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Conserved domains on  [gi|152938182|gb|ABS43031|]
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elongation factor EF-G, partial [Salmonella bongori]

Protein Classification

EF-G domain-containing protein( domain architecture ID 10112010)

EF-G domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 1-211 2.68e-141

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: 394.94  E-value: 2.68e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   1 GVNHKIGEVHEGAATMDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYC 80
Cdd:cd01886   24 GRIHKIGEVHGGGATMDWMEQERERGITIQSAATTCFWKD-------HRINIIDTPGHVDFTIEVERSLRVLDGAVAVFD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  81 AVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLAIGAEEAFTGVVDLVKMKAINWN 160
Cdd:cd01886   97 AVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQLPIGAEDDFEGVVDLIEMKALYWD 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 152938182 161 EEDrGVTFTYEDIPADMQELAEEWHQNLIESAAEASEELMEKYLGGEELTE 211
Cdd:cd01886  177 GEL-GEKIEETDIPEDLLEEAEEAREELIETLAEVDDELMEKYLEGEEITE 226
 
Name Accession Description Interval E-value
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 1-211 2.68e-141

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: 394.94  E-value: 2.68e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   1 GVNHKIGEVHEGAATMDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYC 80
Cdd:cd01886   24 GRIHKIGEVHGGGATMDWMEQERERGITIQSAATTCFWKD-------HRINIIDTPGHVDFTIEVERSLRVLDGAVAVFD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  81 AVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLAIGAEEAFTGVVDLVKMKAINWN 160
Cdd:cd01886   97 AVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQLPIGAEDDFEGVVDLIEMKALYWD 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 152938182 161 EEDrGVTFTYEDIPADMQELAEEWHQNLIESAAEASEELMEKYLGGEELTE 211
Cdd:cd01886  177 GEL-GEKIEETDIPEDLLEEAEEAREELIETLAEVDDELMEKYLEGEEITE 226
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 1-211 3.91e-140

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: 407.12  E-value: 3.91e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   1 GVNHKIGEVHEGAATMDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYC 80
Cdd:COG0480   34 GAIHRIGEVHDGNTVMDWMPEEQERGITITSAATTCEWKG-------HKINIIDTPGHVDFTGEVERSLRVLDGAVVVFD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  81 AVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLAIGAEEAFTGVVDLVKMKAINWN 160
Cdd:COG0480  107 AVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVPLQLPIGAEDDFKGVIDLVTMKAYVYD 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 152938182 161 EEDrGVTFTYEDIPADMQELAEEWHQNLIESAAEASEELMEKYLGGEELTE 211
Cdd:COG0480  187 DEL-GAKYEEEEIPAELKEEAEEAREELIEAVAETDDELMEKYLEGEELTE 236
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
 1-211 9.59e-134

translation elongation factor EF-G; After peptide bond formation, this elongation factor of bacteria and organelles catalyzes the translocation of the tRNA-mRNA complex, with its attached nascent polypeptide chain, from the A-site to the P-site of the ribosome. Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins. The closest homolog to canonical (e.g. E. coli) EF-G in the spirochetes clusters as if it is derived from mitochondrial forms, while a more distant second copy is also present. Synechocystis PCC6803 has a few proteins more closely related to EF-G than to any other characterized protein. Two of these resemble E. coli EF-G more closely than does the best match from the spirochetes; it may be that both function as authentic EF-G. [Protein synthesis, Translation factors]


Pssm-ID: 129575 [Multi-domain]  Cd Length: 689  Bit Score: 390.71  E-value: 9.59e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182    1 GVNHKIGEVHEGAATMDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYC 80
Cdd:TIGR00484  35 GRIHKIGEVHDGAATMDWMEQEKERGITITSAATTVFWKG-------HRINIIDTPGHVDFTVEVERSLRVLDGAVAVLD 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   81 AVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLAIGAEEAFTGVVDLVKMKAINWN 160
Cdd:TIGR00484 108 AVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAVPIQLPIGAEDNFIGVIDLVEMKAYFFN 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 152938182  161 eEDRGVTFTYEDIPADMQELAEEWHQNLIESAAEASEELMEKYLGGEELTE 211
Cdd:TIGR00484 188 -GDKGTKAIEKEIPSDLLEQAKELRENLVEAVAEFDEELMEKYLEGEELTI 237
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
1-211 3.67e-115

