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Conserved domains on  [gi|1888786757|gb|QNC43825|]
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elongation factor 1-alpha, partial [Gasteruption dilutum]

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 ...
 1-185 3.30e-119

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: 344.42  E-value: 3.30e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVK 80
Cdd:PTZ00141   67 RERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVK 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEPPYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSSKMPWFKgwvverkegkaeGK 160
Cdd:PTZ00141  147 QMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GP 214

                         170       180
                  ....*....|....*....|....*
gi 1888786757 161 CLIEALDAILPPTRPTDKALRLPLQ 185
Cdd:PTZ00141  215 TLLEALDTLEPPKRPVDKPLRLPLQ 239
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-185 3.30e-119

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 344.42  E-value: 3.30e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVK 80
Cdd:PTZ00141   67 RERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVK 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEPPYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSSKMPWFKgwvverkegkaeGK 160
Cdd:PTZ00141  147 QMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GP 214

                         170       180
                  ....*....|....*....|....*
gi 1888786757 161 CLIEALDAILPPTRPTDKALRLPLQ 185
Cdd:PTZ00141  215 TLLEALDTLEPPKRPVDKPLRLPLQ 239
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-172 3.18e-112

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: 318.28  E-value: 3.18e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVK 80
Cdd:cd01883    59 RERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVK 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEPPYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSSKMPWFKGWvverkegkaegk 160
Cdd:cd01883   139 QLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------ 206

                         170
                  ....*....|..
gi 1888786757 161 CLIEALDAILPP 172
Cdd:cd01883   207 TLLEALDSLEPP 218
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-185 9.20e-91

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: 271.42  E-value: 9.20e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVK 80
Cdd:COG5256    67 RERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGIN 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEppYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSSKMPWFKgwvverkegkaeGK 160
Cdd:COG5256   140 QLIVAVNKMDAVN--YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GP 205

                         170       180
                  ....*....|....*....|....*
gi 1888786757 161 CLIEALDAILPPTRPTDKALRLPLQ 185
Cdd:COG5256   206 TLLEALDNLKEPEKPVDKPLRIPIQ 230
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-185 2.15e-86

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: 260.18  E-value: 2.15e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAFTLGVK 80
Cdd:TIGR00483  67 RERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGIN 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEppYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSSKMPWFKgwvverkegkaeGK 160
Cdd:TIGR00483 143 QLIVAINKMDSVN--YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GK 208

                         170       180
                  ....*....|....*....|....*
gi 1888786757 161 CLIEALDAILPPTRPTDKALRLPLQ 185
Cdd:TIGR00483 209 TLLEALDALEPPEKPTDKPLRIPIQ 233
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-172 3.52e-53

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: 167.70  E-value: 3.52e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVK 80
Cdd:pfam00009  51 RERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 qLIVGVNKMDSTeppySESRFEEIKKEVSS-YIKKIGYNPAAVAFVPISGWNGDNMLEvsskmpwfkgwvverkegkaeg 159
Cdd:pfam00009 124 -IIVFINKMDRV----DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT---------------------- 176

                         170
                  ....*....|...
gi 1888786757 160 kcLIEALDAILPP 172
Cdd:pfam00009 177 --LLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-185 3.30e-119

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 344.42  E-value: 3.30e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVK 80
Cdd:PTZ00141   67 RERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVK 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEPPYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSSKMPWFKgwvverkegkaeGK 160
Cdd:PTZ00141  147 QMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GP 214

                         170       180
                  ....*....|....*....|....*
gi 1888786757 161 CLIEALDAILPPTRPTDKALRLPLQ 185
Cdd:PTZ00141  215 TLLEALDTLEPPKRPVDKPLRLPLQ 239
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-172 3.18e-112

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: 318.28  E-value: 3.18e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVK 80
Cdd:cd01883    59 RERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVK 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEPPYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSSKMPWFKGWvverkegkaegk 160
Cdd:cd01883   139 QLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------ 206

                         170
                  ....*....|..
gi 1888786757 161 CLIEALDAILPP 172
Cdd:cd01883   207 TLLEALDSLEPP 218
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-185 9.20e-91

