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Conserved domains on  [gi|409029529|gb|AFV07305|]
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elongation factor 1-alpha, partial [Cortinarius aff. salmoneobasis 2 FS-2012]

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 ...
 1-175 6.77e-111

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: 314.81  E-value: 6.77e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   1 WVLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEAGISKDGQTREHA 80
Cdd:cd01883   50 WVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHA 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  81 LLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSNFIKKVGYNPKAVAFVPISGWHGDNMLEESSNMPWFKGWtke 158
Cdd:cd01883  130 LLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP--- 206

                        170
                 ....*....|....*..
gi 409029529 159 tkagvvkgkTLLDAIDA 175
Cdd:cd01883  207 ---------TLLEALDS 214
 
Name Accession Description Interval E-value
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-175 6.77e-111

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: 314.81  E-value: 6.77e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   1 WVLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEAGISKDGQTREHA 80
Cdd:cd01883   50 WVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHA 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  81 LLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSNFIKKVGYNPKAVAFVPISGWHGDNMLEESSNMPWFKGWtke 158
Cdd:cd01883  130 LLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP--- 206

                        170
                 ....*....|....*..
gi 409029529 159 tkagvvkgkTLLDAIDA 175
Cdd:cd01883  207 ---------TLLEALDS 214
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-175 8.62e-111

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 322.85  E-value: 8.62e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   1 WVLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEAGISKDGQTREHA 80
Cdd:PTZ00141  58 WVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHA 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  81 LLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSNFIKKVGYNPKAVAFVPISGWHGDNMLEESSNMPWFkgwtke 158
Cdd:PTZ00141 138 LLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWY------ 211

                        170
                 ....*....|....*..
gi 409029529 159 tkagvvKGKTLLDAIDA 175
Cdd:PTZ00141 212 ------KGPTLLEALDT 222
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-175 1.83e-89

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: 267.88  E-value: 1.83e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529    1 WVLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEagisKDGQTREHA 80
Cdd:TIGR00483  58 WVMDRLKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   81 LLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSNFIKKVGYNPKAVAFVPISGWHGDNMLEESSNMPWFkgwtketk 160
Cdd:TIGR00483 134 FLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWY-------- 205

                         170
                  ....*....|....*
gi 409029529  161 agvvKGKTLLDAIDA 175
Cdd:TIGR00483 206 ----KGKTLLEALDA 216
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-175 9.01e-87

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: 260.64  E-value: 9.01e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   1 WVLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEfeagiskDGQTREHA 80
Cdd:COG5256   58 WVMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  81 LLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSNFIKKVGYNPKAVAFVPISGWHGDNMLEESSNMPWFkgwtketk 160
Cdd:COG5256  131 FLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWY-------- 202

                        170
                 ....*....|....*
gi 409029529 161 agvvKGKTLLDAIDA 175
Cdd:COG5256  203 ----NGPTLLEALDN 213
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 2-144 9.70e-56

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: 173.87  E-value: 9.70e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529    2 VLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGefeagisKDGQTREHAL 81
Cdd:pfam00009  43 GLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLR 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 409029529   82 LAFTLGVRqLIVAVNKMDTTkwSEDRFNEIIKETSN-FIKKVGYNPKAVAFVPISGWHGDNMLE 144
Cdd:pfam00009 116 LARQLGVP-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 ...
 1-175 6.77e-111

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: 314.81  E-value: 6.77e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   1 WVLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEAGISKDGQTREHA 80
Cdd:cd01883   50 WVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHA 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  81 LLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSNFIKKVGYNPKAVAFVPISGWHGDNMLEESSNMPWFKGWtke 158
Cdd:cd01883  130 LLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP--- 206

                        170
                 ....*....|....*..
gi 409029529 159 tkagvvkgkTLLDAIDA 175
Cdd:cd01883  207 ---------TLLEALDS 214
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-175 8.62e-111

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 322.85  E-value: 8.62e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   1 WVLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEAGISKDGQTREHA 80
Cdd:PTZ00141  58 WVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHA 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  81 LLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSNFIKKVGYNPKAVAFVPISGWHGDNMLEESSNMPWFkgwtke 158
Cdd:PTZ00141 138 LLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWY------ 211