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 342.49  E-value: 3.67e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   1 GVNHKIGEVHEGAATMDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYC 80
Cdd:PRK12740  20 GAIHRIGEVEDGTTTMDFMPEERERGISITSAATTCEWKG-------HKINLIDTPGHVDFTGEVERALRVLDGAVVVVC 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  81 AVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLAIGAEEAFTGVVDLVKMKAINWN 160
Cdd:PRK12740  93 AVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLQEKLGAPVVPLQLPIGEGDDFTGVVDLLSMKAYRYD 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 152938182 161 EedrGVTFTYEDIPADMQELAEEWHQNLIESAAEASEELMEKYLGGEELTE 211
Cdd:PRK12740 173 E---GGPSEEIEIPAELLDRAEEAREELLEALAEFDDELMEKYLEGEELSE 220
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-128 3.20e-58

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 181.57  E-value: 3.20e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182    1 GVNHKIGEVH-EGAATMDWMEQEQERGITITSAATTAFWsgmakqyEPHRINIIDTPGHVDFTIEVERSMRVLDGAVMVY 79
Cdd:pfam00009  28 GAISKRGEVKgEGEAGLDNLPEERERGITIKSAAVSFET-------KDYLINLIDTPGHVDFVKEVIRGLAQADGAILVV 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 152938182   80 CAVGGVQPQSETVWRQANKYKVPRIAFVNKMDRM-GANFLKVVGQIKTRL 128
Cdd:pfam00009 101 DAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSREL 150
 
Name Accession Description Interval E-value
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 1-211 2.68e-141

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: 394.94  E-value: 2.68e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   1 GVNHKIGEVHEGAATMDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYC 80
Cdd:cd01886   24 GRIHKIGEVHGGGATMDWMEQERERGITIQSAATTCFWKD-------HRINIIDTPGHVDFTIEVERSLRVLDGAVAVFD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  81 AVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLAIGAEEAFTGVVDLVKMKAINWN 160
Cdd:cd01886   97 AVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQLPIGAEDDFEGVVDLIEMKALYWD 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 152938182 161 EEDrGVTFTYEDIPADMQELAEEWHQNLIESAAEASEELMEKYLGGEELTE 211
Cdd:cd01886  177 GEL-GEKIEETDIPEDLLEEAEEAREELIETLAEVDDELMEKYLEGEEITE 226
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 1-211 3.91e-140

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: 407.12  E-value: 3.91e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   1 GVNHKIGEVHEGAATMDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYC 80
Cdd:COG0480   34 GAIHRIGEVHDGNTVMDWMPEEQERGITITSAATTCEWKG-------HKINIIDTPGHVDFTGEVERSLRVLDGAVVVFD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  81 AVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLAIGAEEAFTGVVDLVKMKAINWN 160
Cdd:COG0480  107 AVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVPLQLPIGAEDDFKGVIDLVTMKAYVYD 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 152938182 161 EEDrGVTFTYEDIPADMQELAEEWHQNLIESAAEASEELMEKYLGGEELTE 211
Cdd:COG0480  187 DEL-GAKYEEEEIPAELKEEAEEAREELIEAVAETDDELMEKYLEGEELTE 236
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
 1-211 9.59e-134

translation elongation factor EF-G; After peptide bond formation, this elongation factor of bacteria and organelles catalyzes the translocation of the tRNA-mRNA complex, with its attached nascent polypeptide chain, from the A-site to the P-site of the ribosome. Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins. The closest homolog to canonical (e.g. E. coli) EF-G in the spirochetes clusters as if it is derived from mitochondrial forms, while a more distant second copy is also present. Synechocystis PCC6803 has a few proteins more closely related to EF-G than to any other characterized protein. Two of these resemble E. coli EF-G more closely than does the best match from the spirochetes; it may be that both function as authentic EF-G. [Protein synthesis, Translation factors]