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: 271.42  E-value: 9.20e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVK 80
Cdd:COG5256    67 RERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGIN 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEppYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSSKMPWFKgwvverkegkaeGK 160
Cdd:COG5256   140 QLIVAVNKMDAVN--YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GP 205

                         170       180
                  ....*....|....*....|....*
gi 1888786757 161 CLIEALDAILPPTRPTDKALRLPLQ 185
Cdd:COG5256   206 TLLEALDNLKEPEKPVDKPLRIPIQ 230
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-185 7.95e-89

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 266.41  E-value: 7.95e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKNGQTREHALLAFTLGVK 80
Cdd:PRK12317   66 RERGVTIDLAHKKFETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGIN 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEppYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSSKMPWFKgwvverkegkaeGK 160
Cdd:PRK12317  141 QLIVAINKMDAVN--YDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYN------------GP 206

                         170       180
                  ....*....|....*....|....*
gi 1888786757 161 CLIEALDAILPPTRPTDKALRLPLQ 185
Cdd:PRK12317  207 TLLEALDNLKPPEKPTDKPLRIPIQ 231
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-185 8.18e-89

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 267.34  E-value: 8.18e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVK 80
Cdd:PLN00043   67 RERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVK 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEPPYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSSKMPWFKgwvverkegkaeGK 160
Cdd:PLN00043  147 QMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYK------------GP 214

                         170       180
                  ....*....|....*....|....*
gi 1888786757 161 CLIEALDAILPPTRPTDKALRLPLQ 185
Cdd:PLN00043  215 TLLEALDQINEPKRPSDKPLRLPLQ 239
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-185 2.15e-86

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: 260.18  E-value: 2.15e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAFTLGVK 80
Cdd:TIGR00483  67 RERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGIN 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEppYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSSKMPWFKgwvverkegkaeGK 160
Cdd:TIGR00483 143 QLIVAINKMDSVN--YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GK 208

                         170       180
                  ....*....|....*....|....*
gi 1888786757 161 CLIEALDAILPPTRPTDKALRLPLQ 185
Cdd:TIGR00483 209 TLLEALDALEPPEKPTDKPLRIPIQ 233
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-172 3.52e-53

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: 167.70  E-value: 3.52e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVK 80
Cdd:pfam00009  51 RERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 qLIVGVNKMDSTeppySESRFEEIKKEVSS-YIKKIGYNPAAVAFVPISGWNGDNMLEvsskmpwfkgwvverkegkaeg 159
Cdd:pfam00009 124 -IIVFINKMDRV----DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT---------------------- 176

                         170
                  ....*....|...
gi 1888786757 160 kcLIEALDAILPP 172
Cdd:pfam00009 177 --LLDALDEYLPS 187
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-185 6.68e-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: 174.12  E-value: 6.68e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:COG2895    77 REQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIR 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEppYSESRFEEIKKEVSSYIKKIGYNPaaVAFVPISGWNGDNMLEVSSKMPWFKgwvverkegkaeGK 160
Cdd:COG2895   150 HVVVAVNKMDLVD--YSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWYD------------GP 213

                         170       180
                  ....*....|....*....|....*
gi 1888786757 161 CLIEALDAILPPTRPTDKALRLPLQ 185
Cdd:COG2895   214 TLLEHLETVEVAEDRNDAPFRFPVQ 238
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-169 8.76e-50

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: 159.66  E-value: 8.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:cd04166    60 REQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIR 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEppYSESRFEEIKKEVSSYIKKIGYNPaaVAFVPISGWNGDNMLEVSSKMPWFKgwvverkegkaeGK 160
Cdd:cd04166   133 HVVVAVNKMDLVD--YDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYK------------GP 196


                  ....*....
gi 1888786757 161 CLIEALDAI 169
Cdd:cd04166   197 TLLEHLETV 205
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-185 1.55e-42

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 147.75  E-value: 1.55e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:PRK05124   89 REQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIK 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEppYSESRFEEIKKEVSSYIKKIGYNPaAVAFVPISGWNGDNMLEVSSKMPWFkgwvverkegkaEGK 160
Cdd:PRK05124  162 HLVVAVNKMDLVD--YSEEVFERIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWY------------SGP 226

                         170       180
                  ....*....|....*....|....*
gi 1888786757 161 CLIEALDAILPPTRPTDKALRLPLQ 185
Cdd:PRK05124  227 TLLEVLETVDIQRVVDAQPFRFPVQ 251
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-185 3.58e-41

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: 142.90  E-value: 3.58e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:TIGR02034  62 REQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIR 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEppYSESRFEEIKKEVSSYIKKIGynPAAVAFVPISGWNGDNMLEVSSKMPWFkgwvverkegkaEGK 160
Cdd:TIGR02034 135 HVVLAVNKMDLVD--YDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY------------SGP 198

                         170       180
                  ....*....|....*....|....*
gi 1888786757 161 CLIEALDAILPPTRPTDKALRLPLQ 185
Cdd:TIGR02034 199 TLLEILETVEVERDAQDLPLRFPVQ 223
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-185 3.40e-40

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 143.53  E-value: 3.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:PRK05506   86 REQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIR 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEppYSESRFEEIKKEVSSYIKKIGYnpAAVAFVPISGWNGDNMLEVSSKMPWFkgwvverkegkaEGK 160
Cdd:PRK05506  159 HVVLAVNKMDLVD--YDQEVFDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWY------------EGP 222

                         170       180
                  ....*....|....*....|....*
gi 1888786757 161 CLIEALDAILPPTRPTDKALRLPLQ 185
Cdd:PRK05506  223 SLLEHLETVEIASDRNLKDFRFPVQ 247
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-137 1.61e-38

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: 130.11  E-value: 1.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFtLGVK 80
Cdd:cd00881    44 RERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGL 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTeppySESRFEEIKKEVSSYIKKIGY---NPAAVAFVPISGWNGDNMLE 137
Cdd:cd00881   116 PIIVAVNKIDRV----GEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-172 2.45e-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: 104.20  E-value: 2.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:cd01884    47 KARGITINTAHVEYETANRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVP 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEppySESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGdnmLEvsskmpwfkgwvvERKEGKAEGK 160
Cdd:cd01884   120 YIVVFLNKADMVD---DEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKA---LE-------------GDDPNKWVDK 180

                         170
                  ....*....|....
gi 1888786757 161 C--LIEALDAILPP 172
Cdd:cd01884   181 IleLLDALDSYIPT 194
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-183 3.61e-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: 3.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:COG0050    57 KERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEPPYSESRFE-EIKKEVSSYikkiGYNPAAVAFVPISGWNGdnmLEVSSKMPWFKGwVVErkegkaeg 159
Cdd:COG0050   130 YIVVFLNKCDMVDDEELLELVEmEVRELLSKY----GFPGDDTPIIRGSALKA---LEGDPDPEWEKK-ILE-------- 193

                         170       180
                  ....*....|....*....|....*
gi 1888786757 160 kcLIEALDAILP-PTRPTDKALRLP 183
Cdd:COG0050   194 --LMDAVDSYIPePERDTDKPFLMP 216
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-185 1.93e-26

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 103.49  E-value: 1.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:PRK12736   57 KERGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEppySESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGW---NGDnmlevsskmpwfkgwvvERKEGKA 157
Cdd:PRK12736  130 YLVVFLNKVDLVD---DEELLELVEMEVRELLSEYDFPGDDIPVIRGSALkalEGD-----------------PKWEDAI 189

                         170       180
                  ....*....|....*....|....*....
gi 1888786757 158 EGkcLIEALDAILP-PTRPTDKALRLPLQ 185
Cdd:PRK12736  190 ME--LMDAVDEYIPtPERDTDKPFLMPVE 216
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-183 9.12e-25

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 99.11  E-value: 9.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:PRK00049   57 KARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEPPYSESRFE-EIKKEVSSYikkigynpaavafvpisGWNGDNmlevsskMPWFKGWVVERKEGKAEG 159
Cdd:PRK00049  130 YIVVFLNKCDMVDDEELLELVEmEVRELLSKY-----------------DFPGDD-------TPIIRGSALKALEGDDDE 185

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1888786757 160 KC------LIEALDAILP-PTRPTDKALRLP 183
Cdd:PRK00049  186 EWekkileLMDAVDSYIPtPERAIDKPFLMP 216
tufA CHL00071
elongation factor Tu
 1-185 1.50e-24

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 98.49  E-value: 1.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:CHL00071   57 KARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEppySESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGdnmLEVSSKMP-WFKG---WVVERKEgk 156
Cdd:CHL00071  130 NIVVFLNKEDQVD---DEELLELVELEVRELLSKYDFPGDDIPIVSGSALLA---LEALTENPkIKRGenkWVDKIYN-- 201

                         170       180       190
                  ....*....|....*....|....*....|
gi 1888786757 157 aegkcLIEALDAILP-PTRPTDKALRLPLQ 185
Cdd:CHL00071  202 -----LMDAVDSYIPtPERDTDKPFLMAIE 226
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-185 5.74e-24

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 97.20  E-value: 5.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:PLN03127  106 KARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVP 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEPPYSESRFEEIKKEVSSYIKkigynpaavafvpisgWNGDNmlevsskMPWFKGWVVERKEGKAE-- 158
Cdd:PLN03127  179 SLVVFLNKVDVVDDEELLELVEMELRELLSFYK----------------FPGDE-------IPIIRGSALSALQGTNDei 235

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1888786757 159 GKC----LIEALDAILP-PTRPTDKALRLPLQ 185
Cdd:PLN03127  236 GKNailkLMDAVDEYIPePVRVLDKPFLMPIE 267
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-185 7.04e-24

translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 96.38  E-value: 7.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:TIGR00485  57 KARGITINTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMD-STEPPYSESRFEEIKKEVSSYikkigynpaavafvpisGWNGDNmlevsskMPWFKGWVVERKEGKAEG 159
Cdd:TIGR00485 130 YIVVFLNKCDmVDDEELLELVEMEVRELLSQY-----------------DFPGDD-------TPIIRGSALKALEGDAEW 185

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1888786757 160 KC----LIEALDAILP-PTRPTDKALRLPLQ 185
Cdd:TIGR00485 186 EAkileLMDAVDEYIPtPEREIDKPFLLPIE 216
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-183 9.54e-24

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 96.06  E-value: 9.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:PRK12735   57 KARGITINTSHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEPPYSESRFE-EIKKEVSSYikkigynpaavafvpisGWNGDNmlevsskMPWFKGWVVERKEGKAEG 159
Cdd:PRK12735  130 YIVVFLNKCDMVDDEELLELVEmEVRELLSKY-----------------DFPGDD-------TPIIRGSALKALEGDDDE 185

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1888786757 160 KC------LIEALDAILP-PTRPTDKALRLP 183
Cdd:PRK12735  186 EWeakileLMDAVDSYIPePERAIDKPFLMP 216
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-133 3.86e-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: 87.66  E-value: 3.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDI--ALWKFETAKYyVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREHALLAFTLG 78
Cdd:cd04171    31 KKRGITIDLgfAYLDLPDGKR-LGFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLG 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1888786757  79 VKQLIVGVNKMDSTEppysESRFEEIKKEVSSYIKKIGYNPAAVafVPISGWNGD 133
Cdd:cd04171   103 IKKGLVVLTKADLVD----EDRLELVEEEILELLAGTFLADAPI--FPVSSVTGE 151
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 1-183 8.30e-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: 8.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDI--ALWKFEtAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREH-ALLAFtL 77
Cdd:COG3276    32 KKRGITIDLgfAYLPLP-DGRRLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAA-----DEGVMP--QTREHlAILDL-L 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  78 GVKQLIVGVNKMDSTEPpyseSRFEEIKKEVSSYIKKigynpaavafvpiSGWNGDNMLEVSSKmpwfkgwvveRKEGKA 157
Cdd:COG3276   103 GIKRGIVVLTKADLVDE----EWLELVEEEIRELLAG-------------TFLEDAPIVPVSAV----------TGEGID 155

                         170       180
                  ....*....|....*....|....*...
gi 1888786757 158 EgkcLIEALDAIL--PPTRPTDKALRLP 183
Cdd:COG3276   156 E---LRAALDALAaaVPARDADGPFRLP 180
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-177 6.11e-21

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 88.90  E-value: 6.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:PLN03126  126 RARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVP 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  81 QLIVGVNKMDSTEppySESRFEEIKKEVSSYIKKIGYNPAAvafVPISGWNGDNMLEVSSKMPwfkgwVVERKEGKAEGK 160
Cdd:PLN03126  199 NMVVFLNKQDQVD---DEELLELVELEVRELLSSYEFPGDD---IPIISGSALLALEALMENP-----NIKRGDNKWVDK 267

                         170       180
                  ....*....|....*....|
gi 1888786757 161 C--LIEALDAILP-PTRPTD 177
Cdd:PLN03126  268 IyeLMDAVDSYIPiPQRQTD 287
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-138 4.98e-19

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: 83.77  E-value: 4.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:TIGR00475  32 KKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDADEGVMT-------QTGEHLAVLDLLGIP 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1888786757  81 QLIVGVNKMDSTEppysESRFEEIKKEVSSYIKKIGYNPAAVAFVpISGWNGDNMLEV 138
Cdd:TIGR00475 105 HTIVVITKADRVN----EEEIKRTEMFMKQILNSYIFLKNAKIFK-TSAKTGQGIGEL 157
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 1-125 1.08e-11

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 62.38  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDI--ALWKFETAKYyVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFeagisknGQTREH-ALLAFTl 77
Cdd:PRK10512   32 KKRGMTIDLgyAYWPQPDGRV-LGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHlAILQLT- 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1888786757  78 GVKQLIVGVNKMDSTEPPysesRFEEIKKEVSSYIKKIGYnPAAVAFV 125
Cdd:PRK10512  103 GNPMLTVALTKADRVDEA----RIAEVRRQVKAVLREYGF-AEAKLFV 145
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-128 6.82e-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: 58.53  E-value: 6.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKF--------------ETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQ 66
Cdd:cd01889    36 QERGITLDLGFSSFevdkpkhlednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQ 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1888786757  67 TREHALLAFTLGvKQLIVGVNKMDSTEPPYSESRFEEIKKEVSSYIKKIgyNPAAVAFVPIS 128
Cdd:cd01889   109 TAECLVIGELLC-KPLIVVLNKIDLIPEEERKRKIEKMKKRLQKTLEKT--RLKDSPIIPVS 167
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 1-112 2.14e-09

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: 54.94  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRehaLLAFTLgvK 80
Cdd:cd04168    46 RQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTR---ILFRLL--R 113

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1888786757  81 QL----IVGVNKMDsTEPPYSESRFEEIKKEVSSYI 112
Cdd:cd04168   114 KLniptIIFVNKID-RAGADLEKVYQEIKEKLSPDI 148
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 21-135 4.58e-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: 52.86  E-value: 4.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  21 VTIIDAPGHRDFiKNMIT-GTSQADCAVLIVAAGTGeFEAgiskngQTRE---HALLAFTlgvkQLIVGVNKMDstEPPY 96
Cdd:cd01887    51 ITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVAINKID--KPYG 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1888786757  97 SESRFEEIKKEVSSY---IKKIGYNpaaVAFVPISGWNGDNM 135
Cdd:cd01887   117 TEADPERVKNELSELglvGEEWGGD---VSIVPISAKTGEGI 155
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 3-135 7.16e-09

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 54.09  E-value: 7.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   3 RGITI-----DIALWKFETAK---YYVT------------------IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGE 56
Cdd:PRK04000   43 RGITIrlgyaDATIRKCPDCEepeAYTTepkcpncgsetellrrvsFVDAPGHETLMATMLSGAALMDGAILVIAANEPC 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  57 FEAgiskngQTREHaLLAFT-LGVKQLIVGVNKMDSTEPPYSESRFEEIKKEVSSYIkkigynpAAVA-FVPISGWNGDN 134
Cdd:PRK04000  123 PQP------QTKEH-LMALDiIGIKNIVIVQNKIDLVSKERALENYEQIKEFVKGTV-------AENApIIPVSALHKVN 188


                  .
gi 1888786757 135 M 135
Cdd:PRK04000  189 I 189
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 21-143 1.30e-08

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


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 52.27  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  21 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefeagiskN-----GQTREHaLLAF-TLGVKQLIVGVNKMDSTEP 94
Cdd:cd01888    79 VSFVDCPGHEILMATMLSGAAVMDGALLLIAA-----------NepcpqPQTSEH-LAALeIMGLKHIIILQNKIDLVKE 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1888786757  95 PYSESRFEEIKKevssYIKKIGYNPAAVafVPIS---GWNGDNMLEVSSKMP 143
Cdd:cd01888   147 EQALENYEQIKE----FVKGTIAENAPI--IPISaqlKYNIDVLCEYIVKKI 192
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 1-108 1.49e-07

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: 49.13  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIdiaLWKfETAKYY----VTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAGTGEFEagiskngQTR-- 68
Cdd:cd01891    47 RERGITI---LAK-NTAITYkdtkINIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP-------QTRfv 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1888786757  69 -EHALLAftlGVKqLIVGVNKMDSteppySESRFEEIKKEV 108
Cdd:cd01891   110 lKKALEA---GLK-PIVVINKIDR-----PDARPEEVVDEV 141
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 21-116 1.69e-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: 49.21  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  21 VTIIDAPGHRDFIKNMITGTS--QADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVKQLIVgVNKMDSTeppySE 98
Cdd:cd04165    86 VTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGANAGI-------IGMTKEHLGLALALKVPVFVV-VTKIDMT----PA 153

                          90
                  ....*....|....*...
gi 1888786757  99 SRFEEIKKEVSSYIKKIG 116
Cdd:cd04165   154 NVLQETLKDLKRLLKSPG 171
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 1-138 2.58e-07

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: 48.30  E-value: 2.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITID---IAL-WKFETAKYYV-TIIDAPGHRDFikNMITGTSQADC--AVLIVAAGTGeFEAgiskngQTREHALL 73
Cdd:cd01890    44 RERGITIKaqaVRLfYKAKDGEEYLlNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------QTLANFYL 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1888786757  74 AFTLGVKQLIVgVNKMD--STEPpysesrfEEIKKEVSSYikkIGYNPAAVafVPISGWNGDNMLEV 138
Cdd:cd01890   115 ALENNLEIIPV-INKIDlpAADP-------DRVKQEIEDV---LGLDASEA--ILVSAKTGLGVEDL 168
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 16-137 4.06e-07

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 48.85  E-value: 4.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757  16 TAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefeagiskN-----GQTREHALLAFTLGVKQLIVGVNKMD 90
Cdd:PTZ00327  114 TLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAA-----------NescpqPQTSEHLAAVEIMKLKHIIILQNKID 182

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1888786757  91 STEPPYSESRFEEIKKEVSSYIKKigynpaAVAFVPIS---GWNGDNMLE 137
Cdd:PTZ00327  183 LVKEAQAQDQYEEIRNFVKGTIAD------NAPIIPISaqlKYNIDVVLE 226
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 1-90 4.98e-07

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 48.86  E-value: 4.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIdialwkfeTAK--------YYVTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgtgeFEagisknG- 65
Cdd:COG1217    51 RERGITI--------LAKntavrykgVKINIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------Gp 106

                          90       100       110
                  ....*....|....*....|....*....|
gi 1888786757  66 --QTR---EHALlafTLGVKqLIVGVNKMD 90
Cdd:COG1217   107 mpQTRfvlKKAL---ELGLK-PIVVINKID 132
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
1-90 7.92e-07

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 48.20  E-value: 7.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRehALLAFT--LG 78
Cdd:PRK12740   42 RERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TVWRQAekYG 112

                          90
                  ....*....|..
gi 1888786757  79 VKQLIVgVNKMD 90
Cdd:PRK12740  113 VPRIIF-VNKMD 123
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 1-145 1.45e-06

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: 46.49  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITI-----DIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTgefeaGISKNGQT--REhall 73
Cdd:cd04167    48 QERGISIksnpiSLVLEDSKGKSYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTSVTERliRH---- 118

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1888786757  74 AFTLGVKQLIVgVNKMDS--TE---PPYSESR-FEEIKKEVSSYIKKIGyNPAAVAFVPISGwngdNMLEVSSKMPWF 145
Cdd:cd04167   119 AIQEGLPMVLV-INKIDRliLElklPPTDAYYkLRHTIDEINNYIASFS-TTEGFLVSPELG----NVLFASSKFGFC 190
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 1-55 1.26e-05

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: 44.65  E-value: 1.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTG 55
Cdd:COG0480    56 QERGITITSAATTCEWKGHKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG 110
PRK10218 PRK10218
translational GTPase TypA;
1-90 2.70e-05

