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Conserved domains on  [gi|349801457|gb|AEQ18808|]
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elongation factor-1 alpha, partial [Xystocheir brachymacris]

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 ...
 1-157 1.32e-98

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


The actual alignment was detected with superfamily member cd01883:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 219  Bit Score: 282.84  E-value: 1.32e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:cd01883   72 FETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVT 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 349801457  81 PPYSESRFDEIRKEVSSYIKKIGYNPVAVAFVPISGWNGDNMLEPSPNMAWHKGWsverkegnangkTLLEALDAVV 157
Cdd:cd01883  152 VNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLE 216
 
Name Accession Description Interval E-value
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-157 1.32e-98

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: 282.84  E-value: 1.32e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:cd01883   72 FETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVT 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 349801457  81 PPYSESRFDEIRKEVSSYIKKIGYNPVAVAFVPISGWNGDNMLEPSPNMAWHKGWsverkegnangkTLLEALDAVV 157
Cdd:cd01883  152 VNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLE 216
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-158 1.01e-93

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 278.55  E-value: 1.01e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:PTZ00141  80 FETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKT 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 349801457  81 PPYSESRFDEIRKEVSSYIKKIGYNPVAVAFVPISGWNGDNMLEPSPNMAWHKgwsverkegnanGKTLLEALDAVVA 158
Cdd:PTZ00141 160 VNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GPTLLEALDTLEP 225
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-155 1.04e-70

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: 218.65  E-value: 1.04e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:COG5256   80 FETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 349801457  81 ppYSESRFDEIRKEVSSYIKKIGYNPVAVAFVPISGWNGDNMLEPSPNMAWHkgwsverkegnaNGKTLLEALDA 155
Cdd:COG5256  153 --YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWY------------NGPTLLEALDN 213
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-156 8.16e-65

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: 203.94  E-value: 8.16e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457    1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:TIGR00483  80 FETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 349801457   81 ppYSESRFDEIRKEVSSYIKKIGYNPVAVAFVPISGWNGDNMLEPSPNMAWHKgwsverkegnanGKTLLEALDAV 156
Cdd:TIGR00483 156 --YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDAL 217
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-124 6.10e-43

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: 140.35  E-value: 6.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457    1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAYTLGVKqLIVGVNKMDTTe 80
Cdd:pfam00009  64 FETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV- 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 349801457   81 ppySESRFDEIRKEVSS-YIKKIGYNPVAVAFVPISGWNGDNMLE 124
Cdd:pfam00009 135 ---DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT 176
 
Name Accession Description Interval E-value
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-157 1.32e-98

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: 282.84  E-value: 1.32e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:cd01883   72 FETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVT 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 349801457  81 PPYSESRFDEIRKEVSSYIKKIGYNPVAVAFVPISGWNGDNMLEPSPNMAWHKGWsverkegnangkTLLEALDAVV 157
Cdd:cd01883  152 VNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLE 216
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-158 1.01e-93

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 278.55  E-value: 1.01e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:PTZ00141  80 FETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKT 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 349801457  81 PPYSESRFDEIRKEVSSYIKKIGYNPVAVAFVPISGWNGDNMLEPSPNMAWHKgwsverkegnanGKTLLEALDAVVA 158
Cdd:PTZ00141 160 VNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GPTLLEALDTLEP 225
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-155 1.04e-70

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: 218.65  E-value: 1.04e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:COG5256   80 FETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 349801457  81 ppYSESRFDEIRKEVSSYIKKIGYNPVAVAFVPISGWNGDNMLEPSPNMAWHkgwsverkegnaNGKTLLEALDA 155
Cdd:COG5256  153 --YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWY------------NGPTLLEALDN 213
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-156 2.52e-70

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 218.42  E-value: 2.52e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:PLN00043  80 FETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATT 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 349801457  81 PPYSESRFDEIRKEVSSYIKKIGYNPVAVAFVPISGWNGDNMLEPSPNMAWHKgwsverkegnanGKTLLEALDAV 156
Cdd:PLN00043 160 PKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYK------------GPTLLEALDQI 223
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-155 6.77e-70

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 216.72  E-value: 6.77e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:PRK12317  79 FETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVN 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 349801457  81 ppYSESRFDEIRKEVSSYIKKIGYNPVAVAFVPISGWNGDNMLEPSPNMAWHkgwsverkegnaNGKTLLEALDA 155
Cdd:PRK12317 154 --YDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWY------------NGPTLLEALDN 214
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-156 8.16e-65

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: 203.94  E-value: 8.16e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457    1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:TIGR00483  80 FETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 349801457   81 ppYSESRFDEIRKEVSSYIKKIGYNPVAVAFVPISGWNGDNMLEPSPNMAWHKgwsverkegnanGKTLLEALDAV 156
Cdd:TIGR00483 156 --YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDAL 217
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-156 5.14e-46

