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Conserved domains on  [gi|1064244138|ref|NP_001332798|]
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translation factor GUF1, mitochondrial isoform 2 [Homo sapiens]

Protein Classification

elongation factor 4 family protein( domain architecture ID 1008438)

elongation factor 4 family protein such as elongation factor 4, a GTPase protein that is required for accurate and efficient protein synthesis under certain stress conditions

EC:  3.6.5.-
Gene Ontology:  GO:0006412|GO:0003924|GO:0005525

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LepA super family cl33901
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
 1-341 0e+00

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


The actual alignment was detected with superfamily member COG0481:

Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 549.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138   1 MKDVTEAQIGDTLCLHKQPV-EPLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLALGAGWRLG 79
Cdd:COG0481   264 IKDVRDARVGDTITLAKNPAaEPLPGFKEVKPMVFAGLYPVDSDDYEDLRDALEKLQLNDASLTYEPETSAALGFGFRCG 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138  80 FLGLLHMEVFNQRLEQEYNASVILTTPTVPYKAVLSSSKlikehrekEITIINPAQFPDKSKVTEYLEPVVLGTIITPDE 159
Cdd:COG0481   344 FLGLLHMEIIQERLEREFDLDLITTAPSVVYEVTLTDGE--------VIEVDNPSDLPDPGKIEEIEEPIVKATIITPSE 415

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 160 YTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIVVDFYDSLKSLSSGYASFDYEDAGYQTAELVKMDILLNGNTV 239
Cdd:COG0481   416 YVGAVMELCQEKRGVQKNMEYLGENRVELTYELPLAEIVFDFFDRLKSITRGYASLDYEFIGYRESDLVKLDILINGEPV 495

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 240 EELVTVVHKDKAHSIGKAICERLKDSLPRQLFEIAIQAAIGSKIIARETVKAYRKNVLAKCYGGDITRKMKLLKRQAEGK 319
Cdd:COG0481   496 DALSFIVHRDKAYSRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVLAKCYGGDISRKRKLLEKQKEGK 575

                         330       340
                  ....*....|....*....|..
gi 1064244138 320 KKLRKIGNVEVPKDAFIKVLKT 341
Cdd:COG0481   576 KRMKQVGNVEIPQEAFLAVLKV 597
 
Name Accession Description Interval E-value
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
 1-341 0e+00

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 549.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138   1 MKDVTEAQIGDTLCLHKQPV-EPLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLALGAGWRLG 79
Cdd:COG0481   264 IKDVRDARVGDTITLAKNPAaEPLPGFKEVKPMVFAGLYPVDSDDYEDLRDALEKLQLNDASLTYEPETSAALGFGFRCG 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138  80 FLGLLHMEVFNQRLEQEYNASVILTTPTVPYKAVLSSSKlikehrekEITIINPAQFPDKSKVTEYLEPVVLGTIITPDE 159
Cdd:COG0481   344 FLGLLHMEIIQERLEREFDLDLITTAPSVVYEVTLTDGE--------VIEVDNPSDLPDPGKIEEIEEPIVKATIITPSE 415

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 160 YTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIVVDFYDSLKSLSSGYASFDYEDAGYQTAELVKMDILLNGNTV 239
Cdd:COG0481   416 YVGAVMELCQEKRGVQKNMEYLGENRVELTYELPLAEIVFDFFDRLKSITRGYASLDYEFIGYRESDLVKLDILINGEPV 495

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 240 EELVTVVHKDKAHSIGKAICERLKDSLPRQLFEIAIQAAIGSKIIARETVKAYRKNVLAKCYGGDITRKMKLLKRQAEGK 319
Cdd:COG0481   496 DALSFIVHRDKAYSRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVLAKCYGGDISRKRKLLEKQKEGK 575

                         330       340
                  ....*....|....*....|..
gi 1064244138 320 KKLRKIGNVEVPKDAFIKVLKT 341
Cdd:COG0481   576 KRMKQVGNVEIPQEAFLAVLKV 597
lepA TIGR01393
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ...
 2-341 1.12e-176

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: 503.01  E-value: 1.12e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138   2 KDVTEAQIGDTLCLHKQPV-EPLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLALGAGWRLGF 80
Cdd:TIGR01393 262 KDVSDVRVGDTITHVKNPAkEPLPGFKEVKPMVFAGLYPIDTEDYEDLRDALEKLKLNDASLTYEPESSPALGFGFRCGF 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138  81 LGLLHMEVFNQRLEQEYNASVILTTPTVPYKAVLSSSKlikehrekEITIINPAQFPDKSKVTEYLEPVVLGTIITPDEY 160
Cdd:TIGR01393 342 LGLLHMEIIQERLEREFNLDLITTAPSVIYRVYLTNGE--------VIEVDNPSDLPDPGKIEHVEEPYVKATIITPTEY 413