                        170
                 ....*....|....*..
gi 409029529 159 tkagvvKGKTLLDAIDA 175
Cdd:PTZ00141 212 ------KGPTLLEALDT 222
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-175 1.83e-89

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: 267.88  E-value: 1.83e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529    1 WVLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEagisKDGQTREHA 80
Cdd:TIGR00483  58 WVMDRLKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   81 LLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSNFIKKVGYNPKAVAFVPISGWHGDNMLEESSNMPWFkgwtketk 160
Cdd:TIGR00483 134 FLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWY-------- 205

                         170
                  ....*....|....*
gi 409029529  161 agvvKGKTLLDAIDA 175
Cdd:TIGR00483 206 ----KGKTLLEALDA 216
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-175 9.01e-87

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: 260.64  E-value: 9.01e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   1 WVLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEfeagiskDGQTREHA 80
Cdd:COG5256   58 WVMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  81 LLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSNFIKKVGYNPKAVAFVPISGWHGDNMLEESSNMPWFkgwtketk 160
Cdd:COG5256  131 FLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWY-------- 202

                        170
                 ....*....|....*
gi 409029529 161 agvvKGKTLLDAIDA 175
Cdd:COG5256  203 ----NGPTLLEALDN 213
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-175 3.18e-85

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 256.78  E-value: 3.18e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   1 WVLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGgtgefEAGISKDGQTREHA 80
Cdd:PRK12317  57 WVMDRLKEERERGVTIDLAHKKFETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHV 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  81 LLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSNFIKKVGYNPKAVAFVPISGWHGDNMLEESSNMPWFkgwtketk 160
Cdd:PRK12317 132 FLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWY-------- 203

                        170
                 ....*....|....*
gi 409029529 161 agvvKGKTLLDAIDA 175
Cdd:PRK12317 204 ----NGPTLLEALDN 214
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-174 4.80e-84

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 254.63  E-value: 4.80e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   1 WVLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEAGISKDGQTREHA 80
Cdd:PLN00043  58 WVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHA 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  81 LLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSNFIKKVGYNPKAVAFVPISGWHGDNMLEESSNMPWFkgwtke 158
Cdd:PLN00043 138 LLAFTLGVKQMICCCNKMDATtpKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWY------ 211

                        170
                 ....*....|....*.
gi 409029529 159 tkagvvKGKTLLDAID 174
Cdd:PLN00043 212 ------KGPTLLEALD 221
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 2-144 9.70e-56

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: 173.87  E-value: 9.70e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529    2 VLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGefeagisKDGQTREHAL 81
Cdd:pfam00009  43 GLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLR 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 409029529   82 LAFTLGVRqLIVAVNKMDTTkwSEDRFNEIIKETSN-FIKKVGYNPKAVAFVPISGWHGDNMLE 144
Cdd:pfam00009 116 LARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT 176
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 2-175 4.94e-55

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: 172.75  E-value: 4.94e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   2 VLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEagiskdgQTREHAL 81
Cdd:cd04166   52 LVDGLQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSY 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  82 LAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSNFIKKVGYNPkaVAFVPISGWHGDNMLEESSNMPWFkgwtketka 161
Cdd:cd04166  125 IASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWY--------- 193

                        170
                 ....*....|....
gi 409029529 162 gvvKGKTLLDAIDA 175
Cdd:cd04166  194 ---KGPTLLEHLET 204
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 3-175 1.75e-53

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: 175.28  E-value: 1.75e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   3 LDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIaggtgefEA--GISKdgQTREHA 80
Cdd:COG2895   70 TDGLQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLI-------DArkGVLE--QTRRHS 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  81 LLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSNFIKKVGYNPkaVAFVPISGWHGDNMLEESSNMPWFkgwtketk 160
Cdd:COG2895  141 YIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWY-------- 210

                        170
                 ....*....|....*
gi 409029529 161 agvvKGKTLLDAIDA 175
Cdd:COG2895  211 ----DGPTLLEHLET 221
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 3-156 9.05e-47

