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Conserved domains on  [gi|157101916|gb|ABV23658|]
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elongation factor-1 alpha, partial [Keyacris sp. P110a]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 1-189 6.53e-123

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PTZ00141:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 446  Bit Score: 354.05  E-value: 6.53e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFT 80
Cdd:PTZ00141  63 LKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFT 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  81 LGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSDKMGWFKgwtierkegk 160
Cdd:PTZ00141 143 LGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK---------- 212

                        170       180
                 ....*....|....*....|....*....
gi 157101916 161 aeGRCLIEALDAILPPSRPTEKPLRLPLQ 189
Cdd:PTZ00141 213 --GPTLLEALDTLEPPKRPVDKPLRLPLQ 239
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-189 6.53e-123

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 354.05  E-value: 6.53e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFT 80
Cdd:PTZ00141  63 LKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFT 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  81 LGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSDKMGWFKgwtierkegk 160
Cdd:PTZ00141 143 LGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK---------- 212

                        170       180
                 ....*....|....*....|....*....
gi 157101916 161 aeGRCLIEALDAILPPSRPTEKPLRLPLQ 189
Cdd:PTZ00141 213 --GPTLLEALDTLEPPKRPVDKPLRLPLQ 239
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-176 8.51e-115

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: 325.21  E-value: 8.51e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFT 80
Cdd:cd01883   55 LKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLART 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  81 LGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSDKMGWFKGWTierkegk 160
Cdd:cd01883  135 LGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPT------- 207

                        170
                 ....*....|....*.
gi 157101916 161 aegrcLIEALDAILPP 176
Cdd:cd01883  208 -----LLEALDSLEPP 218
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-189 1.05e-94

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: 281.44  E-value: 1.05e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFT 80
Cdd:COG5256   63 LKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLART 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  81 LGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSDKMGWFKGWTierkegk 160
Cdd:COG5256  136 LGINQLIVAVNKMDAVN--YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPT------- 206

                        170       180
                 ....*....|....*....|....*....
gi 157101916 161 aegrcLIEALDAILPPSRPTEKPLRLPLQ 189
Cdd:COG5256  207 -----LLEALDNLKEPEKPVDKPLRIPIQ 230
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-189 8.18e-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: 266.73  E-value: 8.18e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916    1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAFT 80
Cdd:TIGR00483  63 LKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLART 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   81 LGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSDKMGWFKGWTierkegk 160
Cdd:TIGR00483 139 LGINQLIVAINKMDSVN--YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKT------- 209

                         170       180
                  ....*....|....*....|....*....
gi 157101916  161 aegrcLIEALDAILPPSRPTEKPLRLPLQ 189
Cdd:TIGR00483 210 -----LLEALDALEPPEKPTDKPLRIPIQ 233
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-176 2.33e-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: 175.79  E-value: 2.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916    1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFT 80
Cdd:pfam00009  47 LPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQ 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   81 LGVKqLIVGVNKMDSTeppySEARFEEIKKEVSN-YIKKIGYNPAAVAFVPISGWHGDNMLEhsdkmgwfkgwtierkeg 159
Cdd:pfam00009 120 LGVP-IIVFINKMDRV----DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT------------------ 176

                         170
                  ....*....|....*..
gi 157101916  160 kaegrcLIEALDAILPP 176
Cdd:pfam00009 177 ------LLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-189 6.53e-123

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 354.05  E-value: 6.53e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFT 80
Cdd:PTZ00141  63 LKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFT 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  81 LGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSDKMGWFKgwtierkegk 160
Cdd:PTZ00141 143 LGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK---------- 212

                        170       180
                 ....*....|....*....|....*....
gi 157101916 161 aeGRCLIEALDAILPPSRPTEKPLRLPLQ 189
Cdd:PTZ00141 213 --GPTLLEALDTLEPPKRPVDKPLRLPLQ 239
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-176 8.51e-115

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: 325.21  E-value: 8.51e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFT 80
Cdd:cd01883   55 LKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLART 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  81 LGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSDKMGWFKGWTierkegk 160
Cdd:cd01883  135 LGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPT------- 207