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 161 TGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIVVDFYDSLKSLSSGYASFDYEDAGYQTAELVKMDILLNGNTVE 240
Cdd:TIGR01393 414 LGPIMTLCQEKRGVQTNMEYLDPNRVELIYEMPLAEIVYDFFDKLKSISRGYASFDYELIGYRPSDLVKLDILINGEPVD 493

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 241 ELVTVVHKDKAHSIGKAICERLKDSLPRQLFEIAIQAAIGSKIIARETVKAYRKNVLAKCYGGDITRKMKLLKRQAEGKK 320
Cdd:TIGR01393 494 ALSFIVHRDKAYSRGREICEKLKELIPRQQFEIPIQAAIGGKIIARETIKALRKDVTAKCYGGDITRKRKLLEKQKEGKK 573

                         330       340
                  ....*....|....*....|.
gi 1064244138 321 KLRKIGNVEVPKDAFIKVLKT 341
Cdd:TIGR01393 574 RMKQIGKVEVPQEAFLAVLKV 594
LepA_C pfam06421
GTP-binding protein LepA C-terminus; This family consists of the C-terminal region of several ...
 234-340 1.90e-68

GTP-binding protein LepA C-terminus; This family consists of the C-terminal region of several pro- and eukaryotic GTP-binding LepA proteins.


Pssm-ID: 461905 [Multi-domain]  Cd Length: 107  Bit Score: 209.57  E-value: 1.90e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 234 LNGNTVEELVTVVHKDKAHSIGKAICERLKDSLPRQLFEIAIQAAIGSKIIARETVKAYRKNVLAKCYGGDITRKMKLLK 313
Cdd:pfam06421   1 INGEPVDALSFIVHRSKAYRRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVTAKCYGGDISRKKKLLE 80

                          90       100
                  ....*....|....*....|....*..
gi 1064244138 314 RQAEGKKKLRKIGNVEVPKDAFIKVLK 340
Cdd:pfam06421  81 KQKEGKKRMKQIGNVEIPQEAFLAVLK 107
EF4_III cd16260
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ...
 31-106 2.00e-46

Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly conserved guanosine triphosphatase found in bacteria and eukaryotic mitochondria and chloroplasts. EF4 functions as a translation factor, which promotes back-translocation of tRNAs on posttranslocational ribosome complexes and competes with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis.


Pssm-ID: 293917 [Multi-domain]  Cd Length: 76  Bit Score: 152.27  E-value: 2.00e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1064244138  31 PMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLALGAGWRLGFLGLLHMEVFNQRLEQEYNASVILTTP 106
Cdd:cd16260     1 PMVFAGLYPVDGSDYEELRDALEKLTLNDASVTFEPETSSALGFGFRCGFLGLLHMEVFQERLEREYGLDLIITAP 76
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
6-223 1.99e-07

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 52.44  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138   6 EAQIGDTLCLHKQPVePLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLA---LGAgwrlgfLG 82
Cdd:PRK12740  362 DAATGDTLCDKGDPI-LLEPMEFPEPVISLAIEPKDKGDEEKLSEALGKLAEEDPTLRVERDEETGqtiLSG------MG 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138  83 LLHMEVFNQRLEQEYNASVILTTPTVPY-----KAVLSSSKLIKE-----------------HREKEITIIN-------P 133
Cdd:PRK12740  435 ELHLDVALERLKREYGVEVETGPPQVPYretirKKAEGHGRHKKQsgghgqfgdvwleveplPRGEGFEFVDkvvggavP 514

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 134 AQF-P--DKS------------------KVTEY---------------------------------LEPVVLGTIITPDE 159
Cdd:PRK12740  515 RQYiPavEKGvrealekgvlagypvvdvKVTLTdgsyhsvdssemafkiaarlafrealpkakpvlLEPIMKVEVSVPEE 594

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1064244138 160 YTGKIMMLCEARRAVQKNMiFIDQNRVMLKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 223
Cdd:PRK12740  595 FVGDVIGDLSSRRGRILGM-ESRGGGDVVRAEVPLAEM-FGYATDLRSLTQGRGSFSMEFSHYE 656
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 146-223 3.10e-03

Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.


