NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|34871942|gb|AAQ83233|]
View 

elongation factor 1-alpha, partial [Phanacis hypochoeridis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-122 2.41e-85

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 cd01883:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 219  Bit Score: 247.79  E-value: 2.41e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEAGISKNGQTREHALLAFTLGVKQLIVGV 80
Cdd:cd01883  65 IDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAV 144

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 34871942  81 NKMDMTDPPYSESRFEEIKKEVSSYIKKIGYNTASVAFVPIS 122
Cdd:cd01883 145 NKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPIS 186
 
Name Accession Description Interval E-value
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-122 2.41e-85

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: 247.79  E-value: 2.41e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEAGISKNGQTREHALLAFTLGVKQLIVGV 80
Cdd:cd01883  65 IDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAV 144

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 34871942  81 NKMDMTDPPYSESRFEEIKKEVSSYIKKIGYNTASVAFVPIS 122
Cdd:cd01883 145 NKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPIS 186
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-122 7.77e-81

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 243.89  E-value: 7.77e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942    1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEAGISKNGQTREHALLAFTLGVKQLIVGV 80
Cdd:PTZ00141  73 IDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCI 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 34871942   81 NKMDMTDPPYSESRFEEIKKEVSSYIKKIGYNTASVAFVPIS 122
Cdd:PTZ00141 153 NKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPIS 194
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-122 9.01e-61

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: 191.69  E-value: 9.01e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEfeagiskNGQTREHALLAFTLGVKQLIVGV 80
Cdd:COG5256  73 IDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAV 145

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 34871942  81 NKMDMTDppYSESRFEEIKKEVSSYIKKIGYNTASVAFVPIS 122
Cdd:COG5256 146 NKMDAVN--YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVS 185
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-122 2.54e-57

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: 182.75  E-value: 2.54e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942     1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagisKNGQTREHALLAFTLGVKQLIVGV 80
Cdd:TIGR00483  73 IDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAI 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 34871942    81 NKMDMTDppYSESRFEEIKKEVSSYIKKIGYNTASVAFVPIS 122
Cdd:TIGR00483 149 NKMDSVN--YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPIS 188
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-122 1.08e-42

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: 138.43  E-value: 1.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942     1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGefeagisKNGQTREHALLAFTLGVKqLIVGV 80
Cdd:pfam00009  57 IKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFI 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 34871942    81 NKMDMTDppysESRFEEIKKEVSS-YIKKIGYNTASVAFVPIS 122
Cdd:pfam00009 129 NKMDRVD----GAELEEVVEEVSReLLEKYGEDGEFVPVVPGS 167
 
Name Accession Description Interval E-value
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-122 2.41e-85

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: 247.79  E-value: 2.41e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEAGISKNGQTREHALLAFTLGVKQLIVGV 80
Cdd:cd01883  65 IDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAV 144

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 34871942  81 NKMDMTDPPYSESRFEEIKKEVSSYIKKIGYNTASVAFVPIS 122
Cdd:cd01883 145 NKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPIS 186
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-122 7.77e-81

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 243.89  E-value: 7.77e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942    1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEAGISKNGQTREHALLAFTLGVKQLIVGV 80
Cdd:PTZ00141  73 IDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCI 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 34871942   81 NKMDMTDPPYSESRFEEIKKEVSSYIKKIGYNTASVAFVPIS 122
Cdd:PTZ00141 153 NKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPIS 194
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-122 1.56e-63

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 199.55  E-value: 1.56e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942    1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEAGISKNGQTREHALLAFTLGVKQLIVGV 80
Cdd:PLN00043  73 IDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCC 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 34871942   81 NKMDMTDPPYSESRFEEIKKEVSSYIKKIGYNTASVAFVPIS 122
Cdd:PLN00043 153 NKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPIS 194
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-122 9.01e-61

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: 191.69  E-value: 9.01e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEfeagiskNGQTREHALLAFTLGVKQLIVGV 80
Cdd:COG5256  73 IDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAV 145

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 34871942  81 NKMDMTDppYSESRFEEIKKEVSSYIKKIGYNTASVAFVPIS 122
Cdd:COG5256 146 NKMDAVN--YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVS 185
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-122 2.19e-60