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 158.54  E-value: 9.05e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   3 LDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEagiskdgQTREHALL 82
Cdd:PRK05124  82 VDGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFI 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 409029529  83 AFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSNFIKKVGYNPKaVAFVPISGWHGDNMLEESSNMPWFKGWT 156
Cdd:PRK05124 155 ATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWYSGPT 227
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 2-154 1.24e-45

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 158.17  E-value: 1.24e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   2 VLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEagiskdgQTREHAL 81
Cdd:PRK05506  78 LVDGLAAEREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSF 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 409029529  82 LAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSNFIKKVGYNpkAVAFVPISGWHGDNMLEESSNMPWFKG 154
Cdd:PRK05506 151 IASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWYEG 221
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-144 2.98e-44

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: 144.36  E-value: 2.98e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   1 WVLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEfeagiskDGQTREHA 80
Cdd:cd00881   35 TFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHL 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409029529  81 LLAFtLGVRQLIVAVNKMDTTKwsEDRFNEIIKETSNFIKKVGY---NPKAVAFVPISGWHGDNMLE 144
Cdd:cd00881  108 NIAL-AGGLPIIVAVNKIDRVG--EEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 2-156 3.11e-43

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: 147.90  E-value: 3.11e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529    2 VLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEagiskdgQTREHAL 81
Cdd:TIGR02034  54 LVDGLQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSY 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 409029529   82 LAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSNFIKKVGynPKAVAFVPISGWHGDNMLEESSNMPWFKGWT 156
Cdd:TIGR02034 127 IASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWYSGPT 199
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 3-99 2.05e-27

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: 105.62  E-value: 2.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   3 LDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGgtgefeagisKDG---QTREH 79
Cdd:COG0050   50 IDKAPEEKERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSA----------TDGpmpQTREH 119

                         90       100
                 ....*....|....*....|
gi 409029529  80 ALLAFTLGVRQLIVAVNKMD 99
Cdd:COG0050  120 ILLARQVGVPYIVVFLNKCD 139
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 4-99 3.08e-27

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: 101.12  E-value: 3.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   4 DKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEagiskdgQTREHALLA 83
Cdd:cd01884   41 DKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLA 113

                         90
                 ....*....|....*.
gi 409029529  84 FTLGVRQLIVAVNKMD 99
Cdd:cd01884  114 RQVGVPYIVVFLNKAD 129
PRK12736 PRK12736
elongation factor Tu; Reviewed
 3-99 6.40e-25

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 98.86  E-value: 6.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   3 LDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAggtgefeagiSKDG---QTREH 79
Cdd:PRK12736  50 IDAAPEEKERGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVA----------ATDGpmpQTREH 119

                         90       100
                 ....*....|....*....|
gi 409029529  80 ALLAFTLGVRQLIVAVNKMD 99
Cdd:PRK12736 120 ILLARQVGVPYLVVFLNKVD 139
PRK00049 PRK00049
elongation factor Tu; Reviewed
 4-99 9.75e-25

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 98.34  E-value: 9.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   4 DKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGtgefeagiskDG---QTREHA 80
Cdd:PRK00049  51 DKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAA----------DGpmpQTREHI 120

                         90
                 ....*....|....*....
gi 409029529  81 LLAFTLGVRQLIVAVNKMD 99
Cdd:PRK00049 121 LLARQVGVPYIVVFLNKCD 139
PRK12735 PRK12735
elongation factor Tu; Reviewed
 4-99 4.76e-23

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 93.75  E-value: 4.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   4 DKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAggtgefeagiSKDG---QTREHA 80
Cdd:PRK12735  51 DNAPEEKARGITINTSHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVS----------AADGpmpQTREHI 120

                         90
                 ....*....|....*....
gi 409029529  81 LLAFTLGVRQLIVAVNKMD 99
Cdd:PRK12735 121 LLARQVGVPYIVVFLNKCD 139
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 4-124 1.97e-22

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: 88.05  E-value: 1.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   4 DKLKAERERGITIDIALWKFETPKYMVT-VIDAPGHRDFIKNMITGTSQADCAILIIAGgtgefEAGISKdgQTREHALL 82
Cdd:cd04171   25 DRLPEEKKRGITIDLGFAYLDLPDGKRLgFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEI 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 409029529  83 AFTLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSNFIKKVGY 124
Cdd:cd04171   98 LELLGIKKGLVVLTKADLV--DEDRLELVEEEILELLAGTFL 137
tufA CHL00071
elongation factor Tu
 9-174 6.33e-22

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 90.79  E-value: 6.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   9 ERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGV 88
Cdd:CHL00071  56 EKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  89 RQLIVAVNKMDttKWSEDRFNEIIK-ETSNFIKKVGYNPKAVAFVPISGWHGDNMLEESSNmpwfkgWTKETKAGVVKGK 167
Cdd:CHL00071 129 PNIVVFLNKED--QVDDEELLELVElEVRELLSKYDFPGDDIPIVSGSALLALEALTENPK------IKRGENKWVDKIY 200


                 ....*..
gi 409029529 168 TLLDAID 174
Cdd:CHL00071 201 NLMDAVD 207
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 3-99 6.81e-22

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: 90.61  E-value: 6.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529    3 LDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEagiskdgQTREHALL 82
Cdd:TIGR00485  50 IDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILL 122

                          90
                  ....*....|....*..
gi 409029529   83 AFTLGVRQLIVAVNKMD 99
Cdd:TIGR00485 123 ARQVGVPYIVVFLNKCD 139
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 4-135 7.34e-22

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: 91.51  E-value: 7.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   4 DKLKAERERGITIDIALWKFETPK-YMVTVIDAPGHRDFIKNMITGTSQADCAILIIAggtgefeagiSKDG---QTREH 79
Cdd:COG3276   26 DRLKEEKKRGITIDLGFAYLPLPDgRRLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVA----------ADEGvmpQTREH 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 409029529  80 -ALLAFtLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSNFIKkvGYNPKAVAFVPIS 135
Cdd:COG3276   96 lAILDL-LGIKRGIVVLTKADLV--DEEWLELVEEEIRELLA--GTFLEDAPIVPVS 147
PLN03127 PLN03127
Elongation factor Tu; Provisional
 3-105 2.36e-21

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 89.50  E-value: 2.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   3 LDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEagiskdgQTREHALL 82
Cdd:PLN03127  99 IDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILL 171

                         90       100
                 ....*....|....*....|...
gi 409029529  83 AFTLGVRQLIVAVNKMDTTKWSE 105
Cdd:PLN03127 172 ARQVGVPSLVVFLNKVDVVDDEE 194
PLN03126 PLN03126
Elongation factor Tu; Provisional
 3-99 4.33e-21

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 88.90  E-value: 4.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   3 LDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEagiskdgQTREHALL 82
Cdd:PLN03126 119 IDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILL 191

                         90
                 ....*....|....*..
gi 409029529  83 AFTLGVRQLIVAVNKMD 99
Cdd:PLN03126 192 AKQVGVPNMVVFLNKQD 208
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 4-132 2.89e-20

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: 86.85  E-value: 2.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529    4 DKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAggtgefeagiSKDG---QTREHA 80
Cdd:TIGR00475  26 DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAGGGGIDAALLVVD----------ADEGvmtQTGEHL 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 409029529   81 LLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSNFIKKVGYNPKAVAFV 132
Cdd:TIGR00475  96 AVLDLLGIPHTIVVITKADRV--NEEEIKRTEMFMKQILNSYIFLKNAKIFK 145
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 3-135 1.96e-12

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: 62.38  E-value: 1.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   3 LDKLKAERERGITIDIALWKFETPK--------------YMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGefea 68
Cdd:cd01889   29 FDKNPQSQERGITLDLGFSSFEVDKpkhlednenpqienYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG---- 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 409029529  69 gisKDGQTREHALLAFTLGVRqLIVAVNKMDTTKWSEdrfneiIKETSNFIKKV------GYNPKAVAFVPIS 135
Cdd:cd01889  105 ---IQTQTAECLVIGELLCKP-LIVVLNKIDLIPEEE------RKRKIEKMKKRlqktleKTRLKDSPIIPVS 167
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 4-111 2.23e-12

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 63.92  E-value: 2.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   4 DKLKAERERGITIDI--ALWKFETPKyMVTVIDAPGHRDFIKNMITGTSQADCAILIIAggtgefeagiSKDG---QTRE 78
Cdd:PRK10512  26 DRLPEEKKRGMTIDLgyAYWPQPDGR-VLGFIDVPGHEKFLSNMLAGVGGIDHALLVVA----------CDDGvmaQTRE 94

                         90       100       110
                 ....*....|....*....|....*....|....
gi 409029529  79 H-ALLAFTlGVRQLIVAVNKMDTTkwSEDRFNEI 111
Cdd:PRK10512  95 HlAILQLT-GNPMLTVALTKADRV--DEARIAEV 125
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 1-142 1.01e-10

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 59.10  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   1 WVlDKLKAERERGITI-----DIALWK---FETPKY------------------MVTVIDAPGHRDFIKNMITGTSQADC 54
Cdd:PRK04000  33 WT-DRHSEELKRGITIrlgyaDATIRKcpdCEEPEAyttepkcpncgsetellrRVSFVDAPGHETLMATMLSGAALMDG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  55 AILIIAGGTGEFEAgiskdgQTREHaLLAFT-LGVRQLIVAVNKMDTTkwSEDRFNEIIKETSNFIKkvGYNPKAVAFVP 133
Cdd:PRK04000 112 AILVIAANEPCPQP------QTKEH-LMALDiIGIKNIVIVQNKIDLV--SKERALENYEQIKEFVK--GTVAENAPIIP 180


                 ....*....
gi 409029529 134 ISGWHGDNM 142
Cdd:PRK04000 181 VSALHKVNI 189
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 4-142 1.13e-10

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: 57.66  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   4 DKLKAERERGITI-----DIALWKFETPKY----------------------MVTVIDAPGHRDFIKNMITGTSQADCAI 56
Cdd:cd01888   26 VRHKEELKRNITIklgyaNAKIYKCPNCGCprpydtpececpgcggetklvrHVSFVDCPGHEILMATMLSGAAVMDGAL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  57 LIIAGGTGefeagiSKDGQTREHaLLAF-TLGVRQLIVAVNKMDTTKwsEDRFNEIIKETSNFIKkvGYNPKAVAFVPIS 135
Cdd:cd01888  106 LLIAANEP------CPQPQTSEH-LAALeIMGLKHIIILQNKIDLVK--EEQALENYEQIKEFVK--GTIAENAPIIPIS 174


                 ....*..
gi 409029529 136 GWHGDNM 142
Cdd:cd01888  175 AQLKYNI 181
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 3-142 1.90e-10

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: 56.33  E-value: 1.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   3 LDKLK----AERE-RGITIDIALWKFETPKY--MVTVIDAPGHRDFiKNMIT-GTSQADCAILIIAGGTGeFEAgiskdg 74
Cdd:cd01887   17 LDKIRktnvAAGEaGGITQHIGAYQVPIDVKipGITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------ 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 409029529  75 QTRE---HALLAFTlgvrQLIVAVNKMDTTKWSE---DRFNEIIKETSNFIKKVGynpKAVAFVPISGWHGDNM 142
Cdd:cd01887   89 QTIEainHAKAANV----PIIVAINKIDKPYGTEadpERVKNELSELGLVGEEWG---GDVSIVPISAKTGEGI 155
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 3-115 3.98e-10

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: 56.48  E-value: 3.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   3 LDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGgtgefeagisKDG---QTReh 79
Cdd:cd04168   39 TDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISA----------VEGvqaQTR-- 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 409029529  80 aLLAFTLgvRQL----IVAVNKMDTTKWSEDRFNEIIKET 115
Cdd:cd04168  107 -ILFRLL--RKLniptIIFVNKIDRAGADLEKVYQEIKEK 143
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 2-99 9.80e-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: 52.15  E-value: 9.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   2 VLDKLKAERERGITID---IAL-WKFETPK-YMVTVIDAPGHRDFikNMITGTSQADC--AILIIAGGTGeFEAgiskdg 74
Cdd:cd01890   36 VLDSMDLERERGITIKaqaVRLfYKAKDGEeYLLNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------ 106