Pssm-ID: 197906 [Multi-domain]  Cd Length: 85  Bit Score: 36.33  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138  146 LEPVVLGTIITPDEYTGKIMMLCEARRAVQKNMifiDQNRVM--LKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 223
Cdd:smart00838   2 LEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGM---EQRGGAqvIKAKVPLSEM-FGYATDLRSATQGRATWSMEFSHYE 77
 
Name Accession Description Interval E-value
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
 1-341 0e+00

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 549.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138   1 MKDVTEAQIGDTLCLHKQPV-EPLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLALGAGWRLG 79
Cdd:COG0481   264 IKDVRDARVGDTITLAKNPAaEPLPGFKEVKPMVFAGLYPVDSDDYEDLRDALEKLQLNDASLTYEPETSAALGFGFRCG 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138  80 FLGLLHMEVFNQRLEQEYNASVILTTPTVPYKAVLSSSKlikehrekEITIINPAQFPDKSKVTEYLEPVVLGTIITPDE 159
Cdd:COG0481   344 FLGLLHMEIIQERLEREFDLDLITTAPSVVYEVTLTDGE--------VIEVDNPSDLPDPGKIEEIEEPIVKATIITPSE 415

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 160 YTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIVVDFYDSLKSLSSGYASFDYEDAGYQTAELVKMDILLNGNTV 239
Cdd:COG0481   416 YVGAVMELCQEKRGVQKNMEYLGENRVELTYELPLAEIVFDFFDRLKSITRGYASLDYEFIGYRESDLVKLDILINGEPV 495

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 240 EELVTVVHKDKAHSIGKAICERLKDSLPRQLFEIAIQAAIGSKIIARETVKAYRKNVLAKCYGGDITRKMKLLKRQAEGK 319
Cdd:COG0481   496 DALSFIVHRDKAYSRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVLAKCYGGDISRKRKLLEKQKEGK 575

                         330       340
                  ....*....|....*....|..
gi 1064244138 320 KKLRKIGNVEVPKDAFIKVLKT 341
Cdd:COG0481   576 KRMKQVGNVEIPQEAFLAVLKV 597
lepA TIGR01393
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ...
 2-341 1.12e-176

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: 503.01  E-value: 1.12e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138   2 KDVTEAQIGDTLCLHKQPV-EPLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLALGAGWRLGF 80
Cdd:TIGR01393 262 KDVSDVRVGDTITHVKNPAkEPLPGFKEVKPMVFAGLYPIDTEDYEDLRDALEKLKLNDASLTYEPESSPALGFGFRCGF 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138  81 LGLLHMEVFNQRLEQEYNASVILTTPTVPYKAVLSSSKlikehrekEITIINPAQFPDKSKVTEYLEPVVLGTIITPDEY 160
Cdd:TIGR01393 342 LGLLHMEIIQERLEREFNLDLITTAPSVIYRVYLTNGE--------VIEVDNPSDLPDPGKIEHVEEPYVKATIITPTEY 413

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 161 TGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIVVDFYDSLKSLSSGYASFDYEDAGYQTAELVKMDILLNGNTVE 240
Cdd:TIGR01393 414 LGPIMTLCQEKRGVQTNMEYLDPNRVELIYEMPLAEIVYDFFDKLKSISRGYASFDYELIGYRPSDLVKLDILINGEPVD 493

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 241 ELVTVVHKDKAHSIGKAICERLKDSLPRQLFEIAIQAAIGSKIIARETVKAYRKNVLAKCYGGDITRKMKLLKRQAEGKK 320
Cdd:TIGR01393 494 ALSFIVHRDKAYSRGREICEKLKELIPRQQFEIPIQAAIGGKIIARETIKALRKDVTAKCYGGDITRKRKLLEKQKEGKK 573

                         330       340
                  ....*....|....*....|.
gi 1064244138 321 KLRKIGNVEVPKDAFIKVLKT 341
Cdd:TIGR01393 574 RMKQIGKVEVPQEAFLAVLKV 594
LepA_C pfam06421
GTP-binding protein LepA C-terminus; This family consists of the C-terminal region of several ...
 234-340 1.90e-68

GTP-binding protein LepA C-terminus; This family consists of the C-terminal region of several pro- and eukaryotic GTP-binding LepA proteins.