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: 154.86  E-value: 5.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKF-YItIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDTT 79
Cdd:COG2895   90 FSTPKRkFI-IADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLV 161

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 349801457  80 EppYSESRFDEIRKEVSSYIKKIGYNPvaVAFVPISGWNGDNMLEPSPNMAWHKgwsverkegnanGKTLLEALDAV 156
Cdd:COG2895  162 D--YSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWYD------------GPTLLEHLETV 222
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-156 2.95e-45

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: 147.33  E-value: 2.95e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:cd04166   73 FSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD 145

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 349801457  81 ppYSESRFDEIRKEVSSYIKKIGYNPvaVAFVPISGWNGDNMLEPSPNMAWHKgwsverkegnanGKTLLEALDAV 156
Cdd:cd04166  146 --YDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETV 205
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-124 6.10e-43

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: 140.35  E-value: 6.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457    1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAYTLGVKqLIVGVNKMDTTe 80
Cdd:pfam00009  64 FETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV- 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 349801457   81 ppySESRFDEIRKEVSS-YIKKIGYNPVAVAFVPISGWNGDNMLE 124
Cdd:pfam00009 135 ---DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT 176
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-156 1.70e-36

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 130.80  E-value: 1.70e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:PRK05124 102 FSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVD 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 349801457  81 ppYSESRFDEIRKEVSSYIKKIGYNPvAVAFVPISGWNGDNMLEPSPNMAWHKgwsverkegnanGKTLLEALDAV 156
Cdd:PRK05124 175 --YSEEVFERIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWYS------------GPTLLEVLETV 235
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-156 1.16e-33

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 124.27  E-value: 1.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:PRK05506  99 FATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVD 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 349801457  81 ppYSESRFDEIRKEVSSYIKKIGYNpvAVAFVPISGWNGDNMLEPSPNMAWHKgwsverkegnanGKTLLEALDAV 156
Cdd:PRK05506 172 --YDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWYE------------GPSLLEHLETV 231
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-156 2.29e-32

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: 118.63  E-value: 2.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457    1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:TIGR02034  75 FSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVD 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 349801457   81 ppYSESRFDEIRKEVSSYIKKIGYNPvaVAFVPISGWNGDNMLEPSPNMAWHKgwsverkegnanGKTLLEALDAV 156
Cdd:TIGR02034 148 --YDEEVFENIKKDYLAFAEQLGFRD--VTFIPLSALKGDNVVSRSESMPWYS------------GPTLLEILETV 207
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-124 6.19e-30

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 107.38  E-value: 6.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAyTLGVKQLIVGVNKMDTTe 80
Cdd:cd00881   57 FEWPKRRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIA-LAGGLPIIVAVNKIDRV- 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 349801457  81 ppySESRFDEIRKEVSSYIKKIGYNPVA---VAFVPISGWNGDNMLE 124
Cdd:cd00881  128 ---GEEDFDEVLREIKELLKLIGFTFLKgkdVPIIPISALTGEGIEE 171
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-77 3.63e-22

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: 87.64  E-value: 3.63e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMD 77
Cdd:cd01884   60 YETANRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKAD 129
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-83 3.19e-20

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: 85.59  E-value: 3.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:COG0050   70 YETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVD 142


                 ...
gi 349801457  81 PPY 83
Cdd:COG0050  143 DEE 145
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-77 8.34e-19

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 81.53  E-value: 8.34e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMD 77
Cdd:PRK12736  70 YETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKVD 139
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 10-98 2.80e-18

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: 76.88  E-value: 2.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457  10 IIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREHALLAYTLGVKQLIVGVNKMDTTEPPYSESRFD 89
Cdd:cd04171   54 FIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLVDEDRLELVEE 126


                 ....*....
gi 349801457  90 EIRKEVSSY 98
Cdd:cd04171  127 EILELLAGT 135
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-77 3.58e-18

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 79.85  E-value: 3.58e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMD 77
Cdd:PRK00049  70 YETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCD 139
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-82 1.14e-17

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 78.71  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:PLN03127 119 YETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVD 191


                 ..
gi 349801457  81 PP 82
Cdd:PLN03127 192 DE 193
tufA CHL00071
elongation factor Tu
 1-98 2.08e-17

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 77.69  E-value: 2.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMD-TT 79
Cdd:CHL00071  70 YETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDqVD 142

                         90
                 ....*....|....*....
gi 349801457  80 EPPYSESRFDEIRKEVSSY 98
Cdd:CHL00071 143 DEELLELVELEVRELLSKY 161
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-77 2.55e-17