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 190.52  E-value: 2.19e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942    1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgigefEAGISKNGQTREHALLAFTLGVKQLIVGV 80
Cdd:PRK12317  72 IDLAHKKFETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAI 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 34871942   81 NKMDMTDppYSESRFEEIKKEVSSYIKKIGYNTASVAFVPIS 122
Cdd:PRK12317 147 NKMDAVN--YDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVS 186
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-122 2.54e-57

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: 182.75  E-value: 2.54e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942     1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagisKNGQTREHALLAFTLGVKQLIVGV 80
Cdd:TIGR00483  73 IDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAI 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 34871942    81 NKMDMTDppYSESRFEEIKKEVSSYIKKIGYNTASVAFVPIS 122
Cdd:TIGR00483 149 NKMDSVN--YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPIS 188
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-122 1.08e-42

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: 138.43  E-value: 1.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942     1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGefeagisKNGQTREHALLAFTLGVKqLIVGV 80
Cdd:pfam00009  57 IKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFI 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 34871942    81 NKMDMTDppysESRFEEIKKEVSS-YIKKIGYNTASVAFVPIS 122
Cdd:pfam00009 129 NKMDRVD----GAELEEVVEEVSReLLEKYGEDGEFVPVVPGS 167
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-122 4.81e-35

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: 119.60  E-value: 4.81e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagiskngQTREHALLAFTLGVKQLIVGV 80
Cdd:cd04166  66 IDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAV 138

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 34871942  81 NKMDMTDppYSESRFEEIKKEVSSYIKKIGYNtaSVAFVPIS 122
Cdd:cd04166 139 NKMDLVD--YDEEVFEEIKADYLAFAASLGIE--DITFIPIS 176
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-122 1.12e-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: 123.66  E-value: 1.12e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GIGEfeagiskngQTREHALLAFTLGVKQLIV 78
Cdd:COG2895  83 IDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDArkGVLE---------QTRRHSYIASLLGIRHVVV 153

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 34871942  79 GVNKMDMTDppYSESRFEEIKKEVSSYIKKIGYntASVAFVPIS 122
Cdd:COG2895 154 AVNKMDLVD--YSEEVFEEIVADYRAFAAKLGL--EDITFIPIS 193
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-121 6.37e-30

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: 105.84  E-value: 6.37e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEfeagiskNGQTREHALLAFtLGVKQLIVGV 80
Cdd:cd00881  50 IKTGVVEFEWPKRRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAV 121

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 34871942  81 NKMDMTDppysESRFEEIKKEVSSYIKKIGYNTASVAFVPI 121
Cdd:cd00881 122 NKIDRVG----EEDFDEVLREIKELLKLIGFTFLKGKDVPI 158
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-122 2.67e-29

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 109.62  E-value: 2.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942    1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagiskngQTREHALLAFTLGVKQLIVGV 80
Cdd:PRK05124  95 IDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAV 167

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 34871942   81 NKMDMTDppYSESRFEEIKKEVSSYIKKIGYNTaSVAFVPIS 122
Cdd:PRK05124 168 NKMDLVD--YSEEVFERIREDYLTFAEQLPGNL-DIRFVPLS 206
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-122 3.17e-27

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: 103.22  E-value: 3.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942     1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagiskngQTREHALLAFTLGVKQLIVGV 80
Cdd:TIGR02034  68 IDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAV 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 34871942    81 NKMDMTDppYSESRFEEIKKEVSSYIKKIGYntASVAFVPIS 122
Cdd:TIGR02034 141 NKMDLVD--YDEEVFENIKKDYLAFAEQLGF--RDVTFIPLS 178
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-122 5.11e-27

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 103.86  E-value: 5.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942    1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagiskngQTREHALLAFTLGVKQLIVGV 80
Cdd:PRK05506  92 IDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAV 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 34871942   81 NKMDMTDppYSESRFEEIKKEVSSYIKKIGYntASVAFVPIS 122
Cdd:PRK05506 165 NKMDLVD--YDQEVFDEIVADYRAFAAKLGL--HDVTFIPIS 202
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-119 2.98e-24

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: 91.49  E-value: 2.98e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagiskngQTREHALLAFTLGVKQLIVGV 80
Cdd:cd01884  53 INTAHVEYETANRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFL 125

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 34871942  81 NKMDMTDppySESRFEEIKKEVSSYIKKIGYNTASVAFV 119
Cdd:cd01884 126 NKADMVD---DEELLELVEMEVRELLSKYGFDGDDTPIV 161
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-90 2.59e-22