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 43.54  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVK 80
Cdd:PRK10218   50 KERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLK 122

                          90
                  ....*....|
gi 1888786757  81 QLIVgVNKMD 90
Cdd:PRK10218  123 PIVV-INKVD 131
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
 1-138 5.79e-05

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 42.70  E-value: 5.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITID---IALwkFETAK----YYVTIIDAPGHRDFiknmitgT-----SQADC--AVLIVAAGTGeFEAgiskngQ 66
Cdd:COG0481    50 RERGITIKaqaVRL--NYKAKdgetYQLNLIDTPGHVDF-------SyevsrSLAACegALLVVDASQG-VEA------Q 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1888786757  67 TREHALLAFTLGVKQLIVgVNKMD--STEPpysesrfEEIKKEVssyIKKIGYNPAAVafVPISGWNGDNMLEV 138
Cdd:COG0481   114 TLANVYLALENDLEIIPV-INKIDlpSADP-------ERVKQEI---EDIIGIDASDA--ILVSAKTGIGIEEI 174
infB CHL00189
translation initiation factor 2; Provisional
 4-137 7.64e-05

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 42.51  E-value: 7.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   4 GITIDIA----LWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREhALLAFTLGV 79
Cdd:CHL00189  276 GITQKIGayevEFEYKDENQKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIE-AINYIQAAN 347

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1888786757  80 KQLIVGVNKMDSTeppysESRFEEIKKEVSSY---IKKIGynpAAVAFVPIS---GWNGDNMLE 137
Cdd:CHL00189  348 VPIIVAINKIDKA-----NANTERIKQQLAKYnliPEKWG---GDTPMIPISasqGTNIDKLLE 403
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 1-90 8.31e-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: 41.81  E-value: 8.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVK 80
Cdd:cd04170    46 KKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWEFLDDAKLP 118

                          90
                  ....*....|
gi 1888786757  81 QLIVgVNKMD 90
Cdd:cd04170   119 RIIF-INKMD 127
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
 1-55 9.02e-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: 41.81  E-value: 9.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1888786757   1 RERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTG 55
Cdd:cd04169    53 KQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
PRK13351 PRK13351
elongation factor G-like protein;
1-90 1.84e-04

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 41.09  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   1 RERGITIDIAL----WKfetaKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGeFEAgiskngQTREHALLAFT 76
Cdd:PRK13351   55 QERGITIESAAtscdWD----NHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTG-VQP------QTETVWRQADR 123

                          90
                  ....*....|....
gi 1888786757  77 LGVKQLIVgVNKMD 90
Cdd:PRK13351  124 YGIPRLIF-INKMD 136
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 5-142 2.22e-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: 39.75  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   5 ITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGT-----SQADCAVLIVAAGTGEFEAGIskngqTREHALLAFTLGV 79
Cdd:cd00882    33 RDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRESEEDA-----KLLILRRLRKEGI 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1888786757  80 KQLIVGvNKMDSTEPPysesrfEEIKKEVSSYIKKIGYNPaavaFVPISGWNGDNMLEVSSKM 142
Cdd:cd00882   108 PIILVG-NKIDLLEER------EVEELLRLEELAKILGVP----VFEVSAKTGEGVDELFEKL 159
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 1-32 5.75e-04

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: 39.40  E-value: 5.75e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1888786757   1 RERGITIDIA----LWKfetaKYYVTIIDAPGHRDF 32
Cdd:cd01886    46 RERGITIQSAattcFWK----DHRINIIDTPGHVDF 77
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 4-137 2.03e-03

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


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 38.07  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888786757   4 GITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefeagisKNG---QTRE---HALLAftl 77
Cdd:COG0532    36 GITQHIGAYQVETNGGKITFLDTPGHEAFTAMRARGAQVTDIVILVVAA----------DDGvmpQTIEainHAKAA--- 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1888786757  78 GVKqLIVGVNKMDstEPpysESRFEEIKKEVSSYikkiGYNPAA----VAFVPIS---GWNGDNMLE 137
Cdd:COG0532   103 GVP-IIVAINKID--KP---GANPDRVKQELAEH----GLVPEEwggdTIFVPVSaktGEGIDELLE 159
 
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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