewed
 14-126 5.25e-25

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 98.37  E-value: 5.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  14 KEAAEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGEF 93
Cdd:PRK12735  34 KVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPM 113

                         90       100       110
                 ....*....|....*....|....*....|...
gi 924919400  94 EagiaksgQTREHALLAYTLGVKQMIVAINKMD 126
Cdd:PRK12735 114 P-------QTREHILLARQVGVPYIVVFLNKCD 139
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 31-126 2.95e-24

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: 92.28  E-value: 2.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  31 DKLKSERERGITIDI--ALWKFETGKYyITIIDAPGHRDFIKNMITGTSQADAAVLVIASptgefEAGIAKsgQTREHAL 108
Cdd:cd04171   25 DRLPEEKKRGITIDLgfAYLDLPDGKR-LGFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLE 96

                         90
                 ....*....|....*...
gi 924919400 109 LAYTLGVKQMIVAINKMD 126
Cdd:cd04171   97 ILELLGIKKGLVVLTKAD 114
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 31-126 3.43e-24

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: 97.29  E-value: 3.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  31 DKLKSERERGITIDI--ALWKFETGKYyITIIDAPGHRDFIKNMITGTSQADAAVLVIAsptgefeagiAKSG---QTRE 105
Cdd:COG3276   26 DRLKEEKKRGITIDLgfAYLPLPDGRR-LGFVDVPGHEKFIKNMLAGAGGIDLVLLVVA----------ADEGvmpQTRE 94

                         90       100
                 ....*....|....*....|..
gi 924919400 106 H-ALLAyTLGVKQMIVAINKMD 126
Cdd:COG3276   95 HlAILD-LLGIKRGIVVLTKAD 115
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 17-126 8.04e-24

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: 95.23  E-value: 8.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400   17 AEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGEFEag 96
Cdd:TIGR00485  37 AKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-- 114

                          90       100       110
                  ....*....|....*....|....*....|
gi 924919400   97 iaksgQTREHALLAYTLGVKQMIVAINKMD 126
Cdd:TIGR00485 115 -----QTREHILLARQVGVPYIVVFLNKCD 139
PLN03127 PLN03127
Elongation factor Tu; Provisional
 30-126 2.28e-23

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 94.51  E-value: 2.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  30 LDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGEFEagiaksgQTREHALL 109
Cdd:PLN03127  99 IDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILL 171

                         90
                 ....*....|....*..
gi 924919400 110 AYTLGVKQMIVAINKMD 126
Cdd:PLN03127 172 ARQVGVPSLVVFLNKVD 188
PLN03126 PLN03126
Elongation factor Tu; Provisional
 17-127 7.24e-23

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 93.14  E-value: 7.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  17 AEMGKGSFKYAWVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGEFEag 96
Cdd:PLN03126 106 ASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-- 183

                         90       100       110
                 ....*....|....*....|....*....|.
gi 924919400  97 iaksgQTREHALLAYTLGVKQMIVAINKMDE 127
Cdd:PLN03126 184 -----QTKEHILLAKQVGVPNMVVFLNKQDQ 209
tufA CHL00071
elongation factor Tu
 16-126 2.24e-22

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 91.56  E-value: 2.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  16 AAEMGKGSFKYAWVlDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGEFEa 95
Cdd:CHL00071  37 AAKGGAKAKKYDEI-DSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP- 114

                         90       100       110
                 ....*....|....*....|....*....|.
gi 924919400  96 giaksgQTREHALLAYTLGVKQMIVAINKMD 126
Cdd:CHL00071 115 ------QTKEHILLAKQVGVPNIVVFLNKED 139
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 31-151 5.02e-21

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: 88.39  E-value: 5.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400   31 DKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASptgefEAGIAKsgQTREHALLA 110
Cdd:TIGR00475  26 DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDA-----DEGVMT--QTGEHLAVL 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 924919400  111 YTLGVKQMIVAINKMDEksVNwsqdryNEIVKETSSFVKKI 151
Cdd:TIGR00475  99 DLLGIPHTIVVITKADR--VN------EEEIKRTEMFMKQI 131
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 30-126 2.88e-14