Pssm-ID: 461905 [Multi-domain]  Cd Length: 107  Bit Score: 209.57  E-value: 1.90e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 234 LNGNTVEELVTVVHKDKAHSIGKAICERLKDSLPRQLFEIAIQAAIGSKIIARETVKAYRKNVLAKCYGGDITRKMKLLK 313
Cdd:pfam06421   1 INGEPVDALSFIVHRSKAYRRGRALVEKLKELIPRQQFEVPIQAAIGGKIIARETIKALRKDVTAKCYGGDISRKKKLLE 80

                          90       100
                  ....*....|....*....|....*..
gi 1064244138 314 RQAEGKKKLRKIGNVEVPKDAFIKVLK 340
Cdd:pfam06421  81 KQKEGKKRMKQIGNVEIPQEAFLAVLK 107
EF4_III cd16260
Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ...
 31-106 2.00e-46

Domain III of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly conserved guanosine triphosphatase found in bacteria and eukaryotic mitochondria and chloroplasts. EF4 functions as a translation factor, which promotes back-translocation of tRNAs on posttranslocational ribosome complexes and competes with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis.


Pssm-ID: 293917 [Multi-domain]  Cd Length: 76  Bit Score: 152.27  E-value: 2.00e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1064244138  31 PMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLALGAGWRLGFLGLLHMEVFNQRLEQEYNASVILTTP 106
Cdd:cd16260     1 PMVFAGLYPVDGSDYEELRDALEKLTLNDASVTFEPETSSALGFGFRCGFLGLLHMEVFQERLEREYGLDLIITAP 76
lepA_C cd03709
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ...
 147-226 3.05e-46

lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized in the cytoplasmic membrane. LepA is ubiquitous in Bacteria and Eukaryota (e.g. Saccharomyces cerevisiae GUF1p), but is missing from Archaea. LepA exhibits significant homology to elongation factors (EFs) Tu and G. The function(s) of the proteins in this family are unknown. The N-terminal domain of LepA is homologous to a domain of similar size found in initiation factor 2 (IF2), and in EF-Tu and EF-G (factors required for translation in Escherichia coli). Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including S. cerevisiae GUF1) originated within the bacterial LepA family. LepA has never been observed in archaea, and eukaryl LepA is organellar. LepA is therefore a true bacterial GTPase, found only in the bacterial lineage.


Pssm-ID: 239680 [Multi-domain]  Cd Length: 80  Bit Score: 151.88  E-value: 3.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 147 EPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIVVDFYDSLKSLSSGYASFDYEDAGYQTAE 226
Cdd:cd03709     1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIVYDFFDKLKSISKGYASLDYELIGYRESD 80
EFG_C pfam00679
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 144-232 2.59e-26

Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.


Pssm-ID: 425814 [Multi-domain]  Cd Length: 88  Bit Score: 99.93  E-value: 2.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 144 EYLEPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 223
Cdd:pfam00679   1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAEL-FGFATELRSLTKGRGSFSMEFSGYQ 79


                  ....*....
gi 1064244138 224 TAELVKMDI 232
Cdd:pfam00679  80 PVPGDILDR 88
Elongation_Factor_C cd01514
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ...
 147-225 2.79e-26

Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of elongation factors (EFs) bacterial EF-G, eukaryotic and archeal EF-2 and eukaryotic mitochondrial mtEFG1s and mtEFG2s. This group also includes proteins similar to the ribosomal protection proteins Tet(M) and Tet(O), BipA, LepA and, spliceosomal proteins: human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and yeast counterpart Snu114p. This domain adopts a ferredoxin-like fold consisting of an alpha-beta sandwich with anti-parallel beta-sheets, resembling the topology of domain III found in the elongation factors EF-G and eukaryotic EF-2, with which it forms the C-terminal block. The two domains however are not superimposable and domain III lacks some of the characteristics of this domain. EF-2/EF-G in complex with GTP, promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome. Tet(M) and Tet(O) mediate Tc resistance. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. Yeast Snu114p is essential for cell viability and for splicing in vivo. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. The function of LepA proteins is unknown.


Pssm-ID: 238772 [Multi-domain]  Cd Length: 79  Bit Score: 99.48  E-value: 2.79e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1064244138 147 EPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQTA 225
Cdd:cd01514     1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEM-FGFATDLRSLTQGRASFSMEFSHYEPV 78
EFG_III-like cd16257
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ...
 31-104 1.13e-10

Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G (EF-G) and related proteins play a role in translation and share a similar domain architecture. Elongation factor EFG participates in the elongation phase during protein biosynthesis on the ribosome by stimulating translocation. Its functional cycles depend on GTP binding and its hydrolysis. Domain III is involved in the activation of GTP hydrolysis. This domain III, which is different from domain III in EF-TU and related elongation factors, is found in several translation factors, like bacterial release factors RF3, elongation factor 4, elongation factor 2, GTP-binding protein BipA and tetracycline resistance protein Tet.


Pssm-ID: 293914 [Multi-domain]  Cd Length: 71  Bit Score: 56.97  E-value: 1.13e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1064244138  31 PMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSlalGAGWRLGFLGLLHMEVFNQRLEQEYNASVILT 104
Cdd:cd16257     1 PVVFVTVEVKNPLDQEKLLEGLERLSEEDPALQVYREES---TGEFILSGLGELHLEIIVARLEREYGVELVVS 71
EFG_mtEFG_C cd03713
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ...
 147-223 1.57e-09

EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational elongation factor (EF) EF-G. Included in this group is the C-terminus of mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2) proteins. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homologue of mtEFG2, MEF2.


Pssm-ID: 239683 [Multi-domain]  Cd Length: 78  Bit Score: 53.69  E-value: 1.57e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1064244138 147 EPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIfIDQNRVMLKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 223
Cdd:cd03713     1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTE-SRGGWKVIKAEVPLAEM-FGYSTDLRSLTQGRGSFTMEFSHYE 75
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
6-223 1.99e-07

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 52.44  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138   6 EAQIGDTLCLHKQPVePLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLA---LGAgwrlgfLG 82
Cdd:PRK12740  362 DAATGDTLCDKGDPI-LLEPMEFPEPVISLAIEPKDKGDEEKLSEALGKLAEEDPTLRVERDEETGqtiLSG------MG 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138  83 LLHMEVFNQRLEQEYNASVILTTPTVPY-----KAVLSSSKLIKE-----------------HREKEITIIN-------P 133
Cdd:PRK12740  435 ELHLDVALERLKREYGVEVETGPPQVPYretirKKAEGHGRHKKQsgghgqfgdvwleveplPRGEGFEFVDkvvggavP 514

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 134 AQF-P--DKS------------------KVTEY---------------------------------LEPVVLGTIITPDE 159
Cdd:PRK12740  515 RQYiPavEKGvrealekgvlagypvvdvKVTLTdgsyhsvdssemafkiaarlafrealpkakpvlLEPIMKVEVSVPEE 594

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1064244138 160 YTGKIMMLCEARRAVQKNMiFIDQNRVMLKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 223
Cdd:PRK12740  595 FVGDVIGDLSSRRGRILGM-ESRGGGDVVRAEVPLAEM-FGYATDLRSLTQGRGSFSMEFSHYE 656
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 1-223 7.29e-07

Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 50.81  E-value: 7.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138   1 MKDVTeaqIGDTLCLHKQPVEpLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLA--LGAGwrl 78
Cdd:COG0480   378 LKDTT---TGDTLCDEDHPIV-LEPIEFPEPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETDEETGqtIISG--- 450

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138  79 gfLGLLHMEVFNQRLEQEYNASVILTTPTVPY-----KAVLSSSKLIKE-----------------HREKEITIIN---- 132
Cdd:COG0480   451 --MGELHLEIIVDRLKREFGVEVNVGKPQVAYretirKKAEAEGKHKKQsgghgqygdvwieieplPRGEGFEFVDkivg 528

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 133 ---PAQF-P--DKS------------------KVTEY---------------------------------LEPVVLGTII 155
Cdd:COG0480   529 gviPKEYiPavEKGireamekgvlagypvvdvKVTLYdgsyhpvdssemafkiaasmafkeaakkakpvlLEPIMKVEVT 608

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 156 TPDEYTGKIMMLCEARRAVQKNMifiDQ--NRVMLKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 223
Cdd:COG0480   609 VPEEYMGDVMGDLNSRRGRILGM---ESrgGAQVIKAEVPLAEM-FGYATDLRSLTQGRGSFTMEFSHYE 674
PRK13351 PRK13351
elongation factor G-like protein;
6-225 2.44e-06

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 49.18  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138   6 EAQIGDTLCLHKQPVEpLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDS----SLALGagwrlgfL 81
Cdd:PRK13351  379 ELETGDTLHDSADPVL-LELLTFPEPVVSLAVEPERRGDEQKLAEALEKLVWEDPSLRVEEDEetgqTILSG-------M 450

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138  82 GLLHMEVFNQRLEQEYNASVILTTPTVPYKAVLSSS-------------------------------------------- 117
Cdd:PRK13351  451 GELHLEVALERLRREFKLEVNTGKPQVAYRETIRKMaegvyrhkkqfggkgqfgevhlrveplergagfifvskvvggai 530

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138 118 -KLIKEHREK-------------------EITIINPAQFPDKSKVT-------------------EYLEPVVLGTIITPD 158
Cdd:PRK13351  531 pEELIPAVEKgirealasgplagypvtdlRVTVLDGKYHPVDSSESafkaaarkafleafrkanpVLLEPIMELEITVPT 610

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1064244138 159 EYTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEiVVDFYDSLKSLSSGYASFDYEDAGYQTA 225
Cdd:PRK13351  611 EHVGDVLGDLSQRRGRIEGTEPRGDGEVLVKAEAPLAE-LFGYATRLRSMTKGRGSFTMEFSHFDPV 676
BipA_TypA_C cd03710
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ...
 147-193 2.16e-04

BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of the elongation factors EF-G and EF-2. A member of the ribosome binding GTPase superfamily, BipA is widely distributed in bacteria and plants. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and, is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion.


Pssm-ID: 239681 [Multi-domain]  Cd Length: 79  Bit Score: 39.41  E-value: 2.16e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1064244138 147 EPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFP 193
Cdd:cd03710     1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIP 47
EFG_III cd16262
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ...
 30-106 9.44e-04

Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial Elongation factor G (EF-G), and mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2), which play an important role during peptide synthesis and tRNA site changes. In bacteria, this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects, and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants of the yeast homolog of mtEFG2, MEF2.


Pssm-ID: 293919 [Multi-domain]  Cd Length: 76  Bit Score: 37.44  E-value: 9.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1064244138  30 KPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRD--SSLALGAGwrlgfLGLLHMEVFNQRLEQEYNASVILTTP 106
Cdd:cd16262     2 EPVISLAIEPKTKADEDKLSKALARLAEEDPTLRVSRDeeTGQTILSG-----MGELHLEIIVERLKREYGVEVEVGKP 75
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
 146-223 3.10e-03

Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.


Pssm-ID: 197906 [Multi-domain]  Cd Length: 85  Bit Score: 36.33  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064244138  146 LEPVVLGTIITPDEYTGKIMMLCEARRAVQKNMifiDQNRVM--LKYLFPLNEIvVDFYDSLKSLSSGYASFDYEDAGYQ 223
Cdd:smart00838   2 LEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGM---EQRGGAqvIKAKVPLSEM-FGYATDLRSATQGRATWSMEFSHYE 77
RF3_III cd16259
Domain III of bacterial Release Factor 3 (RF3); The class II RF3 is a member of one of two ...
 31-104 3.77e-03

Domain III of bacterial Release Factor 3 (RF3); The class II RF3 is a member of one of two release factor (RF) classes required for the termination of protein synthesis by the ribosome. RF3 is a GTPase that removes class I RFs (RF1 or RF2) from the ribosome after release of the nascent polypeptide. RF3 in the GDP state binds to the ribosomal class I RF complex, followed by an exchange of GDP for GTP and release of the class I RF. Sequence comparison of class II release factors with elongation factors shows that prokaryotic RF3 is more similar to EF-G whereas eukaryotic eRF3 is more similar to eEF1A, implying that their precise function may differ.


Pssm-ID: 293916 [Multi-domain]  Cd Length: 70  Bit Score: 35.69  E-value: 3.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1064244138  31 PMVFAGMYPLDQSEYNNLKSAIEKLTlNDSSVTVHRDSSlalGAGWRLGFLGLLHMEVFNQRLEQEYNASVILT 104
Cdd:cd16259     1 PEHFRRVRLKDPMKAKQLRKGLEQLA-EEGAVQVFRPMD---GSDPIVGAVGPLQFEVLQARLENEYGVEVVFE 70
EFG_III pfam14492
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ...
 30-103 5.26e-03

Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a similar structure with domain V (pfam00679). Structural studies in drosophila indicate this is domain 3.


Pssm-ID: 464188 [Multi-domain]  Cd Length: 75  Bit Score: 35.15  E-value: 5.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1064244138  30 KPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSslalGAG-WRLGFLGLLHMEVFNQRLEQEYNASVIL 103
Cdd:pfam14492   3 EPVISVAIEPKTKGDEDKLSKALNRLLEEDPTLRVERDE----ETGeTILSGMGELHLEIVVDRLKRKYGVEVEL 73
 
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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