Pssm-ID: 129575 [Multi-domain]  Cd Length: 689  Bit Score: 390.71  E-value: 9.59e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182    1 GVNHKIGEVHEGAATMDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYC 80
Cdd:TIGR00484  35 GRIHKIGEVHDGAATMDWMEQEKERGITITSAATTVFWKG-------HRINIIDTPGHVDFTVEVERSLRVLDGAVAVLD 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   81 AVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLAIGAEEAFTGVVDLVKMKAINWN 160
Cdd:TIGR00484 108 AVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAVPIQLPIGAEDNFIGVIDLVEMKAYFFN 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 152938182  161 eEDRGVTFTYEDIPADMQELAEEWHQNLIESAAEASEELMEKYLGGEELTE 211
Cdd:TIGR00484 188 -GDKGTKAIEKEIPSDLLEQAKELRENLVEAVAEFDEELMEKYLEGEELTI 237
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
1-211 3.67e-115

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 342.49  E-value: 3.67e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   1 GVNHKIGEVHEGAATMDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYC 80
Cdd:PRK12740  20 GAIHRIGEVEDGTTTMDFMPEERERGISITSAATTCEWKG-------HKINLIDTPGHVDFTGEVERALRVLDGAVVVVC 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  81 AVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLAIGAEEAFTGVVDLVKMKAINWN 160
Cdd:PRK12740  93 AVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLQEKLGAPVVPLQLPIGEGDDFTGVVDLLSMKAYRYD 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 152938182 161 EedrGVTFTYEDIPADMQELAEEWHQNLIESAAEASEELMEKYLGGEELTE 211
Cdd:PRK12740 173 E---GGPSEEIEIPAELLDRAEEAREELLEALAEFDDELMEKYLEGEELSE 220
PRK13351 PRK13351
elongation factor G-like protein;
1-210 2.43e-101

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 307.26  E-value: 2.43e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   1 GVNHKIGEVHEGAATMDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYC 80
Cdd:PRK13351  33 GKIHKMGEVEDGTTVTDWMPQEQERGITIESAATSCDWDN-------HRINLIDTPGHIDFTGEVERSLRVLDGAVVVFD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  81 AVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLAIGAEEAFTGVVDLVKMKAINWN 160
Cdd:PRK13351 106 AVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGKRPLPLQLPIGSEDGFEGVVDLITEPELHFS 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 152938182 161 EEDRGVTFTYEDIPADMQELAEEWHQNLIESAAEASEELMEKYLGGEELT 210
Cdd:PRK13351 186 EGDGGSTVEEGPIPEELLEEVEEAREKLIEALAEFDDELLELYLEGEELS 235
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 1-211 2.75e-65

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: 202.44  E-value: 2.75e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   1 GVNHKIGEVHEGAATMDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYC 80
Cdd:cd04170   24 GAIDRLGRVEDGNTVSDYDPEEKKRKMSIETSVAPLEWNG-------HKINLIDTPGYADFVGETLSALRAVDAALIVVE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  81 AVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLAIGAEEAFTGVVDLVKMKAINWN 160
Cdd:cd04170   97 AQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAFGRPVVPIQLPIGEGDEFTGVVDLLSEKAYRYD 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 152938182 161 EEDRGVTftyEDIPADMQELAEEWHQNLIESAAEASEELMEKYLGGEELTE 211
Cdd:cd04170  177 PGEPSVE---IEIPEELKEKVAEAREELLEAVAETDEELMEKYLEEGELTE 224
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-128 3.20e-58

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 181.57  E-value: 3.20e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182    1 GVNHKIGEVH-EGAATMDWMEQEQERGITITSAATTAFWsgmakqyEPHRINIIDTPGHVDFTIEVERSMRVLDGAVMVY 79
Cdd:pfam00009  28 GAISKRGEVKgEGEAGLDNLPEERERGITIKSAAVSFET-------KDYLINLIDTPGHVDFVKEVIRGLAQADGAILVV 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 152938182   80 CAVGGVQPQSETVWRQANKYKVPRIAFVNKMDRM-GANFLKVVGQIKTRL 128
Cdd:pfam00009 101 DAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSREL 150
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 1-211 7.46e-52

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: 167.03  E-value: 7.46e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   1 GVNHKIGEVHEGAATMDWMEQEQERGITITSAATTAFWSGMakqyephRINIIDTPGHVDFTIEVERSMRVLDGAVMVYC 80
Cdd:cd04168   24 GAIRELGSVDKGTTRTDSMELERQRGITIFSAVASFQWEDT-------KVNIIDTPGHMDFIAEVERSLSVLDGAILVIS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  81 AVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQlaigaeeaftgvvdlvkmkainwn 160
Cdd:cd04168   97 AVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEIKEKLSPDIVPMQ------------------------ 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 152938182 161 eedrgvTFTYEDIPADMQELAEEWhqnlIESAAEASEELMEKYLGGEELTE 211
Cdd:cd04168  153 ------KVGLYPNICDTNNIDDEQ----IETVAEGNDELLEKYLSGGPLEE 193
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-129 1.31e-36

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: 126.26  E-value: 1.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   1 GVNHKIGEVHEGAAT-MDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVY 79
Cdd:cd00881   21 YQTGAIDRRGTRKETfLDTLKEERERGITIKTGVVEFEWPK-------RRINFIDTPGHEDFSKETVRGLAQADGALLVV 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 152938182  80 CAVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMG-ANFLKVVGQIKTRLG 129
Cdd:cd00881   94 DANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLK 144
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 16-112 2.29e-36

Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.


Pssm-ID: 206672 [Multi-domain]  Cd Length: 218  Bit Score: 126.58  E-value: 2.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  16 MDWMEQEQERGITITSAATTAFWSGMAKQY--EPHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVW 93
Cdd:cd01885   38 LDTREDEQERGITIKSSAISLYFEYEEEKMdgNDYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVL 117

                         90
                 ....*....|....*....
gi 152938182  94 RQANKYKVPRIAFVNKMDR 112
Cdd:cd01885  118 RQALEERVKPVLVINKIDR 136
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 16-129 1.37e-34

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 129.21  E-value: 1.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  16 MDWMEQEQERGITITSAATTafwsgMAKQYE--PHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVW 93
Cdd:PRK07560  58 LDFDEEEQARGITIKAANVS-----MVHEYEgkEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVL 132

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 152938182  94 RQANKYKVPRIAFVNKMDRMgANFLKVVGQ-IKTRLG 129
Cdd:PRK07560 133 RQALRERVKPVLFINKVDRL-IKELKLTPQeMQQRLL 168
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
 13-207 8.42e-34

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: 121.55  E-value: 8.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  13 AATMDWMEQEQERGITITSAAttafwsgMAKQYEPHRINIIDTPGHVDFTievERSMRVL---DGAVMVYCAVGGVQPQS 89
Cdd:cd04169   43 HATSDWMEIEKQRGISVTSSV-------MQFEYKGCVINLLDTPGHEDFS---EDTYRTLtavDSAVMVIDAAKGVEPQT 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  90 ETVWRQANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLAIGAEEAFTGVVDLVKMKAINWNEEDRGVTFT 169
Cdd:cd04169  113 RKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIENELGIDCAPMTWPIGMGKDFKGVYDRYDKEIYLYERGAGGAIKA 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 152938182 170 YEDI-----PADMQELAEEWHQNLIES---AAEASEEL-MEKYLGGE 207
Cdd:cd04169  193 PEETkglddPKLDELLGEDLAEQLREElelVEGAGPEFdKELFLAGE 239
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 16-124 3.10e-29

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: 107.68  E-value: 3.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  16 MDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQ 95
Cdd:cd01891   40 MDSNDLERERGITILAKNTAITYKD-------TKINIIDTPGHADFGGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKK 112

                         90       100
                 ....*....|....*....|....*....
gi 152938182  96 ANKYKVPRIAFVNKMDRMGANFLKVVGQI 124
Cdd:cd01891  113 ALEAGLKPIVVINKIDRPDARPEEVVDEV 141
prfC PRK00741
peptide chain release factor 3; Provisional
 14-207 1.95e-27

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 108.30  E-value: 1.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  14 ATMDWMEQEQERGITITSaattafwSGMAKQYEPHRINIIDTPGHVDFTievERSMRVL---DGAVMVYCAVGGVQPQSE 90
Cdd:PRK00741  52 ATSDWMEMEKQRGISVTS-------SVMQFPYRDCLINLLDTPGHEDFS---EDTYRTLtavDSALMVIDAAKGVEPQTR 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  91 T---VWRQANkykVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLAIGAEEAFTGVVDLVK-----MKAINWNEE 162
Cdd:PRK00741 122 KlmeVCRLRD---TPIFTFINKLDRDGREPLELLDEIEEVLGIACAPITWPIGMGKRFKGVYDLYNdevelYQPGEGHTI 198

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 152938182 163 DRGVTFTYEDIPADMQELAEEWHQNL---IESAAEASEEL-MEKYLGGE 207
Cdd:PRK00741 199 QEVEIIKGLDNPELDELLGEDLAEQLreeLELVQGASNEFdLEAFLAGE 247
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
 16-113 1.96e-27

translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]


Pssm-ID: 129581 [Multi-domain]  Cd Length: 720  Bit Score: 108.83  E-value: 1.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   16 MDWMEQEQERGITITSAATTafwsgMAKQYE--PHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVW 93
Cdd:TIGR00490  57 LDFDEQEQERGITINAANVS-----MVHEYEgnEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVL 131

                          90       100
                  ....*....|....*....|
gi 152938182   94 RQANKYKVPRIAFVNKMDRM 113
Cdd:TIGR00490 132 RQALKENVKPVLFINKVDRL 151
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 16-124 4.00e-24

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 99.32  E-value: 4.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  16 MDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQ 95
Cdd:COG1217   44 MDSNDLERERGITILAKNTAVRYKG-------VKINIVDTPGHADFGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKK 116

                         90       100
                 ....*....|....*....|....*....
gi 152938182  96 ANKYKVPRIAFVNKMDRMGANFLKVVGQI 124
Cdd:COG1217  117 ALELGLKPIVVINKIDRPDARPDEVVDEV 145
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 16-132 4.27e-24

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: 93.75  E-value: 4.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  16 MDWMEQEQERGITITSAATTAFWSgmAKQYEPHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQ 95
Cdd:cd01890   37 LDSMDLERERGITIKAQAVRLFYK--AKDGEEYLLNLIDTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYL 114

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 152938182  96 ANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANP 132
Cdd:cd01890  115 ALENNLEIIPVINKIDLPAADPDRVKQEIEDVLGLDA 151
PTZ00416 PTZ00416
elongation factor 2; Provisional
 16-124 1.94e-23

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 97.43  E-value: 1.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  16 MDWMEQEQERGITITSAATTAFWS---GMAKQYEPHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETV 92
Cdd:PTZ00416  57 TDTRADEQERGITIKSTGISLYYEhdlEDGDDKQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETV 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 152938182  93 WRQANKYKVPRIAFVNKMDR-----------MGANFLKVVGQI 124
Cdd:PTZ00416 137 LRQALQERIRPVLFINKVDRailelqldpeeIYQNFVKTIENV 179
lepA TIGR01393
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ...
 13-152 5.66e-22

elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a GTP-binding membrane protein related to EF-G and EF-Tu. Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including GUF1 of yeast) originated within the bacterial LepA family. The function is unknown. [Unknown function, General]


Pssm-ID: 130460 [Multi-domain]  Cd Length: 595  Bit Score: 93.16  E-value: 5.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   13 AATMDWMEQEQERGITITSAATTAFWSgmAKQYEPHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQseTV 92
Cdd:TIGR01393  37 EQVLDSMDLERERGITIKAQAVRLNYK--AKDGETYVLNLIDTPGHVDFSYEVSRSLAACEGALLLVDAAQGIEAQ--TL 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   93 wrqANKYKVPR-----IAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLA-----IGAEEAFTGVVDLV 152
Cdd:TIGR01393 113 ---ANVYLALEndleiIPVINKIDLPSADPERVKKEIEEVIGLDASEAILAsaktgIGIEEILEAIVKRV 179
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 8-112 1.03e-20

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 89.40  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   8 EVHEGAATMDWMEQEQERGITITSAATTAFW---SGMAKQYEPHR------INIIDTPGHVDFTIEVERSMRVLDGAVMV 78
Cdd:PLN00116  49 EVAGDVRMTDTRADEAERGITIKSTGISLYYemtDESLKDFKGERdgneylINLIDSPGHVDFSSEVTAALRITDGALVV 128

                         90       100       110
                 ....*....|....*....|....*....|....
gi 152938182  79 YCAVGGVQPQSETVWRQANKYKVPRIAFVNKMDR 112
Cdd:PLN00116 129 VDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 16-113 4.26e-20

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: 84.24  E-value: 4.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  16 MDWMEQEQERGITITSAATTAFWSGMakQYEPHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQ 95
Cdd:cd04167   41 TDTRKDEQERGISIKSNPISLVLEDS--KGKSYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRH 118

                         90
                 ....*....|....*...
gi 152938182  96 ANKYKVPRIAFVNKMDRM 113
Cdd:cd04167  119 AIQEGLPMVLVINKIDRL 136
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
 16-129 1.62e-18

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 83.14  E-value: 1.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  16 MDWMEQEQERGITITSAATTAFWSgmAKQYEPHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQseTVwrq 95
Cdd:COG0481   43 LDSMDLERERGITIKAQAVRLNYK--AKDGETYQLNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQ--TL--- 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 152938182  96 ANKYK--------VPRIafvNKMDRMGANFLKVVGQIKTRLG 129
Cdd:COG0481  116 ANVYLalendleiIPVI---NKIDLPSADPERVKQEIEDIIG 154
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 6-153 9.52e-18

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 76.64  E-value: 9.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182    6 IGEVHEGAATMDWMEQEQERGITItsaattafwsgmakqyephRINIIDTPGHVDF-------TIEVERSMRVLDGAVMV 78
Cdd:TIGR00231  28 ITEYYPGTTRNYVTTVIEEDGKTY-------------------KFNLLDTAGQEDYdairrlyYPQVERSLRVFDIVILV 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 152938182   79 YCAVGGVQPQSETVWRQAnKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVpLQLAIGAEEAFTGVVDLVK 153
Cdd:TIGR00231  89 LDVEEILEKQTKEIIHHA-DSGVPIILVGNKIDLKDADLKTHVASEFAKLNGEPI-IPLSAETGKNIDSAFKIVE 161
PRK10218 PRK10218
translational GTPase TypA;
16-151 4.82e-17

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 78.98  E-value: 4.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  16 MDWMEQEQERGITITSAATTAFWSGmakqyepHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQ 95
Cdd:PRK10218  43 MDSNDLEKERGITILAKNTAIKWND-------YRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKK 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 152938182  96 ANKYKVPRIAFVNKMDRMGANFLKVVGQI---KTRLGANPVPLQLAIGAEEAFTGVVDL 151
Cdd:PRK10218 116 AFAYGLKPIVVINKVDRPGARPDWVVDQVfdlFVNLDATDEQLDFPIVYASALNGIAGL 174
infB CHL00189
translation initiation factor 2; Provisional
 6-120 6.05e-09

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 55.22  E-value: 6.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182   6 IGEVHEGAATM-DWMEQEQER-----GITITSAATTAFWSgmaKQYEPHRINIIDTPGHVDFTIEVERSMRVLDGAVMVY 79
Cdd:CHL00189 250 LGHVDHGKTTLlDKIRKTQIAqkeagGITQKIGAYEVEFE---YKDENQKIVFLDTPGHEAFSSMRSRGANVTDIAILII 326

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 152938182  80 CAVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKV 120
Cdd:CHL00189 327 AADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERI 367
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 48-112 1.39e-08

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: 52.09  E-value: 1.39e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  48 HRINIIDTPGHVDFTieverSMR-----VLDGAVMVYCAVGGVQPQSETVWRQANKYKVPRIAFVNKMDR 112
Cdd:cd01887   49 PGITFIDTPGHEAFT-----NMRargasVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDK 113
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 13-111 4.16e-06

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: 46.46  E-value: 4.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  13 AATMDWMEQEQERGITItSAATTAFWSgmAKQYephrINIIDTPGHVDFTieveRSMRV----LDGAVMVYCAVGGVQPQ 88
Cdd:COG5256   57 AWVMDRLKEERERGVTI-DLAHKKFET--DKYY----FTIIDAPGHRDFV----KNMITgasqADAAILVVSAKDGVMGQ 125

                         90       100
                 ....*....|....*....|....
gi 152938182  89 SETVWRQANKYKVPRIAF-VNKMD 111
Cdd:COG5256  126 TREHAFLARTLGINQLIVaVNKMD 149
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 48-123 4.45e-06

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


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 46.55  E-value: 4.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  48 HRINIIDTPGHVDFTieverSMR-----VLDGAVMVYCAVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVG 122
Cdd:COG0532   51 GKITFLDTPGHEAFT-----AMRargaqVTDIVILVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDKPGANPDRVKQ 125


                 .
gi 152938182 123 Q 123
Cdd:COG0532  126 E 126
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 17-128 6.37e-06

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: 44.90  E-value: 6.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  17 DWMEQEQERGITIT-SAATTAFWSGmakqyepHRINIIDTPGHVDFTieveRSMRV----LDGAVMVYCAVGGVQPQSET 91
Cdd:cd04171   25 DRLPEEKKRGITIDlGFAYLDLPDG-------KRLGFIDVPGHEKFV----KNMLAgaggIDAVLLVVAADEGIMPQTRE 93

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 152938182  92 VWRQANKYKVPRIAFV-NKMDRMGANFL-KVVGQIKTRL 128
Cdd:cd04171   94 HLEILELLGIKKGLVVlTKADLVDEDRLeLVEEEILELL 132
PLN03127 PLN03127
Elongation factor Tu; Provisional
 16-111 1.98e-05

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 44.43  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  16 MDWMEQEQERGITItsaATTAFWSGMAKQYEPHriniIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQ 95
Cdd:PLN03127  99 IDKAPEEKARGITI---ATAHVEYETAKRHYAH----VDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILL 171

                         90
                 ....*....|....*..
gi 152938182  96 ANKYKVPRIA-FVNKMD 111
Cdd:PLN03127 172 ARQVGVPSLVvFLNKVD 188
PLN03126 PLN03126
Elongation factor Tu; Provisional
 16-113 2.48e-05

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 44.22  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  16 MDWMEQEQERGITITSAatTAFWSGMAKQYePHriniIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQ 95
Cdd:PLN03126 119 IDAAPEERARGITINTA--TVEYETENRHY-AH----VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILL 191

                         90
                 ....*....|....*....
gi 152938182  96 ANKYKVPR-IAFVNKMDRM 113
Cdd:PLN03126 192 AKQVGVPNmVVFLNKQDQV 210
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 13-111 4.65e-05

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 43.38  E-value: 4.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  13 AATMDWMEQEQERGITItSAATTAFWSgmaKQYEphrINIIDTPGHVDFTieveRSMRV----LDGAVMVYCA--VGGVQ 86
Cdd:PRK12317  56 AWVMDRLKEERERGVTI-DLAHKKFET---DKYY---FTIVDCPGHRDFV----KNMITgasqADAAVLVVAAddAGGVM 124

                         90       100
                 ....*....|....*....|....*..
gi 152938182  87 PQS-ETVWrQANKYKVPR-IAFVNKMD 111
Cdd:PRK12317 125 PQTrEHVF-LARTLGINQlIVAINKMD 150
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 16-111 7.28e-05

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: 42.17  E-value: 7.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  16 MDWMEQEQERGITITSA----ATtafwsgmakqyePHR--InIIDTPGHVDFTieveRSM----RVLDGAVMVYCAVGGV 85
Cdd:cd04166   53 VDGLQAEREQGITIDVAyryfST------------PKRkfI-IADTPGHEQYT----RNMvtgaSTADLAILLVDARKGV 115

                         90       100
                 ....*....|....*....|....*..
gi 152938182  86 QPQSETVWRQANKYKVPRIAF-VNKMD 111
Cdd:cd04166  116 LEQTRRHSYIASLLGIRHVVVaVNKMD 142
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 16-61 1.07e-04

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: 41.71  E-value: 1.07e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 152938182  16 MDWMEQEQERGITItSAATTAFwsgmakQYEPHRINIIDTPGHVDF 61
Cdd:cd01883   52 LDKLKEERERGVTI-DVGLAKF------ETEKYRFTIIDAPGHRDF 90
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 34-112 2.44e-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: 40.13  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  34 TTAFWSGMAKQYEP-HRINIIDTPGHVDF-----TIEVERSMRVLDGAVMVYCAVGG--VQPQSETVWRQANKYKVPRIA 105
Cdd:cd00882   32 TRDPDVYVKELDKGkVKLVLVDTPGLDEFgglgrEELARLLLRGADLILLVVDSTDResEEDAKLLILRRLRKEGIPIIL 111


                 ....*..
gi 152938182 106 FVNKMDR 112
Cdd:cd00882  112 VGNKIDL 118
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 22-111 2.50e-04

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: 40.26  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  22 EQERGITItsaATTAFWSGMAKQYEPHriniIDTPGHVDFT---IEVERSMrvlDGAVMVYCAVGGVQPQS-ETVW--RQ 95
Cdd:cd01884   46 EKARGITI---NTAHVEYETANRHYAH----VDCPGHADYIknmITGAAQM---DGAILVVSATDGPMPQTrEHLLlaRQ 115

                         90
                 ....*....|....*..
gi 152938182  96 ANkykVPRIA-FVNKMD 111
Cdd:cd01884  116 VG---VPYIVvFLNKAD 129
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 12-133 5.21e-04

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: 40.07  E-value: 5.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  12 GAATMDW------MEQEQERGITITSA----ATtafwsgmakqyePHR--InIIDTPGHVDFTieveRSMrVL-----DG 74
Cdd:COG2895   60 GTQEIDLalltdgLQAEREQGITIDVAyryfST------------PKRkfI-IADTPGHEQYT----RNM-VTgastaDL 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152938182  75 AVMVYCAVGGVQPQSEtvwRQAnkY-----KVPRIAF-VNKMDRMG---ANFLKVVGQIKT---RLGANPV 133
Cdd:COG2895  122 AILLIDARKGVLEQTR---RHS--YiasllGIRHVVVaVNKMDLVDyseEVFEEIVADYRAfaaKLGLEDI 187
PRK14845 PRK14845
translation initiation factor IF-2; Provisional
 52-113 5.26e-04

translation initiation factor IF-2; Provisional


Pssm-ID: 237833 [Multi-domain]  Cd Length: 1049  Bit Score: 40.64  E-value: 5.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 152938182   52 IIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQANKYKVPRIAFVNKMDRM 113
Cdd:PRK14845  530 FIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTPFVVAANKIDLI 591
PRK04004 PRK04004
translation initiation factor IF-2; Validated
 53-112 1.99e-03

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 38.62  E-value: 1.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 152938182  53 IDTPGHVDFTieverSMR-----VLDGAVMVYCAVGGVQPQSETVWRQANKYKVPRIAFVNKMDR 112
Cdd:PRK04004  76 IDTPGHEAFT-----NLRkrggaLADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDR 135
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 13-61 2.33e-03

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 38.19  E-value: 2.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 152938182  13 AATMDWMEQEQERGITITsaatTAFWSGMAKQYEphrINIIDTPGHVDF 61
Cdd:PTZ00141  57 AWVLDKLKAERERGITID----IALWKFETPKYY---FTIIDAPGHRDF 98
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 22-111 2.67e-03

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: 37.82  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  22 EQERGITITSAATtafwsgmakQYE------PHriniIDTPGHVDFTieveRSMRV----LDGAVMVYCAVGGVQPQS-E 90
Cdd:COG0050   56 EKERGITINTSHV---------EYEtekrhyAH----VDCPGHADYV----KNMITgaaqMDGAILVVSATDGPMPQTrE 118

                         90       100
                 ....*....|....*....|....
gi 152938182  91 TVW--RQANkykVPRIA-FVNKMD 111
Cdd:COG0050  119 HILlaRQVG---VPYIVvFLNKCD 139
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 14-89 4.06e-03

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: 36.96  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  14 ATMDWMEQEQERGITI--------TSAATTAFWSGmAKQYEPHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGV 85
Cdd:cd01889   27 AAFDKNPQSQERGITLdlgfssfeVDKPKHLEDNE-NPQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGI 105


                 ....
gi 152938182  86 QPQS 89
Cdd:cd01889  106 QTQT 109
PRK12736 PRK12736
elongation factor Tu; Reviewed
 21-111 8.45e-03

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 36.46  E-value: 8.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152938182  21 QEQERGITITSA----ATtafwsgmAKQYEPHriniIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQA 96
Cdd:PRK12736  55 EEKERGITINTAhveyET-------EKRHYAH----VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLA 123

                         90
                 ....*....|....*.
gi 152938182  97 NKYKVPRI-AFVNKMD 111
Cdd:PRK12736 124 RQVGVPYLvVFLNKVD 139
 
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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