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 eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 66.62  E-value: 2.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  30 LDKLKSERERGITIDIALWKFETGK--------------YYITIIDAPGHRDFIKNMITGTSQADAAVLVIAsptgefea 95
Cdd:cd01889   29 FDKNPQSQERGITLDLGFSSFEVDKpkhlednenpqienYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVD-------- 100

                         90       100       110
                 ....*....|....*....|....*....|....
gi 924919400  96 giAKSG---QTREHALLAYTLGvKQMIVAINKMD 126
Cdd:cd01889  101 --AKKGiqtQTAECLVIGELLC-KPLIVVLNKID 131
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 31-126 1.38e-13

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 67.00  E-value: 1.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  31 DKLKSERERGITIDI--ALWKFETGKYyITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGEFeagiaksGQTREH-A 107
Cdd:PRK10512  26 DRLPEEKKRGMTIDLgyAYWPQPDGRV-LGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHlA 97

                         90
                 ....*....|....*....
gi 924919400 108 LLAYTlGVKQMIVAINKMD 126
Cdd:PRK10512  98 ILQLT-GNPMLTVALTKAD 115
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 20-149 2.06e-12

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 63.33  E-value: 2.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  20 GKGSFKYA----WVlDKLKSERERGITI-----DIALWKFETGK---YYIT------------------IIDAPGHRDFI 69
Cdd:PRK04000  21 GKTTLVQAltgvWT-DRHSEELKRGITIrlgyaDATIRKCPDCEepeAYTTepkcpncgsetellrrvsFVDAPGHETLM 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  70 KNMITGTSQADAAVLVIAS------PtgefeagiaksgQTREHALLAYTLGVKQMIVAINKMDEKSVNWSQDRYNEIVKe 143
Cdd:PRK04000 100 ATMLSGAALMDGAILVIAAnepcpqP------------QTKEHLMALDIIGIKNIVIVQNKIDLVSKERALENYEQIKE- 166


                 ....*.
gi 924919400 144 tssFVK 149
Cdd:PRK04000 167 ---FVK 169
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 20-149 3.14e-12

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 61.13  E-value: 3.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  20 GKGSFKYA----WVlDKLKSERERGITI-----DIALWKFETGKYY----------------------ITIIDAPGHRDF 68
Cdd:cd01888   12 GKTTLVKAlsgvWT-VRHKEELKRNITIklgyaNAKIYKCPNCGCPrpydtpececpgcggetklvrhVSFVDCPGHEIL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  69 IKNMITGTSQADAAVLVIAS------PtgefeagiaksgQTREHALLAYTLGVKQMIVAINKMDEKSVNWSQDRYNEIVK 142
Cdd:cd01888   91 MATMLSGAAVMDGALLLIAAnepcpqP------------QTSEHLAALEIMGLKHIIILQNKIDLVKEEQALENYEQIKE 158


                 ....*..
gi 924919400 143 etssFVK 149
Cdd:cd01888  159 ----FVK 161
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 30-146 6.04e-12

Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.


Pssm-ID: 206731 [Multi-domain]  Cd Length: 237  Bit Score: 61.10  E-value: 6.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  30 LDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIAsptgefeagiAKSG---QTRE- 105
Cdd:cd04168   39 TDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVIS----------AVEGvqaQTRIl 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 924919400 106 -HALLAYTLGVkqmIVAINKMDEKSVNwSQDRYNEIVKETSS 146
Cdd:cd04168  109 fRLLRKLNIPT---IIFVNKIDRAGAD-LEKVYQEIKEKLSP 146
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
36-126 2.84e-10

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 57.44  E-value: 2.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  36 ERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASptgefEAGIAksGQTRehALLAYT--L 113
Cdd:PRK12740  41 ERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERALRVLDGAVVVVCA-----VGGVE--PQTE--TVWRQAekY 111

                         90
                 ....*....|...
gi 924919400 114 GVKQMIVaINKMD 126
Cdd:PRK12740 112 GVPRIIF-VNKMD 123
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 29-126 8.03e-10

LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.