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: 89.82  E-value: 2.59e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagiskngQTREHALLAFTLGVKQLIVGV 80
Cdd:COG0050  63 INTSHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFL 135

                        90
                ....*....|
gi 34871942  81 NKMDMTDPPY 90
Cdd:COG0050 136 NKCDMVDDEE 145
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-89 3.27e-21

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 86.92  E-value: 3.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942    1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagiskngQTREHALLAFTLGVKQLIVGV 80
Cdd:PRK12736  63 INTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFL 135


                 ....*....
gi 34871942   81 NKMDMTDPP 89
Cdd:PRK12736 136 NKVDLVDDE 144
tufA CHL00071
elongation factor Tu
 1-122 2.04e-20

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 84.62  E-value: 2.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942    1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagiskngQTREHALLAFTLGVKQLIVGV 80
Cdd:CHL00071  63 INTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFL 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 34871942   81 NKMDMTDppySESRFEEIKKEVSSYIKKIGYNTASVAFVPIS 122
Cdd:CHL00071 136 NKEDQVD---DEELLELVELEVRELLSKYDFPGDDIPIVSGS 174
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-89 2.75e-20

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 84.08  E-value: 2.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942    1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagiskngQTREHALLAFTLGVKQLIVGV 80
Cdd:PRK00049  63 INTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFL 135


                 ....*....
gi 34871942   81 NKMDMTDPP 89
Cdd:PRK00049 136 NKCDMVDDE 144
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-89 1.36e-19

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 82.19  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942    1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagiskngQTREHALLAFTLGVKQLIVGV 80
Cdd:PRK12735  63 INTSHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFL 135


                 ....*....
gi 34871942   81 NKMDMTDPP 89
Cdd:PRK12735 136 NKCDMVDDE 144
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-89 1.70e-19

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 82.18  E-value: 1.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942    1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagiskngQTREHALLAFTLGVKQLIVGV 80
Cdd:PLN03127 112 IATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFL 184


                 ....*....
gi 34871942   81 NKMDMTDPP 89
Cdd:PLN03127 185 NKVDVVDDE 193
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 17-119 4.70e-19

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: 77.65  E-value: 4.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942  17 IIDAPGHRDFIKNMITGTSQADCAVLIVAAgigefEAGISKngQTREHALLAFTLGVKQLIVGVNKMDMTDppysESRFE 96
Cdd:cd04171  54 FIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLVD----EDRLE 122

                        90       100
                ....*....|....*....|...
gi 34871942  97 EIKKEVSSYIKKIGYNTASVAFV 119
Cdd:cd04171 123 LVEEEILELLAGTFLADAPIFPV 145
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 15-122 1.22e-18

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: 79.96  E-value: 1.22e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942  15 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GIGEfeagiskngQTREH-ALLAFtLGVKQLIVGVNKMDMTDPpys 91
Cdd:COG3276  53 LGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAAdeGVMP---------QTREHlAILDL-LGIKRGIVVLTKADLVDE--- 119

                        90       100       110
                ....*....|....*....|....*....|.
gi 34871942  92 eSRFEEIKKEVSSYIKkiGYNTASVAFVPIS 122
Cdd:COG3276 120 -EWLELVEEEIRELLA--GTFLEDAPIVPVS 147
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-105 1.69e-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: 79.44  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942     1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagiskngQTREHALLAFTLGVKQLIVGV 80
Cdd:TIGR00485  63 INTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFL 135

                          90       100
                  ....*....|....*....|....*.
gi 34871942    81 NKMDM-TDPPYSESRFEEIKKEVSSY 105
Cdd:TIGR00485 136 NKCDMvDDEELLELVEMEVRELLSQY 161
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-122 2.99e-17

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 76.19  E-value: 2.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942    1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagiskngQTREHALLAFTLGVKQLIVGV 80
Cdd:PLN03126 132 INTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFL 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 34871942   81 NKMDMTDppySESRFEEIKKEVSSYIKKIGYNTASVAFVPIS 122
Cdd:PLN03126 205 NKQDQVD---DEELLELVELEVRELLSSYEFPGDDIPIISGS 243
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-119 5.41e-17

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: 75.29  E-value: 5.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942     1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgigefEAGISKngQTREHALLAFTLGVKQLIVGV 80
Cdd:TIGR00475  38 IDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDA-----DEGVMT--QTGEHLAVLDLLGIPHTIVVI 110