                         90       100
                 ....*....|....*....|....*
gi 409029529  75 QTREHALLAFTLGVrQLIVAVNKMD 99
Cdd:cd01890  107 QTLANFYLALENNL-EIIPVINKID 130
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
2-114 4.25e-08

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 51.67  E-value: 4.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   2 VLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGefeagisKDGQTRehAL 81
Cdd:PRK12740  34 TMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TV 104

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 409029529  82 LAFT--LGV-RqlIVAVNKMDTTKwseDRFNEIIKE 114
Cdd:PRK12740 105 WRQAekYGVpR--IIFVNKMDRAG---ADFFRVLAQ 135
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 2-153 9.62e-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: 49.51  E-value: 9.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   2 VLDKLKAERERGITIdiaLWK---FETPKYMVTVIDAPGHRDF------IKNMitgtsqADCAILIIAggtgefeagiSK 72
Cdd:cd01891   39 VMDSNDLERERGITI---LAKntaITYKDTKINIIDTPGHADFggeverVLSM------VDGVLLLVD----------AS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  73 DG---QTR---EHALLAftlGVRqLIVAVNKMDTtkwSEDRFNEIIKETSNFIKKVGYNPKAVAFvPI------SGWHGD 140
Cdd:cd01891  100 EGpmpQTRfvlKKALEA---GLK-PIVVINKIDR---PDARPEEVVDEVFDLFLELNATDEQLDF-PIvyasakNGWASL 171

                        170
                 ....*....|....
gi 409029529 141 NMLEESSNM-PWFK 153
Cdd:cd01891  172 NLDDPSEDLdPLFE 185
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 2-99 5.26e-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: 48.50  E-value: 5.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   2 VLDKLKAERERGITIDIAL----WKfetpKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGefeagisKDGQTr 77
Cdd:COG0480   48 VMDWMPEEQERGITITSAAttceWK----GHKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG-------VEPQT- 115

                         90       100
                 ....*....|....*....|....*....
gi 409029529  78 EHALlaftlgvRQL-------IVAVNKMD 99
Cdd:COG0480  116 ETVW-------RQAdkygvprIVFVNKMD 137
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 30-135 8.63e-07

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 47.69  E-value: 8.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  30 VTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGefeagiSKDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSE--DR 107
Cdd:PTZ00327 119 VSFVDCPGHDILMATMLNGAAVMDAALLLIAANES------CPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQaqDQ 192

                         90       100
                 ....*....|....*....|....*...
gi 409029529 108 FNEIiketSNFIKkvGYNPKAVAFVPIS 135
Cdd:PTZ00327 193 YEEI----RNFVK--GTIADNAPIIPIS 214
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 29-123 1.16e-06

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: 46.90  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  29 MVTVIDAPGHRDFIKNMITGTS--QADCAILIIAGGtgefeAGISkdGQTREHALLAFTLGVrQLIVAVNKMDTTkwSED 106
Cdd:cd04165   85 VVTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGAN-----AGII--GMTKEHLGLALALKV-PVFVVVTKIDMT--PAN 154

                         90
                 ....*....|....*..
gi 409029529 107 RFNEIIKETSNFIKKVG 123
Cdd:cd04165  155 VLQETLKDLKRLLKSPG 171
PRK10218 PRK10218
translational GTPase TypA;
2-99 1.13e-05

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 44.70  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   2 VLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEagiskdgQTREHAL 81
Cdd:PRK10218  42 VMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTK 114

                         90
                 ....*....|....*...
gi 409029529  82 LAFTLGVRQLIVaVNKMD 99
Cdd:PRK10218 115 KAFAYGLKPIVV-INKVD 131
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
 4-64 1.41e-05