                        170
                 ....*....|....*.
gi 157101916 161 aegrcLIEALDAILPP 176
Cdd:cd01883  208 -----LLEALDSLEPP 218
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-189 1.05e-94

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: 281.44  E-value: 1.05e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFT 80
Cdd:COG5256   63 LKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLART 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  81 LGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSDKMGWFKGWTierkegk 160
Cdd:COG5256  136 LGINQLIVAVNKMDAVN--YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPT------- 206

                        170       180
                 ....*....|....*....|....*....
gi 157101916 161 aegrcLIEALDAILPPSRPTEKPLRLPLQ 189
Cdd:COG5256  207 -----LLEALDNLKEPEKPVDKPLRIPIQ 230
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-189 5.41e-93

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 278.13  E-value: 5.41e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFT 80
Cdd:PLN00043  63 LKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFT 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  81 LGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSDKMGWFKGWTierkegk 160
Cdd:PLN00043 143 LGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPT------- 215

                        170       180
                 ....*....|....*....|....*....
gi 157101916 161 aegrcLIEALDAILPPSRPTEKPLRLPLQ 189
Cdd:PLN00043 216 -----LLEALDQINEPKRPSDKPLRLPLQ 239
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-189 1.03e-92

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 276.42  E-value: 1.03e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKNGQTREHALLAFT 80
Cdd:PRK12317  62 LKEERERGVTIDLAHKKFETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLART 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  81 LGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSDKMGWFKGWTierkegk 160
Cdd:PRK12317 137 LGINQLIVAINKMDAVN--YDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNGPT------- 207

                        170       180
                 ....*....|....*....|....*....
gi 157101916 161 aegrcLIEALDAILPPSRPTEKPLRLPLQ 189
Cdd:PRK12317 208 -----LLEALDNLKPPEKPTDKPLRIPIQ 231
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-189 8.18e-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: 266.73  E-value: 8.18e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916    1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAFT 80
Cdd:TIGR00483  63 LKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLART 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   81 LGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSDKMGWFKGWTierkegk 160
Cdd:TIGR00483 139 LGINQLIVAINKMDSVN--YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKT------- 209

                         170       180
                  ....*....|....*....|....*....
gi 157101916  161 aegrcLIEALDAILPPSRPTEKPLRLPLQ 189
Cdd:TIGR00483 210 -----LLEALDALEPPEKPTDKPLRIPIQ 233
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-189 1.57e-57

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: 186.45  E-value: 1.57e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFT 80
Cdd:COG2895   73 LQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  81 LGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSNYIKKIGYNPaaVAFVPISGWHGDNMLEHSDKMGWFKGWTierkegk 160
Cdd:COG2895  146 LGIRHVVVAVNKMDLVD--YSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWYDGPT------- 214

                        170       180
                 ....*....|....*....|....*....
gi 157101916 161 aegrcLIEALDAILPPSRPTEKPLRLPLQ 189
Cdd:COG2895  215 -----LLEHLETVEVAEDRNDAPFRFPVQ 238
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-176 2.33e-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: 175.79  E-value: 2.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916    1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFT 80
Cdd:pfam00009  47 LPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQ 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   81 LGVKqLIVGVNKMDSTeppySEARFEEIKKEVSN-YIKKIGYNPAAVAFVPISGWHGDNMLEhsdkmgwfkgwtierkeg 159
Cdd:pfam00009 120 LGVP-IIVFINKMDRV----DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT------------------ 176

                         170
                  ....*....|....*..
gi 157101916  160 kaegrcLIEALDAILPP 176
Cdd:pfam00009 177 ------LLDALDEYLPS 187
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-177 1.12e-52

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: 167.36  E-value: 1.12e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFT 80
Cdd:cd04166   56 LQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  81 LGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSNYIKKIGYNPaaVAFVPISGWHGDNMLEHSDKMGWFKGWTierkegk 160
Cdd:cd04166  129 LGIRHVVVAVNKMDLVD--YDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYKGPT------- 197

                        170
                 ....*....|....*..
gi 157101916 161 aegrcLIEALDAILPPS 177
Cdd:cd04166  198 -----LLEHLETVEIAS 209
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-189 7.49e-47

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 159.31  E-value: 7.49e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFT 80
Cdd:PRK05124  85 LQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  81 LGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSNYIKKIGYNPaAVAFVPISGWHGDNMLEHSDKMGWFKGWTierkegk 160
Cdd:PRK05124 158 LGIKHLVVAVNKMDLVD--YSEEVFERIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWYSGPT------- 227

                        170       180
                 ....*....|....*....|....*....
gi 157101916 161 aegrcLIEALDAILPPSRPTEKPLRLPLQ 189
Cdd:PRK05124 228 -----LLEVLETVDIQRVVDAQPFRFPVQ 251
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-189 6.64e-45

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: 152.91  E-value: 6.64e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916    1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFT 80
Cdd:TIGR02034  58 LQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   81 LGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSNYIKKIGynPAAVAFVPISGWHGDNMLEHSDKMGWFKGWTierkegk 160
Cdd:TIGR02034 131 LGIRHVVLAVNKMDLVD--YDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWYSGPT------- 199

                         170       180
                  ....*....|....*....|....*....
gi 157101916  161 aegrcLIEALDAILPPSRPTEKPLRLPLQ 189
Cdd:TIGR02034 200 -----LLEILETVEVERDAQDLPLRFPVQ 223
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-189 1.66e-43

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 152.78  E-value: 1.66e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFT 80
Cdd:PRK05506  82 LAAEREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASL 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  81 LGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSNYIKKIGYnpAAVAFVPISGWHGDNMLEHSDKMGWFkgwtierkegk 160
Cdd:PRK05506 155 LGIRHVVLAVNKMDLVD--YDQEVFDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWY----------- 219

                        170       180
                 ....*....|....*....|....*....
gi 157101916 161 aEGRCLIEALDAILPPSRPTEKPLRLPLQ 189
Cdd:PRK05506 220 -EGPSLLEHLETVEIASDRNLKDFRFPVQ 247
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-141 3.39e-41

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: 137.04  E-value: 3.39e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFt 80
Cdd:cd00881   40 LKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAL- 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157101916  81 LGVKQLIVGVNKMDSTeppySEARFEEIKKEVSNYIKKIGY---NPAAVAFVPISGWHGDNMLE 141
Cdd:cd00881  112 AGGLPIIVAVNKIDRV----GEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 4-176 9.83e-28

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: 103.05  E-value: 9.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGV 83
Cdd:cd01884   46 EKARGITINTAHVEYETANRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  84 KQLIVGVNKMDSTEppySEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWhgdNMLEHSDKMGWFKgwTIERkegkaeg 163
Cdd:cd01884  119 PYIVVFLNKADMVD---DEELLELVEMEVRELLSKYGFDGDDTPIVRGSAL---KALEGDDPNKWVD--KILE------- 183

                        170
                 ....*....|...
gi 157101916 164 rcLIEALDAILPP 176
Cdd:cd01884  184 --LLDALDSYIPT 194
PRK12736 PRK12736
elongation factor Tu; Reviewed
 4-189 3.57e-27

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 105.80  E-value: 3.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGV 83
Cdd:PRK12736  56 EKERGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  84 KQLIVGVNKMDSTEppySEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGdnmLEHSDKmgwfkgWTIERKEgkaeg 163
Cdd:PRK12736 129 PYLVVFLNKVDLVD---DEELLELVEMEVRELLSEYDFPGDDIPVIRGSALKA---LEGDPK------WEDAIME----- 191

                        170       180
                 ....*....|....*....|....*..
gi 157101916 164 rcLIEALDAILP-PSRPTEKPLRLPLQ 189
Cdd:PRK12736 192 --LMDAVDEYIPtPERDTDKPFLMPVE 216
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 4-187 8.37e-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: 104.46  E-value: 8.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGV 83
Cdd:COG0050   56 EKERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  84 KQLIVGVNKMDSTEPPYseaRFEEIKKEVSNYIKKIGYNPAAVAFVPISGW---HGDNMLEHSDKMgwfkgwtIErkegk 160
Cdd:COG0050  129 PYIVVFLNKCDMVDDEE---LLELVEMEVRELLSKYGFPGDDTPIIRGSALkalEGDPDPEWEKKI-------LE----- 193

                        170       180
                 ....*....|....*....|....*...
gi 157101916 161 aegrcLIEALDAILP-PSRPTEKPLRLP 187
Cdd:COG0050  194 -----LMDAVDSYIPePERDTDKPFLMP 216
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-129 1.11e-24

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 94.21  E-value: 1.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDI--ALWKFETSKYyVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREHALLA 78
Cdd:cd04171   27 LPEEKKRGITIDLgfAYLDLPDGKR-LGFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEIL 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157101916  79 FTLGVKQLIVGVNKMDSTEppysEARFEEIKKEVSNYIKKIGYNPAAVAFV 129
Cdd:cd04171   99 ELLGIKKGLVVLTKADLVD----EDRLELVEEEILELLAGTFLADAPIFPV 145
PRK00049 PRK00049
elongation factor Tu; Reviewed
 4-187 1.26e-24

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 98.72  E-value: 1.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGV 83
Cdd:PRK00049  56 EKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  84 KQLIVGVNKMDSTEppySEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGdnmLEHSDKMGWFKgwTIERkegkaeg 163
Cdd:PRK00049 129 PYIVVFLNKCDMVD---DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEK--KILE------- 193

                        170       180
                 ....*....|....*....|....*
gi 157101916 164 rcLIEALDAILP-PSRPTEKPLRLP 187
Cdd:PRK00049 194 --LMDAVDSYIPtPERAIDKPFLMP 216
tufA CHL00071
elongation factor Tu
 4-189 2.44e-24

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 98.11  E-value: 2.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGV 83
Cdd:CHL00071  56 EKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  84 KQLIVGVNKMDSTEppySEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSDKmgwfkgwtIERKEGKAEG 163
Cdd:CHL00071 129 PNIVVFLNKEDQVD---DEELLELVELEVRELLSKYDFPGDDIPIVSGSALLALEALTENPK--------IKRGENKWVD 197

                        170       180
                 ....*....|....*....|....*....
gi 157101916 164 RC--LIEALDAILP-PSRPTEKPLRLPLQ 189
Cdd:CHL00071 198 KIynLMDAVDSYIPtPERDTDKPFLMAIE 226
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 1-187 2.49e-24

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 99.22  E-value: 2.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDI--ALWKFEtSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREH-ALL 77
Cdd:COG3276   28 LKEEKKRGITIDLgfAYLPLP-DGRRLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAA-----DEGVMP--QTREHlAIL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  78 AFtLGVKQLIVGVNKMDSTEPpyseARFEEIKKEVSNYIKKIGYNPAAVafVPISGWHGdnmlehsdkmgwfkgwtierk 157
Cdd:COG3276  100 DL-LGIKRGIVVLTKADLVDE----EWLELVEEEIRELLAGTFLEDAPI--VPVSAVTG--------------------- 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 157101916 158 EGKAEgrcLIEALDAIL--PPSRPTEKPLRLP 187
Cdd:COG3276  152 EGIDE---LRAALDALAaaVPARDADGPFRLP 180
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 4-189 6.89e-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: 96.77  E-value: 6.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916    4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGV 83
Cdd:TIGR00485  56 EKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGV 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   84 KQLIVGVNKMDSTEppySEARFEEIKKEVSNYIKKIGYNPAAVAFVpisgwhgdnmlehsdkmgwfKGWTIERKEGKAEG 163
Cdd:TIGR00485 129 PYIVVFLNKCDMVD---DEELLELVEMEVRELLSQYDFPGDDTPII--------------------RGSALKALEGDAEW 185

                         170       180       190
                  ....*....|....*....|....*....|.
gi 157101916  164 RC----LIEALDAILP-PSRPTEKPLRLPLQ 189
Cdd:TIGR00485 186 EAkileLMDAVDEYIPtPEREIDKPFLLPIE 216
PLN03127 PLN03127
Elongation factor Tu; Provisional
 4-189 1.90e-23

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 96.05  E-value: 1.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGV 83
Cdd:PLN03127 105 EKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGV 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  84 KQLIVGVNKMDSTEPPYSEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNmlehsDKMGwfkgwtierKEGKAEg 163
Cdd:PLN03127 178 PSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSALQGTN-----DEIG---------KNAILK- 242

                        170       180
                 ....*....|....*....|....*..
gi 157101916 164 rcLIEALDAILP-PSRPTEKPLRLPLQ 189
Cdd:PLN03127 243 --LMDAVDEYIPePVRVLDKPFLMPIE 267
PRK12735 PRK12735
elongation factor Tu; Reviewed
 4-187 5.86e-23

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 94.13  E-value: 5.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGV 83
Cdd:PRK12735  56 EKARGITINTSHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  84 KQLIVGVNKMDSTEPPyseARFEEIKKEVSNYIKKIGYNpaavafvpisgwhGDNM----------LEHSDKMGWFKgwT 153
Cdd:PRK12735 129 PYIVVFLNKCDMVDDE---ELLELVEMEVRELLSKYDFP-------------GDDTpiirgsalkaLEGDDDEEWEA--K 190

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 157101916 154 IERkegkaegrcLIEALDAILP-PSRPTEKPLRLP 187
Cdd:PRK12735 191 ILE---------LMDAVDSYIPePERAIDKPFLMP 216
PLN03126 PLN03126
Elongation factor Tu; Provisional
 4-189 2.36e-21

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 90.44  E-value: 2.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGV 83
Cdd:PLN03126 125 ERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGV 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  84 KQLIVGVNKMDSTEppySEARFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSDKmgwfkgwtIERKEGKAEG 163
Cdd:PLN03126 198 PNMVVFLNKQDQVD---DEELLELVELEVRELLSSYEFPGDDIPIISGSALLALEALMENPN--------IKRGDNKWVD 266

                        170       180
                 ....*....|....*....|....*....
gi 157101916 164 RC--LIEALDAILP-PSRPTEKPLRLPLQ 189
Cdd:PLN03126 267 KIyeLMDAVDSYIPiPQRQTDLPFLLAVE 295
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-129 5.88e-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: 86.47  E-value: 5.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916    1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFT 80
Cdd:TIGR00475  28 LPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDADEGVMT-------QTGEHLAVLDL 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 157101916   81 LGVKQLIVGVNKMDSTEppysEARFEEIKKEVSNYIKKIGYNPAAVAFV 129
Cdd:TIGR00475 101 LGIPHTIVVITKADRVN----EEEIKRTEMFMKQILNSYIFLKNAKIFK 145
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 1-129 9.04e-13

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 65.84  E-value: 9.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITIDI--ALWKFETSKYyVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFeagisknGQTREH-ALL 77
Cdd:PRK10512  28 LPEEKKRGMTIDLgyAYWPQPDGRV-LGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHlAIL 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157101916  78 AFTlGVKQLIVGVNKMDSTEppysEARFEEIKKEVSNYIKKIGYnPAAVAFV 129
Cdd:PRK10512 100 QLT-GNPMLTVALTKADRVD----EARIAEVRRQVKAVLREYGF-AEAKLFV 145
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 2-110 3.45e-11

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: 59.30  E-value: 3.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   2 KAERERGITIDIALWKF--------------ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisK 67
Cdd:cd01889   33 PQSQERGITLDLGFSSFevdkpkhlednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------I 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157101916  68 NGQTREHALLAFTLGvKQLIVGVNKMDSTEPPYSEARFEEIKK 110
Cdd:cd01889  106 QTQTAECLVIGELLC-KPLIVVLNKIDLIPEEERKRKIEKMKK 147
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 4-139 1.42e-10

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 59.10  E-value: 1.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITI-----DIALWK---FETSKYYVT------------------IIDAPGHRDFIKNMITGTSQADCAVLIVAAG 57
Cdd:PRK04000  40 ELKRGITIrlgyaDATIRKcpdCEEPEAYTTepkcpncgsetellrrvsFVDAPGHETLMATMLSGAALMDGAILVIAAN 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  58 TGEFEAgiskngQTREHaLLAFT-LGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSNYIkkigynpAAVA-FVPISGWH 135
Cdd:PRK04000 120 EPCPQP------QTKEH-LMALDiIGIKNIVIVQNKIDLVSKERALENYEQIKEFVKGTV-------AENApIIPVSALH 185


                 ....
gi 157101916 136 GDNM 139
Cdd:PRK04000 186 KVNI 189
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 4-116 1.97e-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: 58.02  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRehaLLAFTLgv 83
Cdd:cd04168   45 ERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTR---ILFRLL-- 112

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157101916  84 KQL----IVGVNKMDsTEPPYSEARFEEIKKEVSNYI 116
Cdd:cd04168  113 RKLniptIIFVNKID-RAGADLEKVYQEIKEKLSPDI 148
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 2-139 9.67e-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: 55.35  E-value: 9.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   2 KAERERGITI-----DIALWKFETSKYY----------------------VTIIDAPGHRDFIKNMITGTSQADCAVLIV 54
Cdd:cd01888   29 KEELKRNITIklgyaNAKIYKCPNCGCPrpydtpececpgcggetklvrhVSFVDCPGHEILMATMLSGAAVMDGALLLI 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  55 AAgtgefeagiskN-----GQTREHaLLAF-TLGVKQLIVGVNKMDSTEPPYSEARFEEIKKevsnYIKKIGYNPAAVaf 128
Cdd:cd01888  109 AA-----------NepcpqPQTSEH-LAALeIMGLKHIIILQNKIDLVKEEQALENYEQIKE----FVKGTIAENAPI-- 170

                        170
                 ....*....|.
gi 157101916 129 VPISGWHGDNM 139
Cdd:cd01888  171 IPISAQLKYNI 181
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 3-139 1.79e-09

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: 54.02  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   3 AERE-RGITIDIALWKFETSKYY--VTIIDAPGHRDFiKNMIT-GTSQADCAVLIVAAGTGeFEAgiskngQTRE---HA 75
Cdd:cd01887   26 AAGEaGGITQHIGAYQVPIDVKIpgITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------QTIEainHA 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157101916  76 LLAFTlgvkQLIVGVNKMDstEPPYSEARFEEIKKEVSNY---IKKIGYNpaaVAFVPISGWHGDNM 139
Cdd:cd01887   98 KAANV----PIIVAINKID--KPYGTEADPERVKNELSELglvGEEWGGD---VSIVPISAKTGEGI 155
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 4-112 3.65e-09

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: 53.75  E-value: 3.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIdiaLWKfETSKYY----VTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAGTGEFEagiskngQTR- 72
Cdd:cd01891   46 ERERGITI---LAK-NTAITYkdtkINIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP-------QTRf 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157101916  73 --EHALLAftlGVKqLIVGVNKMDSteppySEARFEEIKKEV 112
Cdd:cd01891  109 vlKKALEA---GLK-PIVVINKIDR-----PDARPEEVVDEV 141
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 1-149 1.90e-08

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


Pssm-ID: 206730 [Multi-domain]  Cd Length: 213  Bit Score: 51.89  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITID---IALwKFETSK---YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTgefeaGISKNGQT--R 72
Cdd:cd04167   44 RKDEQERGISIKsnpISL-VLEDSKgksYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTSVTERliR 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  73 EhallAFTLGVKQLIVgVNKMDS--TE---PPYsEARFE--EIKKEVSNYIKKIGyNPAAVAFVPISGwhgdNMLEHSDK 145
Cdd:cd04167  118 H----AIQEGLPMVLV-INKIDRliLElklPPT-DAYYKlrHTIDEINNYIASFS-TTEGFLVSPELG----NVLFASSK 186


                 ....
gi 157101916 146 MGWF 149
Cdd:cd04167  187 FGFC 190
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 1-116 4.72e-08

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: 50.61  E-value: 4.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITID---IAL-WKFETSKYYV-TIIDAPGHRDFikNMITGTSQADC--AVLIVAAGTGeFEAgiskngQTRE 73
Cdd:cd01890   40 MDLERERGITIKaqaVRLfYKAKDGEEYLlNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------QTLA 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157101916  74 HALLAFTLGVKQLIVgVNKMDsteppYSEARFEEIKKEVSNYI 116
Cdd:cd01890  111 NFYLALENNLEIIPV-INKID-----LPAADPDRVKQEIEDVL 147
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
4-108 4.85e-08

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 51.67  E-value: 4.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRehALLAFT--L 81
Cdd:PRK12740  41 ERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TVWRQAekY 111

                         90       100
                 ....*....|....*....|....*..
gi 157101916  82 GVKQLIVgVNKMDSTeppysEARFEEI 108
Cdd:PRK12740 112 GVPRIIF-VNKMDRA-----GADFFRV 132
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 4-94 7.97e-08

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 51.17  E-value: 7.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIdiaLWKfETSKYY----VTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgtgeFEagisknG---Q 70
Cdd:COG1217   50 ERERGITI---LAK-NTAVRYkgvkINIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQ 109

                         90       100
                 ....*....|....*....|....*..
gi 157101916  71 TR---EHALlafTLGVKqLIVGVNKMD 94
Cdd:COG1217  110 TRfvlKKAL---ELGLK-PIVVINKID 132
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 18-120 1.16e-07

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: 49.98  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  18 FETSKYYVTIIDAPGHRDFIKNMITGTS--QADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVKQLIVgVNKMDS 95
Cdd:cd04165   79 CEKSSKVVTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGANAGI-------IGMTKEHLGLALALKVPVFVV-VTKIDM 150

                         90       100
                 ....*....|....*....|....*
gi 157101916  96 TeppySEARFEEIKKEVSNYIKKIG 120
Cdd:cd04165  151 T----PANVLQETLKDLKRLLKSPG 171
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 20-132 6.88e-07

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 48.46  E-value: 6.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916  20 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefeagiskN-----GQTREHALLAFTLGVKQLIVGVNKMD 94
Cdd:PTZ00327 114 TLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAA-----------NescpqPQTSEHLAAVEIMKLKHIIILQNKID 182

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157101916  95 STEPPYSEARFEEIKkevsNYIKkiGYNPAAVAFVPIS 132
Cdd:PTZ00327 183 LVKEAQAQDQYEEIR----NFVK--GTIADNAPIIPIS 214
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 4-131 1.09e-06

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: 47.73  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGeFEAGISKN-GQTREHAL--LAFt 80
Cdd:COG0480   55 EQERGITITSAATTCEWKGHKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG-VEPQTETVwRQADKYGVprIVF- 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157101916  81 lgvkqlivgVNKMDSTeppysEARFEEIkkeVSNYIKKIGYNPAAVaFVPI 131
Cdd:COG0480  133 ---------VNKMDRE-----GADFDRV---LEQLKERLGANPVPL-QLPI 165
PRK10218 PRK10218
translational GTPase TypA;
4-94 3.16e-06

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 46.63  E-value: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGV 83
Cdd:PRK10218  49 EKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGL 121

                         90
                 ....*....|.
gi 157101916  84 KQLIVgVNKMD 94
Cdd:PRK10218 122 KPIVV-INKVD 131
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 4-94 9.90e-06

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: 44.51  E-value: 9.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGV 83
Cdd:cd04170   45 EKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWEFLDDAKL 117

                         90
                 ....*....|.
gi 157101916  84 KQLIVgVNKMD 94
Cdd:cd04170  118 PRIIF-INKMD 127
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
 4-59 1.44e-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: 44.12  E-value: 1.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157101916   4 ERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTG 59
Cdd:cd04169   52 EKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
 4-116 1.68e-05