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 34871942    81 NKMDMTDppysESRFEEIKKEVSSYIKKIGYNTASVAFV 119
Cdd:TIGR00475 111 TKADRVN----EEEIKRTEMFMKQILNSYIFLKNAKIFK 145
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 18-119 1.34e-10

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 56.98  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   18 IDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFeagisknGQTREH-ALLAFTlGVKQLIVGVNKMDMTDPPysesRFE 96
Cdd:PRK10512  56 IDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHlAILQLT-GNPMLTVALTKADRVDEA----RIA 123

                         90       100
                 ....*....|....*....|...
gi 34871942   97 EIKKEVSSYIKKIGYNTASVaFV 119
Cdd:PRK10512 124 EVRRQVKAVLREYGFAEAKL-FV 145
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 15-122 2.60e-10

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 56.01  E-value: 2.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   15 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgigefeagiskN-----GQTREHaLLAFT-LGVKQLIVGVNKMDMTDP 88
Cdd:PRK04000  87 VSFVDAPGHETLMATMLSGAALMDGAILVIAA-----------NepcpqPQTKEH-LMALDiIGIKNIVIVQNKIDLVSK 154

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 34871942   89 PYSESRFEEIKKEVSSYIkkigyntASVA-FVPIS 122
Cdd:PRK04000 155 ERALENYEQIKEFVKGTV-------AENApIIPVS 182
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 15-122 3.06e-09

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: 52.27  E-value: 3.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942  15 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgigefeagiskN-----GQTREHALLAFTLGVKQLIVGVNKMDMTDPP 89
Cdd:cd01888  79 VSFVDCPGHEILMATMLSGAAVMDGALLLIAA-----------NepcpqPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147

                        90       100       110
                ....*....|....*....|....*....|...
gi 34871942  90 YSESRFEEIKKevssYIKKIGYNTASVafVPIS 122
Cdd:cd01888 148 QALENYEQIKE----FVKGTIAENAPI--IPIS 174
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 15-110 1.06e-08

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: 51.14  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942  15 VTIIDAPGHRDFIKNMITGTS--QADCAVLIVAAGigefeAGIskNGQTREHALLAFTLGVKQLIVgVNKMDMTdppySE 92
Cdd:cd04165  86 VTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGAN-----AGI--IGMTKEHLGLALALKVPVFVV-VTKIDMT----PA 153

                        90
                ....*....|....*...
gi 34871942  93 SRFEEIKKEVSSYIKKIG 110
Cdd:cd04165 154 NVLQETLKDLKRLLKSPG 171
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 10-122 1.21e-08

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 51.54  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   10 TAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgigefeagiskN-----GQTREHALLAFTLGVKQLIVGVNKMD 84
Cdd:PTZ00327 114 TLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAA-----------NescpqPQTSEHLAAVEIMKLKHIIILQNKID 182

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 34871942   85 MTDPPYSESRFEEIKKEVSSYIKKigyntaSVAFVPIS 122
Cdd:PTZ00327 183 LVKEAQAQDQYEEIRNFVKGTIAD------NAPIIPIS 214
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 15-122 1.71e-07

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: 47.08  E-value: 1.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942  15 VTIIDAPGHRDFiKNMIT-GTSQADCAVLIVAA--GIGEfeagiskngQTRE---HALLAFTlgvkQLIVGVNKMDMtdP 88
Cdd:cd01887  51 ITFIDTPGHEAF-TNMRArGASVTDIAILVVAAddGVMP---------QTIEainHAKAANV----PIIVAINKIDK--P 114

                        90       100       110
                ....*....|....*....|....*....|....
gi 34871942  89 PYSESRFEEIKKEVSSYIKKIGYNTASVAFVPIS 122
Cdd:cd01887 115 YGTEADPERVKNELSELGLVGEEWGGDVSIVPIS 148
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 13-110 6.38e-05

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: 40.33  E-value: 6.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942  13 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIgefeaGISKNGQT--REhallAFTLGVKQLIVgVNKMD--MTD- 87
Cdd:cd04167  71 YLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTSVTERliRH----AIQEGLPMVLV-INKIDrlILEl 140

                        90       100
                ....*....|....*....|....*.
gi 34871942  88 --PPYSESR-FEEIKKEVSSYIKKIG 110
Cdd:cd04167 141 klPPTDAYYkLRHTIDEINNYIASFS 166
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 15-84 2.38e-04