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: 43.74  E-value: 1.41e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 409029529   4 DKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTG 64
Cdd:cd04169   47 DWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 2-41 2.36e-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: 43.25  E-value: 2.36e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 409029529   2 VLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDF 41
Cdd:cd01886   38 TMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDF 77
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 9-99 2.46e-05

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 43.47  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   9 ERERGITI---DIAL-WKfetpKYMVTVIDAPGHRDF------IKNMitgtsqADCAILIIAggtgefeagiSKDG---Q 75
Cdd:COG1217   50 ERERGITIlakNTAVrYK----GVKINIVDTPGHADFggeverVLSM------VDGVLLLVD----------AFEGpmpQ 109

                         90       100
                 ....*....|....*....|....*..
gi 409029529  76 TR---EHALlafTLGVRqLIVAVNKMD 99
Cdd:COG1217  110 TRfvlKKAL---ELGLK-PIVVINKID 132
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 13-99 2.97e-05

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: 43.08  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529  13 GITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGgtgefeagisKDG---QTRE---HALLAftl 86
Cdd:COG0532   36 GITQHIGAYQVETNGGKITFLDTPGHEAFTAMRARGAQVTDIVILVVAA----------DDGvmpQTIEainHAKAA--- 102

                         90
                 ....*....|...
gi 409029529  87 GVrQLIVAVNKMD 99
Cdd:COG0532  103 GV-PIIVAINKID 114
PRK13351 PRK13351
elongation factor G-like protein;
2-99 4.08e-05

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 43.02  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   2 VLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGeFEAgiskdgQTRehal 81
Cdd:PRK13351  47 VTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTG-VQP------QTE---- 115

                         90       100
                 ....*....|....*....|....*
gi 409029529  82 laftLGVRQL-------IVAVNKMD 99
Cdd:PRK13351 116 ----TVWRQAdrygiprLIFINKMD 136
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 2-114 4.77e-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: 42.20  E-value: 4.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   2 VLDKLKAERERGITIDIALWKFETPKYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGefeagisKDGQTREHAL 81
Cdd:cd04170   38 VSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWE 110

                         90       100       110
                 ....*....|....*....|....*....|...
gi 409029529  82 LAFTLGVRQLIVaVNKMDTTKwseDRFNEIIKE 114
Cdd:cd04170  111 FLDDAKLPRIIF-INKMDRAR---ADFDKTLAA 139
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 2-41 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
                 ....*....|....*....|....*....|....*....|....
gi 409029529   2 VLDKLKAERERGITIDIA----LWKFETPKYMVTVIDAPGHRDF 41
Cdd:PRK07560  57 ALDFDEEEQARGITIKAAnvsmVHEYEGKEYLINLIDTPGHVDF 100
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 2-59 6.03e-05

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: 41.83  E-value: 6.03e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 409029529   2 VLDKLKAERERGITID---IALwKFETPK-------YMVTVIDAPGHRDFIKNMITGTSQADCAILII 59
Cdd:cd01885   37 YLDTREDEQERGITIKssaISL-YFEYEEekmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVV 103
infB CHL00189
translation initiation factor 2; Provisional
 3-142 1.44e-04

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 41.36  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029529   3 LDKLK----AERERG-ITIDIALWKFETP----KYMVTVIDAPGHRDFIKNMITGTSQADCAILIIAggtgefeagiSKD 73
Cdd:CHL00189 261 LDKIRktqiAQKEAGgITQKIGAYEVEFEykdeNQKIVFLDTPGHEAFSSMRSRGANVTDIAILIIA----------ADD 330

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 409029529  74 G---QTREhALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSNFIKKVGynpKAVAFVPISGWHGDNM 142
Cdd:CHL00189 331 GvkpQTIE-AINYIQAANVPIIVAINKIDKANANTERIKQQLAKYNLIPEKWG---GDTPMIPISASQGTNI 398
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
 2-41 1.05e-03

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 38.85  E-value: 1.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 409029529   2 VLDKLKAERERGITID---IAL-WKF---ETpkYMVTVIDAPGHRDF 41
Cdd:COG0481   42 VLDSMDLERERGITIKaqaVRLnYKAkdgET--YQLNLIDTPGHVDF 86
 
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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