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 77.19  E-value: 2.55e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMD 77
Cdd:PRK12735  70 YETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCD 139
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-98 4.53e-17

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: 76.74  E-value: 4.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457    1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMD-TT 79
Cdd:TIGR00485  70 YETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDmVD 142

                          90
                  ....*....|....*....
gi 349801457   80 EPPYSESRFDEIRKEVSSY 98
Cdd:TIGR00485 143 DEELLELVEMEVRELLSQY 161
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-124 1.48e-16

selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 75.68  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457    1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:TIGR00475  45 FPLPDYRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDADEGVMT-------QTGEHLAVLDLLGIPHTIVVITKADRVN 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 349801457   81 ppysESRFDEIRKEVSSYIKKIGYNPVAVAFVpISGWNGDNMLE 124
Cdd:TIGR00475 118 ----EEEIKRTEMFMKQILNSYIFLKNAKIFK-TSAKTGQGIGE 156
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 8-97 1.39e-15

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: 72.64  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   8 ITIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREH-ALLAyTLGVKQLIVGVNKMDTTEPPYSES 86
Cdd:COG3276   53 LGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAA-----DEGVMP--QTREHlAILD-LLGIKRGIVVLTKADLVDEEWLEL 124

                         90
                 ....*....|.
gi 349801457  87 RFDEIRKEVSS 97
Cdd:COG3276  125 VEEEIRELLAG 135
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-98 5.48e-15

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 71.18  E-value: 5.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   1 FETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDTTE 80
Cdd:PLN03126 139 YETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD 211

                         90       100
                 ....*....|....*....|..
gi 349801457  81 ppySESRFD----EIRKEVSSY 98
Cdd:PLN03126 212 ---DEELLElvelEVRELLSSY 230
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 11-112 1.75e-10

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 58.14  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457  11 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFeagisknGQTREH-ALLAYTlGVKQLIVGVNKMDTTEPPysesRFD 89
Cdd:PRK10512  56 IDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHlAILQLT-GNPMLTVALTKADRVDEA----RIA 123

                         90       100
                 ....*....|....*....|...
gi 349801457  90 EIRKEVSSYIKKIGYNPVAVaFV 112
Cdd:PRK10512 124 EVRRQVKAVLREYGFAEAKL-FV 145
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 8-122 2.06e-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: 53.24  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   8 ITIIDAPGHRDFiKNMIT-GTSQADCAVLIVAAGTGeFEAgiskngQTRE---HALLAYTlgvkQLIVGVNKMDttEPPY 83
Cdd:cd01887   51 ITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVAINKID--KPYG 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 349801457  84 SESRFDEIRKEVSSY---IKKIGYNpvaVAFVPISGWNGDNM 122
Cdd:cd01887  117 TEADPERVKNELSELglvGEEWGGD---VSIVPISAKTGEGI 155
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 8-122 3.17e-08

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 51.39  E-value: 3.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   8 ITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAgiskngQTREHALLAYTLGVKQLIVGVNKMDTTEPPYSESR 87
Cdd:PRK04000  87 VSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEHLMALDIIGIKNIVIVQNKIDLVSKERALEN 160

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 349801457  88 FDEIRKEVSSYIKKIGynPVavafVPISGWNGDNM 122
Cdd:PRK04000 161 YEQIKEFVKGTVAENA--PI----IPVSALHKVNI 189
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 8-103 4.15e-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: 47.67  E-value: 4.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   8 ITIIDAPGHRDFIKNMITGTS--QADCAVLIVAAGTGEfeagiskNGQTREHALLAYTLGVKQLIVgVNKMDTTeppySE 85
Cdd:cd04165   86 VTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGANAGI-------IGMTKEHLGLALALKVPVFVV-VTKIDMT----PA 153

                         90
                 ....*....|....*...
gi 349801457  86 SRFDEIRKEVSSYIKKIG 103
Cdd:cd04165  154 NVLQETLKDLKRLLKSPG 171
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 3-124 8.24e-07

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 47.31  E-value: 8.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   3 TPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefeagiskN-----GQTREHALLAYTLGVKQLIVGVNKMD 77
Cdd:PTZ00327 114 TLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAA-----------NescpqPQTSEHLAAVEIMKLKHIIILQNKID 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 349801457  78 TTEPPYSESRFDEIRKEVSSYIKKigynpvAVAFVPIS---GWNGDNMLE 124
Cdd:PTZ00327 183 LVKEAQAQDQYEEIRNFVKGTIAD------NAPIIPISaqlKYNIDVVLE 226
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 8-99 2.89e-05

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: 42.61  E-value: 2.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   8 ITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRE--HALLAYTLGVkqlIVGVNKMDtTEPPYSE 85
Cdd:cd04168   66 VNIIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTRIlfRLLRKLNIPT---IIFVNKID-RAGADLE 134