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: 38.76  E-value: 2.38e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34871942  15 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GIgefeagiskNGQTRehaLLAFTLgvKQL----IVGVNKMD 84
Cdd:cd04168  66 VNIIDTPGHMDFIAEVERSLSVLDGAILVISAveGV---------QAQTR---ILFRLL--RKLniptIIFVNKID 127
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 13-102 5.84e-04

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: 37.57  E-value: 5.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942  13 YYVTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgigeFEAGISkngQTR---EHALLAftlGVKqLIVGVNKM 83
Cdd:cd01891  65 TKINIIDTPGHADFggeverVLSM------VDGVLLLVDA----SEGPMP---QTRfvlKKALEA---GLK-PIVVINKI 127

                        90
                ....*....|....*....
gi 34871942  84 DMTDppyseSRFEEIKKEV 102
Cdd:cd01891 128 DRPD-----ARPEEVVDEV 141
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 17-84 1.22e-03

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 36.92  E-value: 1.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942  17 IIDAPGHRDF------IKNMitgtsqADCAVLIVAAgigeFEagisknG---QTR---EHALlafTLGVKqLIVGVNKMD 84
Cdd:COG1217  73 IVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlKKAL---ELGLK-PIVVINKID 132
PRK10218 PRK10218
translational GTPase TypA;
13-84 1.70e-03

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 36.61  E-value: 1.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34871942   13 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEagiskngQTREHALLAFTLGVKQLIVgVNKMD 84
Cdd:PRK10218  68 YRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIVV-INKVD 131
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 15-84 2.75e-03

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: 36.15  E-value: 2.75e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34871942  15 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GIGEfeagiskngQTRE---HALLAftlGVKqLIVGVNKMD 84
Cdd:COG0532  53 ITFLDTPGHEAFTAMRARGAQVTDIVILVVAAddGVMP---------QTIEainHAKAA---GVP-IIVAINKID 114
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
15-84 3.12e-03

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 35.87  E-value: 3.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34871942   15 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGefeagisKNGQTRehALLAFT--LGVKQLIVgVNKMD 84
Cdd:PRK12740  62 INLIDTPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TVWRQAekYGVPRIIF-VNKMD 123
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 1-109 3.17e-03

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: 35.51  E-value: 3.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   1 IDIALWKFETAKYYVTIIDAPGHRDFIKNMITGT-----SQADCAVLIVAAGIGEFEAGIskngqTREHALLAFTLGVKQ 75
Cdd:cd00882  35 PDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRESEEDA-----KLLILRRLRKEGIPI 109

                        90       100       110
                ....*....|....*....|....*....|....
gi 34871942  76 LIVGvNKMDMtDPPYSESRFEEIKKEVSSYIKKI 109
Cdd:cd00882 110 ILVG-NKIDL-LEEREVEELLRLEELAKILGVPV 141
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 6-119 4.35e-03

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: 35.20  E-value: 4.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942   6 WKFETAKYYV-TIIDAPGHRDFikNMITGTSQADC--AVLIVAAGIGeFEAgiskngQTREHALLAFTLGVKQLIVgVNK 82
Cdd:cd01890  59 YKAKDGEEYLlNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------QTLANFYLALENNLEIIPV-INK 128

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 34871942  83 MDM--TDPpysesrfEEIKKEVSSYikkIGYNTASVAFV 119
Cdd:cd01890 129 IDLpaADP-------DRVKQEIEDV---LGLDASEAILV 157
infB CHL00189
translation initiation factor 2; Provisional
 6-122 6.21e-03

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 35.19  E-value: 6.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942    6 WKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgigefEAGISKngQTREhALLAFTLGVKQLIVGVNKMDM 85
Cdd:CHL00189 288 FEYKDENQKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAA-----DDGVKP--QTIE-AINYIQAANVPIIVAINKIDK 359

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 34871942   86 TDppyseSRFEEIKKEVSSY---IKKIGyntASVAFVPIS 122
Cdd:CHL00189 360 AN-----ANTERIKQQLAKYnliPEKWG---GDTPMIPIS 391
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 15-84 9.53e-03

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: 34.49  E-value: 9.53e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34871942  15 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgigefEAGISknGQTREHALLAFTLGVKQLIVgVNKMD 84
Cdd:cd04170  66 INLIDTPGYADFVGETLSALRAVDAALIVVEA-----QSGVE--VGTEKVWEFLDDAKLPRIIF-INKMD 127
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH