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Conserved domains on  [gi|1919556299|gb|QOS44220|]
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translation elongation factor 1-alpha, partial [Neonectria neomacrospora]

Protein Classification

elongation factor 1-alpha( domain architecture ID 10111871)

elongation factor 1-alpha is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes; eukaryotic EF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-168 5.66e-121

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: 340.24  E-value: 5.66e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFE 80
Cdd:cd01883    37 EAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  81 AGISKDGQTREHALLAYTLGVKNLIVAINKMDTT--KWSESRFQEIIKETSNFIKKVGYNPKAVAFVPISGFNGDNMLTQ 158
Cdd:cd01883   117 AGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEK 196

                         170
                  ....*....|
gi 1919556299 159 STNCPWYKGW 168
Cdd:cd01883   197 SENMPWYKGP 206
 
Name Accession Description Interval E-value
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-168 5.66e-121

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: 340.24  E-value: 5.66e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFE 80
Cdd:cd01883    37 EAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  81 AGISKDGQTREHALLAYTLGVKNLIVAINKMDTT--KWSESRFQEIIKETSNFIKKVGYNPKAVAFVPISGFNGDNMLTQ 158
Cdd:cd01883   117 AGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEK 196

                         170
                  ....*....|
gi 1919556299 159 STNCPWYKGW 168
Cdd:cd01883   197 SENMPWYKGP 206
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-167 2.75e-120

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 347.12  E-value: 2.75e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFE 80
Cdd:PTZ00141   45 EAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  81 AGISKDGQTREHALLAYTLGVKNLIVAINKMD--TTKWSESRFQEIIKETSNFIKKVGYNPKAVAFVPISGFNGDNMLTQ 158
Cdd:PTZ00141  125 AGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEK 204


                  ....*....
gi 1919556299 159 STNCPWYKG 167
Cdd:PTZ00141  205 SDNMPWYKG 213
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-167 3.16e-95

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: 282.52  E-value: 3.16e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFE 80
Cdd:TIGR00483  45 EAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  81 agisKDGQTREHALLAYTLGVKNLIVAINKMDTTKWSESRFQEIIKETSNFIKKVGYNPKAVAFVPISGFNGDNMLTQST 160
Cdd:TIGR00483 125 ----VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSE 200


                  ....*..
gi 1919556299 161 NCPWYKG 167
Cdd:TIGR00483 201 NTPWYKG 207
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-167 4.09e-95

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: 282.21  E-value: 4.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEfe 80
Cdd:COG5256    45 EAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  81 agiskDGQTREHALLAYTLGVKNLIVAINKMDTTKWSESRFQEIIKETSNFIKKVGYNPKAVAFVPISGFNGDNMLTQST 160
Cdd:COG5256   123 -----MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSD 197


                  ....*..
gi 1919556299 161 NCPWYKG 167
Cdd:COG5256   198 NMPWYNG 204
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 4-157 7.61e-59

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: 181.57  E-value: 7.61e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   4 ELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGefeagi 83
Cdd:pfam00009  32 KRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG------ 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1919556299  84 sKDGQTREHALLAYTLGVKnLIVAINKMDTTkwSESRFQEIIKETSN-FIKKVGYNPKAVAFVPISGFNGDNMLT 157
Cdd:pfam00009 106 -VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT 176
 
Name Accession Description Interval E-value
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-168 5.66e-121

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: 340.24  E-value: 5.66e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFE 80
Cdd:cd01883    37 EAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  81 AGISKDGQTREHALLAYTLGVKNLIVAINKMDTT--KWSESRFQEIIKETSNFIKKVGYNPKAVAFVPISGFNGDNMLTQ 158
Cdd:cd01883   117 AGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEK 196

                         170
                  ....*....|
gi 1919556299 159 STNCPWYKGW 168
Cdd:cd01883   197 SENMPWYKGP 206
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-167 2.75e-120

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 347.12  E-value: 2.75e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFE 80
Cdd:PTZ00141   45 EAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  81 AGISKDGQTREHALLAYTLGVKNLIVAINKMD--TTKWSESRFQEIIKETSNFIKKVGYNPKAVAFVPISGFNGDNMLTQ 158
Cdd:PTZ00141  125 AGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEK 204


                  ....*....
gi 1919556299 159 STNCPWYKG 167
Cdd:PTZ00141  205 SDNMPWYKG 213
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-167 3.16e-95

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: 282.52  E-value: 3.16e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFE 80
Cdd:TIGR00483  45 EAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  81 agisKDGQTREHALLAYTLGVKNLIVAINKMDTTKWSESRFQEIIKETSNFIKKVGYNPKAVAFVPISGFNGDNMLTQST 160
Cdd:TIGR00483 125 ----VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSE 200


                  ....*..
gi 1919556299 161 NCPWYKG 167
Cdd:TIGR00483 201 NTPWYKG 207
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-167 4.09e-95

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: 282.21  E-value: 4.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEfe 80
Cdd:COG5256    45 EAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  81 agiskDGQTREHALLAYTLGVKNLIVAINKMDTTKWSESRFQEIIKETSNFIKKVGYNPKAVAFVPISGFNGDNMLTQST 160
Cdd:COG5256   123 -----MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSD 197


                  ....*..
gi 1919556299 161 NCPWYKG 167
Cdd:COG5256   198 NMPWYNG 204
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-167 4.35e-92

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 275.04  E-value: 4.35e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFE 80
Cdd:PLN00043   45 EAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  81 AGISKDGQTREHALLAYTLGVKNLIVAINKMDTT--KWSESRFQEIIKETSNFIKKVGYNPKAVAFVPISGFNGDNMLTQ 158
Cdd:PLN00043  125 AGISKDGQTREHALLAFTLGVKQMICCCNKMDATtpKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIER 204


                  ....*....
gi 1919556299 159 STNCPWYKG 167
Cdd:PLN00043  205 STNLDWYKG 213
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-167 2.16e-91

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 272.57  E-value: 2.16e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAgtgefE 80
Cdd:PRK12317   44 EAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----D 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  81 AGISKDGQTREHALLAYTLGVKNLIVAINKMDTTKWSESRFQEIIKETSNFIKKVGYNPKAVAFVPISGFNGDNMLTQST 160
Cdd:PRK12317  119 DAGGVMPQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSE 198


                  ....*..
gi 1919556299 161 NCPWYKG 167
Cdd:PRK12317  199 NMPWYNG 205
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 4-157 7.61e-59

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: 181.57  E-value: 7.61e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   4 ELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGefeagi 83
Cdd:pfam00009  32 KRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG------ 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1919556299  84 sKDGQTREHALLAYTLGVKnLIVAINKMDTTkwSESRFQEIIKETSN-FIKKVGYNPKAVAFVPISGFNGDNMLT 157
Cdd:pfam00009 106 -VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT 176
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 6-167 3.20e-56

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: 175.84  E-value: 3.20e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   6 GKGSFKYAWVLDKLKAERERGITIDIALWKFETP-RYFVtVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFEagis 84
Cdd:cd04166    43 QGEKLDLALLVDGLQAEREQGITIDVAYRYFSTPkRKFI-IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE---- 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  85 kdgQTREHALLAYTLGVKNLIVAINKMDTTKWSESRFQEIIKETSNFIKKVGYNPkaVAFVPISGFNGDNMLTQSTNCPW 164
Cdd:cd04166   118 ---QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPW 192


                  ...
gi 1919556299 165 YKG 167
Cdd:cd04166   193 YKG 195
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 6-167 6.64e-56

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: 181.44  E-value: 6.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   6 GKGSFKYAWVLDKLKAERERGITIDIALWKFETP-RYFVtVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFEagis 84
Cdd:COG2895    60 GTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPkRKFI-IADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE---- 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  85 kdgQTREHALLAYTLGVKNLIVAINKMDTTKWSESRFQEIIKETSNFIKKVGYNPkaVAFVPISGFNGDNMLTQSTNCPW 164
Cdd:COG2895   135 ---QTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPW 209


                  ...
gi 1919556299 165 YKG 167
Cdd:COG2895   210 YDG 212
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 12-167 1.33e-48

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 163.55  E-value: 1.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  12 YAWVLDKLKAERERGITIDIALwkfetpRYFVT------VIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFEagisk 85
Cdd:PRK05124   78 LALLVDGLQAEREQGITIDVAY------RYFSTekrkfiIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD----- 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  86 dgQTREHALLAYTLGVKNLIVAINKMDTTKWSESRFQEIIKETSNFIKKVGYNPKaVAFVPISGFNGDNMLTQSTNCPWY 165
Cdd:PRK05124  147 --QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWY 223


                  ..
gi 1919556299 166 KG 167
Cdd:PRK05124  224 SG 225
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 8-167 1.35e-46

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 160.87  E-value: 1.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   8 GSFKYAWVLDKLKAERERGITIDIALWKFETP-RYFVtVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFEagiskd 86
Cdd:PRK05506   71 DEIDLALLVDGLAAEREQGITIDVAYRYFATPkRKFI-VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT------ 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  87 gQTREHALLAYTLGVKNLIVAINKMDTTKWSESRFQEIIKETSNFIKKVGYNpkAVAFVPISGFNGDNMLTQSTNCPWYK 166
Cdd:PRK05506  144 -QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWYE 220


                  .
gi 1919556299 167 G 167
Cdd:PRK05506  221 G 221
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 8-167 4.81e-44

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: 150.22  E-value: 4.81e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   8 GSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFEagiskdg 87
Cdd:TIGR02034  47 GEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE------- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  88 QTREHALLAYTLGVKNLIVAINKMDTTKWSESRFQEIIKETSNFIKKVGynPKAVAFVPISGFNGDNMLTQSTNCPWYKG 167
Cdd:TIGR02034 120 QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWYSG 197
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 14-157 1.34e-43

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: 142.82  E-value: 1.34e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  14 WVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEfeagiskDGQTREHA 93
Cdd:cd00881    35 TFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHL 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1919556299  94 LLAyTLGVKNLIVAINKMDTTKwsESRFQEIIKETSNFIKKVGY---NPKAVAFVPISGFNGDNMLT 157
Cdd:cd00881   108 NIA-LAGGLPIIVAVNKIDRVG--EEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 3-112 1.22e-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: 109.98  E-value: 1.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   3 AELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAgtgefeag 82
Cdd:cd01884    27 AKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSA-------- 98

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1919556299  83 isKDG---QTREHALLAYTLGVKNLIVAINKMD 112
Cdd:cd01884    99 --TDGpmpQTREHLLLARQVGVPYIVVFLNKAD 129
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 3-112 6.59e-30

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: 112.55  E-value: 6.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   3 AELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAgtgefeag 82
Cdd:COG0050    37 AKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSA-------- 108

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1919556299  83 isKDG---QTREHALLAYTLGVKNLIVAINKMD 112
Cdd:COG0050   109 --TDGpmpQTREHILLARQVGVPYIVVFLNKCD 139
PRK00049 PRK00049
elongation factor Tu; Reviewed
 3-112 8.83e-28

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 106.81  E-value: 8.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   3 AELGKGSFK-YAWVlDKLKAERERGITIDIALWKFETP-RYFVTViDAPGHRDFIKNMITGTSQADCAILIIAAGtgefe 80
Cdd:PRK00049   37 AKKGGAEAKaYDQI-DKAPEEKARGITINTAHVEYETEkRHYAHV-DCPGHADYVKNMITGAAQMDGAILVVSAA----- 109

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1919556299  81 agiskDG---QTREHALLAYTLGVKNLIVAINKMD 112
Cdd:PRK00049  110 -----DGpmpQTREHILLARQVGVPYIVVFLNKCD 139
PRK12736 PRK12736
elongation factor Tu; Reviewed
 3-112 3.72e-27

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 105.03  E-value: 3.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   3 AELGKGSFK-YAWVlDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAgtgefea 81
Cdd:PRK12736   37 AERGLNQAKdYDSI-DAAPEEKERGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAA------- 108

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1919556299  82 gisKDG---QTREHALLAYTLGVKNLIVAINKMD 112
Cdd:PRK12736  109 ---TDGpmpQTREHILLARQVGVPYLVVFLNKVD 139
PRK12735 PRK12735
elongation factor Tu; Reviewed
 3-112 1.27e-25

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 101.07  E-value: 1.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   3 AELGKGSFKYAWVLDKLKAERERGITIDIALWKFETP-RYFVTViDAPGHRDFIKNMITGTSQADCAILIIAAGtgefea 81
Cdd:PRK12735   37 AKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETAnRHYAHV-DCPGHADYVKNMITGAAQMDGAILVVSAA------ 109

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1919556299  82 giskDG---QTREHALLAYTLGVKNLIVAINKMD 112
Cdd:PRK12735  110 ----DGpmpQTREHILLARQVGVPYIVVFLNKCD 139
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 17-153 9.74e-25

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: 94.21  E-value: 9.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  17 DKLKAERERGITIDIALWKFETPRYFVT-VIDAPGHRDFIKNMITGTSQADCAILIIAAgtgefEAGISKdgQTREHALL 95
Cdd:cd04171    25 DRLPEEKKRGITIDLGFAYLDLPDGKRLgFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEI 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1919556299  96 AYTLGVKNLIVAINKMDTTkwSESRFQEIIKETSNFIKKVGYnpKAVAFVPISGFNGD 153
Cdd:cd04171    98 LELLGIKKGLVVLTKADLV--DEDRLELVEEEILELLAGTFL--ADAPIFPVSSVTGE 151
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 3-112 1.59e-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: 97.93  E-value: 1.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   3 AELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFEag 82
Cdd:TIGR00485  37 AKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-- 114

                          90       100       110
                  ....*....|....*....|....*....|
gi 1919556299  83 iskdgQTREHALLAYTLGVKNLIVAINKMD 112
Cdd:TIGR00485 115 -----QTREHILLARQVGVPYIVVFLNKCD 139
tufA CHL00071
elongation factor Tu
 2-112 1.96e-23

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 95.02  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   2 AAELGKGSFKYAWVlDKLKAERERGITIDIALWKFETP-RYFVTViDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFE 80
Cdd:CHL00071   37 AAKGGAKAKKYDEI-DSAPEEKARGITINTAHVEYETEnRHYAHV-DCPGHADYVKNMITGAAQMDGAILVVSAADGPMP 114

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1919556299  81 agiskdgQTREHALLAYTLGVKNLIVAINKMD 112
Cdd:CHL00071  115 -------QTKEHILLAKQVGVPNIVVFLNKED 139
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 17-112 3.59e-23

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: 95.37  E-value: 3.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  17 DKLKAERERGITIDI--ALWKFETPRyFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAgtgefeagisKDG---QTRE 91
Cdd:COG3276    26 DRLKEEKKRGITIDLgfAYLPLPDGR-RLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAA----------DEGvmpQTRE 94

                          90       100
                  ....*....|....*....|..
gi 1919556299  92 H-ALLAyTLGVKNLIVAINKMD 112
Cdd:COG3276    95 HlAILD-LLGIKRGIVVLTKAD 115
PLN03127 PLN03127
Elongation factor Tu; Provisional
 16-118 7.98e-23

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 93.74  E-value: 7.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  16 LDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFEagiskdgQTREHALL 95
Cdd:PLN03127   99 IDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILL 171

                          90       100
                  ....*....|....*....|...
gi 1919556299  96 AYTLGVKNLIVAINKMDTTKWSE 118
Cdd:PLN03127  172 ARQVGVPSLVVFLNKVDVVDDEE 194
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 17-130 8.20e-23

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: 94.17  E-value: 8.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  17 DKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAgtgefeagisKDG---QTREHA 93
Cdd:TIGR00475  26 DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDA----------DEGvmtQTGEHL 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1919556299  94 LLAYTLGVKNLIVAINKMDTT-----KWSESRFQEIIKETSN 130
Cdd:TIGR00475  96 AVLDLLGIPHTIVVITKADRVneeeiKRTEMFMKQILNSYIF 137
PLN03126 PLN03126
Elongation factor Tu; Provisional
 3-112 1.11e-21

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 90.83  E-value: 1.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   3 AELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFEag 82
Cdd:PLN03126  106 ASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-- 183

                          90       100       110
                  ....*....|....*....|....*....|
gi 1919556299  83 iskdgQTREHALLAYTLGVKNLIVAINKMD 112
Cdd:PLN03126  184 -----QTKEHILLAKQVGVPNMVVFLNKQD 208
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 16-148 1.83e-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: 67.78  E-value: 1.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  16 LDKLKAERERGITIDIALWKFETP--------------RYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGefea 81
Cdd:cd01889    29 FDKNPQSQERGITLDLGFSSFEVDkpkhlednenpqieNYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG---- 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1919556299  82 gisKDGQTREHALLAYTLGvKNLIVAINKMDTTKWSEsrfqeiIKETSNFIKKV------GYNPKAVAFVPIS 148
Cdd:cd01889   105 ---IQTQTAECLVIGELLC-KPLIVVLNKIDLIPEEE------RKRKIEKMKKRlqktleKTRLKDSPIIPVS 167
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 17-124 3.82e-13

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 66.23  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  17 DKLKAERERGITIDI--ALWKFETPRyFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAgtgefeagisKDG---QTRE 91
Cdd:PRK10512   26 DRLPEEKKRGMTIDLgyAYWPQPDGR-VLGFIDVPGHEKFLSNMLAGVGGIDHALLVVAC----------DDGvmaQTRE 94

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1919556299  92 H-ALLAYTlGVKNLIVAINKMDTTkwSESRFQEI 124
Cdd:PRK10512   95 HlAILQLT-GNPMLTVALTKADRV--DEARIAEV 125
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 6-157 2.72e-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: 61.90  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   6 GKGSFKYA----WVlDKLKAERERGITI-----DIALWKFETPRYF----------------------VTVIDAPGHRDF 54
Cdd:cd01888    12 GKTTLVKAlsgvWT-VRHKEELKRNITIklgyaNAKIYKCPNCGCPrpydtpececpgcggetklvrhVSFVDCPGHEIL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  55 IKNMITGTSQADCAILIIAAGTGefeagiSKDGQTREHALLAYTLGVKNLIVAINKMDTTKwsESRFQEIIKETSNFIKk 134
Cdd:cd01888    91 MATMLSGAAVMDGALLLIAANEP------CPQPQTSEHLAALEIMGLKHIIILQNKIDLVK--EEQALENYEQIKEFVK- 161

                         170       180
                  ....*....|....*....|....*.
gi 1919556299 135 vGYNPKAVAFVPIS---GFNGDNMLT 157
Cdd:cd01888   162 -GTIAENAPIIPISaqlKYNIDVLCE 186
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 16-155 5.30e-12

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: 60.56  E-value: 5.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  16 LDKLK----AERE-RGITIDIALWKFETPRYF--VTVIDAPGHRDFiKNMIT-GTSQADCAILIIAAGTGeFEAgiskdg 87
Cdd:cd01887    17 LDKIRktnvAAGEaGGITQHIGAYQVPIDVKIpgITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------ 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1919556299  88 QTRE---HALLAytlGVKnLIVAINKMDTTKWSES---RFQEIIKETSNFIKKVGynpKAVAFVPISGFNGDNM 155
Cdd:cd01887    89 QTIEainHAKAA---NVP-IIVAINKIDKPYGTEAdpeRVKNELSELGLVGEEWG---GDVSIVPISAKTGEGI 155
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 6-155 6.84e-12

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 62.56  E-value: 6.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299   6 GKGSFKYA----WVlDKLKAERERGITI-----DIALWK---FETPRYFVT------------------VIDAPGHRDFI 55
Cdd:PRK04000   21 GKTTLVQAltgvWT-DRHSEELKRGITIrlgyaDATIRKcpdCEEPEAYTTepkcpncgsetellrrvsFVDAPGHETLM 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  56 KNMITGTSQADCAILIIAAGTGEFEAgiskdgQTREHALLAYTLGVKNLIVAINKMDTTkwSESRFQEIIKETSNFIKkv 135
Cdd:PRK04000  100 ATMLSGAALMDGAILVIAANEPCPQP------QTKEHLMALDIIGIKNIVIVQNKIDLV--SKERALENYEQIKEFVK-- 169

                         170       180
                  ....*....|....*....|
gi 1919556299 136 GYNPKAVAFVPISGFNGDNM 155
Cdd:PRK04000  170 GTVAENAPIIPVSALHKVNI 189
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 16-127 1.93e-11

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: 60.33  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  16 LDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAgtgefeagisKDG---QTRE- 91
Cdd:cd04168    39 TDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISA----------VEGvqaQTRIl 108

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1919556299  92 -HALLAYTLGVknlIVAINKMDTTKwseSRFQEIIKE 127
Cdd:cd04168   109 fRLLRKLNIPT---IIFVNKIDRAG---ADLEKVYQE 139
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 15-112 1.71e-09

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: 54.08  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  15 VLDKLKAERERGITID---IAL-WKFETP-RYFVTVIDAPGHRDFikNMITGTSQADC--AILIIAAGTGeFEAgiskdg 87
Cdd:cd01890    36 VLDSMDLERERGITIKaqaVRLfYKAKDGeEYLLNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------ 106

                          90       100
                  ....*....|....*....|....*
gi 1919556299  88 QTREHALLAYTLGVKnLIVAINKMD 112
Cdd:cd01890   107 QTLANFYLALENNLE-IIPVINKID 130
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
15-127 6.78e-09

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 53.98  E-value: 6.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  15 VLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGefeagisKDGQTRehAL 94
Cdd:PRK12740   34 TMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TV 104

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1919556299  95 LAYT--LGVKNLIVaINKMDTTKwseSRFQEIIKE 127
Cdd:PRK12740  105 WRQAekYGVPRIIF-VNKMDRAG---ADFFRVLAQ 135
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 15-128 1.16e-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: 52.21  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  15 VLDKLKAERERGITIdiaLWK---FETPRYFVTVIDAPGHRDF------IKNMitgtsqADCAILIIAAGTGEFEagisk 85
Cdd:cd01891    39 VMDSNDLERERGITI---LAKntaITYKDTKINIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP----- 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1919556299  86 dgQTR---EHALLAytlGVKnLIVAINKMDTtkwSESRFQEIIKET 128
Cdd:cd01891   105 --QTRfvlKKALEA---GLK-PIVVINKIDR---PDARPEEVVDEV 141
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 43-153 2.94e-08

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 51.93  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  43 VTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGefeagiSKDGQTREHALLAYTLGVKNLIVAINKMDTTKwsESRFQ 122
Cdd:PTZ00327  119 VSFVDCPGHDILMATMLNGAAVMDAALLLIAANES------CPQPQTSEHLAAVEIMKLKHIIILQNKIDLVK--EAQAQ 190

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1919556299 123 EIIKETSNFIKkvGYNPKAVAFVPIS---GFNGD 153
Cdd:PTZ00327  191 DQYEEIRNFVK--GTIADNAPIIPISaqlKYNID 222
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 15-152 3.80e-07

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: 48.89  E-value: 3.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  15 VLDKLKAERERGITIDIAL----WKfetpRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGefeagisKDGQT- 89
Cdd:COG0480    48 VMDWMPEEQERGITITSAAttceWK----GHKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG-------VEPQTe 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1919556299  90 ---REhaLLAYtlgvkNL--IVAINKMDTTKwseSRFQEIIKEtsnfIKKVgYNPKAVAF-VPI---SGFNG 152
Cdd:COG0480   117 tvwRQ--ADKY-----GVprIVFVNKMDREG---ADFDRVLEQ----LKER-LGANPVPLqLPIgaeDDFKG 173
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 22-112 3.84e-07

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 48.86  E-value: 3.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  22 ERERGITI---DIAL-WKfetpRYFVTVIDAPGHRDF------IKNMitgtsqADCAILIIAAgtgeFEagiskdG---Q 88
Cdd:COG1217    50 ERERGITIlakNTAVrYK----GVKINIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQ 109

                          90       100
                  ....*....|....*....|....*..
gi 1919556299  89 TR---EHALlayTLGVKnLIVAINKMD 112
Cdd:COG1217   110 TRfvlKKAL---ELGLK-PIVVINKID 132
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
 6-77 7.11e-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: 47.59  E-value: 7.11e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1919556299   6 GKGSFKYAwVLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTG 77
Cdd:cd04169    37 ARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 26-155 1.47e-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: 46.93  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  26 GITIDIALWKFETPRYFVTVIDAPGHRDFiknmiT-----GTSQADCAILIIAAgtgefeagisKDG---QTRE---HAL 94
Cdd:COG0532    36 GITQHIGAYQVETNGGKITFLDTPGHEAF-----TamrarGAQVTDIVILVVAA----------DDGvmpQTIEainHAK 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1919556299  95 LAytlGVKnLIVAINKMDttkwsesrfqeiiKETSNfIKKV-------GYNPKA----VAFVPISGFNGDNM 155
Cdd:COG0532   101 AA---GVP-IIVAINKID-------------KPGAN-PDRVkqelaehGLVPEEwggdTIFVPVSAKTGEGI 154
PRK10218 PRK10218
translational GTPase TypA;
15-112 6.45e-06