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 44.24  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITID---IAL-WKFETSKYYV-TIIDAPGHRDFiknmitgT-----SQADC--AVLIVAAGTGeFEAgiskngQT 71
Cdd:COG0481   49 ERERGITIKaqaVRLnYKAKDGETYQlNLIDTPGHVDF-------SyevsrSLAACegALLVVDASQG-VEA------QT 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157101916  72 REHALLAFTLGVKQLIVgVNKMD--STEPpysearfEEIKKEVSNYI 116
Cdd:COG0481  115 LANVYLALENDLEIIPV-INKIDlpSADP-------ERVKQEIEDII 153
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 1-36 1.85e-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: 43.63  E-value: 1.85e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 157101916   1 LKAERERGITIDIALWKFETSKYYVTIIDAPGHRDF 36
Cdd:cd01886   42 MEQERERGITIQSAATTCFWKDHRINIIDTPGHVDF 77
PRK13351 PRK13351
elongation factor G-like protein;
4-94 2.61e-05

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 43.79  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIAL----WKfetsKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGeFEAgiskngQTREHALLAF 79
Cdd:PRK13351  54 EQERGITIESAAtscdWD----NHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTG-VQP------QTETVWRQAD 122

                         90
                 ....*....|....*
gi 157101916  80 TLGVKQLIVgVNKMD 94
Cdd:PRK13351 123 RYGIPRLIF-INKMD 136
infB CHL00189
translation initiation factor 2; Provisional
 8-139 3.05e-05

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 43.67  E-value: 3.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   8 GITIDIA----LWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREhALLAFTLGV 83
Cdd:CHL00189 276 GITQKIGayevEFEYKDENQKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIE-AINYIQAAN 347

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157101916  84 KQLIVGVNKMDSTeppysEARFEEIKKEVSNY---IKKIGynpAAVAFVPISGWHGDNM 139
Cdd:CHL00189 348 VPIIVAINKIDKA-----NANTERIKQQLAKYnliPEKWG---GDTPMIPISASQGTNI 398
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 8-132 6.67e-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: 42.31  E-value: 6.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   8 GITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefeagisKNG---QTRE---HALLAftl 81
Cdd:COG0532   36 GITQHIGAYQVETNGGKITFLDTPGHEAFTAMRARGAQVTDIVILVVAA----------DDGvmpQTIEainHAKAA--- 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157101916  82 GVKqLIVGVNKMDstEPpysEARFEEIKKEVSNYikkiGYNPAA----VAFVPIS 132
Cdd:COG0532  103 GVP-IIVAINKID--KP---GANPDRVKQELAEH----GLVPEEwggdTIFVPVS 147
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 1-119 2.99e-04

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: 39.91  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   1 LKAERERGITID---IALwKFETSK-------YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgeFEaGISKngQ 70
Cdd:cd01885   41 REDEQERGITIKssaISL-YFEYEEekmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDA----VE-GVCV--Q 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157101916  71 TreHALL--AFTLGVKQLIVgVNKMDS--TEP--PYSEA--RFEEIKKEVSNYIKKI 119
Cdd:cd01885  113 T--ETVLrqALEERVKPVLV-INKIDRliLELklSPEEAyqRLLRIVEDVNAIIETY 166
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 4-141 6.90e-04

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


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 38.59  E-value: 6.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157101916   4 ERERGITIDIAL--WKFETSKYYVTIIDAPGHRDFIKNMITGT-----SQADCAVLIVAAGTGEFEAGIskngqTREHAL 76
Cdd:cd00882   26 SDVPGTTRDPDVyvKELDKGKVKLVLVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRESEEDA-----KLLILR 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157101916  77 LAFTLGVKQLIVGvNKMDSTEPPysearfEEIKKEVSNYIKKIGYNPaavaFVPISGWHGDNMLE 141
Cdd:cd00882  101 RLRKEGIPIILVG-NKIDLLEER------EVEELLRLEELAKILGVP----VFEVSAKTGEGVDE 154
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 4-36 1.28e-03

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 38.69  E-value: 1.28e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 157101916   4 ERERGITIDIA----LWKFETSKYYVTIIDAPGHRDF 36
Cdd:PRK07560  64 EQARGITIKAAnvsmVHEYEGKEYLINLIDTPGHVDF 100
 
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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