Pssm-ID: 206677 [Multi-domain]  Cd Length: 179  Bit Score: 54.46  E-value: 8.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  29 VLDKLKSERERGITID---IAL-WKFETGKYYI-TIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGeFEAgiaksgQT 103
Cdd:cd01890   36 VLDSMDLERERGITIKaqaVRLfYKAKDGEEYLlNLIDTPGHVDFSYEVSRSLAACEGALLVVDATQG-VEA------QT 108

                         90       100
                 ....*....|....*....|...
gi 924919400 104 REHALLAYTLGVKqMIVAINKMD 126
Cdd:cd01890  109 LANFYLALENNLE-IIPVINKID 130
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 29-126 6.07e-09

Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 53.51  E-value: 6.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  29 VLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIAsptgefeagiAKSG---QTrE 105
Cdd:COG0480   48 VMDWMPEEQERGITITSAATTCEWKGHKINIIDTPGHVDFTGEVERSLRVLDGAVVVFD----------AVAGvepQT-E 116

                         90       100
                 ....*....|....*....|....*...
gi 924919400 106 HALlaytlgvKQM-------IVAINKMD 126
Cdd:COG0480  117 TVW-------RQAdkygvprIVFVNKMD 137
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 29-132 1.35e-08

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 52.21  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  29 VLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIasptgEFEAGIAksGQTREHAL 108
Cdd:cd04170   38 VSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGETLSALRAVDAALIVV-----EAQSGVE--VGTEKVWE 110

                         90       100
                 ....*....|....*....|....
gi 924919400 109 LAYTLGVKQMIVaINKMDEKSVNW 132
Cdd:cd04170  111 FLDDAKLPRIIF-INKMDRARADF 133
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 30-126 3.11e-08

Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.


Pssm-ID: 206730 [Multi-domain]  Cd Length: 213  Bit Score: 50.73  E-value: 3.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  30 LDKLKSERERGITI-----DIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIasptgefEAGIAKSGQTR 104
Cdd:cd04167   41 TDTRKDEQERGISIksnpiSLVLEDSKGKSYLINIIDTPGHVNFMDEVAAALRLCDGVVLVV-------DVVEGLTSVTE 113

                         90       100
                 ....*....|....*....|....*
gi 924919400 105 E---HALLaytLGVKqMIVAINKMD 126
Cdd:cd04167  114 RlirHAIQ---EGLP-MVLVINKID 134
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 29-144 3.41e-08

Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.


Pssm-ID: 206678 [Multi-domain]  Cd Length: 194  Bit Score: 50.28  E-value: 3.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  29 VLDKLKSERERGITIdiaLWKfETGKYY----ITIIDAPGHRDF------IKNMitgtsqADAAVLVIASPTGEFEagia 98
Cdd:cd01891   39 VMDSNDLERERGITI---LAK-NTAITYkdtkINIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP---- 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 924919400  99 ksgQTR---EHALLAytlGVKqMIVAINKMDEKSVnwsqdRYNEIVKET 144
Cdd:cd01891  105 ---QTRfvlKKALEA---GLK-PIVVINKIDRPDA-----RPEEVVDEV 141
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 30-152 3.89e-08

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: 49.78  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  30 LDKLKS----ERE-RGITIDIalwkfetGKYY---------ITIIDAPGHRDFiKNMIT-GTSQADAAVLVIASPTGeFE 94
Cdd:cd01887   17 LDKIRKtnvaAGEaGGITQHI-------GAYQvpidvkipgITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VM 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 924919400  95 AgiaksgQTRE---HALLAYTlgvkQMIVAINKMDEKS-VNWSQDRYNEIVKETSSFVKKIG 152
Cdd:cd01887   88 P------QTIEainHAKAANV----PIIVAINKIDKPYgTEADPERVKNELSELGLVGEEWG 139
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 36-126 7.65e-08

Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 50.40  E-value: 7.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  36 ERERGITIdiaLWK---FETGKYYITIIDAPGHRDF------IKNMitgtsqADAAVLVIASptgeFEagiaksG---QT 103
Cdd:COG1217   50 ERERGITI---LAKntaVRYKGVKINIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQT 110

                         90       100
                 ....*....|....*....|....*.
gi 924919400 104 R---EHALlayTLGVKqMIVAINKMD 126
Cdd:COG1217  111 RfvlKKAL---ELGLK-PIVVINKID 132
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
 20-126 1.18e-07

Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.


Pssm-ID: 206732 [Multi-domain]  Cd Length: 268  Bit Score: 49.52  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  20 GKGSFKYAwVLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGeFEAgiak 99
Cdd:cd04169   37 ARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG-VEP---- 110

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 924919400 100 sgQTRehallaytlgvKQMIVA----------INKMD 126
Cdd:cd04169  111 --QTR-----------KLFEVCrlrgipiitfINKLD 134
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 29-143 1.21e-07

Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.


Pssm-ID: 206672 [Multi-domain]  Cd Length: 218  Bit Score: 49.15  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  29 VLDKLKSERERGITID---IALwKFETGK-------YYITIIDAPGHRDFIKNMITGTSQADAAVLVIasptgEFEAGIA 98
Cdd:cd01885   37 YLDTREDEQERGITIKssaISL-YFEYEEekmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVV-----DAVEGVC 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 924919400  99 KsgQTreHALL--AYTLGVKqMIVAINKMD----EK--SVNWSQDRYNEIVKE 143
Cdd:cd01885  111 V--QT--ETVLrqALEERVK-PVLVINKIDrlilELklSPEEAYQRLLRIVED 158
PRK13351 PRK13351
elongation factor G-like protein;
29-126 1.63e-07

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 49.18  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  29 VLDKLKSERERGITIDIAL----WKfetgKYYITIIDAPGHRDFIKNMITGTSQADAAVLViasptgeFEAGIAKSGQTR 104
Cdd:PRK13351  47 VTDWMPQEQERGITIESAAtscdWD----NHRINLIDTPGHIDFTGEVERSLRVLDGAVVV-------FDAVTGVQPQTE 115

                         90       100
                 ....*....|....*....|..
gi 924919400 105 EHALLAYTLGVKQMIVaINKMD 126
Cdd:PRK13351 116 TVWRQADRYGIPRLIF-INKMD 136
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 29-68 6.54e-07

Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.


Pssm-ID: 206673 [Multi-domain]  Cd Length: 270  Bit Score: 47.10  E-value: 6.54e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 924919400  29 VLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDF 68
Cdd:cd01886   38 TMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDF 77
PRK10218 PRK10218
translational GTPase TypA;
29-136 6.94e-07

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 47.40  E-value: 6.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  29 VLDKLKSERERGITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGEFEagiaksgQTREHAL 108
Cdd:PRK10218  42 VMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTK 114

                         90       100       110
                 ....*....|....*....|....*....|
gi 924919400 109 LAYTLGVKQmIVAINKMDEKSV--NWSQDR 136
Cdd:PRK10218 115 KAFAYGLKP-IVVINKVDRPGArpDWVVDQ 143
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
 1-68 2.38e-06

Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 45.78  E-value: 2.38e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 924919400   1 CGGIDKRtiekfekeaaEMGkgsfkyAWVLDKLKSERERGITID---IAL-WKFETGK-YYITIIDAPGHRDF 68
Cdd:COG0481   30 TGTLSER----------EMK------EQVLDSMDLERERGITIKaqaVRLnYKAKDGEtYQLNLIDTPGHVDF 86
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 54-149 2.81e-06

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 45.77  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  54 KYYITIIDAPGHRDFIKNMITGTSQADAAVLVIAS------PtgefeagiaksgQTREHALLAYTLGVKQMIVAINKMDE 127
Cdd:PTZ00327 116 KRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAAnescpqP------------QTSEHLAAVEIMKLKHIIILQNKIDL 183

                         90       100
                 ....*....|....*....|..
gi 924919400 128 KSVNWSQDRYNEIVKetssFVK 149
Cdd:PTZ00327 184 VKEAQAQDQYEEIRN----FVK 201
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 40-126 4.05e-06

Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 45.39  E-value: 4.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  40 GITIDIALWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIAsptgefeagiAKSG---QTRE---HALLAytl 113
Cdd:COG0532   36 GITQHIGAYQVETNGGKITFLDTPGHEAFTAMRARGAQVTDIVILVVA----------ADDGvmpQTIEainHAKAA--- 102

                         90
                 ....*....|...
gi 924919400 114 GVKqMIVAINKMD 126
Cdd:COG0532  103 GVP-IIVAINKID 114
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 29-68 7.93e-06

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 44.47  E-value: 7.93e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 924919400  29 VLDKLKSERERGITIDIA----LWKFETGKYYITIIDAPGHRDF 68
Cdd:PRK07560  57 ALDFDEEEQARGITIKAAnvsmVHEYEGKEYLINLIDTPGHVDF 100
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 57-155 4.42e-05

GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.


Pssm-ID: 206728 [Multi-domain]  Cd Length: 224  Bit Score: 41.89  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  57 ITIIDAPGHRDFIKNMITGTS--QADAAVLVIASptgefEAGIakSGQTREHALLAYTLGVKqMIVAINKMDEKSVNwsq 134
Cdd:cd04165   86 VTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGA-----NAGI--IGMTKEHLGLALALKVP-VFVVVTKIDMTPAN--- 154

                         90       100
                 ....*....|....*....|.
gi 924919400 135 dryneIVKETSSFVKKIGYNP 155
Cdd:cd04165  155 -----VLQETLKDLKRLLKSP 170
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 20-126 4.89e-04

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 38.21  E-value: 4.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  20 GKGSFKYAWVLDK-LKSERERGITIDIAL--WKFETGKYYITIIDAPGHRDFIKNMITGT-----SQADAAVLVIASPTG 91
Cdd:cd00882    9 GKSSLLNALLGGEvGEVSDVPGTTRDPDVyvKELDKGKVKLVLVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDR 88

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 924919400  92 EFEAGIaksgqTREHALLAYTLGVKqMIVAINKMD 126
Cdd:cd00882   89 ESEEDA-----KLLILRRLRKEGIP-IILVGNKID 117
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
20-126 2.81e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 36.50  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  20 GKGSFKYAWVLDKLKSERE---RGITIDIALWKFETGKYYITIIDAPGHRDFIK---NMITGTSQADAAVLVIASPTGEf 93
Cdd:COG1100   15 GKTSLVNRLVGDIFSLEKYlstNGVTIDKKELKLDGLDVDLVIWDTPGQDEFREtrqFYARQLTGASLYLFVVDGTREE- 93

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 924919400  94 eagiaksgqTREHALLAYTL-----GVKQMIVAINKMD 126
Cdd:COG1100   94 ---------TLQSLYELLESlrrlgKKSPIILVLNKID 122
prfC PRK00741
peptide chain release factor 3; Provisional
 36-126 3.71e-03

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 36.65  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  36 ERERGITIDIALWKFETGKYYITIIDAPGHRDFiknmitgtSQ--------ADAAVLVIASPTGeFEAgiaksgQTReha 107
Cdd:PRK00741  60 EKQRGISVTSSVMQFPYRDCLINLLDTPGHEDF--------SEdtyrtltaVDSALMVIDAAKG-VEP------QTR--- 121

                         90       100
                 ....*....|....*....|....*....
gi 924919400 108 llaytlgvKQMIVA----------INKMD 126
Cdd:PRK00741 122 --------KLMEVCrlrdtpiftfINKLD 142
infB CHL00189
translation initiation factor 2; Provisional
 40-131 6.83e-03

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 35.96  E-value: 6.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924919400  40 GITIDIA----LWKFETGKYYITIIDAPGHRDFIKNMITGTSQADAAVLVIASPTGefeagiaKSGQTREhALLAYTLGV 115
Cdd:CHL00189 276 GITQKIGayevEFEYKDENQKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIE-AINYIQAAN 347

                         90
                 ....*....|....*.
gi 924919400 116 KQMIVAINKMDEKSVN 131
Cdd:CHL00189 348 VPIIVAINKIDKANAN 363
 
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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