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 45.47  E-value: 6.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  15 VLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFEagiskdgQTREHAL 94
Cdd:PRK10218   42 VMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTK 114

                          90
                  ....*....|....*...
gi 1919556299  95 LAYTLGVKNLIVaINKMD 112
Cdd:PRK10218  115 KAFAYGLKPIVV-INKVD 131
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 15-112 7.06e-06

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: 44.53  E-value: 7.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  15 VLDKLKAERERGITID---IALwKFETPR-------YFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAgtgefeagis 84
Cdd:cd01885    37 YLDTREDEQERGITIKssaISL-YFEYEEekmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDA---------- 105

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1919556299  85 KDG---QTreHALL--AYTLGVKNLIVaINKMD 112
Cdd:cd01885   106 VEGvcvQT--ETVLrqALEERVKPVLV-INKID 135
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 15-127 1.47e-05

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: 43.74  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  15 VLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGefeagisKDGQTREHAL 94
Cdd:cd04170    38 VSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWE 110

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1919556299  95 LAYTLGVKNLIVaINKMDTTKwseSRFQEIIKE 127
Cdd:cd04170   111 FLDDAKLPRIIF-INKMDRAR---ADFDKTLAA 139
infB CHL00189
translation initiation factor 2; Provisional
 16-155 2.05e-05

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 44.05  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  16 LDKLK----AERERG-ITIDIALWKFETPRYF----VTVIDAPGHRDFIKNMITGTSQADCAILIIAAgtgefeagisKD 86
Cdd:CHL00189  261 LDKIRktqiAQKEAGgITQKIGAYEVEFEYKDenqkIVFLDTPGHEAFSSMRSRGANVTDIAILIIAA----------DD 330

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1919556299  87 G---QTREhALLAYTLGVKNLIVAINKMDTTKWSESRFQEIIKETSNFIKKVGynpKAVAFVPISGFNGDNM 155
Cdd:CHL00189  331 GvkpQTIE-AINYIQAANVPIIVAINKIDKANANTERIKQQLAKYNLIPEKWG---GDTPMIPISASQGTNI 398
PRK13351 PRK13351
elongation factor G-like protein;
15-112 2.08e-05

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 43.79  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  15 VLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGeFEAgiskdgQTREHAL 94
Cdd:PRK13351   47 VTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTG-VQP------QTETVWR 119

                          90
                  ....*....|....*...
gi 1919556299  95 LAYTLGVKNLIVaINKMD 112
Cdd:PRK13351  120 QADRYGIPRLIF-INKMD 136
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
 15-112 2.21e-05

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 43.85  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  15 VLDKLKAERERGITIdialwKFETPR----------YFVTVIDAPGHRDFiknmitgT-----SQADC--AILIIAAGTG 77
Cdd:COG0481    42 VLDSMDLERERGITI-----KAQAVRlnykakdgetYQLNLIDTPGHVDF-------SyevsrSLAACegALLVVDASQG 109

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1919556299  78 eFEAgiskdgQTREHALLAYTLGVKnLIVAINKMD 112
Cdd:COG0481   110 -VEA------QTLANVYLALENDLE-IIPVINKID 136
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 15-54 3.50e-05

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: 42.86  E-value: 3.50e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1919556299  15 VLDKLKAERERGITIDIALWKFETPRYFVTVIDAPGHRDF 54
Cdd:cd01886    38 TMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDF 77
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 15-140 5.00e-05

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 42.54  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556299  15 VLDKLKAERERGITIDIA----LWKFETPRYFVTVIDAPGHRDFIKNMITGTSQADCAILIIAAGTGEFEagiskdgQT- 89
Cdd:PRK07560   57 ALDFDEEEQARGITIKAAnvsmVHEYEGKEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMP-------QTe 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1919556299  90 -------REHallaytlgVKNlIVAINKMD--------TTKWSESRFQEIIKETSNFIKkvGYNPK 140
Cdd:PRK07560  130 tvlrqalRER--------VKP-VLFINKVDrlikelklTPQEMQQRLLKIIKDVNKLIK--GMAPE 184
 
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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