                         90
                 ....*....|....
gi 349801457  86 SRFDEIRKEVSSYI 99
Cdd:cd04168  135 KVYQEIKEKLSPDI 148
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 8-130 5.31e-05

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: 41.43  E-value: 5.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   8 ITIIDAPGHRDF------IKNMitgtsqADCAVLIVAAGTGEFEagiskngQTR---EHALLAytlGVKqLIVGVNKMDT 78
Cdd:cd01891   67 INIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP-------QTRfvlKKALEA---GLK-PIVVINKIDR 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 349801457  79 teppySESRFDEIRKEVSSYIKKIGYNPVAVAFvPI------SGWNGDNMLEPSPNMA 130
Cdd:cd01891  130 -----PDARPEEVVDEVFDLFLELNATDEQLDF-PIvyasakNGWASLNLDDPSEDLD 181
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
8-121 9.69e-05

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 41.26  E-value: 9.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   8 ITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRehALLAYT--LGVKQLIVgVNKMDTTeppysE 85
Cdd:PRK12740  62 INLIDTPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TVWRQAekYGVPRIIF-VNKMDRA-----G 126

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 349801457  86 SRFDEIRKEVSSyikKIGYNPVAVaFVPIsgWNGDN 121
Cdd:PRK12740 127 ADFFRVLAQLQE---KLGAPVVPL-QLPI--GEGDD 156
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 2-124 4.16e-04

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: 39.23  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   2 ETPKFYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefeagisKNG---QTRE---HALLAytlGVKqLIVGVNK 75
Cdd:COG0532   47 ETNGGKITFLDTPGHEAFTAMRARGAQVTDIVILVVAA----------DDGvmpQTIEainHAKAA---GVP-IIVAINK 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 349801457  76 MDTteppySESRFDEIRKEVSSYikkiGYNPVA----VAFVPIS---GWNGDNMLE 124
Cdd:COG0532  113 IDK-----PGANPDRVKQELAEH----GLVPEEwggdTIFVPVSaktGEGIDELLE 159
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 8-77 4.66e-04

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 39.23  E-value: 4.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   8 ITIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgtgeFEagisknG---QTR---EHALlayTLGVKqLIVGVNK 75
Cdd:COG1217   71 INIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlKKAL---ELGLK-PIVVINK 130


                 ..
gi 349801457  76 MD 77
Cdd:COG1217  131 ID 132
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 8-77 5.59e-04

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: 38.79  E-value: 5.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 349801457   8 ITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTgefeaGISKNG-QTREHALLaytLGVKQLIVgVNKMD 77
Cdd:cd04167   73 INIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTSVTeRLIRHAIQ---EGLPMVLV-INKID 134
infB CHL00189
translation initiation factor 2; Provisional
 8-124 1.28e-03

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 38.27  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   8 ITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRE---HALLAYTlgvkQLIVGVNKMDTTeppys 84
Cdd:CHL00189 297 IVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIEainYIQAANV----PIIVAINKIDKA----- 360

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 349801457  85 ESRFDEIRKEVSSY---IKKIGYNpvaVAFVPIS---GWNGDNMLE 124
Cdd:CHL00189 361 NANTERIKQQLAKYnliPEKWGGD---TPMIPISasqGTNIDKLLE 403
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 8-77 2.91e-03

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 36.80  E-value: 2.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   8 ITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAYTLGVKQLIVgVNKMD 77
Cdd:cd04170   66 INLIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWEFLDDAKLPRIIF-INKMD 127
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 2-124 4.04e-03

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


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 35.90  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   2 ETPKFYITIIDAPGHRDFIKNMITGT-----SQADCAVLIVAAGTGEFEAGIskngqTREHALLAYTLGVKQLIVGvNKM 76
Cdd:cd00882   43 DKGKVKLVLVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRESEEDA-----KLLILRRLRKEGIPIILVG-NKI 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 349801457  77 DTTEPPysesrfDEIRKEVSSYIKKIGYNPVavafVPISGWNGDNMLE 124
Cdd:cd00882  117 DLLEER------EVEELLRLEELAKILGVPV----FEVSAKTGEGVDE 154
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 8-121 6.97e-03

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: 35.79  E-value: 6.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349801457   8 ITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAYTLGVKQLIVgVNKMDTTeppysESR 87
Cdd:COG0480   76 INIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG-------VEPQTETVWRQADKYGVPRIVF-VNKMDRE-----GAD 142

                         90       100       110
                 ....*....|....*....|....*....|....
gi 349801457  88 FDEIrkeVSSYIKKIGYNPVAVaFVPIsgWNGDN 121
Cdd:COG0480  143 FDRV---LEQLKERLGANPVPL-QLPI--GAEDD 170
 
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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